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Conserved domains on  [gi|30267738|gb|AAP21670|]
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Shy23 [Streptomyces hygroscopicus subsp. yingchengensis]

Protein Classification

SDR family oxidoreductase( domain architecture ID 10143144)

SDR family NAD(P)-dependent oxidoreductase with similarity to mammalian carbonyl reductase, which catalyzes the NADPH-dependent reduction of a wide range of substrates including quinones, prostaglandins, and other carbonyl-containing compounds

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 23-257 3.71e-95

Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR which catalyzes the NADPH-dependent reduction of ketones on steroids and prostaglandins. Unlike most SDRs, PTCR functions as a monomer. This subgroup also includes human carbonyl reductase 1 (CBR1) and CBR3. CBR1 is an NADPH-dependent SDR with broad substrate specificity and may be responsible for the in vivo reduction of quinones, prostaglandins, and other carbonyl-containing compounds. In addition it includes poppy NADPH-dependent salutaridine reductase which catalyzes the stereospecific reduction of salutaridine to 7(S)-salutaridinol in the biosynthesis of morphine, and Arabidopsis SDR1,a menthone reductase, which catalyzes the reduction of menthone to neomenthol, a compound with antimicrobial activity; SDR1 can also carry out neomenthol oxidation. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


:

Pssm-ID: 187585 [Multi-domain]  Cd Length: 225  Bit Score: 278.74  E-value: 3.71e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  23 RTALVTGANKGIGKHIARVLVAEG-LTVYVGSRDRGLGQRAVEEI---GAGARLLVLDVTDLDGIARATTQV----DRLD 94
Cdd:cd05324   1 KVALVTGANRGIGFEIVRQLAKSGpGTVILTARDVERGQAAVEKLraeGLSVRFHQLDVTDDASIEAAADFVeekyGGLD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  95 VLVNNAGISPSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTASLTWstnpnpqftpgsgga 174
Cdd:cd05324  81 ILVNNAGIAFKGFDDSTPTREQARETMKTNFFGTVDVTQALLPLLKKSPAGRIVNVSSGLGSLTS--------------- 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738 175 aAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDLNPLAAAagDDPAEAAQGAARLALLPDDGPTGGFFSWDGTP 254
Cdd:cd05324 146 -AYGVSKAALNALTRILAKELKETGIKVNACCPGWVKTDMGGGKAP--KTPEEGAETPVYLALLPPDGEPTGKFFSDKKV 222


                ...
gi 30267738 255 VPW 257
Cdd:cd05324 223 VPW 225
 
Name Accession Description Interval E-value
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 23-257 3.71e-95

Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR which catalyzes the NADPH-dependent reduction of ketones on steroids and prostaglandins. Unlike most SDRs, PTCR functions as a monomer. This subgroup also includes human carbonyl reductase 1 (CBR1) and CBR3. CBR1 is an NADPH-dependent SDR with broad substrate specificity and may be responsible for the in vivo reduction of quinones, prostaglandins, and other carbonyl-containing compounds. In addition it includes poppy NADPH-dependent salutaridine reductase which catalyzes the stereospecific reduction of salutaridine to 7(S)-salutaridinol in the biosynthesis of morphine, and Arabidopsis SDR1,a menthone reductase, which catalyzes the reduction of menthone to neomenthol, a compound with antimicrobial activity; SDR1 can also carry out neomenthol oxidation. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187585 [Multi-domain]  Cd Length: 225  Bit Score: 278.74  E-value: 3.71e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  23 RTALVTGANKGIGKHIARVLVAEG-LTVYVGSRDRGLGQRAVEEI---GAGARLLVLDVTDLDGIARATTQV----DRLD 94
Cdd:cd05324   1 KVALVTGANRGIGFEIVRQLAKSGpGTVILTARDVERGQAAVEKLraeGLSVRFHQLDVTDDASIEAAADFVeekyGGLD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  95 VLVNNAGISPSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTASLTWstnpnpqftpgsgga 174
Cdd:cd05324  81 ILVNNAGIAFKGFDDSTPTREQARETMKTNFFGTVDVTQALLPLLKKSPAGRIVNVSSGLGSLTS--------------- 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738 175 aAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDLNPLAAAagDDPAEAAQGAARLALLPDDGPTGGFFSWDGTP 254
Cdd:cd05324 146 -AYGVSKAALNALTRILAKELKETGIKVNACCPGWVKTDMGGGKAP--KTPEEGAETPVYLALLPPDGEPTGKFFSDKKV 222


                ...
gi 30267738 255 VPW 257
Cdd:cd05324 223 VPW 225
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 20-237 4.54e-54

NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and metabolism]; NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440651 [Multi-domain]  Cd Length: 249  Bit Score: 174.59  E-value: 4.54e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  20 MNDRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEI---GAGARLLVLDVTDLDGIARATTQV----DR 92
Cdd:COG1028   4 LKGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAELraaGGRALAVAADVTDEAAVEALVAAAvaafGR 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  93 LDVLVNNAGISPSlAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTASLtwstnpnpqftpGSG 172
Cdd:COG1028  84 LDILVNNAGITPP-GPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIAGLR------------GSP 150

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30267738 173 GAAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATdlnPLAAAAGDDPAEAAQGAARLAL 237
Cdd:COG1028 151 GQAAYAASKAAVVGLTRSLALELAPRGIRVNAVAPGPIDT---PMTRALLGAEEVREALAARIPL 212
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 23-215 1.49e-44

short chain dehydrogenase; This family contains a wide variety of dehydrogenases.


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 148.53  E-value: 1.49e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738    23 RTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEIGA---GARLLVLDVTDLDGIARATTQV----DRLDV 95
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKELGAlggKALFIQGDVTDRAQVKALVEQAverlGRLDI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738    96 LVNNAGISPsLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTAsltwsTNPNPQFtpgsggaA 175
Cdd:pfam00106  81 LVNNAGITG-LGPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNISSVAG-----LVPYPGG-------S 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 30267738   176 AYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDLN 215
Cdd:pfam00106 148 AYSASKAAVIGFTRSLALELAPHGIRVNAVAPGGVDTDMT 187
PRK08264 PRK08264
SDR family oxidoreductase;
20-237 4.51e-41

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 141.18  E-value: 4.51e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   20 MNDRTALVTGANKGIGKHIARVLVAEGLT-VYVGSRDrglgQRAVEEIGAGARLLVLDVTDLDGIARATTQVDRLDVLVN 98
Cdd:PRK08264   4 IKGKVVLVTGANRGIGRAFVEQLLARGAAkVYAAARD----PESVTDLGPRVVPLQLDVTDPASVAAAAEAASDVTILVN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   99 NAGISPSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSgtaSLTWSTNPNpqftpgsggAAAYR 178
Cdd:PRK08264  80 NAGIFRTGSLLLEGDEDALRAEMETNYFGPLAMARAFAPVLAANGGGAIVNVLS---VLSWVNFPN---------LGTYS 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 30267738  179 SSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDLnplaAAAGDDPAEAAQGAARLAL 237
Cdd:PRK08264 148 ASKAAAWSLTQALRAELAPQGTRVLGVHPGPIDTDM----AAGLDAPKASPADVARQIL 202
3oxo_ACP_reduc TIGR01830
3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, ...
 25-213 6.05e-25

3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, also called 3-ketoacyl-acyl carrier protein reductase, an enzyme of fatty acid biosynthesis. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 273824 [Multi-domain]  Cd Length: 239  Bit Score: 98.82  E-value: 6.05e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738    25 ALVTGANKGIGKHIARVLVAEGLTVYV-GSRDRGLGQRAVEEI---GAGARLLVLDVTDLD----GIARATTQVDRLDVL 96
Cdd:TIGR01830   1 ALVTGASRGIGRAIALKLAKEGAKVIItYRSSEEGAEEVVEELkalGVKALGVVLDVSDREdvkaVVEEIEEELGTIDIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738    97 VNNAGISpslappADT-----SVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTASLtwstnpnpqftpGS 171
Cdd:TIGR01830  81 VNNAGIT------RDNllmrmKEEDWDAVIDTNLTGVFNLTQAVLRIMIKQRSGRIINISSVVGLM------------GN 142

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 30267738   172 GGAAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATD 213
Cdd:TIGR01830 143 AGQANYAASKAGVIGFTKSLAKELASRNITVNAVAPGFIDTD 184
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 23-187 6.42e-06

This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.


Pssm-ID: 214833 [Multi-domain]  Cd Length: 180  Bit Score: 45.55  E-value: 6.42e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738     23 RTALVTGANKGIGKHIARVLVAEG-----LTVYVGSRDRGLGQRAVEEIGAGARLLVL--DVTDLDGIARATTQVD---- 91
Cdd:smart00822   1 GTYLITGGLGGLGRALARWLAERGarrlvLLSRSGPDAPGAAALLAELEAAGARVTVVacDVADRDALAAVLAAIPaveg 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738     92 RLDVLVNNAGIsPSLAPPADTSVEEFRRTYETNVFGVVAVTNAFlpalRRSPHPRIVNISSGTASLtwstnpnpqftpGS 171
Cdd:smart00822  81 PLTGVIHAAGV-LDDGVLASLTPERFAAVLAPKAAGAWNLHELT----ADLPLDFFVLFSSIAGVL------------GS 143

                          170
                   ....*....|....*.
gi 30267738    172 GGAAAYRSSKAALNAL 187
Cdd:smart00822 144 PGQANYAAANAFLDAL 159
 
Name Accession Description Interval E-value
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 23-257 3.71e-95

Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR which catalyzes the NADPH-dependent reduction of ketones on steroids and prostaglandins. Unlike most SDRs, PTCR functions as a monomer. This subgroup also includes human carbonyl reductase 1 (CBR1) and CBR3. CBR1 is an NADPH-dependent SDR with broad substrate specificity and may be responsible for the in vivo reduction of quinones, prostaglandins, and other carbonyl-containing compounds. In addition it includes poppy NADPH-dependent salutaridine reductase which catalyzes the stereospecific reduction of salutaridine to 7(S)-salutaridinol in the biosynthesis of morphine, and Arabidopsis SDR1,a menthone reductase, which catalyzes the reduction of menthone to neomenthol, a compound with antimicrobial activity; SDR1 can also carry out neomenthol oxidation. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187585 [Multi-domain]  Cd Length: 225  Bit Score: 278.74  E-value: 3.71e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  23 RTALVTGANKGIGKHIARVLVAEG-LTVYVGSRDRGLGQRAVEEI---GAGARLLVLDVTDLDGIARATTQV----DRLD 94
Cdd:cd05324   1 KVALVTGANRGIGFEIVRQLAKSGpGTVILTARDVERGQAAVEKLraeGLSVRFHQLDVTDDASIEAAADFVeekyGGLD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  95 VLVNNAGISPSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTASLTWstnpnpqftpgsgga 174
Cdd:cd05324  81 ILVNNAGIAFKGFDDSTPTREQARETMKTNFFGTVDVTQALLPLLKKSPAGRIVNVSSGLGSLTS--------------- 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738 175 aAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDLNPLAAAagDDPAEAAQGAARLALLPDDGPTGGFFSWDGTP 254
Cdd:cd05324 146 -AYGVSKAALNALTRILAKELKETGIKVNACCPGWVKTDMGGGKAP--KTPEEGAETPVYLALLPPDGEPTGKFFSDKKV 222


                ...
gi 30267738 255 VPW 257
Cdd:cd05324 223 VPW 225
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 20-237 4.54e-54

NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and metabolism]; NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440651 [Multi-domain]  Cd Length: 249  Bit Score: 174.59  E-value: 4.54e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  20 MNDRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEI---GAGARLLVLDVTDLDGIARATTQV----DR 92
Cdd:COG1028   4 LKGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAELraaGGRALAVAADVTDEAAVEALVAAAvaafGR 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  93 LDVLVNNAGISPSlAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTASLtwstnpnpqftpGSG 172
Cdd:COG1028  84 LDILVNNAGITPP-GPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIAGLR------------GSP 150

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30267738 173 GAAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATdlnPLAAAAGDDPAEAAQGAARLAL 237
Cdd:COG1028 151 GQAAYAASKAAVVGLTRSLALELAPRGIRVNAVAPGPIDT---PMTRALLGAEEVREALAARIPL 212
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 21-241 4.90e-53

NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; NADP-dependent 3-hydroxy acid dehydrogenase YdfG is part of the Pathway/BioSystem: Pyrimidine degradation


Pssm-ID: 443365 [Multi-domain]  Cd Length: 240  Bit Score: 171.90  E-value: 4.90e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  21 NDRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEIGAGARLLVLDVTDLDGIARATTQV----DRLDVL 96
Cdd:COG4221   4 KGKVALITGASSGIGAATARALAAAGARVVLAARRAERLEALAAELGGRALAVPLDVTDEAAVEAAVAAAvaefGRLDVL 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  97 VNNAGISPsLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSgtaslTWSTNPNPqftpgsgGAAA 176
Cdd:COG4221  84 VNNAGVAL-LGPLEELDPEDWDRMIDVNVKGVLYVTRAALPAMRARGSGHIVNISS-----IAGLRPYP-------GGAV 150

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30267738 177 YRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDLNpLAAAAGDDPAEAAQGAARLALLPDD 241
Cdd:COG4221 151 YAATKAAVRGLSESLRAELRPTGIRVTVIEPGAVDTEFL-DSVFDGDAEAAAAVYEGLEPLTPED 214
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
 25-257 6.00e-52

carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl reductase of the classical SDR family. Studies in Drosophila melanogaster implicate Sniffer in the prevention of neurodegeneration due to aging and oxidative-stress. This subgroup also includes Rhodococcus sp. AD45 IsoH, which is an NAD-dependent 1-hydroxy-2-glutathionyl-2-methyl-3-butene dehydrogenase involved in isoprene metabolism, Aspergillus nidulans StcE encoded by a gene which is part of a proposed sterigmatocystin biosynthesis gene cluster, Bacillus circulans SANK 72073 BtrF encoded by a gene found in the butirosin biosynthesis gene cluster, and Aspergillus parasiticus nor-1 involved in the biosynthesis of aflatoxins. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187586 [Multi-domain]  Cd Length: 233  Bit Score: 169.01  E-value: 6.00e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  25 ALVTGANKGIGKHIARVLVAEG-LTVYVGSRDRGLGQRAVEEIGAGARL--LVLDVTDLDGIA----RATTQVDRLDVLV 97
Cdd:cd05325   1 VLITGASRGIGLELVRQLLARGnNTVIATCRDPSAATELAALGASHSRLhiLELDVTDEIAESaeavAERLGDAGLDVLI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  98 NNAGISPSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTASLTWSTnpnpqftpgSGGAAAY 177
Cdd:cd05325  81 NNAGILHSYGPASEVDSEDLLEVFQVNVLGPLLLTQAFLPLLLKGARAKIINISSRVGSIGDNT---------SGGWYSY 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738 178 RSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDL-NPLAAAAGD-DPAEAAQGA-ARLALLpDDGPTGGFFSWDGTP 254
Cdd:cd05325 152 RASKAALNMLTKSLAVELKRDGITVVSLHPGWVRTDMgGPFAKNKGPiTPEESVAGLlKVIDNL-NEEDSGKFLDYDGTE 230


                ...
gi 30267738 255 VPW 257
Cdd:cd05325 231 IPW 233
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
19-237 1.90e-51

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 168.12  E-value: 1.90e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  19 AMNDRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEI---GAGARLLVLDVTDLDGIARATTQVD---- 91
Cdd:COG0300   2 SLTGKTVLITGASSGIGRALARALAARGARVVLVARDAERLEALAAELraaGARVEVVALDVTDPDAVAALAEAVLarfg 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  92 RLDVLVNNAGISPSlAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTASLtwstnpnpqftpGS 171
Cdd:COG0300  82 PIDVLVNNAGVGGG-GPFEELDLEDLRRVFEVNVFGPVRLTRALLPLMRARGRGRIVNVSSVAGLR------------GL 148

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30267738 172 GGAAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDLNPLAAAAGDDPAEAAQGAARLAL 237
Cdd:COG0300 149 PGMAAYAASKAALEGFSESLRAELAPTGVRVTAVCPGPVDTPFTARAGAPAGRPLLSPEEVARAIL 214
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
 23-208 1.07e-46

17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187632 [Multi-domain]  Cd Length: 248  Bit Score: 155.85  E-value: 1.07e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  23 RTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEIGAGARLLVLDVTDLDGIARATTQVD----RLDVLVN 98
Cdd:cd05374   1 KVVLITGCSSGIGLALALALAAQGYRVIATARNPDKLESLGELLNDNLEVLELDVTDEESIKAAVKEVIerfgRIDVLVN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  99 NAGISpSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSgtaslTWSTNPNPqftpgsgGAAAYR 178
Cdd:cd05374  81 NAGYG-LFGPLEETSIEEVRELFEVNVFGPLRVTRAFLPLMRKQGSGRIVNVSS-----VAGLVPTP-------FLGPYC 147

                       170       180       190
                ....*....|....*....|....*....|
gi 30267738 179 SSKAALNALTVLYAQTLAEDGFKVNALAPG 208
Cdd:cd05374 148 ASKAALEALSESLRLELAPFGIKVTIIEPG 177
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
 22-256 1.08e-46

retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) OxidoReductase (LPOR) and related proteins, classical (c) SDRs; Classical SDR subgroup containing retinol-DHs, LPORs, and related proteins. Retinol is processed by a medium chain alcohol dehydrogenase followed by retinol-DHs. Pchlide reductases act in chlorophyll biosynthesis. There are distinct enzymes that catalyze Pchlide reduction in light or dark conditions. Light-dependent reduction is via an NADP-dependent SDR, LPOR. Proteins in this subfamily share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. This subgroup includes the human proteins: retinol dehydrogenase -12, -13 ,and -14, dehydrogenase/reductase SDR family member (DHRS)-12 , -13 and -X (a DHRS on chromosome X), and WWOX (WW domain-containing oxidoreductase), as well as a Neurospora crassa SDR encoded by the blue light inducible bli-4 gene. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212492 [Multi-domain]  Cd Length: 269  Bit Score: 156.62  E-value: 1.08e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  22 DRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEI-----GAGARLLVLDVTDLDGIARATTQV----DR 92
Cdd:cd05327   1 GKVVVITGANSGIGKETARELAKRGAHVIIACRNEEKGEEAAAEIkketgNAKVEVIQLDLSSLASVRQFAEEFlarfPR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  93 LDVLVNNAGIspsLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTASLTWS--TNPNPQFTPG 170
Cdd:cd05327  81 LDILINNAGI---MAPPRRLTKDGFELQFAVNYLGHFLLTNLLLPVLKASAPSRIVNVSSIAHRAGPIdfNDLDLENNKE 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738 171 SGGAAAYRSSKAALnaltVLYAQTLAE----DGFKVNALAPGMRATDL---NPLAAAA--------GDDPAEAAQGAARL 235
Cdd:cd05327 158 YSPYKAYGQSKLAN----ILFTRELARrlegTGVTVNALHPGVVRTELlrrNGSFFLLykllrpflKKSPEQGAQTALYA 233

                       250       260
                ....*....|....*....|..
gi 30267738 236 ALLPDD-GPTGGFFSWDGTPVP 256
Cdd:cd05327 234 ATSPELeGVSGKYFSDCKIKMS 255
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 25-241 3.30e-46

classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212491 [Multi-domain]  Cd Length: 234  Bit Score: 153.98  E-value: 3.30e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  25 ALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAV--EEIGAGARLLVLDVTDLDGIARATTQVD----RLDVLVN 98
Cdd:cd05233   1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEALAELAaiEALGGNAVAVQADVSDEEDVEALVEEALeefgRLDILVN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  99 NAGISPsLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTASLtwstnpnpqftpGSGGAAAYR 178
Cdd:cd05233  81 NAGIAR-PGPLEELTDEDWDRVLDVNLTGVFLLTRAALPHMKKQGGGRIVNISSVAGLR------------PLPGQAAYA 147

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30267738 179 SSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDLNPLAAAAGDDPAEAAQGAARLALLPDD 241
Cdd:cd05233 148 ASKAALEGLTRSLALELAPYGIRVNAVAPGLVDTPMLAKLGPEEAEKELAAAIPLGRLGTPEE 210
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 23-215 1.49e-44

short chain dehydrogenase; This family contains a wide variety of dehydrogenases.


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 148.53  E-value: 1.49e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738    23 RTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEIGA---GARLLVLDVTDLDGIARATTQV----DRLDV 95
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKELGAlggKALFIQGDVTDRAQVKALVEQAverlGRLDI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738    96 LVNNAGISPsLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTAsltwsTNPNPQFtpgsggaA 175
Cdd:pfam00106  81 LVNNAGITG-LGPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNISSVAG-----LVPYPGG-------S 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 30267738   176 AYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDLN 215
Cdd:pfam00106 148 AYSASKAAVIGFTRSLALELAPHGIRVNAVAPGGVDTDMT 187
PRK08264 PRK08264
SDR family oxidoreductase;
20-237 4.51e-41

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 141.18  E-value: 4.51e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   20 MNDRTALVTGANKGIGKHIARVLVAEGLT-VYVGSRDrglgQRAVEEIGAGARLLVLDVTDLDGIARATTQVDRLDVLVN 98
Cdd:PRK08264   4 IKGKVVLVTGANRGIGRAFVEQLLARGAAkVYAAARD----PESVTDLGPRVVPLQLDVTDPASVAAAAEAASDVTILVN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   99 NAGISPSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSgtaSLTWSTNPNpqftpgsggAAAYR 178
Cdd:PRK08264  80 NAGIFRTGSLLLEGDEDALRAEMETNYFGPLAMARAFAPVLAANGGGAIVNVLS---VLSWVNFPN---------LGTYS 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 30267738  179 SSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDLnplaAAAGDDPAEAAQGAARLAL 237
Cdd:PRK08264 148 ASKAAAWSLTQALRAELAPQGTRVLGVHPGPIDTDM----AAGLDAPKASPADVARQIL 202
FabG-like PRK07231
SDR family oxidoreductase;
22-233 6.34e-39

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 135.73  E-value: 6.34e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   22 DRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEIGAGARLLVL--DVTDLDGIARATTQVD----RLDV 95
Cdd:PRK07231   5 GKVAIVTGASSGIGEGIARRFAAEGARVVVTDRNEEAAERVAAEILAGGRAIAVaaDVSDEADVEAAVAAALerfgSVDI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   96 LVNNAGISPSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSgTASLTwstnpnpqftpGSGGAA 175
Cdd:PRK07231  85 LVNNAGTTHRNGPLLDVDEAEFDRIFAVNVKSPYLWTQAAVPAMRGEGGGAIVNVAS-TAGLR-----------PRPGLG 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 30267738  176 AYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDLnpLAAAAGDDPAEAAQGAA 233
Cdd:PRK07231 153 WYNASKGAVITLTKALAAELGPDKIRVNAVAPVVVETGL--LEAFMGEPTPENRAKFL 208
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
20-229 8.11e-38

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 132.98  E-value: 8.11e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   20 MNDRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEI---GAGARLLVLDVTDLD----GIARATTQVDR 92
Cdd:PRK05653   3 LQGKTALVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEALAAELraaGGEARVLVFDVSDEAavraLIEAAVEAFGA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   93 LDVLVNNAGISPSlAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTASLtwstnpnpqftpGSG 172
Cdd:PRK05653  83 LDILVNNAGITRD-ALLPRMSEEDWDRVIDVNLTGTFNVVRAALPPMIKARYGRIVNISSVSGVT------------GNP 149

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 30267738  173 GAAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDLNplaAAAGDDPAEAA 229
Cdd:PRK05653 150 GQTNYSAAKAGVIGFTKALALELASRGITVNAVAPGFIDTDMT---EGLPEEVKAEI 203
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
 20-230 2.86e-37

3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes members identified as 3beta17beta hydroxysteroid dehydrogenase, 20beta hydroxysteroid dehydrogenase, and R-alcohol dehydrogenase. These proteins exhibit the canonical active site tetrad and glycine rich NAD(P)-binding motif of the classical SDRs. 17beta-dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens, and include members of the SDR family. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187600 [Multi-domain]  Cd Length: 247  Bit Score: 131.35  E-value: 2.86e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  20 MNDRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEIGAGARLLVLDVTDLDG----IARATTQVDRLDV 95
Cdd:cd05341   3 LKGKVAIVTGGARGLGLAHARLLVAEGAKVVLSDILDEEGQAAAAELGDAARFFHLDVTDEDGwtavVDTAREAFGRLDV 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  96 LVNNAGISpSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSgTASLTwstnpnpqftpGSGGAA 175
Cdd:cd05341  83 LVNNAGIL-TGGTVETTTLEEWRRLLDINLTGVFLGTRAVIPPMKEAGGGSIINMSS-IEGLV-----------GDPALA 149

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 30267738 176 AYRSSKAALNALTVLYAQTLA--EDGFKVNALAPGMRATdlnPLAAAAGDDPAEAAQ 230
Cdd:cd05341 150 AYNASKGAVRGLTKSAALECAtqGYGIRVNSVHPGYIYT---PMTDELLIAQGEMGN 203
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
 20-231 3.67e-37

classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a canonical active site triad (and also an active site Asn) and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187612 [Multi-domain]  Cd Length: 235  Bit Score: 130.99  E-value: 3.67e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  20 MNDRTALVTGANKGIGKHIARVLVAEGLT-VYVGSRDRGLGQRAVEEIGAGARLLVLDVTDLDGIARATTQVDRLDVLVN 98
Cdd:cd05354   1 IKDKTVLVTGANRGIGKAFVESLLAHGAKkVYAAVRDPGSAAHLVAKYGDKVVPLRLDVTDPESIKAAAAQAKDVDVVIN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  99 NAGISPSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSgtaSLTWSTNPNpqftpgsggAAAYR 178
Cdd:cd05354  81 NAGVLKPATLLEEGALEALKQEMDVNVFGLLRLAQAFAPVLKANGGGAIVNLNS---VASLKNFPA---------MGTYS 148

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 30267738 179 SSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDLNPLAAAAGDDPAEAAQG 231
Cdd:cd05354 149 ASKSAAYSLTQGLRAELAAQGTLVLSVHPGPIDTRMAAGAGGPKESPETVAEA 201
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
 23-226 2.23e-35

gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent conversion of carbon source D-gluconate and 5-keto-D-gluconate. This SDR subgroup has a classical Gly-rich NAD(P)-binding motif and a conserved active site tetrad pattern. However, it has been proposed that Arg104 (Streptococcus suis Ga5DH numbering), as well as an active site Ca2+, play a critical role in catalysis. In addition to Ga5DHs this subgroup contains Erwinia chrysanthemi KduD which is involved in pectin degradation, and is a putative 2,5-diketo-3-deoxygluconate dehydrogenase. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107,15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187605 [Multi-domain]  Cd Length: 248  Bit Score: 126.70  E-value: 2.23e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  23 RTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEI---GAGARLLVLDVTDLDGIARATTQVD----RLDV 95
Cdd:cd05347   6 KVALVTGASRGIGFGIASGLAEAGANIVINSRNEEKAEEAQQLIekeGVEATAFTCDVSDEEAIKAAVEAIEedfgKIDI 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  96 LVNNAGISpSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTASLTWSTNPnpqftpgsggaa 175
Cdd:cd05347  86 LVNNAGII-RRHPAEEFPEAEWRDVIDVNLNGVFFVSQAVARHMIKQGHGKIINICSLLSELGGPPVP------------ 152

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 30267738 176 AYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATdlnPLAAAAGDDPA 226
Cdd:cd05347 153 AYAASKGGVAGLTKALATEWARHGIQVNAIAPGYFAT---EMTEAVVADPE 200
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 20-216 9.18e-35

3-ketoacyl-(acyl-carrier-protein) reductase; Validated


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 124.92  E-value: 9.18e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   20 MNDRTALVTGANKGIGKHIARVLVAEGLTVYVGSR-DRGLGQRAVEEI---GAGARLLVLDVTDLDGIAR----ATTQVD 91
Cdd:PRK05557   3 LEGKVALVTGASRGIGRAIAERLAAQGANVVINYAsSEAGAEALVAEIgalGGKALAVQGDVSDAESVERavdeAKAEFG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   92 RLDVLVNNAGISpSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSgTASLTwstnpnpqftpGS 171
Cdd:PRK05557  83 GVDILVNNAGIT-RDNLLMRMKEEDWDRVIDTNLTGVFNLTKAVARPMMKQRSGRIINISS-VVGLM-----------GN 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 30267738  172 GGAAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDLNP 216
Cdd:PRK05557 150 PGQANYAASKAGVIGFTKSLARELASRGITVNAVAPGFIETDMTD 194
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 20-213 2.11e-34

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 123.83  E-value: 2.11e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   20 MNDRTALVTGANKGIGKHIARVLVAEG--LTVYVGSRDRGLG--QRAVEEIGAGARLLVLDVTDLDGIARATTQV----D 91
Cdd:PRK12825   4 LMGRVALVTGAARGLGRAIALRLARAGadVVVHYRSDEEAAEelVEAVEALGRRAQAVQADVTDKAALEAAVAAAverfG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   92 RLDVLVNNAGISPSlAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTASltwstnpnpqftPGS 171
Cdd:PRK12825  84 RIDILVNNAGIFED-KPLADMSDDEWDEVIDVNLSGVFHLLRAVVPPMRKQRGGRIVNISSVAGL------------PGW 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 30267738  172 GGAAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATD 213
Cdd:PRK12825 151 PGRSNYAAAKAGLVGLTKALARELAEYGITVNMVAPGDIDTD 192
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 31-237 6.47e-34

Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) reductases.


Pssm-ID: 433310 [Multi-domain]  Cd Length: 236  Bit Score: 122.54  E-value: 6.47e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738    31 NKGIGKHIARVLVAEGLTV---YVGSRDRGLGQRAVEEIGAgaRLLVLDVTDLDGIARATTQV----DRLDVLVNNAGIS 103
Cdd:pfam13561   5 ESGIGWAIARALAEEGAEVvltDLNEALAKRVEELAEELGA--AVLPCDVTDEEQVEALVAAAvekfGRLDILVNNAGFA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   104 PSLAPP-ADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPhpRIVNISSGTASLTWstnpnpqftpgsGGAAAYRSSKA 182
Cdd:pfam13561  83 PKLKGPfLDTSREDFDRALDVNLYSLFLLAKAALPLMKEGG--SIVNLSSIGAERVV------------PNYNAYGAAKA 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 30267738   183 ALNALTVLYAQTLAEDGFKVNALAPGMRATdlnPLAAAAGDDPAEAAQGAARLAL 237
Cdd:pfam13561 149 ALEALTRYLAVELGPRGIRVNAISPGPIKT---LAASGIPGFDELLAAAEARAPL 200
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
 22-213 6.78e-34

putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup resembles the SDR family, but does not have a perfect match to the NAD-binding motif or the catalytic tetrad characteristic of the SDRs. It includes the SDRs, Q9HYA2 from Pseudomonas aeruginosa PAO1 and APE0912 from Aeropyrum pernix K1. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187602 [Multi-domain]  Cd Length: 253  Bit Score: 122.77  E-value: 6.78e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  22 DRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEI---GAGARLLVLDVTDLDGIAR----ATTQVDRLD 94
Cdd:cd05344   1 GKVALVTAASSGIGLAIARALAREGARVAICARNRENLERAASELragGAGVLAVVADLTDPEDIDRlvekAGDAFGRVD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  95 VLVNNAGiSPSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTASltwstNPNPQFTPGSGga 174
Cdd:cd05344  81 ILVNNAG-GPPPGPFAELTDEDWLEAFDLKLLSVIRIVRAVLPGMKERGWGRIVNISSLTVK-----EPEPNLVLSNV-- 152

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 30267738 175 aayrsSKAALNALTVLYAQTLAEDGFKVNALAPGMRATD 213
Cdd:cd05344 153 -----ARAGLIGLVKTLSRELAPDGVTVNSVLPGYIDTE 186
PRK12826 PRK12826
SDR family oxidoreductase;
23-239 9.80e-34

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 122.33  E-value: 9.80e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   23 RTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQ---RAVEEIGAGARLLVLDVTDLDGIARATTQVD----RLDV 95
Cdd:PRK12826   7 RVALVTGAARGIGRAIAVRLAADGAEVIVVDICGDDAAataELVEAAGGKARARQVDVRDRAALKAAVAAGVedfgRLDI 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   96 LVNNAGISPsLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTASLTwstnPNPqftpgsgGAA 175
Cdd:PRK12826  87 LVANAGIFP-LTPFAEMDDEQWERVIDVNLTGTFLLTQAALPALIRAGGGRIVLTSSVAGPRV----GYP-------GLA 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30267738  176 AYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDlnplaaaAGDDPAEAAQGAARLALLP 239
Cdd:PRK12826 155 HYAASKAGLVGFTRALALELAARNITVNSVHPGGVDTP-------MAGNLGDAQWAEAIAAAIP 211
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 23-214 2.22e-33

beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; This subgroup includes the Escherichai coli K12 BKR, FabG. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet) NAD(P)(H) binding region and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H) binding pattern: TGxxxGxG in classical SDRs. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P) binding motif and an altered active site motif (YXXXN). Fungal type type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P) binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr-151 and Lys-155, and well as Asn-111 (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187594 [Multi-domain]  Cd Length: 240  Bit Score: 121.12  E-value: 2.22e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  23 RTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEI---GAGARLLVLDVTDLDGIARATTQV----DRLDV 95
Cdd:cd05333   1 KVALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAAETVEEIkalGGNAAALEADVSDREAVEALVEKVeaefGPVDI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  96 LVNNAGISpslappADT-----SVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTASLtwstnpnpqftpG 170
Cdd:cd05333  81 LVNNAGIT------RDNllmrmSEEDWDAVINVNLTGVFNVTQAVIRAMIKRRSGRIINISSVVGLI------------G 142

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 30267738 171 SGGAAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDL 214
Cdd:cd05333 143 NPGQANYAASKAGVIGFTKSLAKELASRGITVNAVAPGFIDTDM 186
PRK07326 PRK07326
SDR family oxidoreductase;
19-215 3.81e-33

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 120.50  E-value: 3.81e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   19 AMNDRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEIGAGARLLVL--DVTDLDGIARATTQV----DR 92
Cdd:PRK07326   3 SLKGKVALITGGSKGIGFAIAEALLAEGYKVAITARDQKELEEAAAELNNKGNVLGLaaDVRDEADVQRAVDAIvaafGG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   93 LDVLVNNAGISpSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSpHPRIVNISSGTasltwSTNPnpqFtpgsG 172
Cdd:PRK07326  83 LDVLIANAGVG-HFAPVEELTPEEWRLVIDTNLTGAFYTIKAAVPALKRG-GGYIINISSLA-----GTNF---F----A 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 30267738  173 GAAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDLN 215
Cdd:PRK07326 149 GGAAYNASKFGLVGFSEAAMLDLRQYGIKVSTIMPGSVATHFN 191
PRK12939 PRK12939
short chain dehydrogenase; Provisional
 16-215 5.25e-33

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 120.46  E-value: 5.25e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   16 TVVAMNDRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEI---GAGARLLVLDVTDLDGIAR----ATT 88
Cdd:PRK12939   1 MASNLAGKRALVTGAARGLGAAFAEALAEAGATVAFNDGLAAEARELAAALeaaGGRAHAIAADLADPASVQRffdaAAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   89 QVDRLDVLVNNAGISPSlAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTASLtwstnpnpqft 168
Cdd:PRK12939  81 ALGGLDGLVNNAGITNS-KSATELDIDTWDAVMNVNVRGTFLMLRAALPHLRDSGRGRIVNLASDTALW----------- 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 30267738  169 pGSGGAAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDLN 215
Cdd:PRK12939 149 -GAPKLGAYVASKGAVIGMTRSLARELGGRGITVNAIAPGLTATEAT 194
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
 20-216 8.80e-33

Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall/membrane/envelope biogenesis, Lipid transport and metabolism];


Pssm-ID: 443167 [Multi-domain]  Cd Length: 246  Bit Score: 119.50  E-value: 8.80e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  20 MNDRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEIGaGARLLVLDVTDLDGIARATTQV----DRLDV 95
Cdd:COG3967   3 LTGNTILITGGTSGIGLALAKRLHARGNTVIITGRREEKLEEAAAANP-GLHTIVLDVADPASIAALAEQVtaefPDLNV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  96 LVNNAGISPS---LAPPADTsvEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTAsltwstnpnpqFTPGSg 172
Cdd:COG3967  82 LINNAGIMRAedlLDEAEDL--ADAEREITTNLLGPIRLTAAFLPHLKAQPEAAIVNVSSGLA-----------FVPLA- 147

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 30267738 173 GAAAYRSSKAALNALTV-LYAQtLAEDGFKVNALAPGMRATDLNP 216
Cdd:COG3967 148 VTPTYSATKAALHSYTQsLRHQ-LKDTSVKVIELAPPAVDTDLTG 191
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
23-207 1.08e-31

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 122.65  E-value: 1.08e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   23 RTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEIGAGARLL--VLDVTDLDGIARATTQVDR----LDVL 96
Cdd:PRK08324 423 KVALVTGAAGGIGKATAKRLAAEGACVVLADLDEEAAEAAAAELGGPDRALgvACDVTDEAAVQAAFEEAALafggVDIV 502

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   97 VNNAGISPSlAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHP-RIVNISSGTAsltwsTNPNPqftpgsgGAA 175
Cdd:PRK08324 503 VSNAGIAIS-GPIEETSDEDWRRSFDVNATGHFLVAREAVRIMKAQGLGgSIVFIASKNA-----VNPGP-------NFG 569

                        170       180       190
                 ....*....|....*....|....*....|..
gi 30267738  176 AYRSSKAALNALTVLYAQTLAEDGFKVNALAP 207
Cdd:PRK08324 570 AYGAAKAAELHLVRQLALELGPDGIRVNGVNP 601
PRK06179 PRK06179
short chain dehydrogenase; Provisional
 20-152 1.24e-31

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 117.31  E-value: 1.24e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   20 MNDRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAveeigAGARLLVLDVTDLDGIARATTQV----DRLDV 95
Cdd:PRK06179   2 SNSKVALVTGASSGIGRATAEKLARAGYRVFGTSRNPARAAPI-----PGVELLELDVTDDASVQAAVDEViaraGRIDV 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 30267738   96 LVNNAGISpSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISS 152
Cdd:PRK06179  77 LVNNAGVG-LAGAAEESSIAQAQALFDTNVFGILRMTRAVLPHMRAQGSGRIINISS 132
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
 24-213 3.39e-31

sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, catalyzes the NADP-dependent reduction of sepiaptern to 7,8-dihydrobiopterin (BH2). In addition to SPRs, this subgroup also contains Bacillus cereus yueD, a benzil reductase, which catalyzes the stereospecific reduction of benzil to (S)-benzoin. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187625 [Multi-domain]  Cd Length: 241  Bit Score: 115.46  E-value: 3.39e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  24 TALVTGANKGIGKHIARVLVAEGLT--VYVGSRDRGLGQRAVEEIGAGARL--LVLDVTDLDGIARATTQVD----RLDV 95
Cdd:cd05367   1 VIILTGASRGIGRALAEELLKRGSPsvVVLLARSEEPLQELKEELRPGLRVttVKADLSDAAGVEQLLEAIRkldgERDL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  96 LVNNAGISPSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPR-IVNISSGTASltwstNPNPqftpgsgGA 174
Cdd:cd05367  81 LINNAGSLGPVSKIEFIDLDELQKYFDLNLTSPVCLTSTLLRAFKKRGLKKtVVNVSSGAAV-----NPFK-------GW 148

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 30267738 175 AAYRSSKAALNaltvLYAQTLA--EDGFKVNALAPGMRATD 213
Cdd:cd05367 149 GLYCSSKAARD----MFFRVLAaeEPDVRVLSYAPGVVDTD 185
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 21-215 3.74e-31

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 115.32  E-value: 3.74e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   21 NDRTALVTGANKGIGKHIARVLVAEGLTVYVG-SRDRGLGQRAVEEI---GAGARLLVLDVTDLDGIARATTQVDR---- 92
Cdd:PRK05565   4 MGKVAIVTGASGGIGRAIAELLAKEGAKVVIAyDINEEAAQELLEEIkeeGGDAIAVKADVSSEEDVENLVEQIVEkfgk 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   93 LDVLVNNAGISpSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSgtaslTWstnpnpqftpGSG 172
Cdd:PRK05565  84 IDILVNNAGIS-NFGLVTDMTDEEWDRVIDVNLTGVMLLTRYALPYMIKRKSGVIVNISS-----IW----------GLI 147

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 30267738  173 GA---AAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDLN 215
Cdd:PRK05565 148 GAsceVLYSASKGAVNAFTKALAKELAPSGIRVNAVAPGAIDTEMW 193
PRK08219 PRK08219
SDR family oxidoreductase;
20-188 4.62e-31

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 114.65  E-value: 4.62e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   20 MNDRTALVTGANKGIGKHIARVLvAEGLTVYVGSRDRGLGQRAVEEIgAGARLLVLDVTDLDGIARATTQVDRLDVLVNN 99
Cdd:PRK08219   1 MERPTALITGASRGIGAAIAREL-APTHTLLLGGRPAERLDELAAEL-PGATPFPVDLTDPEAIAAAVEQLGRLDVLVHN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  100 AGISpSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSpHPRIVNISSGTAsltwsTNPNPqftpgsgGAAAYRS 179
Cdd:PRK08219  79 AGVA-DLGPVAESTVDEWRATLEVNVVAPAELTRLLLPALRAA-HGHVVFINSGAG-----LRANP-------GWGSYAA 144


                 ....*....
gi 30267738  180 SKAALNALT 188
Cdd:PRK08219 145 SKFALRALA 153
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
 25-241 2.05e-30

1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup contains classical SDR proteins, including members identified as 1-cyclohexenylcarbonyl coenzyme A reductase. ChcA of Streptomyces collinus is implicated in the final reduction step of shikimic acid to ansatrienin. ChcA shows sequence similarity to the SDR family of NAD-binding proteins, but it lacks the conserved Tyr of the characteristic catalytic site. This subgroup also contains the NADH-dependent enoyl-[acyl-carrier-protein(ACP)] reductase FabL from Bacillus subtilis. This enzyme participates in bacterial fatty acid synthesis, in type II fatty-acid synthases and catalyzes the last step in each elongation cycle. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187617 [Multi-domain]  Cd Length: 242  Bit Score: 113.60  E-value: 2.05e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  25 ALVTGANKGIGKHIARVLVAEGLTV---YVGSRDRGLG-QRAVEEIGAGARLLVLDVTDLDGIARATTQV----DRLDVL 96
Cdd:cd05359   1 ALVTGGSRGIGKAIALRLAERGADVvinYRKSKDAAAEvAAEIEELGGKAVVVRADVSQPQDVEEMFAAVkerfGRLDVL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  97 VNNAGISPsLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTASLTWSTNpnpqftpgsggaAA 176
Cdd:cd05359  81 VSNAAAGA-FRPLSELTPAHWDAKMNTNLKALVHCAQQAAKLMRERGGGRIVAISSLGSIRALPNY------------LA 147

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30267738 177 YRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDlnPLAAAAGDDP---AEAAQGAARLALLPDD 241
Cdd:cd05359 148 VGTAKAALEALVRYLAVELGPRGIRVNAVSPGVIDTD--ALAHFPNREDlleAAAANTPAGRVGTPQD 213
PRK06182 PRK06182
short chain dehydrogenase; Validated
 20-233 4.29e-30

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 113.52  E-value: 4.29e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   20 MNDRTALVTGANKGIGKHIARVLVAEGLTVYVGSrdrglgqRAVEEI----GAGARLLVLDVTDLDGIARATTQV----D 91
Cdd:PRK06182   1 MQKKVALVTGASSGIGKATARRLAAQGYTVYGAA-------RRVDKMedlaSLGVHPLSLDVTDEASIKAAVDTIiaeeG 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   92 RLDVLVNNAGISpSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTASLTwstnpnpqfTPgs 171
Cdd:PRK06182  74 RIDVLVNNAGYG-SYGAIEDVPIDEARRQFEVNLFGAARLTQLVLPHMRAQRSGRIINISSMGGKIY---------TP-- 141

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30267738  172 gGAAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDL-----NPLAAAAGDDP-AEAAQGAA 233
Cdd:PRK06182 142 -LGAWYHATKFALEGFSDALRLEVAPFGIDVVVIEPGGIKTEWgdiaaDHLLKTSGNGAyAEQAQAVA 208
PRK06180 PRK06180
short chain dehydrogenase; Provisional
 20-213 1.05e-29

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 112.32  E-value: 1.05e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   20 MNDRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGlGQRAVEEIGAG-ARLLVLDVTDLDGI----ARATTQVDRLD 94
Cdd:PRK06180   2 SSMKTWLITGVSSGFGRALAQAALAAGHRVVGTVRSEA-ARADFEALHPDrALARLLDVTDFDAIdavvADAEATFGPID 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   95 VLVNNAGISpSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISS--GTAsltwsTNPnpqftpgsg 172
Cdd:PRK06180  81 VLVNNAGYG-HEGAIEESPLAEMRRQFEVNVFGAVAMTKAVLPGMRARRRGHIVNITSmgGLI-----TMP--------- 145

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 30267738  173 GAAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATD 213
Cdd:PRK06180 146 GIGYYCGSKFALEGISESLAKEVAPFGIHVTAVEPGSFRTD 186
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
 23-215 1.59e-29

HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC 7120 HetN, a putative oxidoreductase involved in heterocyst differentiation, and related proteins. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212493 [Multi-domain]  Cd Length: 223  Bit Score: 110.53  E-value: 1.59e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  23 RTALVTGANKGIGKHIARVLVAEGLTVYVGSRDrglGQRAVEEIGAGARLLVL--DVTDLDGIAR----ATTQVDRLDVL 96
Cdd:cd08932   1 KVALVTGASRGIGIEIARALARDGYRVSLGLRN---PEDLAALSASGGDVEAVpyDARDPEDARAlvdaLRDRFGRIDVL 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  97 VNNAGISPSlAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTASLTwstnpnpqftpgSGGAAA 176
Cdd:cd08932  78 VHNAGIGRP-TTLREGSDAELEAHFSINVIAPAELTRALLPALREAGSGRVVFLNSLSGKRV------------LAGNAG 144

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 30267738 177 YRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDLN 215
Cdd:cd08932 145 YSASKFALRALAHALRQEGWDHGVRVSAVCPGFVDTPMA 183
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
 23-235 1.83e-29

classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site tetrad and glycine-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187648 [Multi-domain]  Cd Length: 246  Bit Score: 111.04  E-value: 1.83e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  23 RTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEIGAGARLLVLDVTD----LDGIARATTQVDRLDVLVN 98
Cdd:cd08944   4 KVAIVTGAGAGIGAACAARLAREGARVVVADIDGGAAQAVVAQIAGGALALRVDVTDeqqvAALFERAVEEFGGLDLLVN 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  99 NAGISPSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTAsltwstnpnpqfTPGSGGAAAYR 178
Cdd:cd08944  84 NAGAMHLTPAIIDTDLAVWDQTMAINLRGTFLCCRHAAPRMIARGGGSIVNLSSIAG------------QSGDPGYGAYG 151

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 30267738 179 SSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDLNpLAAAAGDDPAEAAQGAARL 235
Cdd:cd08944 152 ASKAAIRNLTRTLAAELRHAGIRCNALAPGLIDTPLL-LAKLAGFEGALGPGGFHLL 207
PRK08628 PRK08628
SDR family oxidoreductase;
20-227 2.57e-29

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 110.82  E-value: 2.57e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   20 MNDRTALVTGANKGIGKHIARVLVAEG-LTVYVGSRDRGLG-QRAVEEIGAGARLLVLDVTDLDGIARATTQVD----RL 93
Cdd:PRK08628   5 LKDKVVIVTGGASGIGAAISLRLAEEGaIPVIFGRSAPDDEfAEELRALQPRAEFVQVDLTDDAQCRDAVEQTVakfgRI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   94 DVLVNNAGISPSLAppADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSpHPRIVNISSGTAsLTwstnpnpqftpGSGG 173
Cdd:PRK08628  85 DGLVNNAGVNDGVG--LEAGREAFVASLERNLIHYYVMAHYCLPHLKAS-RGAIVNISSKTA-LT-----------GQGG 149

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 30267738  174 AAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDLNPLAAAAGDDPAE 227
Cdd:PRK08628 150 TSGYAAAKGAQLALTREWAVALAKDGVRVNAVIPAEVMTPLYENWIATFDDPEA 203
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
 23-252 2.71e-28

tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6,8-tetrahydroxynaphthalene reductase (4HNR) of Magnaporthe grisea and the related 1,3,8-trihydroxynaphthalene reductase (3HNR) are typical members of the SDR family containing the canonical glycine rich NAD(P)-binding site and active site tetrad, and function in fungal melanin biosynthesis. This subgroup also includes an SDR from Norway spruce that may function to protect against both biotic and abitoic stress. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187620 [Multi-domain]  Cd Length: 243  Bit Score: 107.75  E-value: 2.71e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  23 RTALVTGANKGIGKHIARVLVAEGLTV---YVGSRDrgLGQRAVEEI---GAGARLLVLDVTDLDGIAR----ATTQVDR 92
Cdd:cd05362   4 KVALVTGASRGIGRAIAKRLARDGASVvvnYASSKA--AAEEVVAEIeaaGGKAIAVQADVSDPSQVARlfdaAEKAFGG 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  93 LDVLVNNAGISPsLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRrsPHPRIVNISSGTASLTwstnpnpqftpgSG 172
Cdd:cd05362  82 VDILVNNAGVML-KKPIAETSEEEFDRMFTVNTKGAFFVLQEAAKRLR--DGGRIINISSSLTAAY------------TP 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738 173 GAAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDLNPLAAAAGDDPAEAAQGA-ARLALLPDDGPTGGFFSWD 251
Cdd:cd05362 147 NYGAYAGSKAAVEAFTRVLAKELGGRGITVNAVAPGPVDTDMFYAGKTEEAVEGYAKMSPlGRLGEPEDIAPVVAFLASP 226


                .
gi 30267738 252 G 252
Cdd:cd05362 227 D 227
PRK07060 PRK07060
short chain dehydrogenase; Provisional
 23-237 3.33e-28

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 107.88  E-value: 3.33e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   23 RTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEIGAGArlLVLDVTDLDGIARATTQVDRLDVLVNNAGI 102
Cdd:PRK07060  10 KSVLVTGASSGIGRACAVALAQRGARVVAAARNAAALDRLAGETGCEP--LRLDVGDDAAIRAALAAAGAFDGLVNCAGI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  103 SpSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPA-LRRSPHPRIVNISSGTASLtwstnpnpqftpGSGGAAAYRSSK 181
Cdd:PRK07060  88 A-SLESALDMTAEGFDRVMAVNARGAALVARHVARAmIAAGRGGSIVNVSSQAALV------------GLPDHLAYCASK 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 30267738  182 AALNALTVLYAQTLAEDGFKVNALAPGMRATdlnPLAAAAGDDPAEAAQGAARLAL 237
Cdd:PRK07060 155 AALDAITRVLCVELGPHGIRVNSVNPTVTLT---PMAAEAWSDPQKSGPMLAAIPL 207
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
 23-215 3.62e-28

classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka Tyrosine-dependent oxidoreductases) are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187628 [Multi-domain]  Cd Length: 228  Bit Score: 107.01  E-value: 3.62e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  23 RTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEIGaGARLLVLDVTDLDGIARATTQVDR----LDVLVN 98
Cdd:cd05370   6 NTVLITGGTSGIGLALARKFLEAGNTVIITGRREERLAEAKKELP-NIHTIVLDVGDAESVEALAEALLSeypnLDILIN 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  99 NAGI--SPSLAPPADTsVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTASLTWSTNPNpqftpgsggaaa 176
Cdd:cd05370  85 NAGIqrPIDLRDPASD-LDKADTEIDTNLIGPIRLIKAFLPHLKKQPEATIVNVSSGLAFVPMAANPV------------ 151

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 30267738 177 YRSSKAALNALTV-LYAQtLAEDGFKVNALAPGMRATDLN 215
Cdd:cd05370 152 YCATKAALHSYTLaLRHQ-LKDTGVEVVEIVPPAVDTELH 190
PRK09242 PRK09242
SDR family oxidoreductase;
20-207 3.77e-28

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 107.91  E-value: 3.77e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   20 MNDRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEI-----GAGARLLVLDVTDLDGIARATTQV---- 90
Cdd:PRK09242   7 LDGQTALITGASKGIGLAIAREFLGLGADVLIVARDADALAQARDELaeefpEREVHGLAADVSDDEDRRAILDWVedhw 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   91 DRLDVLVNNAGISPSLApPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSgTASLTwstnpnpqfTPG 170
Cdd:PRK09242  87 DGLHILVNNAGGNIRKA-AIDYTEDEWRGIFETNLFSAFELSRYAHPLLKQHASSAIVNIGS-VSGLT---------HVR 155

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 30267738  171 SGgaAAYRSSKAALNALTVLYAQTLAEDGFKVNALAP 207
Cdd:PRK09242 156 SG--APYGMTKAALLQMTRNLAVEWAEDGIRVNAVAP 190
PRK12829 PRK12829
short chain dehydrogenase; Provisional
 22-209 6.51e-28

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 107.45  E-value: 6.51e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   22 DRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEI-GAGARLLVLDVTDLDGIAR----ATTQVDRLDVL 96
Cdd:PRK12829  11 GLRVLVTGGASGIGRAIAEAFAEAGARVHVCDVSEAALAATAARLpGAKVTATVADVADPAQVERvfdtAVERFGGLDVL 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   97 VNNAGISPSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTASLTwstnpnpqftpGSGGAAA 176
Cdd:PRK12829  91 VNNAGIAGPTGGIDEITPEQWEQTLAVNLNGQFYFARAAVPLLKASGHGGVIIALSSVAGRL-----------GYPGRTP 159

                        170       180       190
                 ....*....|....*....|....*....|...
gi 30267738  177 YRSSKAALNALTVLYAQTLAEDGFKVNALAPGM 209
Cdd:PRK12829 160 YAASKWAVVGLVKSLAIELGPLGIRVNAILPGI 192
PRK06914 PRK06914
SDR family oxidoreductase;
20-152 1.28e-27

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 107.03  E-value: 1.28e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   20 MNDRTALVTGANKGIGKHIARVLVAEGLTVYVGSRD---RGLGQRAVEEIGAGARLLV--LDVTDLDGIARAT---TQVD 91
Cdd:PRK06914   1 MNKKIAIVTGASSGFGLLTTLELAKKGYLVIATMRNpekQENLLSQATQLNLQQNIKVqqLDVTDQNSIHNFQlvlKEIG 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30267738   92 RLDVLVNNAGISpsLAPPA-DTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISS 152
Cdd:PRK06914  81 RIDLLVNNAGYA--NGGFVeEIPVEEYRKQFETNVFGAISVTQAVLPYMRKQKSGKIINISS 140
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 22-234 2.78e-27

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 105.04  E-value: 2.78e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   22 DRTALVTGANKGIGKHIARVLVAEGLTVYvgsrdrGLGQRAVEEIGAGARLLVLDVTDldGIARATTQVDRLDVLVNNAG 101
Cdd:PRK06550   5 TKTVLITGAASGIGLAQARAFLAQGAQVY------GVDKQDKPDLSGNFHFLQLDLSD--DLEPLFDWVPSVDILCNTAG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  102 ISPSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSgTASLTwstnpnpqftpGSGGAAAYRSSK 181
Cdd:PRK06550  77 ILDDYKPLLDTSLEEWQHIFDTNLTSTFLLTRAYLPQMLERKSGIIINMCS-IASFV-----------AGGGGAAYTASK 144

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 30267738  182 AALNALTVLYAQTLAEDGFKVNALAPGMRATDLNplaaAAGDDPAEAAQGAAR 234
Cdd:PRK06550 145 HALAGFTKQLALDYAKDGIQVFGIAPGAVKTPMT----AADFEPGGLADWVAR 193
PRK08265 PRK08265
short chain dehydrogenase; Provisional
 19-238 2.83e-27

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 105.48  E-value: 2.83e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   19 AMNDRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEIGAGARLLVLDVTDLDGIARATTQV----DRLD 94
Cdd:PRK08265   3 GLAGKVAIVTGGATLIGAAVARALVAAGARVAIVDIDADNGAAVAASLGERARFIATDITDDAAIERAVATVvarfGRVD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   95 VLVNNAGIspSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRsPHPRIVNISSGTASLtwstnpnpqftpGSGGA 174
Cdd:PRK08265  83 ILVNLACT--YLDDGLASSRADWLAALDVNLVSAAMLAQAAHPHLAR-GGGAIVNFTSISAKF------------AQTGR 147

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30267738  175 AAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMraTDLNPLAAAAGDDPAEAAQGAARLALL 238
Cdd:PRK08265 148 WLYPASKAAIRQLTRSMAMDLAPDGIRVNSVSPGW--TWSRVMDELSGGDRAKADRVAAPFHLL 209
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
 23-230 3.12e-27

glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR family, it catalyzes the NAD(P)-dependent oxidation of beta-D-glucose to D-glucono-delta-lactone. GlcDH has a typical NAD-binding site glycine-rich pattern as well as the canonical active site tetrad (YXXXK motif plus upstream Ser and Asn). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187616 [Multi-domain]  Cd Length: 253  Bit Score: 105.16  E-value: 3.12e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  23 RTALVTGANKGIGKHIARVLVAEGLTV---YVGSRDRGlgQRAVEEI---GAGARLLVLDVTDLDGIARATTQVDR---- 92
Cdd:cd05358   4 KVALVTGASSGIGKAIAIRLATAGANVvvnYRSKEDAA--EEVVEEIkavGGKAIAVQADVSKEEDVVALFQSAIKefgt 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  93 LDVLVNNAGISPSlAPPADTSVEEFRRTYETNVFGVVAVTNAflpALRRSPHPR----IVNISSGTASLTWSTNpnpqft 168
Cdd:cd05358  82 LDILVNNAGLQGD-ASSHEMTLEDWNKVIDVNLTGQFLCARE---AIKRFRKSKikgkIINMSSVHEKIPWPGH------ 151

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30267738 169 pgsggaAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDLNplaAAAGDDPAEAAQ 230
Cdd:cd05358 152 ------VNYAASKGGVKMMTKTLAQEYAPKGIRVNAIAPGAINTPIN---AEAWDDPEQRAD 204
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 26-208 3.91e-27

human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; 17beta-hydroxysteroid dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. This classical-SDR subgroup includes the human proteins: type 2 17beta-HSD, type 6 17beta-HSD, type 2 11beta-HSD, dehydrogenase/reductase SDR family member 9, short-chain dehydrogenase/reductase family 9C member 7, 3-hydroxybutyrate dehydrogenase type 1, and retinol dehydrogenase 5. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187665 [Multi-domain]  Cd Length: 281  Bit Score: 105.82  E-value: 3.91e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  26 LVTGANKGIGKHIARVLVAEGLTVYVGsrdrglgqrAVEEIGAGA-----------RLLVLDVTDLDGIARATTQV---- 90
Cdd:cd09805   4 LITGCDSGFGNLLAKKLDSLGFTVLAG---------CLTKNGPGAkelrrvcsdrlRTLQLDVTKPEQIKRAAQWVkehv 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  91 -DR-LDVLVNNAGISPSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSpHPRIVNISSGTASLtwstnPNPQFt 168
Cdd:cd09805  75 gEKgLWGLVNNAGILGFGGDEELLPMDDYRKCMEVNLFGTVEVTKAFLPLLRRA-KGRVVNVSSMGGRV-----PFPAG- 147

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 30267738 169 pgsggaAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPG 208
Cdd:cd09805 148 ------GAYCASKAAVEAFSDSLRRELQPWGVKVSIIEPG 181
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 20-214 4.62e-27

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 104.39  E-value: 4.62e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   20 MNDRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEI---GAGARLLVLDVTDLDGIARATTQVD----R 92
Cdd:PRK07666   5 LQGKNALITGAGRGIGRAVAIALAKEGVNVGLLARTEENLKAVAEEVeayGVKVVIATADVSDYEEVTAAIEQLKnelgS 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   93 LDVLVNNAGISpSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSgTASLTwstnpnpqftpGSG 172
Cdd:PRK07666  85 IDILINNAGIS-KFGKFLELDPAEWEKIIQVNLMGVYYATRAVLPSMIERQSGDIINISS-TAGQK-----------GAA 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 30267738  173 GAAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDL 214
Cdd:PRK07666 152 VTSAYSASKFGVLGLTESLMQEVRKHNIRVTALTPSTVATDM 193
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
23-224 4.64e-27

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 104.85  E-value: 4.64e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   23 RTALVTGANKGIGKHIARVLVAEGLTVYvgSRDRGLGQRAVE------EIGAGARLLVLDVTDLDGIARATTQVD----R 92
Cdd:PRK12824   3 KIALVTGAKRGIGSAIARELLNDGYRVI--ATYFSGNDCAKDwfeeygFTEDQVRLKELDVTDTEECAEALAEIEeeegP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   93 LDVLVNNAGISPSLApPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISS--GTASltwstnpnpQFtpg 170
Cdd:PRK12824  81 VDILVNNAGITRDSV-FKRMSHQEWNDVINTNLNSVFNVTQPLFAAMCEQGYGRIINISSvnGLKG---------QF--- 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 30267738  171 sgGAAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATdlnPLAAAAGDD 224
Cdd:PRK12824 148 --GQTNYSAAKAGMIGFTKALASEGARYGITVNCIAPGYIAT---PMVEQMGPE 196
PRK12937 PRK12937
short chain dehydrogenase; Provisional
 23-247 8.66e-27

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 104.05  E-value: 8.66e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   23 RTALVTGANKGIGKHIARVLVAEGLTV---YVGSRDRGlgQRAVEEI---GAGARLLVLDVTDLDGIAR----ATTQVDR 92
Cdd:PRK12937   6 KVAIVTGASRGIGAAIARRLAADGFAVavnYAGSAAAA--DELVAEIeaaGGRAIAVQADVADAAAVTRlfdaAETAFGR 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   93 LDVLVNNAGISPsLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPhpRIVNISSGTASLTWStnpnpqftpgsg 172
Cdd:PRK12937  84 IDVLVNNAGVMP-LGTIADFDLEDFDRTIATNLRGAFVVLREAARHLGQGG--RIINLSTSVIALPLP------------ 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  173 GAAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDLnplaAAAGDDPAEAAQ--GAARLALL--PDD------- 241
Cdd:PRK12937 149 GYGPYAASKAAVEGLVHVLANELRGRGITVNAVAPGPVATEL----FFNGKSAEQIDQlaGLAPLERLgtPEEiaaavaf 224


                 ....*...
gi 30267738  242 --GPTGGF 247
Cdd:PRK12937 225 laGPDGAW 232
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
 23-215 1.32e-26

classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187634 [Multi-domain]  Cd Length: 226  Bit Score: 102.97  E-value: 1.32e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  23 RTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEIGAGARLLVLDVTDLDGIARATTQVDR----LDVLVN 98
Cdd:cd08929   1 KAALVTGASRGIGEATARLLHAEGYRVGICARDEARLAAAAAQELEGVLGLAGDVRDEADVRRAVDAMEEafggLDALVN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  99 NAGISpSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTasltwSTNPnpqftpgSGGAAAYR 178
Cdd:cd08929  81 NAGVG-VMKPVEELTPEEWRLVLDTNLTGAFYCIHKAAPALLRRGGGTIVNVGSLA-----GKNA-------FKGGAAYN 147

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 30267738 179 SSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDLN 215
Cdd:cd08929 148 ASKFGLLGLSEAAMLDLREANIRVVNVMPGSVDTGFA 184
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
23-212 1.61e-26

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 103.65  E-value: 1.61e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   23 RTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEI---GAGARLLVLDVTDLDGIARATTQVDR----LDV 95
Cdd:PRK08643   3 KVALVTGAGQGIGFAIAKRLVEDGFKVAIVDYNEETAQAAADKLskdGGKAIAVKADVSDRDQVFAAVRQVVDtfgdLNV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   96 LVNNAGISPSlaPPADTSVEE-FRRTYETNVFGVVAVTNAFLPALRRSPHP-RIVNISSGTASLtwstnpnpqftpGSGG 173
Cdd:PRK08643  83 VVNNAGVAPT--TPIETITEEqFDKVYNINVGGVIWGIQAAQEAFKKLGHGgKIINATSQAGVV------------GNPE 148

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 30267738  174 AAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRAT 212
Cdd:PRK08643 149 LAVYSSTKFAVRGLTQTAARDLASEGITVNAYAPGIVKT 187
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
 20-214 3.13e-26

classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187622 [Multi-domain]  Cd Length: 253  Bit Score: 102.87  E-value: 3.13e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  20 MNDRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQ---RAVEEIGAGAR---LLVLDVTDLDGIARATTQV--- 90
Cdd:cd05364   1 LSGKVAIITGSSSGIGAGTAILFARLGARLALTGRDAERLEetrQSCLQAGVSEKkilLVVADLTEEEGQDRIISTTlak 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  91 -DRLDVLVNNAGIspsLAPPA--DTSVEEFRRTYETNVFGVVAVTNAFLPALRRSpHPRIVNISSgtasltwsTNPNPQF 167
Cdd:cd05364  81 fGRLDILVNNAGI---LAKGGgeDQDIEEYDKVMNLNLRAVIYLTKLAVPHLIKT-KGEIVNVSS--------VAGGRSF 148

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 30267738 168 TpgsgGAAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDL 214
Cdd:cd05364 149 P----GVLYYCISKAALDQFTRCTALELAPKGVRVNSVSPGVIVTGF 191
PRK06841 PRK06841
short chain dehydrogenase; Provisional
 20-214 6.11e-26

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 102.04  E-value: 6.11e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   20 MNDRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEIGAGARLLVLDVTDLDGIARATTQV----DRLDV 95
Cdd:PRK06841  13 LSGKVAVVTGGASGIGHAIAELFAAKGARVALLDRSEDVAEVAAQLLGGNAKGLVCDVSDSQSVEAAVAAVisafGRIDI 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   96 LVNNAGISPsLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTASLtwstnpnpqftpGSGGAA 175
Cdd:PRK06841  93 LVNSAGVAL-LAPAEDVSEEDWDKTIDINLKGSFLMAQAVGRHMIAAGGGKIVNLASQAGVV------------ALERHV 159

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 30267738  176 AYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDL 214
Cdd:PRK06841 160 AYCASKAGVVGMTKVLALEWGPYGITVNAISPTVVLTEL 198
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 22-208 8.21e-26

3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These proteins include members identified as KDSR, ribitol type dehydrogenase, and others. The group shows strong conservation of the active site tetrad and glycine rich NAD-binding motif of the classical SDRs. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187643 [Multi-domain]  Cd Length: 239  Bit Score: 101.18  E-value: 8.21e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  22 DRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEIGAGARLL-------VLDVTDLDGIARATTQVDRL- 93
Cdd:cd08939   1 GKHVLITGGSSGIGKALAKELVKEGANVIIVARSESKLEEAVEEIEAEANASgqkvsyiSADLSDYEEVEQAFAQAVEKg 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  94 ---DVLVNNAGISPSlAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTASLtwstnpnpqftpG 170
Cdd:cd08939  81 gppDLVVNCAGISIP-GLFEDLTAEEFERGMDVNYFGSLNVAHAVLPLMKEQRPGHIVFVSSQAALV------------G 147

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 30267738 171 SGGAAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPG 208
Cdd:cd08939 148 IYGYSAYCPSKFALRGLAESLRQELKPYNIRVSVVYPP 185
PRK06701 PRK06701
short chain dehydrogenase; Provisional
 22-223 1.02e-25

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 102.03  E-value: 1.02e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   22 DRTALVTGANKGIGKHIArVLVA-EGLTVYVG----SRDRGLGQRAVEEIGAGARLLVLDVTDL----DGIARATTQVDR 92
Cdd:PRK06701  46 GKVALITGGDSGIGRAVA-VLFAkEGADIAIVyldeHEDANETKQRVEKEGVKCLLIPGDVSDEafckDAVEETVRELGR 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   93 LDVLVNNAGISPSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRrsPHPRIVNISSGTASLtwstnpnpqftpGSG 172
Cdd:PRK06701 125 LDILVNNAAFQYPQQSLEDITAEQLDKTFKTNIYSYFHMTKAALPHLK--QGSAIINTGSITGYE------------GNE 190

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 30267738  173 GAAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDLNPLAAAAGD 223
Cdd:PRK06701 191 TLIDYSATKGAIHAFTRSLAQSLVQKGIRVNAVAPGPIWTPLIPSDFDEEK 241
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
 20-215 1.43e-25

clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent reduction of clavulanate-9-aldehyde to clavulanic acid, a beta-lactamase inhibitor. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187639 [Multi-domain]  Cd Length: 243  Bit Score: 100.69  E-value: 1.43e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  20 MNDRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEI---GAGARLLVLDVTD----LDGIARATTQVDR 92
Cdd:cd08934   1 LQGKVALVTGASSGIGEATARALAAEGAAVAIAARRVDRLEALADELeaeGGKALVLELDVTDeqqvDAAVERTVEALGR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  93 LDVLVNNAGISpSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTASLTwstnpnpqftpgSG 172
Cdd:cd08934  81 LDILVNNAGIM-LLGPVEDADTTDWTRMIDTNLLGLMYTTHAALPHHLLRNKGTIVNISSVAGRVA------------VR 147

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 30267738 173 GAAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDLN 215
Cdd:cd08934 148 NSAVYNATKFGVNAFSEGLRQEVTERGVRVVVIEPGTVDTELR 190
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
 22-230 2.31e-25

putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) SDR; This subgroup includes the putative Brucella melitensis biovar Abortus 2308 BKR, FabG, Mesorhizobium loti MAFF303099 FabG, and other classical SDRs. BKR, a member of the SDR family, catalyzes the NADPH-dependent reduction of acyl carrier protein in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of 4 elongation steps, which are repeated to extend the fatty acid chain thru the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I Fas utilizes one or 2 multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187603 [Multi-domain]  Cd Length: 248  Bit Score: 100.16  E-value: 2.31e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  22 DRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEIGAGARLLVLDVTDLDGIAR----ATTQVDRLDVLV 97
Cdd:cd05345   5 GKVAIVTGAGSGFGEGIARRFAQEGARVVIADINADGAERVAADIGEAAIAIQADVTKRADVEAmveaALSKFGRLDILV 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  98 NNAGISPSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTASltwstNPNPqftpgsgGAAAY 177
Cdd:cd05345  85 NNAGITHRNKPMLEVDEEEFDRVFAVNVKSIYLSAQALVPHMEEQGGGVIINIASTAGL-----RPRP-------GLTWY 152

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 30267738 178 RSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDLnpLAAAAGDDPAEAAQ 230
Cdd:cd05345 153 NASKGWVVTATKAMAVELAPRNIRVNCLCPVAGETPL--LSMFMGEDTPENRA 203
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
 23-207 2.56e-25

rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has bifunctional proteins with an N-terminal aldolase and a C-terminal classical SDR domain. One member is identified as a rhamnulose-1-phosphate aldolase/alcohol dehydrogenase. The SDR domain has a canonical SDR glycine-rich NAD(P) binding motif and a match to the characteristic active site triad. However, it lacks an upstream active site Asn typical of SDRs. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187647 [Multi-domain]  Cd Length: 250  Bit Score: 100.16  E-value: 2.56e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  23 RTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEI--GAGARLLVLDVTD----LDGIARATTQVDRLDVL 96
Cdd:cd08943   2 KVALVTGGASGIGLAIAKRLAAEGAAVVVADIDPEIAEKVAEAAqgGPRALGVQCDVTSeaqvQSAFEQAVLEFGGLDIV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  97 VNNAGISPSlAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSP-HPRIVNISSGTAsltwsTNPNPqftpgsgGAA 175
Cdd:cd08943  82 VSNAGIATS-SPIAETSLEDWNRSMDINLTGHFLVSREAFRIMKSQGiGGNIVFNASKNA-----VAPGP-------NAA 148

                       170       180       190
                ....*....|....*....|....*....|..
gi 30267738 176 AYRSSKAALNALTVLYAQTLAEDGFKVNALAP 207
Cdd:cd08943 149 AYSAAKAAEAHLARCLALEGGEDGIRVNTVNP 180
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
 22-253 3.32e-25

retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members identified as retinol dehydrogenases, which convert retinol to retinal, a property that overlaps with 17betaHSD activity. 17beta-dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens, and include members of the short-chain dehydrogenases/reductase family. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187638 [Multi-domain]  Cd Length: 261  Bit Score: 100.30  E-value: 3.32e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  22 DRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEIGA----GARLLVLDVTDLDGIARATTQV----DRL 93
Cdd:cd08933   9 DKVVIVTGGSRGIGRGIVRAFVENGAKVVFCARGEAAGQALESELNRagpgSCKFVPCDVTKEEDIKTLISVTverfGRI 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  94 DVLVNNAGISPSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSpHPRIVNISSGTASLtwstnpnpqftpGSGG 173
Cdd:cd08933  89 DCLVNNAGWHPPHQTTDETSAQEFRDLLNLNLISYFLASKYALPHLRKS-QGNIINLSSLVGSI------------GQKQ 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738 174 AAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDL-NPLAAAAGDDPA-----EAAQGAARLALLPDDGPTGGF 247
Cdd:cd08933 156 AAPYVATKGAITAMTKALAVDESRYGVRVNCISPGNIWTPLwEELAAQTPDTLAtikegELAQLLGRMGTEAESGLAALF 235


                ....*.
gi 30267738 248 FSWDGT 253
Cdd:cd08933 236 LAAEAT 241
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 22-214 3.58e-25

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 99.86  E-value: 3.58e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   22 DRTALVTGANKGIGKHIARVLVAEGLTV---YVGSRDRGLgqrAVEEIGAgaRLLVLDVTDLDGIARATTQVD----RLD 94
Cdd:PRK06463   7 GKVALITGGTRGIGRAIAEAFLREGAKVavlYNSAENEAK---ELREKGV--FTIKCDVGNRDQVKKSKEVVEkefgRVD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   95 VLVNNAGISpSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISS----GTASLtwstnpnpqftpg 170
Cdd:PRK06463  82 VLVNNAGIM-YLMPFEEFDEEKYNKMIKINLNGAIYTTYEFLPLLKLSKNGAIVNIASnagiGTAAE------------- 147

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 30267738  171 sgGAAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDL 214
Cdd:PRK06463 148 --GTTFYAITKAGIIILTRRLAFELGKYGIRVNAVAPGWVETDM 189
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
 25-215 3.78e-25

classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a canonical active site tetrad and a fairly well conserved typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187608 [Multi-domain]  Cd Length: 239  Bit Score: 99.33  E-value: 3.78e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  25 ALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEIG---AGARLLVLDVTD----LDGIARATTQVDRLDVLV 97
Cdd:cd05350   1 VLITGASSGIGRALAREFAKAGYNVALAARRTDRLDELKAELLnpnPSVEVEILDVTDeernQLVIAELEAELGGLDLVI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  98 NNAGISPSlAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTASLTWstnpnpqftpgsGGAAAY 177
Cdd:cd05350  81 INAGVGKG-TSLGDLSFKAFRETIDTNLLGAAAILEAALPQFRAKGRGHLVLISSVAALRGL------------PGAAAY 147

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 30267738 178 RSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDLN 215
Cdd:cd05350 148 SASKAALSSLAESLRYDVKKRGIRVTVINPGFIDTPLT 185
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
 20-228 4.00e-25

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 99.96  E-value: 4.00e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   20 MNDRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEI---GAGARLLVLDVTDL----DGIARATTQVDR 92
Cdd:PRK12429   2 LKGKVALVTGAASGIGLEIALALAKEGAKVVIADLNDEAAAAAAEALqkaGGKAIGVAMDVTDEeainAGIDYAVETFGG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   93 LDVLVNNAGISpSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSgTASLTwstnpnpqftpGSG 172
Cdd:PRK12429  82 VDILVNNAGIQ-HVAPIEDFPTEKWKKMIAIMLDGAFLTTKAALPIMKAQGGGRIINMAS-VHGLV-----------GSA 148

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30267738  173 GAAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDL-----NPLAAAAGDDPAEA 228
Cdd:PRK12429 149 GKAAYVSAKHGLIGLTKVVALEGATHGVTVNAICPGYVDTPLvrkqiPDLAKERGISEEEV 209
3oxo_ACP_reduc TIGR01830
3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, ...
 25-213 6.05e-25

3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, also called 3-ketoacyl-acyl carrier protein reductase, an enzyme of fatty acid biosynthesis. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 273824 [Multi-domain]  Cd Length: 239  Bit Score: 98.82  E-value: 6.05e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738    25 ALVTGANKGIGKHIARVLVAEGLTVYV-GSRDRGLGQRAVEEI---GAGARLLVLDVTDLD----GIARATTQVDRLDVL 96
Cdd:TIGR01830   1 ALVTGASRGIGRAIALKLAKEGAKVIItYRSSEEGAEEVVEELkalGVKALGVVLDVSDREdvkaVVEEIEEELGTIDIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738    97 VNNAGISpslappADT-----SVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTASLtwstnpnpqftpGS 171
Cdd:TIGR01830  81 VNNAGIT------RDNllmrmKEEDWDAVIDTNLTGVFNLTQAVLRIMIKQRSGRIINISSVVGLM------------GN 142

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 30267738   172 GGAAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATD 213
Cdd:TIGR01830 143 AGQANYAASKAGVIGFTKSLAKELASRNITVNAVAPGFIDTD 184
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
 23-225 8.79e-25

tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup includes TR-I and TR-II; these proteins are members of the SDR family. TRs catalyze the NADPH-dependent reductions of the 3-carbonyl group of tropinone, to a beta-hydroxyl group. TR-I and TR-II produce different stereoisomers from tropinone, TR-I produces tropine (3alpha-hydroxytropane), and TR-II, produces pseudotropine (sigma-tropine, 3beta-hydroxytropane). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187590 [Multi-domain]  Cd Length: 251  Bit Score: 98.67  E-value: 8.79e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  23 RTALVTGANKGIGKHIARVLVAEGLTVYVGSRDrglgQRAVEEI-------GAGARLLVLDVTDLDGIARATTQV----- 90
Cdd:cd05329   7 KTALVTGGTKGIGYAIVEELAGLGAEVYTCARN----QKELDECltewrekGFKVEGSVCDVSSRSERQELMDTVashfg 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  91 DRLDVLVNNAGISPSlAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTASLTWSTnpnpqftpg 170
Cdd:cd05329  83 GKLNILVNNAGTNIR-KEAKDYTEEDYSLIMSTNFEAAYHLSRLAHPLLKASGNGNIVFISSVAGVIAVPS--------- 152

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 30267738 171 sggAAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATdlnPLAAAAGDDP 225
Cdd:cd05329 153 ---GAPYGATKGALNQLTRSLACEWAKDNIRVNAVAPWVIAT---PLVEPVIQQK 201
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
 23-249 1.19e-24

retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup containing retinol-DHs and related proteins. Retinol is processed by a medium chain alcohol dehydrogenase followed by retinol-DHs. Proteins in this subfamily share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. This subgroup includes the human proteins: retinol dehydrogenase -12, -13 ,and -14. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212495 [Multi-domain]  Cd Length: 274  Bit Score: 99.08  E-value: 1.19e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  23 RTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEIGAGAR---LLV--LDVTDLDGI----ARATTQVDRL 93
Cdd:cd09807   2 KTVIITGANTGIGKETARELARRGARVIMACRDMAKCEEAAAEIRRDTLnheVIVrhLDLASLKSIrafaAEFLAEEDRL 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  94 DVLVNNAGIspsLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISS--------GTASLTWSTNPNP 165
Cdd:cd09807  82 DVLINNAGV---MRCPYSKTEDGFEMQFGVNHLGHFLLTNLLLDLLKKSAPSRIVNVSSlahkagkiNFDDLNSEKSYNT 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738 166 QFtpgsggaaAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDL---------------NPLAAAAGDDPAEAAQ 230
Cdd:cd09807 159 GF--------AYCQSKLANVLFTRELARRLQGTGVTVNALHPGVVRTELgrhtgihhlflstllNPLFWPFVKTPREGAQ 230

                       250       260
                ....*....|....*....|
gi 30267738 231 GAARLALLPD-DGPTGGFFS 249
Cdd:cd09807 231 TSIYLALAEElEGVSGKYFS 250
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
 20-208 1.37e-24

RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is an SDR-family beta-ketoacyl reductase involved in Rhamnolipid biosynthesis. RhlG is similar to but distinct from the FabG family of beta-ketoacyl-acyl carrier protein (ACP) of type II fatty acid synthesis. RhlG and related proteins are classical SDRs, with a canonical active site tetrad and glycine-rich NAD(P)-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187646 [Multi-domain]  Cd Length: 250  Bit Score: 98.32  E-value: 1.37e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  20 MNDRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEIGAGARLLVL--DVTDLDGIARATTQV----DRL 93
Cdd:cd08942   4 VAGKIVLVTGGSRGIGRMIAQGFLEAGARVIISARKAEACADAAEELSAYGECIAIpaDLSSEEGIEALVARVaersDRL 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  94 DVLVNNAGISPSlAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSP---HP-RIVNISS-GTASLTWSTNpnpqft 168
Cdd:cd08942  84 DVLVNNAGATWG-APLEAFPESGWDKVMDINVKSVFFLTQALLPLLRAAAtaeNPaRVINIGSiAGIVVSGLEN------ 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 30267738 169 pgsggaAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPG 208
Cdd:cd08942 157 ------YSYGASKAAVHQLTRKLAKELAGEHITVNAIAPG 190
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
20-208 2.59e-24

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 97.79  E-value: 2.59e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   20 MNDRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEIGAGARLLVLDVTDLDGIARATTQVDR----LDV 95
Cdd:PRK07067   4 LQGKVALLTGAASGIGEAVAERYLAEGARVVIADIKPARARLAALEIGPAAIAVSLDVTRQDSIDRIVAAAVErfggIDI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   96 LVNNAGISpSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPAL-RRSPHPRIVNISSGTASltwstnpnpqftPGSGGA 174
Cdd:PRK07067  84 LFNNAALF-DMAPILDISRDSYDRLFAVNVKGLFFLMQAVARHMvEQGRGGKIINMASQAGR------------RGEALV 150

                        170       180       190
                 ....*....|....*....|....*....|....
gi 30267738  175 AAYRSSKAALNALTVLYAQTLAEDGFKVNALAPG 208
Cdd:PRK07067 151 SHYCATKAAVISYTQSAALALIRHGINVNAIAPG 184
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
 14-186 3.40e-24

11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human 11beta_HSD1 catalyzes the NADP(H)-dependent interconversion of cortisone and cortisol. This subgroup also includes human dehydrogenase/reductase SDR family member 7C (DHRS7C) and DHRS7B. These proteins have the GxxxGxG nucleotide binding motif and S-Y-K catalytic triad characteristic of the SDRs, but have an atypical C-terminal domain that contributes to homodimerization contacts. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187593 [Multi-domain]  Cd Length: 257  Bit Score: 97.27  E-value: 3.40e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  14 QGTVVamndrtaLVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEI----GAGARLLVLDVTDLDGIARATTQ 89
Cdd:cd05332   2 QGKVV-------IITGASSGIGEELAYHLARLGARLVLSARREERLEEVKSEClelgAPSPHVVPLDMSDLEDAEQVVEE 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  90 V----DRLDVLVNNAGISpSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTASLtwstnpnp 165
Cdd:cd05332  75 AlklfGGLDILINNAGIS-MRSLFHDTSIDVDRKIMEVNYFGPVALTKAALPHLIERSQGSIVVVSSIAGKI-------- 145

                       170       180
                ....*....|....*....|.
gi 30267738 166 qftpGSGGAAAYRSSKAALNA 186
Cdd:cd05332 146 ----GVPFRTAYAASKHALQG 162
PRK05693 PRK05693
SDR family oxidoreductase;
24-212 5.24e-24

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 97.17  E-value: 5.24e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   24 TALVTGANKGIGKHIARVLVAEGLTVYVGSRDrglgQRAVEEIG-AGARLLVLDVTDLDGIARATTQVD----RLDVLVN 98
Cdd:PRK05693   3 VVLITGCSSGIGRALADAFKAAGYEVWATARK----AEDVEALAaAGFTAVQLDVNDGAALARLAEELEaehgGLDVLIN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   99 NAGISpSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSpHPRIVNISSGTASLTwstnpnpqfTPGSGgaaAYR 178
Cdd:PRK05693  79 NAGYG-AMGPLLDGGVEAMRRQFETNVFAVVGVTRALFPLLRRS-RGLVVNIGSVSGVLV---------TPFAG---AYC 144

                        170       180       190
                 ....*....|....*....|....*....|....
gi 30267738  179 SSKAALNALTVLYAQTLAEDGFKVNALAPGMRAT 212
Cdd:PRK05693 145 ASKAAVHALSDALRLELAPFGVQVMEVQPGAIAS 178
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 24-214 6.71e-24

human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid dehydrogenases (17betaHSD) are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. 17betaHSD type XI, a classical SDR, preferentially converts 3alpha-Adiol to androsterone but not numerous other tested steroids. This subgroup of classical SDRs also includes members identified as retinol dehydrogenases, which convert retinol to retinal, a property that overlaps with 17betaHSD activity. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187598 [Multi-domain]  Cd Length: 243  Bit Score: 96.16  E-value: 6.71e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  24 TALVTGANKGIGKHIARVLVAEGLTVYV-GSRDRGLGQRA--VEEIGAGARLLVLDVTDLDGIARATTQVDR----LDVL 96
Cdd:cd05339   1 IVLITGGGSGIGRLLALEFAKRGAKVVIlDINEKGAEETAnnVRKAGGKVHYYKCDVSKREEVYEAAKKIKKevgdVTIL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  97 VNNAGIsPSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTASLtwstnpnpqftpGSGGAAA 176
Cdd:cd05339  81 INNAGV-VSGKKLLELPDEEIEKTFEVNTLAHFWTTKAFLPDMLERNHGHIVTIASVAGLI------------SPAGLAD 147

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 30267738 177 YRSSKAALnaltVLYAQTLAE-------DGFKVNALAPGMRATDL 214
Cdd:cd05339 148 YCASKAAA----VGFHESLRLelkaygkPGIKTTLVCPYFINTGM 188
PRK06124 PRK06124
SDR family oxidoreductase;
23-237 7.44e-24

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 96.32  E-value: 7.44e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   23 RTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEI---GAGARLLVLDVTDLDGIARATTQVD----RLDV 95
Cdd:PRK06124  12 QVALVTGSARGLGFEIARALAGAGAHVLVNGRNAATLEAAVAALraaGGAAEALAFDIADEEAVAAAFARIDaehgRLDI 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   96 LVNNAGiSPSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTASLTWStnpnpqftpgsgGAA 175
Cdd:PRK06124  92 LVNNVG-ARDRRPLAELDDAAIRALLETDLVAPILLSRLAAQRMKRQGYGRIIAITSIAGQVARA------------GDA 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30267738  176 AYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDLNplaAAAGDDPAEAAQGAARLAL 237
Cdd:PRK06124 159 VYPAAKQGLTGLMRALAAEFGPHGITSNAIAPGYFATETN---AAMAADPAVGPWLAQRTPL 217
PRK07062 PRK07062
SDR family oxidoreductase;
20-209 9.08e-24

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 96.26  E-value: 9.08e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   20 MNDRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEIG---AGARLL-----VLDVTDLDGIARATTQ-V 90
Cdd:PRK07062   6 LEGRVAVVTGGSSGIGLATVELLLEAGASVAICGRDEERLASAEARLRekfPGARLLaarcdVLDEADVAAFAAAVEArF 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   91 DRLDVLVNNAGISpSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTASltwstNPNPQFtpg 170
Cdd:PRK07062  86 GGVDMLVNNAGQG-RVSTFADTTDDAWRDELELKYFSVINPTRAFLPLLRASAAASIVCVNSLLAL-----QPEPHM--- 156

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 30267738  171 sggaAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGM 209
Cdd:PRK07062 157 ----VATSAARAGLLNLVKSLATELAPKGVRVNSILLGL 191
PRK07063 PRK07063
SDR family oxidoreductase;
23-239 1.00e-23

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 96.27  E-value: 1.00e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   23 RTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEI---GAGARLLVL--DVTDLDGI----ARATTQVDRL 93
Cdd:PRK07063   8 KVALVTGAAQGIGAAIARAFAREGAAVALADLDAALAERAAAAIardVAGARVLAVpaDVTDAASVaaavAAAEEAFGPL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   94 DVLVNNAGISpSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTASltwstnpnpQFTPgsgG 173
Cdd:PRK07063  88 DVLVNNAGIN-VFADPLAMTDEDWRRCFAVDLDGAWNGCRAVLPGMVERGRGSIVNIASTHAF---------KIIP---G 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30267738  174 AAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDLNPLAAAAGDDPAEAAQGAarLALLP 239
Cdd:PRK07063 155 CFPYPVAKHGLLGLTRALGIEYAARNVRVNAIAPGYIETQLTEDWWNAQPDPAAARAET--LALQP 218
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
 25-213 1.04e-23

7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial subgroup contains 7 alpha-HSDHs, including Escherichia coli 7 alpha-HSDH. 7 alpha-HSDH, a member of the SDR family, catalyzes the NAD+ -dependent dehydrogenation of a hydroxyl group at position 7 of the steroid skeleton of bile acids. In humans the two primary bile acids are cholic and chenodeoxycholic acids, these are formed from cholesterol in the liver. Escherichia coli 7 alpha-HSDH dehydroxylates these bile acids in the human intestine. Mammalian 7 alpha-HSDH activity has been found in livers. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187623 [Multi-domain]  Cd Length: 242  Bit Score: 95.71  E-value: 1.04e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  25 ALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEI---GAGARLLVLDVTDLDGIAR----ATTQVDRLDVLV 97
Cdd:cd05365   2 AIVTGGAAGIGKAIAGTLAKAGASVVIADLKSEGAEAVAAAIqqaGGQAIGLECNVTSEQDLEAvvkaTVSQFGGITILV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  98 NNAGISPSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTasltwSTNPNPQFTpgsggaaAY 177
Cdd:cd05365  82 NNAGGGGPKPFDMPMTEEDFEWAFKLNLFSAFRLSQLCAPHMQKAGGGAILNISSMS-----SENKNVRIA-------AY 149

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 30267738 178 RSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATD 213
Cdd:cd05365 150 GSSKAAVNHMTRNLAFDLGPKGIRVNAVAPGAVKTD 185
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
 22-216 1.41e-23

classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187613 [Multi-domain]  Cd Length: 270  Bit Score: 95.82  E-value: 1.41e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  22 DRTALVTGANKGIGKHIARVLVAEGLTV---YVGSRDRGLGQ--RAVEEIGAGARLLVLDVTDLDGIARATTQV----DR 92
Cdd:cd05355  26 GKKALITGGDSGIGRAVAIAFAREGADVainYLPEEEDDAEEtkKLIEEEGRKCLLIPGDLGDESFCRDLVKEVvkefGK 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  93 LDVLVNNAG---ISPSLAppaDTSVEEFRRTYETNVFGVVAVTNAFLPALRrsPHPRIVNISSGTAsltwsTNPNPQFTP 169
Cdd:cd05355 106 LDILVNNAAyqhPQESIE---DITTEQLEKTFRTNIFSMFYLTKAALPHLK--KGSSIINTTSVTA-----YKGSPHLLD 175

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 30267738 170 gsggaaaYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDLNP 216
Cdd:cd05355 176 -------YAATKGAIVAFTRGLSLQLAEKGIRVNAVAPGPIWTPLIP 215
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 23-214 2.04e-23

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 95.41  E-value: 2.04e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   23 RTALVTGANKGIGKHIARVLVAEGLTVYVGSR--DRGLG--QRAVEEIGAGARLLVLDVTDLDGIARATTQV----DRLD 94
Cdd:PRK12745   3 PVALVTGGRRGIGLGIARALAAAGFDLAINDRpdDEELAatQQELRALGVEVIFFPADVADLSAHEAMLDAAqaawGRID 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   95 VLVNNAGISPSL-APPADTSVEEFRRTYETNVFGVVAVTNAFL------PALRRSPHPRIVNISSGTASLTwSTNpnpqf 167
Cdd:PRK12745  83 CLVNNAGVGVKVrGDLLDLTPESFDRVLAINLRGPFFLTQAVAkrmlaqPEPEELPHRSIVFVSSVNAIMV-SPN----- 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 30267738  168 tpgsggAAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDL 214
Cdd:PRK12745 157 ------RGEYCISKAGLSMAAQLFAARLAEEGIGVYEVRPGLIKTDM 197
PRK06398 PRK06398
aldose dehydrogenase; Validated
 20-225 2.27e-23

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 95.28  E-value: 2.27e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   20 MNDRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDrglgqravEEIGAGARLLVLDVTD----LDGIARATTQVDRLDV 95
Cdd:PRK06398   4 LKDKVAIVTGGSQGIGKAVVNRLKEEGSNVINFDIK--------EPSYNDVDYFKVDVSNkeqvIKGIDYVISKYGRIDI 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   96 LVNNAGISpSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTASLTwstnpnpqftpgSGGAA 175
Cdd:PRK06398  76 LVNNAGIE-SYGAIHAVEEDEWDRIINVNVNGIFLMSKYTIPYMLKQDKGVIINIASVQSFAV------------TRNAA 142

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 30267738  176 AYRSSKAALNALT----VLYAQTLaedgfKVNALAPGMRATDLNPLAAA--AGDDP 225
Cdd:PRK06398 143 AYVTSKHAVLGLTrsiaVDYAPTI-----RCVAVCPGSIRTPLLEWAAEleVGKDP 193
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
 23-212 2.27e-23

meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases (BDHs) catalyze the NAD+ dependent conversion of 2,3-butanediol to acetonin; BDHs are classified into types according to their stereospecificity as to substrates and products. Included in this subgroup are Klebsiella pneumonia meso-BDH which catalyzes meso-2,3-butanediol to D(-)-acetonin, and Corynebacterium glutamicum L-BDH which catalyzes lX+)-2,3-butanediol to L(+)-acetonin. This subgroup is comprised of classical SDRs with the characteristic catalytic triad and NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187624 [Multi-domain]  Cd Length: 257  Bit Score: 95.14  E-value: 2.27e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  23 RTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVE----EIGAGARLLVLDVTDLDGIARATTQVDR----LD 94
Cdd:cd05366   3 KVAIITGAAQGIGRAIAERLAADGFNIVLADLNLEEAAKSTIqeisEAGYNAVAVGADVTDKDDVEALIDQAVEkfgsFD 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  95 VLVNNAGISPSlAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHP-RIVNISSGTASLTwstNPNpqftpgsgg 173
Cdd:cd05366  83 VMVNNAGIAPI-TPLLTITEEDLKKVYAVNVFGVLFGIQAAARQFKKLGHGgKIINASSIAGVQG---FPN--------- 149

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 30267738 174 AAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRAT 212
Cdd:cd05366 150 LGAYSASKFAVRGLTQTAAQELAPKGITVNAYAPGIVKT 188
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
 25-214 2.70e-23

17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) SDRs; This subgroup includes various 17-beta-hydroxysteroid dehydrogenases and 3-ketoacyl-CoA reductase, these are members of the SDR family, and contain the canonical active site tetrad and glycine-rich NAD-binding motif of the classical SDRs. 3-ketoacyl-CoA reductase (KAR, aka 17beta-HSD type 12, encoded by HSD17B12) acts in fatty acid elongation; 17beta- hydroxysteroid dehydrogenases are isozymes that catalyze activation and inactivation of estrogen and androgens, and include members of the SDR family. 17beta-estradiol dehydrogenase (aka 17beta-HSD type 1, encoded by HSD17B1) converts estrone to estradiol. Estradiol is the predominant female sex hormone. 17beta-HSD type 3 (aka testosterone 17-beta-dehydrogenase 3, encoded by HSD17B3) catalyses the reduction of androstenedione to testosterone, it also accepts estrogens as substrates. This subgroup also contains a putative steroid dehydrogenase let-767 from Caenorhabditis elegans, mutation in which results in hypersensitivity to cholesterol limitation. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187614 [Multi-domain]  Cd Length: 239  Bit Score: 94.59  E-value: 2.70e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  25 ALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEI----GAGARLLVLDVTDLDGI-ARATTQVDRLDV--LV 97
Cdd:cd05356   4 AVVTGATDGIGKAYAEELAKRGFNVILISRTQEKLDAVAKEIeekyGVETKTIAADFSAGDDIyERIEKELEGLDIgiLV 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  98 NNAGISPSLA-PPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTASLtwstnPNPQFtpgsggaAA 176
Cdd:cd05356  84 NNVGISHSIPeYFLETPEDELQDIINVNVMATLKMTRLILPGMVKRKKGAIVNISSFAGLI-----PTPLL-------AT 151

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 30267738 177 YRSSKAALNALT-VLYAQtLAEDGFKVNALAPGMRATDL 214
Cdd:cd05356 152 YSASKAFLDFFSrALYEE-YKSQGIDVQSLLPYLVATKM 189
PRK09072 PRK09072
SDR family oxidoreductase;
21-230 3.05e-23

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 95.01  E-value: 3.05e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   21 NDRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEIGAGARL--LVLDVTDLDGIA---RATTQVDRLDV 95
Cdd:PRK09072   4 KDKRVLLTGASGGIGQALAEALAAAGARLLLVGRNAEKLEALAARLPYPGRHrwVVADLTSEAGREavlARAREMGGINV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   96 LVNNAGISpSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTASLtwstnpnpqftpGSGGAA 175
Cdd:PRK09072  84 LINNAGVN-HFALLEDQDPEAIERLLALNLTAPMQLTRALLPLLRAQPSAMVVNVGSTFGSI------------GYPGYA 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30267738  176 AYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDLNPLAA--------AAGDDPAEAAQ 230
Cdd:PRK09072 151 SYCASKFALRGFSEALRRELADTGVRVLYLAPRATRTAMNSEAVqalnralgNAMDDPEDVAA 213
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
 23-228 3.58e-23

human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are classical SDRs, with a canonical active site tetrad and a close match to the typical Gly-rich NAD-binding motif. Human DHRS6 is a cytosolic type 2 (R)-hydroxybutyrate dehydrogenase, which catalyses the conversion of (R)-hydroxybutyrate to acetoacetate. Also included in this subgroup is Escherichia coli UcpA (upstream cys P). Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction. Note: removed : needed to make this chiodl smaller when drew final trees: rmeoved text form description: Other proteins in this subgroup include Thermoplasma acidophilum aldohexose dehydrogenase, which has high dehydrogenase activity against D-mannose, Bacillus subtilis BacC involved in the biosynthesis of the dipeptide bacilysin and its antibiotic moiety anticapsin, Sphingomonas paucimobilis strain B90 LinC, involved in the degradation of hexachlorocyclohexane isomers...... P).


Pssm-ID: 187626 [Multi-domain]  Cd Length: 241  Bit Score: 94.46  E-value: 3.58e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  23 RTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAveEIGAGARLLVLDVTDLDGIARATTQVDRLDVLVNNAGI 102
Cdd:cd05368   3 KVALITAAAQGIGRAIALAFAREGANVIATDINEEKLKEL--ERGPGITTRVLDVTDKEQVAALAKEEGRIDVLFNCAGF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738 103 SPsLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTASLTwstnpnpqftpGSGGAAAYRSSKA 182
Cdd:cd05368  81 VH-HGSILDCEDDDWDFAMNLNVRSMYLMIKAVLPKMLARKDGSIINMSSVASSIK-----------GVPNRFVYSTTKA 148

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 30267738 183 ALNALTVLYAQTLAEDGFKVNALAPGMRATDLNPLAAAAGDDPAEA 228
Cdd:cd05368 149 AVIGLTKSVAADFAQQGIRCNAICPGTVDTPSLEERIQAQPDPEEA 194
PRK07577 PRK07577
SDR family oxidoreductase;
20-224 3.88e-23

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 94.02  E-value: 3.88e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   20 MNDRTALVTGANKGIGKHIARVLVAEGLTVYvgsrdrGLGQRAVEEIGAgaRLLVLDVTDLDGIARATTQV---DRLDVL 96
Cdd:PRK07577   1 MSSRTVLVTGATKGIGLALSLRLANLGHQVI------GIARSAIDDFPG--ELFACDLADIEQTAATLAQIneiHPVDAI 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   97 VNNAGISpSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTasltwstnpnpqfTPGSGGAAA 176
Cdd:PRK07577  73 VNNVGIA-LPQPLGKIDLAALQDVYDLNVRAAVQVTQAFLEGMKLREQGRIVNICSRA-------------IFGALDRTS 138

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 30267738  177 YRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDLNPLAAAAGDD 224
Cdd:PRK07577 139 YSAAKSALVGCTRTWALELAEYGITVNAVAPGPIETELFRQTRPVGSE 186
PRK12828 PRK12828
short chain dehydrogenase; Provisional
 20-236 1.38e-22

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 92.55  E-value: 1.38e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   20 MNDRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEIGA-GARLLVLDVTDLDGIARA----TTQVDRLD 94
Cdd:PRK12828   5 LQGKVVAITGGFGGLGRATAAWLAARGARVALIGRGAAPLSQTLPGVPAdALRIGGIDLVDPQAARRAvdevNRQFGRLD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   95 VLVNNAGISPSlAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTASLTwstnpnpqfTPGSGga 174
Cdd:PRK12828  85 ALVNIAGAFVW-GTIADGDADTWDRMYGVNVKTTLNASKAALPALTASGGGRIVNIGAGAALKA---------GPGMG-- 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30267738  175 aAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDLNPLAAAAGD-----DPAEAAQGAARLA 236
Cdd:PRK12828 153 -AYAAAKAGVARLTEALAAELLDRGITVNAVLPSIIDTPPNRADMPDADfsrwvTPEQIAAVIAFLL 218
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
 23-241 1.43e-22

putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) SDR; This subgroup includes Escherichia coli CFT073 FabG. The Escherichai coli K12 BKR, FabG, belongs to a different subgroup. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet) NAD(P)(H) binding region and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H) binding pattern: TGxxxGxG in classical SDRs. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P) binding motif and an altered active site motif (YXXXN). Fungal type type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P) binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr-151 and Lys-155, and well as Asn-111 (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187596 [Multi-domain]  Cd Length: 255  Bit Score: 92.91  E-value: 1.43e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  23 RTALVTGANKGIGKHIARVLVAEG--LTVYVGSRDRGLG--QRAVEEIGAGARLLVLDVTDLDG----IARATTQVDRLD 94
Cdd:cd05337   2 PVAIVTGASRGIGRAIATELAARGfdIAINDLPDDDQATevVAEVLAAGRRAIYFQADIGELSDhealLDQAWEDFGRLD 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  95 VLVNNAGISPS-LAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHP------RIVNISSGTASLTwstnpnpqf 167
Cdd:cd05337  82 CLVNNAGIAVRpRGDLLDLTEDSFDRLIAINLRGPFFLTQAVARRMVEQPDRfdgphrSIIFVTSINAYLV--------- 152

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30267738 168 tpgSGGAAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDLNPLAAAAGDDPAEAAQGAARLALLPDD 241
Cdd:cd05337 153 ---SPNRGEYCISKAGLSMATRLLAYRLADEGIAVHEIRPGLIHTDMTAPVKEKYDELIAAGLVPIRRWGQPED 223
PRK06197 PRK06197
short chain dehydrogenase; Provisional
 23-214 2.08e-22

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 93.55  E-value: 2.08e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   23 RTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEI-----GAGARLLVLDVTDLDGIARATTQV----DRL 93
Cdd:PRK06197  17 RVAVVTGANTGLGYETAAALAAKGAHVVLAVRNLDKGKAAAARItaatpGADVTLQELDLTSLASVRAAADALraayPRI 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   94 DVLVNNAGIspsLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSG----TASLTWStnpNPQFTP 169
Cdd:PRK06197  97 DLLINNAGV---MYTPKQTTADGFELQFGTNHLGHFALTGLLLDRLLPVPGSRVVTVSSGghriRAAIHFD---DLQWER 170

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 30267738  170 GSGGAAAYRSSKAALNALTVLYAQTLAEDGFKVNALA--PGMRATDL 214
Cdd:PRK06197 171 RYNRVAAYGQSKLANLLFTYELQRRLAAAGATTIAVAahPGVSNTEL 217
PRK07478 PRK07478
short chain dehydrogenase; Provisional
 20-225 2.78e-22

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 92.30  E-value: 2.78e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   20 MNDRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEI---GAGARLLVLDVTDLD----GIARATTQVDR 92
Cdd:PRK07478   4 LNGKVAIITGASSGIGRAAAKLFAREGAKVVVGARRQAELDQLVAEIraeGGEAVALAGDVRDEAyakaLVALAVERFGG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   93 LDVLVNNAGISPSLAPPADTSVEEFRRTYETNvfgvvaVTNAFLPALRRSPHprivNISSGTASLTWsTNPNPQFTPGSG 172
Cdd:PRK07478  84 LDIAFNNAGTLGEMGPVAEMSLEGWRETLATN------LTSAFLGAKHQIPA----MLARGGGSLIF-TSTFVGHTAGFP 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 30267738  173 GAAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGmrATDlNPLAAAAGDDP 225
Cdd:PRK07478 153 GMAAYAASKAGLIGLTQVLAAEYGAQGIRVNALLPG--GTD-TPMGRAMGDTP 202
PRK07774 PRK07774
SDR family oxidoreductase;
22-215 3.19e-22

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 92.11  E-value: 3.19e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   22 DRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEI---GAGARLLVLDVTDLDGI----ARATTQVDRLD 94
Cdd:PRK07774   6 DKVAIVTGAAGGIGQAYAEALAREGASVVVADINAEGAERVAKQIvadGGTAIAVQVDVSDPDSAkamaDATVSAFGGID 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   95 VLVNNAGI--SPSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSgTASLTWSTnpnpqftpgsg 172
Cdd:PRK07774  86 YLVNNAAIygGMKLDLLITVPWDYYKKFMSVNLDGALVCTRAVYKHMAKRGGGAIVNQSS-TAAWLYSN----------- 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 30267738  173 gaaAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDLN 215
Cdd:PRK07774 154 ---FYGLAKVGLNGLTQQLARELGGMNIRVNAIAPGPIDTEAT 193
PRK08263 PRK08263
short chain dehydrogenase; Provisional
 20-240 3.40e-22

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 92.41  E-value: 3.40e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   20 MNDRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEIGAGARLLVLDVTDLDG----IARATTQVDRLDV 95
Cdd:PRK08263   1 MMEKVWFITGASRGFGRAWTEAALERGDRVVATARDTATLADLAEKYGDRLLPLALDVTDRAAvfaaVETAVEHFGRLDI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   96 LVNNAGISpSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSgTASLtwSTNPNpqftpgsggAA 175
Cdd:PRK08263  81 VVNNAGYG-LFGMIEEVTESEARAQIDTNFFGALWVTQAVLPYLREQRSGHIIQISS-IGGI--SAFPM---------SG 147

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30267738  176 AYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDLNPLAA--AAGDDP-----AEAAQGAARLALLPD 240
Cdd:PRK08263 148 IYHASKWALEGMSEALAQEVAEFGIKVTLVEPGGYSTDWAGTSAkrATPLDAydtlrEELAEQWSERSVDGD 219
PRK06484 PRK06484
short chain dehydrogenase; Validated
 23-230 4.96e-22

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 94.53  E-value: 4.96e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   23 RTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEIGAGARLLVLDVTDLDGIARATTQVD----RLDVLVN 98
Cdd:PRK06484   6 RVVLVTGAAGGIGRAACQRFARAGDQVVVADRNVERARERADSLGPDHHALAMDVSDEAQIREGFEQLHrefgRIDVLVN 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   99 NAGIS-PSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPH-PRIVNISSGTASLtwsTNPnpqftpgsgGAAA 176
Cdd:PRK06484  86 NAGVTdPTMTATLDTTLEEFARLQAINLTGAYLVAREALRLMIEQGHgAAIVNVASGAGLV---ALP---------KRTA 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 30267738  177 YRSSKAALNALTVLYAQTLAEDGFKVNALAPG-MRATDLNPLAAAAGDDPAEAAQ 230
Cdd:PRK06484 154 YSASKAAVISLTRSLACEWAAKGIRVNAVLPGyVRTQMVAELERAGKLDPSAVRS 208
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
 23-212 9.39e-22

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 90.89  E-value: 9.39e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   23 RTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGL---GQRAVEEIGAGARLLVLDVTDLDGIARATTQVDR----LDV 95
Cdd:PRK07097  11 KIALITGASYGIGFAIAKAYAKAGATIVFNDINQELvdkGLAAYRELGIEAHGYVCDVTDEDGVQAMVSQIEKevgvIDI 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   96 LVNNAGISPSLaPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTASLtwstnpnpqftpGSGGAA 175
Cdd:PRK07097  91 LVNNAGIIKRI-PMLEMSAEDFRQVIDIDLNAPFIVSKAVIPSMIKKGHGKIINICSMMSEL------------GRETVS 157

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 30267738  176 AYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRAT 212
Cdd:PRK07097 158 AYAAAKGGLKMLTKNIASEYGEANIQCNGIGPGYIAT 194
PRK07890 PRK07890
short chain dehydrogenase; Provisional
 22-242 1.04e-21

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 90.79  E-value: 1.04e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   22 DRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEI-GAGARLLVL--DVTDLDGIAR----ATTQVDRLD 94
Cdd:PRK07890   5 GKVVVVSGVGPGLGRTLAVRAARAGADVVLAARTAERLDEVAAEIdDLGRRALAVptDITDEDQCANlvalALERFGRVD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   95 VLVNNAGISPSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSpHPRIVNISSgtaslTWSTNPNPQFtpgsgga 174
Cdd:PRK07890  85 ALVNNAFRVPSMKPLADADFAHWRAVIELNVLGTLRLTQAFTPALAES-GGSIVMINS-----MVLRHSQPKY------- 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30267738  175 AAYRSSKAALNALTVLYAQTLAEDGFKVNALAPG-MRATDL----NPLAAAAGDDPAEA-AQGAARLAL--LPDDG 242
Cdd:PRK07890 152 GAYKMAKGALLAASQSLATELGPQGIRVNSVAPGyIWGDPLkgyfRHQAGKYGVTVEQIyAETAANSDLkrLPTDD 227
PRK07825 PRK07825
short chain dehydrogenase; Provisional
 20-214 1.05e-21

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 91.16  E-value: 1.05e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   20 MNDRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEIGAgARLLVLDVTDLDGIAR----ATTQVDRLDV 95
Cdd:PRK07825   3 LRGKVVAITGGARGIGLATARALAALGARVAIGDLDEALAKETAAELGL-VVGGPLDVTDPASFAAfldaVEADLGPIDV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   96 LVNNAGISPsLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTASLTwstnpnpqfTPgsgGAA 175
Cdd:PRK07825  82 LVNNAGVMP-VGPFLDEPDAVTRRILDVNVYGVILGSKLAAPRMVPRGRGHVVNVASLAGKIP---------VP---GMA 148

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 30267738  176 AYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDL 214
Cdd:PRK07825 149 TYCASKHAVVGFTDAARLELRGTGVHVSVVLPSFVNTEL 187
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 25-236 1.16e-21

insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains insect type ADH, and 15-hydroxyprostaglandin dehydrogenase (15-PGDH) type I; these proteins are classical SDRs. ADH catalyzes the NAD+-dependent oxidation of alcohols to aldehydes/ketones. This subgroup is distinct from the zinc-dependent alcohol dehydrogenases of the medium chain dehydrogenase/reductase family, and evolved in fruit flies to allow the digestion of fermenting fruit. 15-PGDH catalyzes the NAD-dependent interconversion of (5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-13-enoate and (5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-13-enoate, and has a typical SDR glycine-rich NAD-binding motif, which is not fully present in ADH. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187584 [Multi-domain]  Cd Length: 244  Bit Score: 90.44  E-value: 1.16e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  25 ALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLG-QRAVEEI--GAGARLLVLDVTDLDGIARATTQV----DRLDVLV 97
Cdd:cd05323   3 AIITGGASGIGLATAKLLLKKGAKVAILDRNENPGaAAELQAInpKVKATFVQCDVTSWEQLAAAFKKAiekfGRVDILI 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  98 NNAGISPSLAPPADTSVEE-FRRTYETNVFGVVAVTNAFLPALRRSPHP---RIVNISSgTASLtwstNPNPQFtpgsgg 173
Cdd:cd05323  83 NNAGILDEKSYLFAGKLPPpWEKTIDVNLTGVINTTYLALHYMDKNKGGkggVIVNIGS-VAGL----YPAPQF------ 151

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30267738 174 aAAYRSSKAALNALTVLYAQTLAED-GFKVNALAPGMRATDLNPLAAAAGDD---------PAEAAQGAARLA 236
Cdd:cd05323 152 -PVYSASKHGVVGFTRSLADLLEYKtGVRVNAICPGFTNTPLLPDLVAKEAEmlpsaptqsPEVVAKAIVYLI 223
PRK05650 PRK05650
SDR family oxidoreductase;
26-230 1.24e-21

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 90.87  E-value: 1.24e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   26 LVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEIG-AGARLLVL--DVTDLDGI-ARATTQVDR---LDVLVN 98
Cdd:PRK05650   4 MITGAASGLGRAIALRWAREGWRLALADVNEEGGEETLKLLReAGGDGFYQrcDVRDYSQLtALAQACEEKwggIDVIVN 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   99 NAGISpSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSgTASLTwstnPNPqftpgsgGAAAYR 178
Cdd:PRK05650  84 NAGVA-SGGFFEELSLEDWDWQIAINLMGVVKGCKAFLPLFKRQKSGRIVNIAS-MAGLM----QGP-------AMSSYN 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 30267738  179 SSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDLnpLAAAAGDDPAEAAQ 230
Cdd:PRK05650 151 VAKAGVVALSETLLVELADDEIGVHVVCPSFFQTNL--LDSFRGPNPAMKAQ 200
PRK09291 PRK09291
SDR family oxidoreductase;
23-215 1.29e-21

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 90.44  E-value: 1.29e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   23 RTALVTGANKGIGKHIARVLVAEGLTVYVGSRD----RGLgQRAVEEIGAGARLLVLDVTDLDGIARATTQvdRLDVLVN 98
Cdd:PRK09291   3 KTILITGAGSGFGREVALRLARKGHNVIAGVQIapqvTAL-RAEAARRGLALRVEKLDLTDAIDRAQAAEW--DVDVLLN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   99 NAGISPSlAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSgTASLtwstnpnpqFTPGSGGaaAYR 178
Cdd:PRK09291  80 NAGIGEA-GAVVDIPVELVRELFETNVFGPLELTQGFVRKMVARGKGKVVFTSS-MAGL---------ITGPFTG--AYC 146

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 30267738  179 SSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDLN 215
Cdd:PRK09291 147 ASKHALEAIAEAMHAELKPFGIQVATVNPGPYLTGFN 183
PRK06949 PRK06949
SDR family oxidoreductase;
23-239 1.47e-21

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 90.21  E-value: 1.47e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   23 RTALVTGANKGIGKHIARVLVAEGLTVYVGSR--DRGLGQRA-VEEIGAGARLLVLDVTDLDGI----ARATTQVDRLDV 95
Cdd:PRK06949  10 KVALVTGASSGLGARFAQVLAQAGAKVVLASRrvERLKELRAeIEAEGGAAHVVSLDVTDYQSIkaavAHAETEAGTIDI 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   96 LVNNAGISpSLAPPADTSVEEFRRTYETNVFGV--VA--VTNAFLPALRRSPHP----RIVNISSgTASLtwstNPNPQF 167
Cdd:PRK06949  90 LVNNSGVS-TTQKLVDVTPADFDFVFDTNTRGAffVAqeVAKRMIARAKGAGNTkpggRIINIAS-VAGL----RVLPQI 163

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30267738  168 tpgsggaAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDLNplaaaagDDPAEAAQGAARLALLP 239
Cdd:PRK06949 164 -------GLYCMSKAAVVHMTRAMALEWGRHGINVNAICPGYIDTEIN-------HHHWETEQGQKLVSMLP 221
PRK07035 PRK07035
SDR family oxidoreductase;
23-212 1.68e-21

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 90.08  E-value: 1.68e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   23 RTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEI---GAGARLLVLDVTDLDGIARATTQVD----RLDV 95
Cdd:PRK07035   9 KIALVTGASRGIGEAIAKLLAQQGAHVIVSSRKLDGCQAVADAIvaaGGKAEALACHIGEMEQIDALFAHIRerhgRLDI 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   96 LVNNAGISPSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTAsltwstnpnpqFTPGsGGAA 175
Cdd:PRK07035  89 LVNNAAANPYFGHILDTDLGAFQKTVDVNIRGYFFMSVEAGKLMKEQGGGSIVNVASVNG-----------VSPG-DFQG 156

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 30267738  176 AYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRAT 212
Cdd:PRK07035 157 IYSITKAAVISMTKAFAKECAPFGIRVNALLPGLTDT 193
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
 20-221 1.84e-21

human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup includes human DHRS1 and human HSDL2 and related proteins. These are members of the classical SDR family, with a canonical Gly-rich NAD-binding motif and the typical YXXXK active site motif. However, the rest of the catalytic tetrad is not strongly conserved. DHRS1 mRNA has been detected in many tissues, liver, heart, skeletal muscle, kidney and pancreas; a longer transcript is predominantly expressed in the liver , a shorter one in the heart. HSDL2 may play a part in fatty acid metabolism, as it is found in peroxisomes. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187597 [Multi-domain]  Cd Length: 246  Bit Score: 89.76  E-value: 1.84e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  20 MNDRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQ---------------RAVEEIGAGARLLVLDVTDLDGIA 84
Cdd:cd05338   1 LSGKVAFVTGASRGIGRAIALRLAKAGATVVVAAKTASEGDngsakslpgtieetaEEIEAAGGQALPIVVDVRDEDQVR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  85 RATTQVD----RLDVLVNNAGISpSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTASltws 160
Cdd:cd05338  81 ALVEATVdqfgRLDILVNNAGAI-WLSLVEDTPAKRFDLMQRVNLRGTYLLSQAALPHMVKAGQGHILNISPPLSL---- 155

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30267738 161 tNPNPqftpgsgGAAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPG-----MRATDLNPLAAAA 221
Cdd:cd05338 156 -RPAR-------GDVAYAAGKAGMSRLTLGLAAELRRHGIAVNSLWPStaietPAATELSGGSDPA 213
PRK06138 PRK06138
SDR family oxidoreductase;
20-228 1.96e-21

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 89.83  E-value: 1.96e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   20 MNDRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEIGAG--ARLLVLDVTDLDGIARATTQV----DRL 93
Cdd:PRK06138   3 LAGRVAIVTGAGSGIGRATAKLFAREGARVVVADRDAEAAERVAAAIAAGgrAFARQGDVGSAEAVEALVDFVaarwGRL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   94 DVLVNNAGISpSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTAsltwstnpnpqfTPGSGG 173
Cdd:PRK06138  83 DVLVNNAGFG-CGGTVVTTDEADWDAVMRVNVGGVFLWAKYAIPIMQRQGGGSIVNTASQLA------------LAGGRG 149

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 30267738  174 AAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDLNPLAAAAGDDPAEA 228
Cdd:PRK06138 150 RAAYVASKGAIASLTRAMALDHATDGIRVNAVAPGTIDTPYFRRIFARHADPEAL 204
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
 20-241 2.13e-21

secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; Podophyllum secoisolariciresinol-DH is a homo tetrameric, classical SDR that catalyzes the NAD-dependent conversion of (-)-secoisolariciresinol to (-)-matairesinol via a (-)-lactol intermediate. (-)-Matairesinol is an intermediate to various 8'-lignans, including the cancer-preventive mammalian lignan, and those involved in vascular plant defense. This subgroup also includes rice momilactone A synthase which catalyzes the conversion of 3beta-hydroxy-9betaH-pimara-7,15-dien-19,6beta-olide into momilactone A, Arabidopsis ABA2 which during abscisic acid (ABA) biosynthesis, catalyzes the conversion of xanthoxin to abscisic aldehyde and, maize Tasselseed2 which participate in the maize sex determination pathway. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187587 [Multi-domain]  Cd Length: 249  Bit Score: 89.82  E-value: 2.13e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  20 MNDRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEIGAGARLLV-LDVTDLDGIARAttqVD------- 91
Cdd:cd05326   2 LDGKVAIITGGASGIGEATARLFAKHGARVVIADIDDDAGQAVAAELGDPDISFVhCDVTVEADVRAA---VDtavarfg 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  92 RLDVLVNNAGISPSLAPP-ADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTASLtwstnpnpqftpG 170
Cdd:cd05326  79 RLDIMFNNAGVLGAPCYSiLETSLEEFERVLDVNVYGAFLGTKHAARVMIPAKKGSIVSVASVAGVV------------G 146

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30267738 171 SGGAAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDLnpLAAAAGDDPA---EAAQGAARL---ALLPDD 241
Cdd:cd05326 147 GLGPHAYTASKHAVLGLTRSAATELGEHGIRVNCVSPYGVATPL--LTAGFGVEDEaieEAVRGAANLkgtALRPED 221
PRK07856 PRK07856
SDR family oxidoreductase;
21-241 2.38e-21

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 89.61  E-value: 2.38e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   21 NDRTALVTGANKGIGKHIARVLVAEGLTVYVgsrdrgLGQRAVEEI-GAGARLLVLDVTDLDGIARATTQV----DRLDV 95
Cdd:PRK07856   5 TGRVVLVTGGTRGIGAGIARAFLAAGATVVV------CGRRAPETVdGRPAEFHAADVRDPDQVAALVDAIverhGRLDV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   96 LVNNAGISPSlAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHP-RIVNISSGTAsltwsTNPNPqftpgsgGA 174
Cdd:PRK07856  79 LVNNAGGSPY-ALAAEASPRFHEKIVELNLLAPLLVAQAANAVMQQQPGGgSIVNIGSVSG-----RRPSP-------GT 145

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30267738  175 AAYRSSKAALNALTVLYAQTLAEDgFKVNALAPGMRATDLnpLAAAAGDDPAEAAQGAA----RLAlLPDD 241
Cdd:PRK07856 146 AAYGAAKAGLLNLTRSLAVEWAPK-VRVNAVVVGLVRTEQ--SELHYGDAEGIAAVAATvplgRLA-TPAD 212
PRK06128 PRK06128
SDR family oxidoreductase;
7-227 2.51e-21

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 90.69  E-value: 2.51e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738    7 PWQGAHSQGTVVAMNDRTALVTGANKGIGKHIARVLVAEGLTV---YVGSRDRGLGQ--RAVEEIGAGARLLVLDVTD-- 79
Cdd:PRK06128  40 PDHGEQSYKGFGRLQGRKALITGADSGIGRATAIAFAREGADIalnYLPEEEQDAAEvvQLIQAEGRKAVALPGDLKDea 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   80 --LDGIARATTQVDRLDVLVNNAGISPSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRrsPHPRIVNissgTASL 157
Cdd:PRK06128 120 fcRQLVERAVKELGGLDILVNIAGKQTAVKDIADITTEQFDATFKTNVYAMFWLCKAAIPHLP--PGASIIN----TGSI 193

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  158 TwSTNPNPqftpgsgGAAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDLNPlaaaAGDDPAE 227
Cdd:PRK06128 194 Q-SYQPSP-------TLLDYASTKAAIVAFTKALAKQVAEKGIRVNAVAPGPVWTPLQP----SGGQPPE 251
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
 24-241 2.92e-21

classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187604 [Multi-domain]  Cd Length: 249  Bit Score: 89.26  E-value: 2.92e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  24 TALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEIGAGARLLV----LDVTDLDGIARATTQV----DRLDV 95
Cdd:cd05346   2 TVLITGASSGIGEATARRFAKAGAKLILTGRRAERLQELADELGAKFPVKVlplqLDVSDRESIEAALENLpeefRDIDI 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  96 LVNNAGISPSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTASLTWStnpnpqftpgsgGAA 175
Cdd:cd05346  82 LVNNAGLALGLDPAQEADLEDWETMIDTNVKGLLNVTRLILPIMIARNQGHIINLGSIAGRYPYA------------GGN 149

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30267738 176 AYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDLNpLAAAAGDDPAEAAQGAARLALLPDD 241
Cdd:cd05346 150 VYCATKAAVRQFSLNLRKDLIGTGIRVTNIEPGLVETEFS-LVRFHGDKEKADKVYEGVEPLTPED 214
PRK07454 PRK07454
SDR family oxidoreductase;
23-239 3.46e-21

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 88.86  E-value: 3.46e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   23 RTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEI---GAGARLLVLDVTDLD----GIARATTQVDRLDV 95
Cdd:PRK07454   7 PRALITGASSGIGKATALAFAKAGWDLALVARSQDALEALAAELrstGVKAAAYSIDLSNPEaiapGIAELLEQFGCPDV 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   96 LVNNAGISPSlAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTASltwstNPNPQFtpgsggaA 175
Cdd:PRK07454  87 LINNAGMAYT-GPLLEMPLSDWQWVIQLNLTSVFQCCSAVLPGMRARGGGLIINVSSIAAR-----NAFPQW-------G 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30267738  176 AYRSSKAALNALTvlyaQTLAED----GFKVNALAPGMRATDLNPLAAAAGD-------DPAEAAQGAARLALLP 239
Cdd:PRK07454 154 AYCVSKAALAAFT----KCLAEEershGIRVCTITLGAVNTPLWDTETVQADfdrsamlSPEQVAQTILHLAQLP 224
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
23-251 3.62e-21

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 89.47  E-value: 3.62e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   23 RTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEIGAGARL--LVLDVTDLDGIARATTQVD----RLDVL 96
Cdd:PRK08226   7 KTALITGALQGIGEGIARVFARHGANLILLDISPEIEKLADELCGRGHRCtaVVADVRDPASVAAAIKRAKekegRIDIL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   97 VNNAGISpSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTASLTwstnpnpqftpGSGGAAA 176
Cdd:PRK08226  87 VNNAGVC-RLGSFLDMSDEDRDFHIDINIKGVWNVTKAVLPEMIARKDGRIVMMSSVTGDMV-----------ADPGETA 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  177 YRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATdlnPLAAAAG-----DDPAEAAQGAA------RLALLPDDGPTG 245
Cdd:PRK08226 155 YALTKAAIVGLTKSLAVEYAQSGIRVNAICPGYVRT---PMAESIArqsnpEDPESVLTEMAkaiplrRLADPLEVGELA 231


                 ....*.
gi 30267738  246 GFFSWD 251
Cdd:PRK08226 232 AFLASD 237
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
 20-213 4.99e-21

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 88.75  E-value: 4.99e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   20 MNDRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEI---GAGARLLVLDVT---DLDGIARAT-TQVDR 92
Cdd:PRK06113   9 LDGKCAIITGAGAGIGKEIAITFATAGASVVVSDINADAANHVVDEIqqlGGQAFACRCDITseqELSALADFAlSKLGK 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   93 LDVLVNNAGispSLAP-PADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTASltwSTNPNpqftpgs 171
Cdd:PRK06113  89 VDILVNNAG---GGGPkPFDMPMADFRRAYELNVFSFFHLSQLVAPEMEKNGGGVILTITSMAAE---NKNIN------- 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 30267738  172 ggAAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATD 213
Cdd:PRK06113 156 --MTSYASSKAAASHLVRNMAFDLGEKNIRVNGIAPGAILTD 195
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
 20-214 5.16e-21

2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 88.79  E-value: 5.16e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   20 MNDRTALVTGANKGIGKHIARVLVAEGLTVYvgsrdrGLGQRAVEEIGAGARLLVLDVTDLDGIARATTQVD----RLDV 95
Cdd:PRK08220   6 FSGKTVWVTGAAQGIGYAVALAFVEAGAKVI------GFDQAFLTQEDYPFATFVLDVSDAAAVAQVCQRLLaetgPLDV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   96 LVNNAGISpSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTASltwstnpnpqfTPGSgGAA 175
Cdd:PRK08220  80 LVNAAGIL-RMGATDSLSDEDWQQTFAVNAGGAFNLFRAVMPQFRRQRSGAIVTVGSNAAH-----------VPRI-GMA 146

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 30267738  176 AYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDL 214
Cdd:PRK08220 147 AYGASKAALTSLAKCVGLELAPYGVRCNVVSPGSTDTDM 185
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
 22-214 6.58e-21

mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes the conversion of fructose to mannitol, an acyclic 6-carbon sugar. MDH is a tetrameric member of the SDR family. This subgroup also includes various other tetrameric SDRs, including Pichia stipitis D-arabinitol dehydrogenase (aka polyol dehydrogenase), Candida albicans Sou1p, a sorbose reductase, and Candida parapsilosis (S)-specific carbonyl reductase (SCR, aka S-specific alcohol dehydrogenase) which catalyzes the enantioselective reduction of 2-hydroxyacetophenone into (S)-1-phenyl-1,2-ethanediol. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser).


Pssm-ID: 187610 [Multi-domain]  Cd Length: 252  Bit Score: 88.54  E-value: 6.58e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  22 DRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEI----GAGARLLVLDVTDLDGIARATTQVD----RL 93
Cdd:cd05352   8 GKVAIVTGGSRGIGLAIARALAEAGADVAIIYNSAPRAEEKAEELakkyGVKTKAYKCDVSSQESVEKTFKQIQkdfgKI 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  94 DVLVNNAGISpsLAPPA-DTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTASLTwsTNPNPQftpgsg 172
Cdd:cd05352  88 DILIANAGIT--VHKPAlDYTYEQWNKVIDVNLNGVFNCAQAAAKIFKKQGKGSLIITASMSGTIV--NRPQPQ------ 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 30267738 173 gaAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDL 214
Cdd:cd05352 158 --AAYNASKAAVIHLAKSLAVEWAKYFIRVNSISPGYIDTDL 197
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
 25-214 6.97e-21

2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 dihydrozybenzoate dehydrogenase shares the characteristics of the classical SDRs. This subgroup includes Escherichai coli EntA which catalyzes the NAD+-dependent oxidation of 2,3-dihydro-2,3-dihydroxybenzoate to 2,3-dihydroxybenzoate during biosynthesis of the siderophore Enterobactin. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187592 [Multi-domain]  Cd Length: 244  Bit Score: 88.30  E-value: 6.97e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  25 ALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLgqraVEEIGAGARLLVLDVTDLDGIA----RATTQVDRLDVLVNNA 100
Cdd:cd05331   1 VIVTGAAQGIGRAVARHLLQAGATVIALDLPFVL----LLEYGDPLRLTPLDVADAAAVRevcsRLLAEHGPIDALVNCA 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738 101 GISpSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTASltwstnpnpqfTPGSGgAAAYRSS 180
Cdd:cd05331  77 GVL-RPGATDPLSTEDWEQTFAVNVTGVFNLLQAVAPHMKDRRTGAIVTVASNAAH-----------VPRIS-MAAYGAS 143

                       170       180       190
                ....*....|....*....|....*....|....
gi 30267738 181 KAALNALTVLYAQTLAEDGFKVNALAPGMRATDL 214
Cdd:cd05331 144 KAALASLSKCLGLELAPYGVRCNVVSPGSTDTAM 177
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
23-214 7.77e-21

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 88.20  E-value: 7.77e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   23 RTALVTGANKGIGKHIARVLVAEGLTVYVGSR-DRGLGQRAVEEIGAGARLLVLDVTDLDGIARATTQVDR---LD---- 94
Cdd:PRK06924   2 RYVIITGTSQGLGEAIANQLLEKGTHVISISRtENKELTKLAEQYNSNLTFHSLDLQDVHELETNFNEILSsiqEDnvss 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   95 -VLVNNAGISPSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALR-RSPHPRIVNISSGTASltwstnpNPQFtpgsg 172
Cdd:PRK06924  82 iHLINNAGMVAPIKPIEKAESEELITNVHLNLLAPMILTSTFMKHTKdWKVDKRVINISSGAAK-------NPYF----- 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 30267738  173 GAAAYRSSKAALNALT--VLYAQTLAEDGFKVNALAPGMRATDL 214
Cdd:PRK06924 150 GWSAYCSSKAGLDMFTqtVATEQEEEEYPVKIVAFSPGVMDTNM 193
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
 23-213 8.59e-21

putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) SDR; This subgroup includes Rhizobium sp. NGR234 FabG1. The Escherichai coli K12 BKR, FabG, belongs to a different subgroup. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187607 [Multi-domain]  Cd Length: 246  Bit Score: 87.90  E-value: 8.59e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  23 RTALVTGANKGIGKHIARVLVAEGLTVYVG-SRDRGLGQRAVEEIGAGARLLVLDVTDLD----GIARATTQVDRLDVLV 97
Cdd:cd05349   1 QVVLVTGASRGLGAAIARSFAREGARVVVNyYRSTESAEAVAAEAGERAIAIQADVRDRDqvqaMIEEAKNHFGPVDTIV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  98 NNAGI----SPSLAPPADT-SVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTASltwstNPNPQFtpgsg 172
Cdd:cd05349  81 NNALIdfpfDPDQRKTFDTiDWEDYQQQLEGAVKGALNLLQAVLPDFKERGSGRVINIGTNLFQ-----NPVVPY----- 150

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 30267738 173 gaAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPG-MRATD 213
Cdd:cd05349 151 --HDYTTAKAALLGFTRNMAKELGPYGITVNMVSGGlLKVTD 190
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
 23-208 8.60e-21

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 88.08  E-value: 8.60e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   23 RTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEI---GAGARLLVLDVTDLDGIARATTQV----DRLDV 95
Cdd:PRK08213  13 KTALVTGGSRGLGLQIAEALGEAGARVVLSARKAEELEEAAAHLealGIDALWIAADVADEADIERLAEETlerfGHVDI 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   96 LVNNAGISPSlAPPADTSVEEFRRTYETNVFGVVAVTNAflpALRRSPHPR----IVNISSgTASLtwstNPNPqftPGS 171
Cdd:PRK08213  93 LVNNAGATWG-APAEDHPVEAWDKVMNLNVRGLFLLSQA---VAKRSMIPRgygrIINVAS-VAGL----GGNP---PEV 160

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 30267738  172 GGAAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPG 208
Cdd:PRK08213 161 MDTIAYNTSKGAVINFTRALAAEWGPHGIRVNAIAPG 197
PRK06196 PRK06196
oxidoreductase; Provisional
 10-214 8.83e-21

oxidoreductase; Provisional


Pssm-ID: 235736 [Multi-domain]  Cd Length: 315  Bit Score: 89.36  E-value: 8.83e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   10 GAHSQ-GTVVAMND---RTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEIgAGARLLVLDVTDLDGIAR 85
Cdd:PRK06196  10 GAASTaEEVLAGHDlsgKTAIVTGGYSGLGLETTRALAQAGAHVIVPARRPDVAREALAGI-DGVEVVMLDLADLESVRA 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   86 ATTQV----DRLDVLVNNAGIspsLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTASLTWST 161
Cdd:PRK06196  89 FAERFldsgRRIDILINNAGV---MACPETRVGDGWEAQFATNHLGHFALVNLLWPALAAGAGARVVALSSAGHRRSPIR 165

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 30267738  162 NPNPQFTPGSGGAAAYRSSKAAlNALTVLYAQTL-AEDGFKVNALAPGMRATDL 214
Cdd:PRK06196 166 WDDPHFTRGYDKWLAYGQSKTA-NALFAVHLDKLgKDQGVRAFSVHPGGILTPL 218
PRK12743 PRK12743
SDR family oxidoreductase;
22-227 1.01e-20

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 88.17  E-value: 1.01e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   22 DRTALVTGANKGIGKHIARVLVAEGLTVYVG-SRDRGLGQRAVEEI-GAGARLLV--LDVTDLDGIARATTQV----DRL 93
Cdd:PRK12743   2 AQVAIVTASDSGIGKACALLLAQQGFDIGITwHSDEEGAKETAEEVrSHGVRAEIrqLDLSDLPEGAQALDKLiqrlGRI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   94 DVLVNNAGISpSLAPPADTSVEEFRRTYETNVFGvvavtnAFLPALRRSPH-------PRIVNISSGTasltwstnpnpQ 166
Cdd:PRK12743  82 DVLVNNAGAM-TKAPFLDMDFDEWRKIFTVDVDG------AFLCSQIAARHmvkqgqgGRIINITSVH-----------E 143

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30267738  167 FTPgSGGAAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATdlnPLAAAAGDDPAE 227
Cdd:PRK12743 144 HTP-LPGASAYTAAKHALGGLTKAMALELVEHGILVNAVAPGAIAT---PMNGMDDSDVKP 200
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
 22-237 1.04e-20

xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins identified as L-xylulose reductase (XR) and carbonyl reductase; they are members of the SDR family. XR, catalyzes the NADP-dependent reduction of L-xyulose and other sugars. Tetrameric mouse carbonyl reductase is involved in the metabolism of biogenic and xenobiotic carbonyl compounds. This subgroup also includes tetrameric chicken liver D-erythrulose reductase, which catalyzes the reduction of D-erythrulose to D-threitol. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser).


Pssm-ID: 187609 [Multi-domain]  Cd Length: 244  Bit Score: 87.91  E-value: 1.04e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  22 DRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEIgAGARLLVLDVTDLDGIARATTQVDRLDVLVNNAG 101
Cdd:cd05351   7 GKRALVTGAGKGIGRATVKALAKAGARVVAVSRTQADLDSLVREC-PGIEPVCVDLSDWDATEEALGSVGPVDLLVNNAA 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738 102 ISpSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHP-RIVNISSGTASLTWstnpnpqftpgsGGAAAYRSS 180
Cdd:cd05351  86 VA-ILQPFLEVTKEAFDRSFDVNVRAVIHVSQIVARGMIARGVPgSIVNVSSQASQRAL------------TNHTVYCST 152

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 30267738 181 KAALNALTVLYAQTLAEDGFKVNALAPGMRATDlnpLAAAAGDDPAEAAQGAARLAL 237
Cdd:cd05351 153 KAALDMLTKVMALELGPHKIRVNSVNPTVVMTD---MGRDNWSDPEKAKKMLNRIPL 206
PRK05875 PRK05875
short chain dehydrogenase; Provisional
 19-233 1.09e-20

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 88.32  E-value: 1.09e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   19 AMNDRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEIGAGA-----RLLVLDVTDLDGIAR----ATTQ 89
Cdd:PRK05875   4 SFQDRTYLVTGGGSGIGKGVAAGLVAAGAAVMIVGRNPDKLAAAAEEIEALKgagavRYEPADVTDEDQVARavdaATAW 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   90 VDRLDVLVNNAGISPSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTASltwstNPNPQFtp 169
Cdd:PRK05875  84 HGRLHGVVHCAGGSETIGPITQIDSDAWRRTVDLNVNGTMYVLKHAARELVRGGGGSFVGISSIAAS-----NTHRWF-- 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30267738  170 gsggaAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDlnpLAAAAGDDPAEAAQGAA 233
Cdd:PRK05875 157 -----GAYGVTKSAVDHLMKLAADELGPSWVRVNSIRPGLIRTD---LVAPITESPELSADYRA 212
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
 23-229 1.41e-20

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 87.52  E-value: 1.41e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   23 RTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEIGAG---ARLLVLDVTDLD----GIARATTQVDRLDV 95
Cdd:PRK07523  11 RRALVTGSSQGIGYALAEGLAQAGAEVILNGRDPAKLAAAAESLKGQglsAHALAFDVTDHDavraAIDAFEAEIGPIDI 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   96 LVNNAGISPSlAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTASLtwstnpnpqftpGSGGAA 175
Cdd:PRK07523  91 LVNNAGMQFR-TPLEDFPADAFERLLRTNISSVFYVGQAVARHMIARGAGKIINIASVQSAL------------ARPGIA 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 30267738  176 AYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATdlnPLAAAAGDDPAEAA 229
Cdd:PRK07523 158 PYTATKGAVGNLTKGMATDWAKHGLQCNAIAPGYFDT---PLNAALVADPEFSA 208
PRK06057 PRK06057
short chain dehydrogenase; Provisional
 22-239 1.69e-20

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 87.48  E-value: 1.69e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   22 DRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEIGAgarLLV-LDVTDLDGI----ARATTQVDRLDVL 96
Cdd:PRK06057   7 GRVAVITGGGSGIGLATARRLAAEGATVVVGDIDPEAGKAAADEVGG---LFVpTDVTDEDAVnalfDTAAETYGSVDIA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   97 VNNAGISpslaPPADTSVEE-----FRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTASLTWSTNpnpqftpgs 171
Cdd:PRK06057  84 FNNAGIS----PPEDDSILNtgldaWQRVQDVNLTSVYLCCKAALPHMVRQGKGSIINTASFVAVMGSATS--------- 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30267738  172 ggAAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDLnpLAAAAGDDPAEAAQgaaRLALLP 239
Cdd:PRK06057 151 --QISYTASKGGVLAMSRELGVQFARQGIRVNALCPGPVNTPL--LQELFAKDPERAAR---RLVHVP 211
PRK05855 PRK05855
SDR family oxidoreductase;
22-235 2.30e-20

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 89.65  E-value: 2.30e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   22 DRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEI---GAGARLLVLDVTDLDGIARATTQV-DRL---D 94
Cdd:PRK05855 315 GKLVVVTGAGSGIGRETALAFAREGAEVVASDIDEAAAERTAELIraaGAVAHAYRVDVSDADAMEAFAEWVrAEHgvpD 394

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   95 VLVNNAGISPSlAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALR-RSPHPRIVNISSGTAsltwstnpnpqFTPgSGG 173
Cdd:PRK05855 395 IVVNNAGIGMA-GGFLDTSAEDWDRVLDVNLWGVIHGCRLFGRQMVeRGTGGHIVNVASAAA-----------YAP-SRS 461

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30267738  174 AAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDLNPLAAAAGDDPAEAAQGAARL 235
Cdd:PRK05855 462 LPAYATSKAAVLMLSECLRAELAAAGIGVTAICPGFVDTNIVATTRFAGADAEDEARRRGRA 523
PRK06484 PRK06484
short chain dehydrogenase; Validated
 23-236 4.18e-20

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 89.14  E-value: 4.18e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   23 RTALVTGANKGIGKHIARVLVAEGLTVYVGSRDrGLGQRAVEEIGAGARLLV-LDVTDLDGI----ARATTQVDRLDVLV 97
Cdd:PRK06484 270 RVVAITGGARGIGRAVADRFAAAGDRLLIIDRD-AEGAKKLAEALGDEHLSVqADITDEAAVesafAQIQARWGRLDVLV 348

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   98 NNAGISPSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSphPRIVNISSGTASLTWStnpnpqftpgsgGAAAY 177
Cdd:PRK06484 349 NNAGIAEVFKPSLEQSAEDFTRVYDVNLSGAFACARAAARLMSQG--GVIVNLGSIASLLALP------------PRNAY 414

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30267738  178 RSSKAALNALTVLYAQTLAEDGFKVNALAPG-MRATDLNPLAAAAG---------------DDPAEAAQGAARLA 236
Cdd:PRK06484 415 CASKAAVTMLSRSLACEWAPAGIRVNTVAPGyIETPAVLALKASGRadfdsirrriplgrlGDPEEVAEAIAFLA 489
PRK06947 PRK06947
SDR family oxidoreductase;
23-233 4.43e-20

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 86.01  E-value: 4.43e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   23 RTALVTGANKGIGKHIARVLVAEGLTVYVG-SRDRGLGQRAVEEIG-AGARLLVL--DVT-DLDGIA---RATTQVDRLD 94
Cdd:PRK06947   3 KVVLITGASRGIGRATAVLAAARGWSVGINyARDAAAAEETADAVRaAGGRACVVagDVAnEADVIAmfdAVQSAFGRLD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   95 VLVNNAGISPSLAPPADTSVEEFRRTYETNVFGvvavtnAFL---PALRRSPHPR------IVNISSGTASLtwsTNPNP 165
Cdd:PRK06947  83 ALVNNAGIVAPSMPLADMDAARLRRMFDTNVLG------AYLcarEAARRLSTDRggrggaIVNVSSIASRL---GSPNE 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30267738  166 QFTpgsggaaaYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDLNplaaAAGDDPAEAAQ-GAA 233
Cdd:PRK06947 154 YVD--------YAGSKGAVDTLTLGLAKELGPHGVRVNAVRPGLIETEIH----ASGGQPGRAARlGAQ 210
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 20-215 5.39e-20

putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes the NAD-dependent interconversion of D-mannonate and D-fructuronate. This subgroup includes Bacillus subtitils UxuB/YjmF, a putative D-mannonate oxidoreductase; the B. subtilis UxuB gene is part of a putative ten-gene operon (the Yjm operon) involved in hexuronate catabolism. Escherichia coli UxuB does not belong to this subgroup. This subgroup has a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187640 [Multi-domain]  Cd Length: 271  Bit Score: 86.36  E-value: 5.39e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  20 MNDRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEI---GAGARLLVLDVTDLDGIARA----TTQVDR 92
Cdd:cd08935   3 LKNKVAVITGGTGVLGGAMARALAQAGAKVAALGRNQEKGDKVAKEItalGGRAIALAADVLDRASLERAreeiVAQFGT 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  93 LDVLVNNAGispSLAPPADTSVEEFRRTYETNVF-----GVVAVTN-----AFLPA------LRRSPHPRIVNISSGTAs 156
Cdd:cd08935  83 VDILINGAG---GNHPDATTDPEHYEPETEQNFFdldeeGWEFVFDlnlngSFLPSqvfgkdMLEQKGGSIINISSMNA- 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 30267738 157 ltwstnpnpqFTPgSGGAAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDLN 215
Cdd:cd08935 159 ----------FSP-LTKVPAYSAAKAAVSNFTQWLAVEFATTGVRVNAIAPGFFVTPQN 206
PRK05872 PRK05872
short chain dehydrogenase; Provisional
 20-239 5.76e-20

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 86.56  E-value: 5.76e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   20 MNDRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEIGAGARLL--VLDVTDLDGIARATTQVD----RL 93
Cdd:PRK05872   7 LAGKVVVVTGAARGIGAELARRLHARGAKLALVDLEEAELAALAAELGGDDRVLtvVADVTDLAAMQAAAEEAVerfgGI 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   94 DVLVNNAGISPSlAPPADTSVEEFRRTYETNVFGVVAVTNAFLPAL-RRSPHprIVNISSGTAsltwstnpnpqFTPGSG 172
Cdd:PRK05872  87 DVVVANAGIASG-GSVAQVDPDAFRRVIDVNLLGVFHTVRATLPALiERRGY--VLQVSSLAA-----------FAAAPG 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30267738  173 GaAAYRSSKAALNAltvlYAQTL----AEDGFKVNALAPGMRATDLnpLAAAAGDDPAeaaqGAARLALLP 239
Cdd:PRK05872 153 M-AAYCASKAGVEA----FANALrlevAHHGVTVGSAYLSWIDTDL--VRDADADLPA----FRELRARLP 212
PRK08267 PRK08267
SDR family oxidoreductase;
26-241 7.78e-20

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 85.76  E-value: 7.78e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   26 LVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEIGAG-ARLLVLDVTD-------LDGIARATTQvdRLDVLV 97
Cdd:PRK08267   5 FITGAASGIGRATALLFAAEGWRVGAYDINEAGLAALAAELGAGnAWTGALDVTDraawdaaLADFAAATGG--RLDVLF 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   98 NNAGIsPSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTAsltwstnpnpqfTPGSGGAAAY 177
Cdd:PRK08267  83 NNAGI-LRGGPFEDIPLEAHDRVIDINVKGVLNGAHAALPYLKATPGARVINTSSASA------------IYGQPGLAVY 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30267738  178 RSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATdlnPLAAAAGDDPAEAAQGAARLALLPDD 241
Cdd:PRK08267 150 SATKFAVRGLTEALDLEWRRHGIRVADVMPLFVDT---AMLDGTSNEVDAGSTKRLGVRLTPED 210
PRK06172 PRK06172
SDR family oxidoreductase;
22-233 9.08e-20

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 85.57  E-value: 9.08e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   22 DRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQ---RAVEEIGAGARLLVLDVT-DLDG---IARATTQVDRLD 94
Cdd:PRK06172   7 GKVALVTGGAAGIGRATALAFAREGAKVVVADRDAAGGEetvALIREAGGEALFVACDVTrDAEVkalVEQTIAAYGRLD 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   95 VLVNNAGISPSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGtASLTwstnpnpqftpGSGGA 174
Cdd:PRK06172  87 YAFNNAGIEIEQGRLAEGSEAEFDAIMGVNVKGVWLCMKYQIPLMLAQGGGAIVNTASV-AGLG-----------AAPKM 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 30267738  175 AAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDLnpLAAAAGDDPAEAAQGAA 233
Cdd:PRK06172 155 SIYAASKHAVIGLTKSAAIEYAKKGIRVNAVCPAVIDTDM--FRRAYEADPRKAEFAAA 211
PRK06125 PRK06125
short chain dehydrogenase; Provisional
 20-213 1.21e-19

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 85.10  E-value: 1.21e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   20 MNDRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEI----GAGARLLVLDVTDLDGIARATTQVDRLDV 95
Cdd:PRK06125   5 LAGKRVLITGASKGIGAAAAEAFAAEGCHLHLVARDADALEALAADLraahGVDVAVHALDLSSPEAREQLAAEAGDIDI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   96 LVNNAGISPSlAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTASltwstNPNPQFTPGSGGaa 175
Cdd:PRK06125  85 LVNNAGAIPG-GGLDDVDDAAWRAGWELKVFGYIDLTRLAYPRMKARGSGVIVNVIGAAGE-----NPDADYICGSAG-- 156

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 30267738  176 ayrssKAALNALT-VLYAQTLaEDGFKVNALAPGMRATD 213
Cdd:PRK06125 157 -----NAALMAFTrALGGKSL-DDGVRVVGVNPGPVATD 189
PRK07069 PRK07069
short chain dehydrogenase; Validated
 25-228 1.79e-19

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 84.38  E-value: 1.79e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   25 ALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAV-EEIGAG-----ARLLVLDVTD----LDGIARATTQVDRLD 94
Cdd:PRK07069   2 AFITGAAGGLGRAIARRMAEQGAKVFLTDINDAAGLDAFaAEINAAhgegvAFAAVQDVTDeaqwQALLAQAADAMGGLS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   95 VLVNNAGISpSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTASLTwstnpNPQFTpgsgga 174
Cdd:PRK07069  82 VLVNNAGVG-SFGAIEQIELDEWRRVMAINVESIFLGCKHALPYLRASQPASIVNISSVAAFKA-----EPDYT------ 149

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 30267738  175 aAYRSSKAALNALTVLYAQTLAEDGFKV--NALAPG-MRATDLNPLAAAAGDDPAEA 228
Cdd:PRK07069 150 -AYNASKAAVASLTKSIALDCARRGLDVrcNSIHPTfIRTGIVDPIFQRLGEEEATR 205
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
 23-208 2.10e-19

pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR family, catalyzes the NAD-dependent reduction of folic acid, dihydrofolate and related compounds. In Leishmania, pteridine reductase (PTR1) acts to circumvent the anti-protozoan drugs that attack dihydrofolate reductase activity. Proteins in this subgroup have an N-terminal NAD-binding motif and a YxxxK active site motif, but have an Asp instead of the usual upstream catalytic Ser. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187615 [Multi-domain]  Cd Length: 234  Bit Score: 83.87  E-value: 2.10e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  23 RTALVTGANKGIGKHIARVLVAEGLTVYVGSRD-RGLGQRA---VEEIGAGARLLVLDVTDLDG----IARATTQVDRLD 94
Cdd:cd05357   1 AVALVTGAAKRIGRAIAEALAAEGYRVVVHYNRsEAEAQRLkdeLNALRNSAVLVQADLSDFAAcadlVAAAFRAFGRCD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  95 VLVNNAGISPsLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTASLtwstnPNPQFTpgsgga 174
Cdd:cd05357  81 VLVNNASAFY-PTPLGQGSEDAWAELFGINLKAPYLLIQAFARRLAGSRNGSIINIIDAMTDR-----PLTGYF------ 148

                       170       180       190
                ....*....|....*....|....*....|....
gi 30267738 175 aAYRSSKAALNALTVLYAQTLAEDgFKVNALAPG 208
Cdd:cd05357 149 -AYCMSKAALEGLTRSAALELAPN-IRVNGIAPG 180
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
 23-152 3.39e-19

human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, classical (c) SDRs; 17beta-hydroxysteroid dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. This classical SDR subgroup includes human type 1 17beta-HSD, human retinol dehydrogenase 8, zebrafish photoreceptor associated retinol dehydrogenase type 2, and a chicken ovary-specific 17beta-hydroxysteroid dehydrogenase. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187666 [Multi-domain]  Cd Length: 258  Bit Score: 84.05  E-value: 3.39e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  23 RTALVTGANKGIGKHIARVLVAEG---LTVYVGSRDRGLGQRAVEEIGAGA----RLLVLDVTDLDGIARATTQV--DRL 93
Cdd:cd09806   1 TVVLITGCSSGIGLHLAVRLASDPskrFKVYATMRDLKKKGRLWEAAGALAggtlETLQLDVCDSKSVAAAVERVteRHV 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 30267738  94 DVLVNNAGISpSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISS 152
Cdd:cd09806  81 DVLVCNAGVG-LLGPLEALSEDAMASVFDVNVFGTVRMLQAFLPDMKRRGSGRILVTSS 138
PRK05867 PRK05867
SDR family oxidoreductase;
20-218 3.90e-19

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 83.55  E-value: 3.90e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   20 MNDRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEI---GAGARLLVLDVTDLDGIA----RATTQVDR 92
Cdd:PRK05867   7 LHGKRALITGASTGIGKRVALAYVEAGAQVAIAARHLDALEKLADEIgtsGGKVVPVCCDVSQHQQVTsmldQVTAELGG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   93 LDVLVNNAGISpSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPAL-RRSPHPRIVNissgTASLTWSTNPNPQftpgs 171
Cdd:PRK05867  87 IDIAVCNAGII-TVTPMLDMPLEEFQRLQNTNVTGVFLTAQAAAKAMvKQGQGGVIIN----TASMSGHIINVPQ----- 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 30267738  172 gGAAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDL-NPLA 218
Cdd:PRK05867 157 -QVSHYCASKAAVIHLTKAMAVELAPHKIRVNSVSPGYILTELvEPYT 203
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
 21-249 4.28e-19

d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, catalyzes the interconversion of D-3-hydroxybutyrate and acetoacetate. It is a classical SDR, with the canonical NAD-binding motif and active site tetrad. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187644 [Multi-domain]  Cd Length: 258  Bit Score: 83.65  E-value: 4.28e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  21 NDRTALVTGANKGIGKHIARVLVAEGLTVYVG-----SRDRGLGQRAVEEIGAGARLLVLDVTDL----DGIARATTQVD 91
Cdd:cd08940   1 KGKVALVTGSTSGIGLGIARALAAAGANIVLNgfgdaAEIEAVRAGLAAKHGVKVLYHGADLSKPaaieDMVAYAQRQFG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  92 RLDVLVNNAGISpSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTASLtwstnpnpqftpGS 171
Cdd:cd08940  81 GVDILVNNAGIQ-HVAPIEDFPTEKWDAIIALNLSAVFHTTRLALPHMKKQGWGRIINIASVHGLV------------AS 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738 172 GGAAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDL-----NPLAAAAGDDPAEAAQgaarlALLPDDGPTGG 246
Cdd:cd08940 148 ANKSAYVAAKHGVVGLTKVVALETAGTGVTCNAICPGWVLTPLvekqiSALAQKNGVPQEQAAR-----ELLLEKQPSKQ 222


                ...
gi 30267738 247 FFS 249
Cdd:cd08940 223 FVT 225
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
 21-215 5.32e-19

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 83.80  E-value: 5.32e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   21 NDRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEIGAG---ARLLVLDVTDLDGIARATTQV----DRL 93
Cdd:PRK08277   9 KGKVAVITGGGGVLGGAMAKELARAGAKVAILDRNQEKAEAVVAEIKAAggeALAVKADVLDKESLEQARQQIledfGPC 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   94 DVLVNNAG----------ISPSLAPPADT----SVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTAsltw 159
Cdd:PRK08277  89 DILINGAGgnhpkattdnEFHELIEPTKTffdlDEEGFEFVFDLNLLGTLLPTQVFAKDMVGRKGGNIINISSMNA---- 164

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 30267738  160 stnpnpqFTPGSGgAAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDLN 215
Cdd:PRK08277 165 -------FTPLTK-VPAYSAAKAAISNFTQWLAVHFAKVGIRVNAIAPGFFLTEQN 212
PRK08278 PRK08278
SDR family oxidoreductase;
20-207 5.45e-19

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 83.80  E-value: 5.45e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   20 MNDRTALVTGANKGIGKHIARVLVAEGL-----------------TVYVGSRDrglgqraVEEIGAGARLLVLDVTDLDG 82
Cdd:PRK08278   4 LSGKTLFITGASRGIGLAIALRAARDGAniviaaktaephpklpgTIHTAAEE-------IEAAGGQALPLVGDVRDEDQ 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   83 IARATTQ-VDR---LDVLVNNAGiSPSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSgtaslt 158
Cdd:PRK08278  77 VAAAVAKaVERfggIDICVNNAS-AINLTGTEDTPMKRFDLMQQINVRGTFLVSQACLPHLKKSENPHILTLSP------ 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 30267738  159 wSTNPNPQFTPGSggaAAYRSSKAALNALTVLYAQTLAEDGFKVNALAP 207
Cdd:PRK08278 150 -PLNLDPKWFAPH---TAYTMAKYGMSLCTLGLAEEFRDDGIAVNALWP 194
PRK07985 PRK07985
SDR family oxidoreductase;
20-208 5.53e-19

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 83.89  E-value: 5.53e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   20 MNDRTALVTGANKGIGKHIARVLVAEGLTVYVG-----SRDRGLGQRAVEEIGAGARLLVLDVTD----LDGIARATTQV 90
Cdd:PRK07985  47 LKDRKALVTGGDSGIGRAAAIAYAREGADVAISylpveEEDAQDVKKIIEECGRKAVLLPGDLSDekfaRSLVHEAHKAL 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   91 DRLDVLVNNAGISPSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRrsPHPRIVNISSGTAsltwsTNPNPQFTPg 170
Cdd:PRK07985 127 GGLDIMALVAGKQVAIPDIADLTSEQFQKTFAINVFALFWLTQEAIPLLP--KGASIITTSSIQA-----YQPSPHLLD- 198

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 30267738  171 sggaaaYRSSKAALNALTVLYAQTLAEDGFKVNALAPG 208
Cdd:PRK07985 199 ------YAATKAAILNYSRGLAKQVAEKGIRVNIVAPG 230
PRK12746 PRK12746
SDR family oxidoreductase;
20-225 6.95e-19

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 83.16  E-value: 6.95e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   20 MNDRTALVTGANKGIGKHIARVLVAEGLTVYVG-SRDRGLGQRAVEEI---GAGARLLVLDVTDLDGIARATTQV----- 90
Cdd:PRK12746   4 LDGKVALVTGASRGIGRAIAMRLANDGALVAIHyGRNKQAADETIREIesnGGKAFLIEADLNSIDGVKKLVEQLknelq 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   91 -----DRLDVLVNNAGISpSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRrsPHPRIVNISSGTASLtwstnpnp 165
Cdd:PRK12746  84 irvgtSEIDILVNNAGIG-TQGTIENTTEEIFDEIMAVNIKAPFFLIQQTLPLLR--AEGRVINISSAEVRL-------- 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  166 qftpGSGGAAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDLNplaAAAGDDP 225
Cdd:PRK12746 153 ----GFTGSIAYGLSKGALNTMTLPLAKHLGERGITVNTIMPGYTKTDIN---AKLLDDP 205
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
 20-214 7.12e-19

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 83.14  E-value: 7.12e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   20 MNDRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGlgqravEEIGAGARLLVLDVTDLD----GIARATTQVDRLDV 95
Cdd:PRK06171   7 LQGKIIIVTGGSSGIGLAIVKELLANGANVVNADIHGG------DGQHENYQFVPTDVSSAEevnhTVAEIIEKFGRIDG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   96 LVNNAGI-SPSL-------APPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSgTASLTwstnpnpqf 167
Cdd:PRK06171  81 LVNNAGInIPRLlvdekdpAGKYELNEAAFDKMFNINQKGVFLMSQAVARQMVKQHDGVIVNMSS-EAGLE--------- 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 30267738  168 tpGSGGAAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPG-MRATDL 214
Cdd:PRK06171 151 --GSEGQSCYAATKAALNSFTRSWAKELGKHNIRVVGVAPGiLEATGL 196
PRK07201 PRK07201
SDR family oxidoreductase;
12-199 7.23e-19

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 85.39  E-value: 7.23e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   12 HSQGTVVAmndRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEI---GAGARLLVLDVTDLDGIARATT 88
Cdd:PRK07201 364 DLRGPLVG---KVVLITGASSGIGRATAIKVAEAGATVFLVARNGEALDELVAEIrakGGTAHAYTCDLTDSAAVDHTVK 440

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   89 QV----DRLDVLVNNAG--ISPSLAPPADTSvEEFRRTYETNVFGVVAVTNAFLPAL--RRSPHprIVNISS-GTasltw 159
Cdd:PRK07201 441 DIlaehGHVDYLVNNAGrsIRRSVENSTDRF-HDYERTMAVNYFGAVRLILGLLPHMreRRFGH--VVNVSSiGV----- 512

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 30267738  160 STNpNPQFtpgsggaAAYRSSKAALNALTVLYAQTLAEDG 199
Cdd:PRK07201 513 QTN-APRF-------SAYVASKAALDAFSDVAASETLSDG 544
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
 20-247 8.08e-19

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 83.02  E-value: 8.08e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   20 MNDRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEIG-AGARL--LVLDVTDLD----GIARATTQVDR 92
Cdd:PRK13394   5 LNGKTAVVTGAASGIGKEIALELARAGAAVAIADLNQDGANAVADEINkAGGKAigVAMDVTNEDavnaGIDKVAERFGS 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   93 LDVLVNNAGISpSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPH-PRIVNISSGTASLtwstnpnpqftpGS 171
Cdd:PRK13394  85 VDILVSNAGIQ-IVNPIENYSFADWKKMQAIHVDGAFLTTKAALKHMYKDDRgGVVIYMGSVHSHE------------AS 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30267738  172 GGAAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATdlnPLAAAAGDDPAEA---AQGAARLALLPDDGPTGGF 247
Cdd:PRK13394 152 PLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVCPGFVRT---PLVDKQIPEQAKElgiSEEEVVKKVMLGKTVDGVF 227
PRK12827 PRK12827
short chain dehydrogenase; Provisional
 23-215 8.72e-19

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 82.46  E-value: 8.72e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   23 RTALVTGANKGIGKHIARVLVAEGLTVYVGS----RDRGLGQRAVEEIGAG---ARLLVLDVTDLDGiARATTQVD---- 91
Cdd:PRK12827   7 RRVLITGGSGGLGRAIAVRLAADGADVIVLDihpmRGRAEADAVAAGIEAAggkALGLAFDVRDFAA-TRAALDAGveef 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   92 -RLDVLVNNAGISPSlAPPADTSVEEFRRTYETNVFGVVAVTNAFL-PALRRSPHPRIVNISSgTASLTwstnpnpqftp 169
Cdd:PRK12827  86 gRLDILVNNAGIATD-AAFAELSIEEWDDVIDVNLDGFFNVTQAALpPMIRARRGGRIVNIAS-VAGVR----------- 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 30267738  170 GSGGAAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDLN 215
Cdd:PRK12827 153 GNRGQVNYAASKAGLIGLTKTLANELAPRGITVNAVAPGAINTPMA 198
PRK05993 PRK05993
SDR family oxidoreductase;
19-220 1.88e-18

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 82.38  E-value: 1.88e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   19 AMNdRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEigaGARLLVLDVTDLDGIARATTQV-----DRL 93
Cdd:PRK05993   2 DMK-RSILITGCSSGIGAYCARALQSDGWRVFATCRKEEDVAALEAE---GLEAFQLDYAEPESIAALVAQVlelsgGRL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   94 DVLVNNAGISpslAPPA--DTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISS--GTASLTWStnpnpqftp 169
Cdd:PRK05993  78 DALFNNGAYG---QPGAveDLPTEALRAQFEANFFGWHDLTRRVIPVMRKQGQGRIVQCSSilGLVPMKYR--------- 145

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 30267738  170 gsggaAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDL--NPLAAA 220
Cdd:PRK05993 146 -----GAYNASKFAIEGLSLTLRMELQGSGIHVSLIEPGPIETRFraNALAAF 193
PRK07109 PRK07109
short chain dehydrogenase; Provisional
 20-155 3.72e-18

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 82.28  E-value: 3.72e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   20 MNDRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEI---GAGARLLVLDVTDLDGIARATTQVD----R 92
Cdd:PRK07109   6 IGRQVVVITGASAGVGRATARAFARRGAKVVLLARGEEGLEALAAEIraaGGEALAVVADVADAEAVQAAADRAEeelgP 85

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30267738   93 LDVLVNNAGISpSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTA 155
Cdd:PRK07109  86 IDTWVNNAMVT-VFGPFEDVTPEEFRRVTEVTYLGVVHGTLAALRHMRPRDRGAIIQVGSALA 147
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
20-213 4.34e-18

enoyl-[acyl-carrier-protein] reductase FabL;


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 80.92  E-value: 4.34e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   20 MNDRTALVTGANKGIGKHIARVLVAEGLTVYVG-SRDRGLGQRAVEEIGA-GARLLVL--DVTDLDGIARATTQVD---- 91
Cdd:PRK08063   2 FSGKVALVTGSSRGIGKAIALRLAEEGYDIAVNyARSRKAAEETAEEIEAlGRKALAVkaNVGDVEKIKEMFAQIDeefg 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   92 RLDVLVNNAGiSPSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTASLTWstnpnPQFTpgS 171
Cdd:PRK08063  82 RLDVFVNNAA-SGVLRPAMELEESHWDWTMNINAKALLFCAQEAAKLMEKVGGGKIISLSSLGSIRYL-----ENYT--T 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 30267738  172 GGAaayrsSKAALNALTVLYAQTLAEDGFKVNALAPGMRATD 213
Cdd:PRK08063 154 VGV-----SKAALEALTRYLAVELAPKGIAVNAVSGGAVDTD 190
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
 20-214 5.22e-18

human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This subgroup includes human DHRS1 and related proteins. These are members of the classical SDR family, with a canonical Gly-rich NAD-binding motif and the typical YXXXK active site motif. However, the rest of the catalytic tetrad is not strongly conserved. DHRS1 mRNA has been detected in many tissues, liver, heart, skeletal muscle, kidney and pancreas; a longer transcript is predominantly expressed in the liver , a shorter one in the heart. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187664 [Multi-domain]  Cd Length: 265  Bit Score: 80.95  E-value: 5.22e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  20 MNDRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAV-EEI---GAGARLLVLDVTDLDGIARATTQVD---- 91
Cdd:cd09763   1 LSGKIALVTGASRGIGRGIALQLGEAGATVYITGRTILPQLPGTaEEIearGGKCIPVRCDHSDDDEVEALFERVAreqq 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  92 -RLDVLVNNA--GISPSLAPPADTSVEE------------FRRTYETNVFGVvavtnaflPALRRSPHPRIVNISSgTAS 156
Cdd:cd09763  81 gRLDILVNNAyaAVQLILVGVAKPFWEEpptiwddinnvgLRAHYACSVYAA--------PLMVKAGKGLIVIISS-TGG 151

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 30267738 157 LTWSTNPnpqftpgsggaaAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDL 214
Cdd:cd09763 152 LEYLFNV------------AYGVGKAAIDRMAADMAHELKPHGVAVVSLWPGFVRTEL 197
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
 22-208 5.61e-18

1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; DHB DH (aka 1,2-dihydroxycyclohexa-3,5-diene-1-carboxylate dehydrogenase) catalyzes the NAD-dependent conversion of 1,2-dihydroxycyclohexa-3,4-diene carboxylate to a catechol. This subgroup also contains Pseudomonas putida F1 CmtB, 2,3-dihydroxy-2,3-dihydro-p-cumate dehydrogenase, the second enzyme in the pathway for catabolism of p-cumate catabolism. This subgroup shares the glycine-rich NAD-binding motif of the classical SDRs and shares the same catalytic triad; however, the upstream Asn implicated in cofactor binding or catalysis in other SDRs is generally substituted by a Ser. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187642 [Multi-domain]  Cd Length: 256  Bit Score: 80.65  E-value: 5.61e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  22 DRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEIGAGARLLVLdVTDLDGIARATTQVD-------RLD 94
Cdd:cd08937   4 GKVVVVTGAAQGIGRGVAERLAGEGARVLLVDRSELVHEVLAEILAAGDAAHVH-TADLETYAGAQGVVRaaverfgRVD 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  95 VLVNNAGISPSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTASltwstnpnpqftpgSGGA 174
Cdd:cd08937  83 VLINNVGGTIWAKPYEHYEEEQIEAEIRRSLFPTLWCCRAVLPHMLERQQGVIVNVSSIATR--------------GIYR 148

                       170       180       190
                ....*....|....*....|....*....|....
gi 30267738 175 AAYRSSKAALNALTVLYAQTLAEDGFKVNALAPG 208
Cdd:cd08937 149 IPYSAAKGGVNALTASLAFEHARDGIRVNAVAPG 182
PRK06114 PRK06114
SDR family oxidoreductase;
20-215 6.84e-18

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 80.21  E-value: 6.84e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   20 MNDRTALVTGANKGIGKHIARVLVAEGLTVYVGSR--DRGLGQRA--VEEIGAGARLLVLDVTDL----DGIARATTQVD 91
Cdd:PRK06114   6 LDGQVAFVTGAGSGIGQRIAIGLAQAGADVALFDLrtDDGLAETAehIEAAGRRAIQIAADVTSKadlrAAVARTEAELG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   92 RLDVLVNNAGISPSlAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTASLTwstnpNPQFTpgs 171
Cdd:PRK06114  86 ALTLAVNAAGIANA-NPAEEMEEEQWQTVMDINLTGVFLSCQAEARAMLENGGGSIVNIASMSGIIV-----NRGLL--- 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 30267738  172 ggAAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDLN 215
Cdd:PRK06114 157 --QAHYNASKAGVIHLSKSLAMEWVGRGIRVNSISPGYTATPMN 198
PRK07074 PRK07074
SDR family oxidoreductase;
22-208 9.69e-18

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 79.81  E-value: 9.69e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   22 DRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEIGAGARL-LVLDVTDLDGI----ARATTQVDRLDVL 96
Cdd:PRK07074   2 KRTALVTGAAGGIGQALARRFLAAGDRVLALDIDAAALAAFADALGDARFVpVACDLTDAASLaaalANAAAERGPVDVL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   97 VNNAGISPSLApPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISS--GTASLtwstnpnpqftpgsgGA 174
Cdd:PRK07074  82 VANAGAARAAS-LHDTTPASWRADNALNLEAAYLCVEAVLEGMLKRSRGAVVNIGSvnGMAAL---------------GH 145

                        170       180       190
                 ....*....|....*....|....*....|....
gi 30267738  175 AAYRSSKAALNALTVLYAQTLAEDGFKVNALAPG 208
Cdd:PRK07074 146 PAYSAAKAGLIHYTKLLAVEYGRFGIRANAVAPG 179
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
 22-208 1.08e-17

Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER is a peroxisomal protein with a proposed role in fatty acid elongation. Fatty acid synthesis is known to occur in the both endoplasmic reticulum and mitochondria; peroxisomal TER has been proposed as an additional fatty acid elongation system, it reduces the double bond at C-2 as the last step of elongation. This system resembles the mitochondrial system in that acetyl-CoA is used as a carbon donor. TER may also function in phytol metabolism, reducting phytenoyl-CoA to phytanoyl-CoA in peroxisomes. DECR processes double bonds in fatty acids to increase their utility in fatty acid metabolism; it reduces 2,4-dienoyl-CoA to an enoyl-CoA. DECR is active in mitochondria and peroxisomes. This subgroup has the Gly-rich NAD-binding motif of the classical SDR family, but does not display strong identity to the canonical active site tetrad, and lacks the characteristic Tyr at the usual position. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187627 [Multi-domain]  Cd Length: 249  Bit Score: 79.55  E-value: 1.08e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  22 DRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEIGA--GARLLVL--DVTDLDGIARATTQVD----RL 93
Cdd:cd05369   3 GKVAFITGGGTGIGKAIAKAFAELGASVAIAGRKPEVLEAAAEEISSatGGRAHPIqcDVRDPEAVEAAVDETLkefgKI 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  94 DVLVNNAGiSPSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHP-RIVNISsgtASLTWStnpnpqftpGSG 172
Cdd:cd05369  83 DILINNAA-GNFLAPAESLSPNGFKTVIDIDLNGTFNTTKAVGKRLIEAKHGgSILNIS---ATYAYT---------GSP 149

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 30267738 173 GAAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPG 208
Cdd:cd05369 150 FQVHSAAAKAGVDALTRSLAVEWGPYGIRVNAIAPG 185
PRK06198 PRK06198
short chain dehydrogenase; Provisional
 21-213 1.18e-17

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 79.66  E-value: 1.18e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   21 NDRTALVTGANKGIGKHIARVLVAEGLTVYVGS-RDRGLGQRAVEEI---GAGARLLVLDVTDLDG----IARATTQVDR 92
Cdd:PRK06198   5 DGKVALVTGGTQGLGAAIARAFAERGAAGLVICgRNAEKGEAQAAELealGAKAVFVQADLSDVEDcrrvVAAADEAFGR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   93 LDVLVNNAGISpSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHP-RIVNISSGTASltwstnpnpqftPGS 171
Cdd:PRK06198  85 LDALVNAAGLT-DRGTILDTSPELFDRHFAVNVRAPFFLMQEAIKLMRRRKAEgTIVNIGSMSAH------------GGQ 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 30267738  172 GGAAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATD 213
Cdd:PRK06198 152 PFLAAYCASKGALATLTRNAAYALLRNRIRVNGLNIGWMATE 193
PRK06181 PRK06181
SDR family oxidoreductase;
22-226 1.87e-17

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 79.25  E-value: 1.87e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   22 DRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEI---GAGARLLVLDVTDLDGIARATTQV----DRLD 94
Cdd:PRK06181   1 GKVVIITGASEGIGRALAVRLARAGAQLVLAARNETRLASLAQELadhGGEALVVPTDVSDAEACERLIEAAvarfGGID 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   95 VLVNNAGISpSLAPPADTS-VEEFRRTYETNVFGVVAVTNAFLPALRRSpHPRIVNISSGTAsltwstnpnpqfTPGSGG 173
Cdd:PRK06181  81 ILVNNAGIT-MWSRFDELTdLSVFERVMRVNYLGAVYCTHAALPHLKAS-RGQIVVVSSLAG------------LTGVPT 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 30267738  174 AAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDLNPLAAAAGDDPA 226
Cdd:PRK06181 147 RSGYAASKHALHGFFDSLRIELADDGVAVTVVCPGFVATDIRKRALDGDGKPL 199
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
 20-220 2.27e-17

Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR with a characteristic NAD-binding pattern and active site tetrad. Aromatic polyketides include various aromatic compounds of pharmaceutical interest. Polyketide KR, part of the type II polyketide synthase (PKS) complex, is comprised of stand-alone domains that resemble the domains found in fatty acid synthase and multidomain type I PKS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187649 [Multi-domain]  Cd Length: 258  Bit Score: 79.12  E-value: 2.27e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  20 MNDRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEI---GAGARLLVLDVTDLDGI----ARATTQVDR 92
Cdd:cd08945   1 QDSEVALVTGATSGIGLAIARRLGKEGLRVFVCARGEEGLATTVKELreaGVEADGRTCDVRSVPEIealvAAAVARYGP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  93 LDVLVNNAGISPSLApPADTSVEEFRRTYETNVFGVVAVTNAFLPA--LRRSPHPRIVNISSgtasltwstnpnpqfTPG 170
Cdd:cd08945  81 IDVLVNNAGRSGGGA-TAELADELWLDVVETNLTGVFRVTKEVLKAggMLERGTGRIINIAS---------------TGG 144

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 30267738 171 SGG---AAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATdlnPLAAA 220
Cdd:cd08945 145 KQGvvhAAPYSASKHGVVGFTKALGLELARTGITVNAVCPGFVET---PMAAS 194
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
 17-214 2.91e-17

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 78.51  E-value: 2.91e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   17 VVAMNDRTALVTGANKGIGKHIARVLVAEGLTVYVG-SRDRGLGQRAVEEI---GAGARLLVLDVTDLDGIAR----ATT 88
Cdd:PRK12935   1 MVQLNGKVAIVTGGAKGIGKAITVALAQEGAKVVINyNSSKEAAENLVNELgkeGHDVYAVQADVSKVEDANRlveeAVN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   89 QVDRLDVLVNNAGISPSLApPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISS--GTAsltwstnpnpq 166
Cdd:PRK12935  81 HFGKVDILVNNAGITRDRT-FKKLNREDWERVIDVNLSSVFNTTSAVLPYITEAEEGRIISISSiiGQA----------- 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 30267738  167 ftpGSGGAAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDL 214
Cdd:PRK12935 149 ---GGFGQTNYSAAKAGMLGFTKSLALELAKTNVTVNAICPGFIDTEM 193
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
 21-214 3.51e-17

17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as amyloid-peptide-binding alcohol dehydrogenase (ABAD), was previously identified as a L-3-hydroxyacyl-CoA dehydrogenase, HADH2. In fatty acid metabolism, HADH2 catalyzes the third step of beta-oxidation, the conversion of a hydroxyl to a keto group in the NAD-dependent oxidation of L-3-hydroxyacyl CoA. In addition to alcohol dehydrogenase and HADH2 activites, HSD10 has steroid dehydrogenase activity. Although the mechanism is unclear, HSD10 is implicated in the formation of amyloid beta-petide in the brain (which is linked to the development of Alzheimer's disease). Although HSD10 is normally concentrated in the mitochondria, in the presence of amyloid beta-peptide it translocates into the plasma membrane, where it's action may generate cytotoxic aldehydes and may lower estrogen levels through its use of 17-beta-estradiol as a substrate. HSD10 is a member of the SRD family, but differs from other SDRs by the presence of two insertions of unknown function. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187629 [Multi-domain]  Cd Length: 252  Bit Score: 78.48  E-value: 3.51e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  21 NDRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRaVEEIGAGARLLVLDVTDLD----GIARATTQVDRLDVL 96
Cdd:cd05371   1 KGLVAVVTGGASGLGLATVERLLAQGAKVVILDLPNSPGET-VAKLGDNCRFVPVDVTSEKdvkaALALAKAKFGRLDIV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  97 VNNAGIspslAPPADT---------SVEEFRRTYETNVFGVVAVTNAFLPALRRSPhPR-------IVNISSGTAsltws 160
Cdd:cd05371  80 VNCAGI----AVAAKTynkkgqqphSLELFQRVINVNLIGTFNVIRLAAGAMGKNE-PDqggergvIINTASVAA----- 149

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 30267738 161 tnpnpqfTPGSGGAAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDL 214
Cdd:cd05371 150 -------FEGQIGQAAYSASKGGIVGMTLPIARDLAPQGIRVVTIAPGLFDTPL 196
PRK05717 PRK05717
SDR family oxidoreductase;
21-208 3.71e-17

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 78.39  E-value: 3.71e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   21 NDRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEIGAGARLLVLDVTDLD----GIARATTQVDRLDVL 96
Cdd:PRK05717   9 NGRVALVTGAARGIGLGIAAWLIAEGWQVVLADLDRERGSKVAKALGENAWFIAMDVADEAqvaaGVAEVLGQFGRLDAL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   97 VNNAGIspslAPPADTSVEEFRRTYETNVFGvVAVTNAFLPALRRSPHPR-----IVNISSGTASltwSTNPNPQftpgs 171
Cdd:PRK05717  89 VCNAAI----ADPHNTTLESLSLAHWNRVLA-VNLTGPMLLAKHCAPYLRahngaIVNLASTRAR---QSEPDTE----- 155

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 30267738  172 ggaaAYRSSKAALNALTVLYAQTLAEDgFKVNALAPG 208
Cdd:PRK05717 156 ----AYAASKGGLLALTHALAISLGPE-IRVNAVSPG 187
PRK06500 PRK06500
SDR family oxidoreductase;
22-254 4.35e-17

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 78.07  E-value: 4.35e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   22 DRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEIGAGARLLVLDVTDLDGiARATTQV-----DRLDVL 96
Cdd:PRK06500   6 GKTALITGGTSGIGLETARQFLAEGARVAITGRDPASLEAARAELGESALVIRADAGDVAA-QKALAQAlaeafGRLDAV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   97 VNNAGISpSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSphprivnissgtASLTWSTNPNPQFtpGSGGAAA 176
Cdd:PRK06500  85 FINAGVA-KFAPLEDWDEAMFDRSFNTNVKGPYFLIQALLPLLANP------------ASIVLNGSINAHI--GMPNSSV 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30267738  177 YRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATdlnPLAAAAGDDPAEAAQGAARLALLPddgPTGGFfswdGTP 254
Cdd:PRK06500 150 YAASKAALLSLAKTLSGELLPRGIRVNAVSPGPVQT---PLYGKLGLPEATLDAVAAQIQALV---PLGRF----GTP 217
PRK09730 PRK09730
SDR family oxidoreductase;
24-225 4.95e-17

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 77.97  E-value: 4.95e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   24 TALVTGANKGIGKHIARVLVAEGLTVYVG-SRDRGLGQRAVEEI-GAGARLLVL--DVTDLDGIARATTQVDR----LDV 95
Cdd:PRK09730   3 IALVTGGSRGIGRATALLLAQEGYTVAVNyQQNLHAAQEVVNLItQAGGKAFVLqaDISDENQVVAMFTAIDQhdepLAA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   96 LVNNAGISPSLAPPADTSVEEFRRTYETNvfgvvaVTNAFL---PALRRSPHPR------IVNISSGTASLTwstnpnpq 166
Cdd:PRK09730  83 LVNNAGILFTQCTVENLTAERINRVLSTN------VTGYFLccrEAVKRMALKHggsggaIVNVSSAASRLG-------- 148

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 30267738  167 fTPGSggAAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDLNplaaAAGDDP 225
Cdd:PRK09730 149 -APGE--YVDYAASKGAIDTLTTGLSLEVAAQGIRVNCVRPGFIYTEMH----ASGGEP 200
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
 20-230 6.27e-17

cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol reductases,including (6R)-2,2,6-trimethyl-1,4-cyclohexanedione (levodione) reductase of Corynebacterium aquaticum, catalyze the reversible oxidoreduction of hydroxycyclohexanone derivatives. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187591 [Multi-domain]  Cd Length: 257  Bit Score: 77.56  E-value: 6.27e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  20 MNDRTALVTGANKGIGKHIARVLVAEGLT-VYVGSRDRGL--GQRAVEEIGAGARLL-----VLDVTDLDGIARATT-QV 90
Cdd:cd05330   1 FKDKVVLITGGGSGLGLATAVRLAKEGAKlSLVDLNEEGLeaAKAALLEIAPDAEVLlikadVSDEAQVEAYVDATVeQF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  91 DRLDVLVNNAGISPSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTAsltwstnpnpqfTPG 170
Cdd:cd05330  81 GRIDGFFNNAGIEGKQNLTEDFGADEFDKVVSINLRGVFYGLEKVLKVMREQGSGMIVNTASVGG------------IRG 148

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30267738 171 SGGAAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDL--NPLAAAAGDDPAEAAQ 230
Cdd:cd05330 149 VGNQSGYAAAKHGVVGLTRNSAVEYGQYGIRINAIAPGAILTPMveGSLKQLGPENPEEAGE 210
PRK06953 PRK06953
SDR family oxidoreductase;
23-257 1.27e-16

SDR family oxidoreductase;


Pssm-ID: 180774 [Multi-domain]  Cd Length: 222  Bit Score: 76.26  E-value: 1.27e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   23 RTALVTGANKGIGKHIARVLVAEGLTVYVGSRDrglgQRAVEEIGA-GARLLVLDVTDLDGIARATTQVD--RLDVLVNN 99
Cdd:PRK06953   2 KTVLIVGASRGIGREFVRQYRADGWRVIATARD----AAALAALQAlGAEALALDVADPASVAGLAWKLDgeALDAAVYV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  100 AGI---SPSLAPPadTSVEEFRRTYETNVFGVVAVTNAFLPaLRRSPHPRIVNISSGTASLTWSTnpnpqftpgSGGAAA 176
Cdd:PRK06953  78 AGVygpRTEGVEP--ITREDFDAVMHTNVLGPMQLLPILLP-LVEAAGGVLAVLSSRMGSIGDAT---------GTTGWL 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  177 YRSSKAALNAltVLYAQTLAEDGFKVNALAPGMRATDLNplAAAAGDDPAEAAQGAARLALLPDDGPTGGFFSWDGTPVP 256
Cdd:PRK06953 146 YRASKAALND--ALRAASLQARHATCIALHPGWVRTDMG--GAQAALDPAQSVAGMRRVIAQATRRDNGRFFQYDGVELS 221


                 .
gi 30267738  257 W 257
Cdd:PRK06953 222 W 222
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
 20-230 2.11e-16

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 76.30  E-value: 2.11e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   20 MNDRTALVTGANKGIGKHIARVLVAEGLTVYVGSR-DRGLGQRAVEEI-GAGARLLVL--DVTDLDGIAR----ATTQVD 91
Cdd:PRK08936   5 LEGKVVVITGGSTGLGRAMAVRFGKEKAKVVINYRsDEEEANDVAEEIkKAGGEAIAVkgDVTVESDVVNliqtAVKEFG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   92 RLDVLVNNAGISPSlAPPADTSVEEFRRTYETNvfgvvaVTNAFLPA-------LRRSPHPRIVNISSGTASLTWstnpn 164
Cdd:PRK08936  85 TLDVMINNAGIENA-VPSHEMSLEDWNKVINTN------LTGAFLGSreaikyfVEHDIKGNIINMSSVHEQIPW----- 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30267738  165 PQFtpgsggaAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATdlnPLAAAAGDDPAEAAQ 230
Cdd:PRK08936 153 PLF-------VHYAASKGGVKLMTETLAMEYAPKGIRVNNIGPGAINT---PINAEKFADPKQRAD 208
LPOR_like_SDR_c_like cd09810
light-dependent protochlorophyllide reductase (LPOR)-like, classical (c)-like SDRs; Classical ...
 24-254 2.64e-16

light-dependent protochlorophyllide reductase (LPOR)-like, classical (c)-like SDRs; Classical SDR-like subgroup containing LPOR and related proteins. Protochlorophyllide (Pchlide) reductases act in chlorophyll biosynthesis. There are distinct enzymes that catalyze Pchlide reduction in light or dark conditions. Light-dependent reduction is via an NADP-dependent SDR, LPOR. Proteins in this subfamily share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187670 [Multi-domain]  Cd Length: 311  Bit Score: 76.79  E-value: 2.64e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  24 TALVTGANKGIGKHIARVLVAEGL-TVYVGSRDRGLGQRAVEEIGAGA---RLLVLDVTDLDGIARATTQVDR----LDV 95
Cdd:cd09810   3 TVVITGASSGLGLAAAKALARRGEwHVVMACRDFLKAEQAAQEVGMPKdsySVLHCDLASLDSVRQFVDNFRRtgrpLDA 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  96 LVNNAGISPSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSP--HPRIVNISSGTASL-TWSTNPNPQFTPGS- 171
Cdd:cd09810  83 LVCNAAVYLPTAKEPRFTADGFELTVGVNHLGHFLLTNLLLEDLQRSEnaSPRIVIVGSITHNPnTLAGNVPPRATLGDl 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738 172 -------------------GGAAAYRSSKAAlNALTV--LYAQTLAEDGFKVNALAPGMRATD---------LNPLAAAA 221
Cdd:cd09810 163 eglagglkgfnsmidggefEGAKAYKDSKVC-NMLTTyeLHRRLHEETGITFNSLYPGCIAETglfrehyplFRTLFPPF 241

                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 30267738 222 GDDPA-------EAAQGAARLALLPDDGPTGGFFSWDGTP 254
Cdd:cd09810 242 QKYITkgyvseeEAGERLAAVIADPSLGVSGVYWSWGKAS 281
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
 20-209 3.10e-16

Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter sphaeroides SDH, and other SDHs. SDH preferentially interconverts D-sorbitol (D-glucitol) and D-fructose, but also interconverts L-iditol/L-sorbose and galactitol/D-tagatose. SDH is NAD-dependent and is a dimeric member of the SDR family. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187621 [Multi-domain]  Cd Length: 254  Bit Score: 75.73  E-value: 3.10e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  20 MNDRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEIGAGARLLVLDVTDLDGIARATTQ-VDR---LDV 95
Cdd:cd05363   1 LDGKTALITGSARGIGRAFAQAYVREGARVAIADINLEAARATAAEIGPAACAISLDVTDQASIDRCVAAlVDRwgsIDI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  96 LVNNAGISpSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPH-PRIVNISSGTASltwstnpnpqftPGSGGA 174
Cdd:cd05363  81 LVNNAALF-DLAPIVDITRESYDRLFAINVSGTLFMMQAVARAMIAQGRgGKIINMASQAGR------------RGEALV 147

                       170       180       190
                ....*....|....*....|....*....|....*
gi 30267738 175 AAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGM 209
Cdd:cd05363 148 GVYCATKAAVISLTQSAGLNLIRHGINVNAIAPGV 182
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
 20-224 3.29e-16

2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 75.76  E-value: 3.29e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   20 MNDRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEIGAGARLLVLDVTDLD----GIARATTQVDRLDV 95
Cdd:PRK06200   4 LHGQVALITGGGSGIGRALVERFLAEGARVAVLERSAEKLASLRQRFGDHVLVVEGDVTSYAdnqrAVDQTVDAFGKLDC 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   96 LVNNAGISPSLAPPADTSVEE----FRRTYETNVFGVVAVTNAFLPALRRsphprivniSSGTASLTWStnpNPQFTPGS 171
Cdd:PRK06200  84 FVGNAGIWDYNTSLVDIPAETldtaFDEIFNVNVKGYLLGAKAALPALKA---------SGGSMIFTLS---NSSFYPGG 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 30267738  172 GGaAAYRSSKAALNALTVLYAQTLAEDgFKVNALAPGMRATDLNPLAAAAGDD 224
Cdd:PRK06200 152 GG-PLYTASKHAVVGLVRQLAYELAPK-IRVNGVAPGGTVTDLRGPASLGQGE 202
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
 27-241 5.95e-16

classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and NAD-binding motif of the classical SDRs. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187636 [Multi-domain]  Cd Length: 227  Bit Score: 74.41  E-value: 5.95e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  27 VTGANKGIGKHIARVLVAEGLtvYVGSRDR---GLGQRAVEeIGAGARLL-VLDVTD-------LDGIARATTQvdRLDV 95
Cdd:cd08931   5 ITGAASGIGRETALLFARNGW--FVGLYDIdedGLAALAAE-LGAENVVAgALDVTDraawaaaLADFAAATGG--RLDA 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  96 LVNNAGISPSlAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTAsltwstnpnpqfTPGSGGAA 175
Cdd:cd08931  80 LFNNAGVGRG-GPFEDVPLAAHDRMVDINVKGVLNGAYAALPYLKATPGARVINTASSSA------------IYGQPDLA 146

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30267738 176 AYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDLnplaAAAGDDPAEAAQGAARLaLLPDD 241
Cdd:cd08931 147 VYSATKFAVRGLTEALDVEWARHGIRVADVWPWFVDTPI----LTKGETGAAPKKGLGRV-LPVSD 207
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
 20-208 6.12e-16

3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 74.95  E-value: 6.12e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   20 MNDRTALVTGANKGIGKHIARVLVAEGLTVYV-GSRDRGLGQRAVeEIGAGARLLVLDVTDLDGIA----RATTQVDRLD 94
Cdd:PRK12936   4 LSGRKALVTGASGGIGEEIARLLHAQGAIVGLhGTRVEKLEALAA-ELGERVKIFPANLSDRDEVKalgqKAEADLEGVD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   95 VLVNNAGISPSlAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTASLtwstnpnpqftpGSGGA 174
Cdd:PRK12936  83 ILVNNAGITKD-GLFVRMSDEDWDSVLEVNLTATFRLTRELTHPMMRRRYGRIINITSVVGVT------------GNPGQ 149

                        170       180       190
                 ....*....|....*....|....*....|....
gi 30267738  175 AAYRSSKAALNALTVLYAQTLAEDGFKVNALAPG 208
Cdd:PRK12936 150 ANYCASKAGMIGFSKSLAQEIATRNVTVNCVAPG 183
DHRS-12_like_SDR_c-like cd09808
human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like ...
 23-255 6.77e-16

human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like SDRs; Classical SDR-like subgroup containing human DHRS-12/FLJ13639, the 36K protein of zebrafish CNS myelin, and related proteins. DHRS-12/FLJ13639 is expressed in neurons and oligodendrocytes in the human cerebral cortex. Proteins in this subgroup share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187668 [Multi-domain]  Cd Length: 255  Bit Score: 74.94  E-value: 6.77e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  23 RTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEIGA--GARLLVLDVTDL-------DGIARATTQVDRL 93
Cdd:cd09808   2 RSFLITGANSGIGKAAALAIAKRGGTVHMVCRNQTRAEEARKEIETesGNQNIFLHIVDMsdpkqvwEFVEEFKEEGKKL 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  94 DVLVNNAGispSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTASLTWSTNPNPQFTPGS-G 172
Cdd:cd09808  82 HVLINNAG---CMVNKRELTEDGLEKNFATNTLGTYILTTHLIPVLEKEEDPRVITVSSGGMLVQKLNTNNLQSERTAfD 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738 173 GAAAYRSSKAALNALTVLYAQTLAEDGFKVN----ALAPGMRATdLNPLAAAAGDDPAEAAQGAARLALL-----PDDGP 243
Cdd:cd09808 159 GTMVYAQNKRQQVIMTEQWAKKHPEIHFSVMhpgwADTPAVRNS-MPDFHARFKDRLRSEEQGADTVVWLalssaAAKAP 237

                       250
                ....*....|..
gi 30267738 244 TGGFFSwDGTPV 255
Cdd:cd09808 238 SGRFYQ-DRKPV 248
PRK06523 PRK06523
short chain dehydrogenase; Provisional
 23-230 8.06e-16

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 74.56  E-value: 8.06e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   23 RTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGlgqravEEIGAGARLLVLDVTDLDGIARATTQV-DRL---DVLVN 98
Cdd:PRK06523  10 KRALVTGGTKGIGAATVARLLEAGARVVTTARSRP------DDLPEGVEFVAADLTTAEGCAAVARAVlERLggvDILVH 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   99 NAGisPSLAPP---ADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTASLtwstnPNPQFTpgsggaA 175
Cdd:PRK06523  84 VLG--GSSAPAggfAALTDEEWQDELNLNLLAAVRLDRALLPGMIARGSGVIIHVTSIQRRL-----PLPEST------T 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  176 AYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATD-----LNPLAAAAGDDPAEAAQ 230
Cdd:PRK06523 151 AYAAAKAALSTYSKSLSKEVAPKGVRVNTVSPGWIETEaavalAERLAEAAGTDYEGAKQ 210
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 23-208 1.03e-15

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 74.34  E-value: 1.03e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   23 RTALVTGANK--GIGKHIARVLVAEGLTVYVGS---RDRGLG-----------QRAVEEIGAGARLLVLDVTDLDGIAR- 85
Cdd:PRK12748   6 KIALVTGASRlnGIGAAVCRRLAAKGIDIFFTYwspYDKTMPwgmhdkepvllKEEIESYGVRCEHMEIDLSQPYAPNRv 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   86 ---ATTQVDRLDVLVNNAGISpSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGtasltWSTN 162
Cdd:PRK12748  86 fyaVSERLGDPSILINNAAYS-THTRLEELTAEQLDKHYAVNVRATMLLSSAFAKQYDGKAGGRIINLTSG-----QSLG 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 30267738  163 PNPqftpgsgGAAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPG 208
Cdd:PRK12748 160 PMP-------DELAYAATKGAIEAFTKSLAPELAEKGITVNAVNPG 198
PRK12747 PRK12747
short chain dehydrogenase; Provisional
 20-215 1.39e-15

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 73.96  E-value: 1.39e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   20 MNDRTALVTGANKGIGKHIARVLVAEG--LTVYVGSRdRGLGQRAVEEI---GAGARLLVLDVTDLDGIARATTQVD--- 91
Cdd:PRK12747   2 LKGKVALVTGASRGIGRAIAKRLANDGalVAIHYGNR-KEEAEETVYEIqsnGGSAFSIGANLESLHGVEALYSSLDnel 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   92 -------RLDVLVNNAGISPSlAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRrsPHPRIVNISSGTASLTWstnpn 164
Cdd:PRK12747  81 qnrtgstKFDILINNAGIGPG-AFIEETTEQFFDRMVSVNAKAPFFIIQQALSRLR--DNSRIINISSAATRISL----- 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 30267738  165 PQFTpgsggaaAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDLN 215
Cdd:PRK12747 153 PDFI-------AYSMTKGAINTMTFTLAKQLGARGITVNAILPGFIKTDMN 196
PRK07791 PRK07791
short chain dehydrogenase; Provisional
 19-210 1.41e-15

short chain dehydrogenase; Provisional


Pssm-ID: 236099 [Multi-domain]  Cd Length: 286  Bit Score: 74.32  E-value: 1.41e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   19 AMNDRTALVTGANKGIGKHIARVLVAEGLTVYV---------GSRDRGLGQRAVEEI-GAGARLLV--LDVTDLDG---- 82
Cdd:PRK07791   3 LLDGRVVIVTGAGGGIGRAHALAFAAEGARVVVndigvgldgSASGGSAAQAVVDEIvAAGGEAVAngDDIADWDGaanl 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   83 IARATTQVDRLDVLVNNAGISPSlAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALR------RSPHPRIVNISSGtAS 156
Cdd:PRK07791  83 VDAAVETFGGLDVLVNNAGILRD-RMIANMSEEEWDAVIAVHLKGHFATLRHAAAYWRaeskagRAVDARIINTSSG-AG 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 30267738  157 LTwstnpnpqftpGSGGAAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMR 210
Cdd:PRK07791 161 LQ-----------GSVGQGNYSAAKAGIAALTLVAAAELGRYGVTVNAIAPAAR 203
PRK08017 PRK08017
SDR family oxidoreductase;
23-241 1.53e-15

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 73.97  E-value: 1.53e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   23 RTALVTGANKGIGKHIARVLVAEGLTVYVGSRD-------RGLGQRAVEeigagarllvLDVTDLDGIARATTQV----- 90
Cdd:PRK08017   3 KSVLITGCSSGIGLEAALELKRRGYRVLAACRKpddvarmNSLGFTGIL----------LDLDDPESVERAADEVialtd 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   91 DRLDVLVNNAGISpsLAPPADT-SVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISS--GTASltwstnpnpqf 167
Cdd:PRK08017  73 NRLYGLFNNAGFG--VYGPLSTiSRQQMEQQFSTNFFGTHQLTMLLLPAMLPHGEGRIVMTSSvmGLIS----------- 139

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30267738  168 TPGSGgaaAYRSSKAALNALTVLYAQTLAEDGFKVNALAPG---MRATDlnPLAAAAGDDPAEAAQGAARLALLPDD 241
Cdd:PRK08017 140 TPGRG---AYAASKYALEAWSDALRMELRHSGIKVSLIEPGpirTRFTD--NVNQTQSDKPVENPGIAARFTLGPEA 211
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
 23-208 1.63e-15

Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, classical (c) SDRs; This subgroup includes a putative carbohydrate or polyalcohol metabolizing SDR (A3DFK9) from Clostridium thermocellum. Its members have a TGXXXGXG classical-SDR glycine-rich NAD-binding motif, and some have a canonical SDR active site tetrad (A3DFK9 lacks the upstream Asn). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187662 [Multi-domain]  Cd Length: 242  Bit Score: 73.77  E-value: 1.63e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  23 RTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEIGAGARLLVLDVTDLDGIA----RATTQVDRLDVLVN 98
Cdd:cd09761   2 KVAIVTGGGHGIGKQICLDFLEAGDKVVFADIDEERGADFAEAEGPNLFFVHGDVADETLVKfvvyAMLEKLGRIDVLVN 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  99 NAGISpSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSpHPRIVNISSGTASltwstnpnpQFTPGSggaAAYR 178
Cdd:cd09761  82 NAARG-SKGILSSLLLEEWDRILSVNLTGPYELSRYCRDELIKN-KGRIINIASTRAF---------QSEPDS---EAYA 147

                       170       180       190
                ....*....|....*....|....*....|
gi 30267738 179 SSKAALNALTVLYAQTLAEDgFKVNALAPG 208
Cdd:cd09761 148 ASKGGLVALTHALAMSLGPD-IRVNCISPG 176
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
 27-188 1.86e-15

classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a canonical active site triad (and also active site Asn) and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187618 [Multi-domain]  Cd Length: 233  Bit Score: 73.19  E-value: 1.86e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  27 VTGANKGIGKHIARVLVAEGLTVYVGSRD-RGLGQ--RAVEEIGAGARLLVLDVTDLDGIAR-ATTQVDRL---DVLVNN 99
Cdd:cd05360   5 ITGASSGIGRATALAFAERGAKVVLAARSaEALHElaREVRELGGEAIAVVADVADAAQVERaADTAVERFgriDTWVNN 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738 100 AGISpSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISS--GTASLTWstnpnpqftpgsggAAAY 177
Cdd:cd05360  85 AGVA-VFGRFEDVTPEEFRRVFDVNYLGHVYGTLAALPHLRRRGGGALINVGSllGYRSAPL--------------QAAY 149

                       170
                ....*....|.
gi 30267738 178 RSSKAALNALT 188
Cdd:cd05360 150 SASKHAVRGFT 160
PRK07832 PRK07832
SDR family oxidoreductase;
25-214 1.89e-15

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 73.92  E-value: 1.89e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   25 ALVTGANKGIGKHIARVLVAEGLTVYVGSRD-RGLGQrAVEEIGAG----ARLLVLDVTDLDGIARATTQVDR----LDV 95
Cdd:PRK07832   3 CFVTGAASGIGRATALRLAAQGAELFLTDRDaDGLAQ-TVADARALggtvPEHRALDISDYDAVAAFAADIHAahgsMDV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   96 LVNNAGISpSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPAL---RRSPHprIVNISS--GTASLTWStnpnpqftpg 170
Cdd:PRK07832  82 VMNIAGIS-AWGTVDRLTHEQWRRMVDVNLMGPIHVIETFVPPMvaaGRGGH--LVNVSSaaGLVALPWH---------- 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 30267738  171 sggaAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDL 214
Cdd:PRK07832 149 ----AAYSASKFGLRGLSEVLRFDLARHGIGVSVVVPGAVKTPL 188
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 20-221 1.96e-15

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 73.59  E-value: 1.96e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   20 MNDRTALVTGANKGIGKHIARVLVAEGLTV---YVGSRDRglGQRAVEEIGAGARLLVLDVTDLDGIARATTQVDR---- 92
Cdd:PRK08642   3 ISEQTVLVTGGSRGLGAAIARAFAREGARVvvnYHQSEDA--AEALADELGDRAIALQADVTDREQVQAMFATATEhfgk 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   93 -LDVLVNNAGISPSLAPPA-----DTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNIssgtasltwSTN--PN 164
Cdd:PRK08642  81 pITTVVNNALADFSFDGDArkkadDITWEDFQQQLEGSVKGALNTIQAALPGMREQGFGRIINI---------GTNlfQN 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 30267738  165 PqFTPgsggAAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPG-MRATDlnplAAAA 221
Cdd:PRK08642 152 P-VVP----YHDYTTAKAALLGLTRNLAAELGPYGITVNMVSGGlLRTTD----ASAA 200
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
20-212 2.05e-15

2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 73.62  E-value: 2.05e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   20 MNDRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLG--QRAVEEIGAGARLLVLDVTDLDG----IARATTQVDRL 93
Cdd:PRK06935  13 LDGKVAIVTGGNTGLGQGYAVALAKAGADIIITTHGTNWDetRRLIEKEGRKVTFVQVDLTKPESaekvVKEALEEFGKI 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   94 DVLVNNAGISPSlAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSgtaSLTWSTNpnpQFTPgsgg 173
Cdd:PRK06935  93 DILVNNAGTIRR-APLLEYKDEDWNAVMDINLNSVYHLSQAVAKVMAKQGSGKIINIAS---MLSFQGG---KFVP---- 161

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 30267738  174 aaAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRAT 212
Cdd:PRK06935 162 --AYTASKHGVAGLTKAFANELAAYNIQVNAIAPGYIKT 198
PRK07814 PRK07814
SDR family oxidoreductase;
20-229 2.23e-15

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 73.66  E-value: 2.23e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   20 MNDRTALVTGANKGIGKHIARVLVAEGLTVYVGSR-DRGLGQRA--VEEIGAGARLLVLDVTDLDGIA----RATTQVDR 92
Cdd:PRK07814   8 LDDQVAVVTGAGRGLGAAIALAFAEAGADVLIAARtESQLDEVAeqIRAAGRRAHVVAADLAHPEATAglagQAVEAFGR 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   93 LDVLVNNAGISPSlAPPADTSVEEFRRTYETNVFGVVAVTNAFLP-ALRRSPHPRIVNISSGTASLtwstnPNPQFtpgs 171
Cdd:PRK07814  88 LDIVVNNVGGTMP-NPLLSTSTKDLADAFTFNVATAHALTVAAVPlMLEHSGGGSVINISSTMGRL-----AGRGF---- 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 30267738  172 ggaAAYRSSKAALNALTVLYAQTLAEDgFKVNALAPGMRATdlNPLAAAAGDDPAEAA 229
Cdd:PRK07814 158 ---AAYGTAKAALAHYTRLAALDLCPR-IRVNAIAPGSILT--SALEVVAANDELRAP 209
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
 21-210 2.25e-15

(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids in eukaryotes occurs by a four-reaction cycle, that may take place in mitochondria or in peroxisomes. (3R)-hydroxyacyl-CoA dehydrogenase is part of rat peroxisomal multifunctional MFE-2, it is a member of the NAD-dependent SDRs, but contains an additional small C-terminal domain that completes the active site pocket and participates in dimerization. The atypical, additional C-terminal extension allows for more extensive dimerization contact than other SDRs. MFE-2 catalyzes the second and third reactions of the peroxisomal beta oxidation cycle. Proteins in this subgroup have a typical catalytic triad, but have a His in place of the usual upstream Asn. This subgroup also contains members identified as 17-beta-hydroxysteroid dehydrogenases, including human peroxisomal 17-beta-hydroxysteroid dehydrogenase type 4 (17beta-HSD type 4, aka MFE-2, encoded by HSD17B4 gene) which is involved in fatty acid beta-oxidation and steroid metabolism. This subgroup also includes two SDR domains of the Neurospora crassa and Saccharomyces cerevisiae multifunctional beta-oxidation protein (MFP, aka Fox2). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187611 [Multi-domain]  Cd Length: 250  Bit Score: 73.13  E-value: 2.25e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  21 NDRTALVTGANKGIGKHIARVLVAEGLTVYV----GSRD-RGLGQRA----VEEIGAGARLLVLDVTDLDG----IARAT 87
Cdd:cd05353   4 DGRVVLVTGAGGGLGRAYALAFAERGAKVVVndlgGDRKgSGKSSSAadkvVDEIKAAGGKAVANYDSVEDgekiVKTAI 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  88 TQVDRLDVLVNNAGI--SPSLAppaDTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSgTASLTwstnpnp 165
Cdd:cd05353  84 DAFGRVDILVNNAGIlrDRSFA---KMSEEDWDLVMRVHLKGSFKVTRAAWPYMRKQKFGRIINTSS-AAGLY------- 152

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 30267738 166 qftpGSGGAAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMR 210
Cdd:cd05353 153 ----GNFGQANYSAAKLGLLGLSNTLAIEGAKYNITCNTIAPAAG 193
PRK07024 PRK07024
SDR family oxidoreductase;
27-234 2.26e-15

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 73.43  E-value: 2.26e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   27 VTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEIGAGARLLV--LDVTDLDGIARATT----QVDRLDVLVNNA 100
Cdd:PRK07024   7 ITGASSGIGQALAREYARQGATLGLVARRTDALQAFAARLPKAARVSVyaADVRDADALAAAAAdfiaAHGLPDVVIANA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  101 GISPS--LAPPADTSVeeFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISS--GTASLtwstnpnpqftPGSGgaaA 176
Cdd:PRK07024  87 GISVGtlTEEREDLAV--FREVMDTNYFGMVATFQPFIAPMRAARRGTLVGIASvaGVRGL-----------PGAG---A 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30267738  177 YRSSKAA----LNALTVlyaqTLAEDGFKVNALAPGMRATDL---NPLAAAAGDDPAEAAQGAAR 234
Cdd:PRK07024 151 YSASKAAaikyLESLRV----ELRPAGVRVVTIAPGYIRTPMtahNPYPMPFLMDADRFAARAAR 211
PRK08177 PRK08177
SDR family oxidoreductase;
23-257 3.68e-15

SDR family oxidoreductase;


Pssm-ID: 236173 [Multi-domain]  Cd Length: 225  Bit Score: 72.37  E-value: 3.68e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   23 RTALVTGANKGIGKHIARVLVAEGLTVYVGSRD--RGLGQRAVeeigAGARLLVLDVTD---LDGIARATtQVDRLDVLV 97
Cdd:PRK08177   2 RTALIIGASRGLGLGLVDRLLERGWQVTATVRGpqQDTALQAL----PGVHIEKLDMNDpasLDQLLQRL-QGQRFDLLF 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   98 NNAGIS-PSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSpHPRIVNISSGTASLTwstnpnpqfTPGSGGAAA 176
Cdd:PRK08177  77 VNAGISgPAHQSAADATAAEIGQLFLTNAIAPIRLARRLLGQVRPG-QGVLAFMSSQLGSVE---------LPDGGEMPL 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  177 YRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDLNplAAAAGDDPAEAAQGAarLALLPDDGPTGG--FFSWDGTP 254
Cdd:PRK08177 147 YKASKAALNSMTRSFVAELGEPTLTVLSMHPGWVKTDMG--GDNAPLDVETSVKGL--VEQIEAASGKGGhrFIDYQGET 222


                 ...
gi 30267738  255 VPW 257
Cdd:PRK08177 223 LPW 225
PRK12742 PRK12742
SDR family oxidoreductase;
19-216 4.71e-15

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 72.10  E-value: 4.71e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   19 AMNDRTALVTGANKGIGKHIARVLVAEGLTV---YVGSRDrglgqrAVEEIGA--GARLLVLDVTDLDGIARATTQVDRL 93
Cdd:PRK12742   3 AFTGKKVLVLGGSRGIGAAIVRRFVTDGANVrftYAGSKD------AAERLAQetGATAVQTDSADRDAVIDVVRKSGAL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   94 DVLVNNAGISpSLAPPADTSVEEFRRTYETNVFgvvAVTNAFLPALRRSPHP-RIVNISSgtasltwstnPNPQFTPGSG 172
Cdd:PRK12742  77 DILVVNAGIA-VFGDALELDADDIDRLFKINIH---APYHASVEAARQMPEGgRIIIIGS----------VNGDRMPVAG 142

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 30267738  173 GAAaYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDLNP 216
Cdd:PRK12742 143 MAA-YAASKSALQGMARGLARDFGPRGITINVVQPGPIDTDANP 185
PRK06123 PRK06123
SDR family oxidoreductase;
22-225 5.26e-15

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 72.12  E-value: 5.26e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   22 DRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAV----EEIGAGARLLVLDVTDLDGIARATTQVDR----L 93
Cdd:PRK06123   2 RKVMIITGASRGIGAATALLAAERGYAVCLNYLRNRDAAEAVvqaiRRQGGEALAVAADVADEADVLRLFEAVDRelgrL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   94 DVLVNNAGISPSLAPPADTSVEEFRRTYETNVFGvvavtnAFL---PALRRSPhPR-------IVNISSGTASLTwstnp 163
Cdd:PRK06123  82 DALVNNAGILEAQMRLEQMDAARLTRIFATNVVG------SFLcarEAVKRMS-TRhggrggaIVNVSSMAARLG----- 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30267738  164 npqftpGSGGAAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDLNplaaAAGDDP 225
Cdd:PRK06123 150 ------SPGEYIDYAASKGAIDTMTIGLAKEVAAEGIRVNAVRPGVIYTEIH----ASGGEP 201
PRK05854 PRK05854
SDR family oxidoreductase;
16-219 5.46e-15

SDR family oxidoreductase;


Pssm-ID: 235627 [Multi-domain]  Cd Length: 313  Bit Score: 73.18  E-value: 5.46e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   16 TVVAMNDRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEI-----GAGARLLVLDVTDLDGIA---RAT 87
Cdd:PRK05854   8 TVPDLSGKRAVVTGASDGLGLGLARRLAAAGAEVILPVRNRAKGEAAVAAIrtavpDAKLSLRALDLSSLASVAalgEQL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   88 TQVDR-LDVLVNNAGIspsLAPPA-DTSVEEFRRTYETNVFGVVAVTNAFLPALrRSPHPRIVNISSGTA---SLTWStn 162
Cdd:PRK05854  88 RAEGRpIHLLINNAGV---MTPPErQTTADGFELQFGTNHLGHFALTAHLLPLL-RAGRARVTSQSSIAArrgAINWD-- 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 30267738  163 pNPQFTPGSGGAAAYRSSKAA--LNALTVLYAQTLAEDGFKVNALAPGMRATDLnpLAA 219
Cdd:PRK05854 162 -DLNWERSYAGMRAYSQSKIAvgLFALELDRRSRAAGWGITSNLAHPGVAPTNL--LAA 217
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
20-214 8.08e-15

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 71.58  E-value: 8.08e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   20 MNDRTALVTGANKGIGKHIARVLVAEGLTVYVG------SRDRGLGQRavEEIGAGARLLVLDVTDLDGIARA----TTQ 89
Cdd:PRK12938   1 MSQRIAYVTGGMGGIGTSICQRLHKDGFKVVAGcgpnspRRVKWLEDQ--KALGFDFIASEGNVGDWDSTKAAfdkvKAE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   90 VDRLDVLVNNAGISPSLAPPADTSvEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSgtasltwstnPNPQftP 169
Cdd:PRK12938  79 VGEIDVLVNNAGITRDVVFRKMTR-EDWTAVIDTNLTSLFNVTKQVIDGMVERGWGRIINISS----------VNGQ--K 145

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 30267738  170 GSGGAAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDL 214
Cdd:PRK12938 146 GQFGQTNYSTAKAGIHGFTMSLAQEVATKGVTVNTVSPGYIGTDM 190
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
 22-241 1.08e-14

human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These proteins are members of the SDR family, with a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187601 [Multi-domain]  Cd Length: 250  Bit Score: 71.39  E-value: 1.08e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  22 DRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRG-LGQRAVEEIGAGARLLV---LDVTDLDGIARA----TTQVDRL 93
Cdd:cd05343   6 GRVALVTGASVGIGAAVARALVQHGMKVVGCARRVDkIEALAAECQSAGYPTLFpyqCDLSNEEQILSMfsaiRTQHQGV 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  94 DVLVNNAGIS-PSlaPPADTSVEEFRRTYETNVFGVVAVTNAFLPAL--RRSPHPRIVNISSgtaSLTWSTNPNPQFtpg 170
Cdd:cd05343  86 DVCINNAGLArPE--PLLSGKTEGWKEMFDVNVLALSICTREAYQSMkeRNVDDGHIININS---MSGHRVPPVSVF--- 157

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30267738 171 sggaAAYRSSKAALNALTVLYAQTL--AEDGFKVNALAPGMRATDLnpLAAAAGDDPAEAAQGAARLALL-PDD 241
Cdd:cd05343 158 ----HFYAATKHAVTALTEGLRQELreAKTHIRATSISPGLVETEF--AFKLHDNDPEKAAATYESIPCLkPED 225
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
 26-156 1.13e-14

bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase YdfG;


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 71.33  E-value: 1.13e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   26 LVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEIGAGARLLVLDVTDLDGIARATTQV----DRLDVLVNNAG 101
Cdd:PRK10538   4 LVTGATAGFGECITRRFIQQGHKVIATGRRQERLQELKDELGDNLYIAQLDVRNRAAIEEMLASLpaewRNIDVLVNNAG 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 30267738  102 ISPSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTAS 156
Cdd:PRK10538  84 LALGLEPAHKASVEDWETMIDTNNKGLVYMTRAVLPGMVERNHGHIINIGSTAGS 138
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
 22-208 1.26e-14

1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 71.51  E-value: 1.26e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   22 DRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEIGAGARLLVLdVTDLDG-------IARATTQVDRLD 94
Cdd:PRK12823   8 GKVVVVTGAAQGIGRGVALRAAAEGARVVLVDRSELVHEVAAELRAAGGEALAL-TADLETyagaqaaMAAAVEAFGRID 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   95 VLVNNAGISPSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTaslTWSTNPNPqftpgsgga 174
Cdd:PRK12823  87 VLINNVGGTIWAKPFEEYEEEQIEAEIRRSLFPTLWCCRAVLPHMLAQGGGAIVNVSSIA---TRGINRVP--------- 154

                        170       180       190
                 ....*....|....*....|....*....|....
gi 30267738  175 aaYRSSKAALNALTVLYAQTLAEDGFKVNALAPG 208
Cdd:PRK12823 155 --YSAAKGGVNALTASLAFEYAEHGIRVNAVAPG 186
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 23-208 1.34e-14

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 72.56  E-value: 1.34e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   23 RTALVTGANKGIGKHIARVLVAEGLTVY---VGSRDRGLgQRAVEEIGAGArlLVLDVTDLDGIAR----ATTQVDRLDV 95
Cdd:PRK08261 211 KVALVTGAARGIGAAIAEVLARDGAHVVcldVPAAGEAL-AAVANRVGGTA--LALDITAPDAPARiaehLAERHGGLDI 287

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   96 LVNNAGIS--PSLappADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISS--GTAsltwstnpnpqftpGS 171
Cdd:PRK08261 288 VVHNAGITrdKTL---ANMDEARWDSVLAVNLLAPLRITEALLAAGALGDGGRIVGVSSisGIA--------------GN 350

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 30267738  172 GGAAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPG 208
Cdd:PRK08261 351 RGQTNYAASKAGVIGLVQALAPLLAERGITINAVAPG 387
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
 22-208 1.44e-14

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 71.22  E-value: 1.44e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   22 DRTALVTGANKGIGKHIARVLVAEGLTVYV----GSRDRGLGQRAVEEIGAGARL-LVLDVTDLDGIARATTQVD----R 92
Cdd:PRK12384   2 NQVAVVIGGGQTLGAFLCHGLAEEGYRVAVadinSEKAANVAQEINAEYGEGMAYgFGADATSEQSVLALSRGVDeifgR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   93 LDVLVNNAGISPSlAPPADTSVEEFRRTYETNVFGVvavtnaFLPA-------LRRSPHPRIVNISSGTASLtwstnpnp 165
Cdd:PRK12384  82 VDLLVYNAGIAKA-AFITDFQLGDFDRSLQVNLVGY------FLCArefsrlmIRDGIQGRIIQINSKSGKV-------- 146

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 30267738  166 qftpGSGGAAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPG 208
Cdd:PRK12384 147 ----GSKHNSGYSAAKFGGVGLTQSLALDLAEYGITVHSLMLG 185
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
 21-208 1.81e-14

classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad and domain size of the classical SDRs, but has an atypical NAD-binding motif ([ST]G[GA]XGXXG). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187635 [Multi-domain]  Cd Length: 250  Bit Score: 70.83  E-value: 1.81e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  21 NDRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEIGA--GARL--LVLDVTDLDGIA----RATTQVDR 92
Cdd:cd08930   1 EDKIILITGAAGLIGKAFCKALLSAGARLILADINAPALEQLKEELTNlyKNRViaLELDITSKESIKelieSYLEKFGR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  93 LDVLVNNAGISPSL--APPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISS--GTASLTWSTNPNPQFT 168
Cdd:cd08930  81 IDILINNAYPSPKVwgSRFEEFPYEQWNEVLNVNLGGAFLCSQAFIKLFKKQGKGSIINIASiyGVIAPDFRIYENTQMY 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 30267738 169 pgsgGAAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPG 208
Cdd:cd08930 161 ----SPVEYSVIKAGIIHLTKYLAKYYADTGIRVNAISPG 196
PRK05866 PRK05866
SDR family oxidoreductase;
15-230 2.55e-14

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 70.93  E-value: 2.55e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   15 GTVVAMNDRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEI---GAGARLLVLDVTDLDGI----ARAT 87
Cdd:PRK05866  33 RQPVDLTGKRILLTGASSGIGEAAAEQFARRGATVVAVARREDLLDAVADRItraGGDAMAVPCDLSDLDAVdalvADVE 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   88 TQVDRLDVLVNNAGisPSLAPPADTSVE---EFRRTYETNVFGVVAVTNAFLPAL--RRSPHprIVNISsgtaslTWSTN 162
Cdd:PRK05866 113 KRIGGVDILINNAG--RSIRRPLAESLDrwhDVERTMVLNYYAPLRLIRGLAPGMleRGDGH--IINVA------TWGVL 182

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30267738  163 PN--PQFtpgsggaAAYRSSKAALNALTVLYAQTLAEDGFKVNALA-PGMRATDLNPLAA---AAGDDPAEAAQ 230
Cdd:PRK05866 183 SEasPLF-------SVYNASKAALSAVSRVIETEWGDRGVHSTTLYyPLVATPMIAPTKAydgLPALTADEAAE 249
PRK06482 PRK06482
SDR family oxidoreductase;
23-242 2.64e-14

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 70.53  E-value: 2.64e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   23 RTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEIGAGARLLVLDVTDLDGI----ARATTQVDRLDVLVN 98
Cdd:PRK06482   3 KTWFITGASSGFGRGMTERLLARGDRVAATVRRPDALDDLKARYGDRLWVLQLDVTDSAAVravvDRAFAALGRIDVVVS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   99 NAGISpSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTASLTWStnpnpqftpgsgGAAAYR 178
Cdd:PRK06482  83 NAGYG-LFGAAEELSDAQIRRQIDTNLIGSIQVIRAALPHLRRQGGGRIVQVSSEGGQIAYP------------GFSLYH 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30267738  179 SSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDLNPLAAAAGDDPAEAAQGAARLALLPDDG 242
Cdd:PRK06482 150 ATKWGIEGFVEAVAQEVAPFGIEFTIVEPGPARTNFGAGLDRGAPLDAYDDTPVGDLRRALADG 213
PRK09134 PRK09134
SDR family oxidoreductase;
23-208 4.79e-14

SDR family oxidoreductase;


Pssm-ID: 236389 [Multi-domain]  Cd Length: 258  Bit Score: 69.57  E-value: 4.79e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   23 RTALVTGANKGIGKHIARVLVAEGLTV---YVGSRDRglGQRAVEEIGA-GARLLVL--DVTDLDG----IARATTQVDR 92
Cdd:PRK09134  10 RAALVTGAARRIGRAIALDLAAHGFDVavhYNRSRDE--AEALAAEIRAlGRRAVALqaDLADEAEvralVARASAALGP 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   93 LDVLVNNAGI--SPSLappADTSVEEFRRTYETNVFGVVAVTNAFLPALrrsPHPR---IVNIssgTASLTWstNPNPQF 167
Cdd:PRK09134  88 ITLLVNNASLfeYDSA---ASFTRASWDRHMATNLRAPFVLAQAFARAL---PADArglVVNM---IDQRVW--NLNPDF 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 30267738  168 tpgsggaAAYRSSKAALNALTVLYAQTLAEDgFKVNALAPG 208
Cdd:PRK09134 157 -------LSYTLSKAALWTATRTLAQALAPR-IRVNAIGPG 189
PRK08703 PRK08703
SDR family oxidoreductase;
19-208 5.26e-14

SDR family oxidoreductase;


Pssm-ID: 169556 [Multi-domain]  Cd Length: 239  Bit Score: 69.19  E-value: 5.26e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   19 AMNDRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEIGAGA-------RLLVLDVTDLD------GIAR 85
Cdd:PRK08703   3 TLSDKTILVTGASQGLGEQVAKAYAAAGATVILVARHQKKLEKVYDAIVEAGhpepfaiRFDLMSAEEKEfeqfaaTIAE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   86 ATTqvDRLDVLVNNAGISPSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSgtaslTWSTNPNP 165
Cdd:PRK08703  83 ATQ--GKLDGIVHCAGYFYALSPLDFQTVAEWVNQYRINTVAPMGLTRALFPLLKQSPDASVIFVGE-----SHGETPKA 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 30267738  166 QFtpgsggaAAYRSSKAALNALTVLYAQTLAEDG-FKVNALAPG 208
Cdd:PRK08703 156 YW-------GGFGASKAALNYLCKVAADEWERFGnLRANVLVPG 192
haloalcohol_DH_SDR_c-like cd05361
haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. ...
 23-207 6.12e-14

haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. Haloalcohol dehalogenase show low sequence similarity to short-chain dehydrogenases/reductases (SDRs). Like the SDRs, haloalcohol dehalogenases have a conserved catalytic triad (Ser-Tyr-Lys/Arg), and form a Rossmann fold. However, the normal classical SDR NAD(P)-binding motif (TGXXGXG) and NAD-binding function is replaced with a halide binding site, allowing the enzyme to catalyze a dehalogenation reaction. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187619 [Multi-domain]  Cd Length: 242  Bit Score: 69.14  E-value: 6.12e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  23 RTALVTGANKGIGKHIARVLVAEGLTVYvgSRDRGLGQRAVEEIGAGA--RLLVLDVTDLDGIARATTQV-DRLDVLVNN 99
Cdd:cd05361   2 SIALVTHARHFAGPASAEALTEDGYTVV--CHDASFADAAERQAFESEnpGTKALSEQKPEELVDAVLQAgGAIDVLVSN 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738 100 AGISPSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTASLTWSTNPnpqftpgsggaaAYRS 179
Cdd:cd05361  80 DYIPRPMNPIDGTSEADIRQAFEALSIFPFALLQAAIAQMKKAGGGSIIFITSAVPKKPLAYNS------------LYGP 147

                       170       180
                ....*....|....*....|....*...
gi 30267738 180 SKAALNALTVLYAQTLAEDGFKVNALAP 207
Cdd:cd05361 148 ARAAAVALAESLAKELSRDNILVYAIGP 175
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
 20-224 6.94e-14

cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB) is a classical SDR, it is of particular importance for its role in the degradation of biphenyl/polychlorinated biphenyls(PCBs); PCBs are a significant source of environmental contamination. This subgroup also includes Pseudomonas putida F1 cis-biphenyl-1,2-dihydrodiol-1,2-dehydrogenase (aka cis-benzene glycol dehydrogenase, encoded by the bnzE gene), which participates in benzene metabolism. In addition it includes Pseudomonas sp. C18 putative 1,2-dihydroxy-1,2-dihydronaphthalene dehydrogenase (aka dibenzothiophene dihydrodiol dehydrogenase, encoded by the doxE gene) which participates in an upper naphthalene catabolic pathway. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187606 [Multi-domain]  Cd Length: 257  Bit Score: 69.30  E-value: 6.94e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  20 MNDRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEIGAGARLLVLDVTDLD----GIARATTQVDRLDV 95
Cdd:cd05348   2 LKGEVALITGGGSGLGRALVERFVAEGAKVAVLDRSAEKVAELRADFGDAVVGVEGDVRSLAdnerAVARCVERFGKLDC 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  96 LVNNAGI---SPSLA-PPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRsphprivniSSGTASLTWStnpNPQFTPGs 171
Cdd:cd05348  82 FIGNAGIwdySTSLVdIPEEKLDEAFDELFHINVKGYILGAKAALPALYA---------TEGSVIFTVS---NAGFYPG- 148

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 30267738 172 GGAAAYRSSKAALNALTVLYAQTLAEDgFKVNALAPGMRATDLNPLAAAAGDD 224
Cdd:cd05348 149 GGGPLYTASKHAVVGLVKQLAYELAPH-IRVNGVAPGGMVTDLRGPASLGQGE 200
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 23-208 1.43e-13

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 68.27  E-value: 1.43e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   23 RTALVTGAN--KGIGKHIARVLVAEGLTV---YVGSRDRGLG-----------QRAVEEIGAGARLLVLDVTDLDG---- 82
Cdd:PRK12859   7 KVAVVTGVSrlDGIGAAICKELAEAGADIfftYWTAYDKEMPwgvdqdeqiqlQEELLKNGVKVSSMELDLTQNDApkel 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   83 IARATTQVDRLDVLVNNAGISPSLAPPADTSvEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTasltwSTN 162
Cdd:PRK12859  87 LNKVTEQLGYPHILVNNAAYSTNNDFSNLTA-EELDKHYMVNVRATTLLSSQFARGFDKKSGGRIINMTSGQ-----FQG 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 30267738  163 PNPqftpgsgGAAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPG 208
Cdd:PRK12859 161 PMV-------GELAYAATKGAIDALTSSLAAEVAHLGITVNAINPG 199
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 20-214 1.65e-13

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 68.21  E-value: 1.65e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   20 MNDRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQ----RAVEEIGAGARLLVLDVTDLDG---IARATTQV-D 91
Cdd:PRK06077   4 LKDKVVVVTGSGRGIGRAIAVRLAKEGSLVVVNAKKRAEEMnetlKMVKENGGEGIGVLADVSTREGcetLAKATIDRyG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   92 RLDVLVNNAGI---SPSLAppADTSVEEfrRTYETNVFGVVAVTNAFLPALRRSphPRIVNISSgTASLTwstnPNPqft 168
Cdd:PRK06077  84 VADILVNNAGLglfSPFLN--VDDKLID--KHISTDFKSVIYCSQELAKEMREG--GAIVNIAS-VAGIR----PAY--- 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 30267738  169 pgsgGAAAYRSSKAALNALTVLYAQTLAEDgFKVNALAPGMRATDL 214
Cdd:PRK06077 150 ----GLSIYGAMKAAVINLTKYLALELAPK-IRVNAIAPGFVKTKL 190
FabI COG0623
Enoyl-[acyl-carrier-protein] reductase FabI [Lipid transport and metabolism]; Enoyl- ...
 20-221 1.98e-13

Enoyl-[acyl-carrier-protein] reductase FabI [Lipid transport and metabolism]; Enoyl-[acyl-carrier-protein] reductase FabI is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440388 [Multi-domain]  Cd Length: 254  Bit Score: 67.74  E-value: 1.98e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  20 MNDRTALVTGA--NKGIGKHIARVLVAEGLTV---YVGSRDRGLGQRAVEEIGAgARLLVLDVTDLDGIARATTQV---- 90
Cdd:COG0623   3 LKGKRGLITGVanDRSIAWGIAKALHEEGAELaftYQGEALKKRVEPLAEELGS-ALVLPCDVTDDEQIDALFDEIkekw 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  91 DRLDVLVNNAGISPSLA---PPADTSVEEFRRTYETNVFGVVAVTNAFLPALRrsPHPRIVNISSGTASLTWstnpnpqf 167
Cdd:COG0623  82 GKLDFLVHSIAFAPKEElggRFLDTSREGFLLAMDISAYSLVALAKAAEPLMN--EGGSIVTLTYLGAERVV-------- 151

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 30267738 168 tPGSG--GAAayrssKAALNALTVLYAQTLAEDGFKVNALAPGMRATdlnpLAAAA 221
Cdd:COG0623 152 -PNYNvmGVA-----KAALEASVRYLAADLGPKGIRVNAISAGPIKT----LAASG 197
PRK08589 PRK08589
SDR family oxidoreductase;
20-228 2.27e-13

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 67.88  E-value: 2.27e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   20 MNDRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLgQRAVEEI---GAGARLLVLDVTDLDGIARATTQVD----R 92
Cdd:PRK08589   4 LENKVAVITGASTGIGQASAIALAQEGAYVLAVDIAEAV-SETVDKIksnGGKAKAYHVDISDEQQVKDFASEIKeqfgR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   93 LDVLVNNAGISPSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPaLRRSPHPRIVNISSgtasltwstnpnpqftpGSG 172
Cdd:PRK08589  83 VDVLFNNAGVDNAAGRIHEYPVDVFDKIMAVDMRGTFLMTKMLLP-LMMEQGGSIINTSS-----------------FSG 144

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30267738  173 GAA-----AYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDL-NPLAAAAGDDPAEA 228
Cdd:PRK08589 145 QAAdlyrsGYNAAKGAVINFTKSIAIEYGRDGIRANAIAPGTIETPLvDKLTGTSEDEAGKT 206
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
 24-242 2.98e-13

alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, which catalyzes the NAD-dependent oxidoreduction of hydroxysteroids, is a dimeric member of the classical SDR family. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187589 [Multi-domain]  Cd Length: 250  Bit Score: 67.52  E-value: 2.98e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  24 TALVTGANKGIGKHIARVLVAEGLTVYvgsrdrGLGQRAVEEIGagarllvlDVTDLDGIARATTQV-----DRLDVLVN 98
Cdd:cd05328   1 TIVITGAASGIGAATAELLEDAGHTVI------GIDLREADVIA--------DLSTPEGRAAAIADVlarcsGVLDGLVN 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  99 NAGISPSLapPADTSVEefrrtyeTNVFGVVAVTNAFLPALRRSPHPRIVNISSgTASLTWSTNPNPQFTPGSGGA---- 174
Cdd:cd05328  67 CAGVGGTT--VAGLVLK-------VNYFGLRALMEALLPRLRKGHGPAAVVVSS-IAGAGWAQDKLELAKALAAGTeara 136

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738 175 ------------AAYRSSKAALNALTVLYAQT-LAEDGFKVNALAPG---------MRATDLNPLAAAAGDDP----AEA 228
Cdd:cd05328 137 valaehagqpgyLAYAGSKEALTVWTRRRAATwLYGAGVRVNTVAPGpvetpilqaFLQDPRGGESVDAFVTPmgrrAEP 216

                       250
                ....*....|....
gi 30267738 229 AQGAARLALLPDDG 242
Cdd:cd05328 217 DEIAPVIAFLASDA 230
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
 19-212 3.50e-13

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 67.21  E-value: 3.50e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   19 AMNDRTALVTGANKGIGKHIARVLVAEGLTVYVgsrdrgLGQ-----RAV-EEI----GAGARLLVLD---VTDLDGIAR 85
Cdd:PRK08945   9 LLKDRIILVTGAGDGIGREAALTYARHGATVIL------LGRteeklEAVyDEIeaagGPQPAIIPLDlltATPQNYQQL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   86 ATT---QVDRLDVLVNNAGISPSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTasltwstn 162
Cdd:PRK08945  83 ADTieeQFGRLDGVLHNAGLLGELGPMEQQDPEVWQDVMQVNVNATFMLTQALLPLLLKSPAASLVFTSSSV-------- 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30267738  163 pnpqftpGSGGAA---AYRSSKAALNALtvlyAQTLAED----GFKVNALAPG-----MRAT 212
Cdd:PRK08945 155 -------GRQGRAnwgAYAVSKFATEGM----MQVLADEyqgtNLRVNCINPGgtrtaMRAS 205
PLN02253 PLN02253
xanthoxin dehydrogenase
 23-214 8.10e-13

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 66.39  E-value: 8.10e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   23 RTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEIGAGARLLVL--DVTDLDGIARATT-QVDR---LDVL 96
Cdd:PLN02253  19 KVALVTGGATGIGESIVRLFHKHGAKVCIVDLQDDLGQNVCDSLGGEPNVCFFhcDVTVEDDVSRAVDfTVDKfgtLDIM 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   97 VNNAGIS-PSLAPPADTSVEEFRRTYETNVFGV-VAVTNA---FLPALRRSphprIVNISSGTASLtwstnpnpqftpGS 171
Cdd:PLN02253  99 VNNAGLTgPPCPDIRNVELSEFEKVFDVNVKGVfLGMKHAariMIPLKKGS----IVSLCSVASAI------------GG 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 30267738  172 GGAAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDL 214
Cdd:PLN02253 163 LGPHAYTGSKHAVLGLTRSVAAELGKHGIRVNCVSPYAVPTAL 205
HSDL2_SDR_c cd09762
human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup ...
 20-207 1.02e-12

human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup includes human HSDL2 and related protens. These are members of the classical SDR family, with a canonical Gly-rich NAD-binding motif and the typical YXXXK active site motif. However, the rest of the catalytic tetrad is not strongly conserved. HSDL2 may play a part in fatty acid metabolism, as it is found in peroxisomes. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187663 [Multi-domain]  Cd Length: 243  Bit Score: 65.93  E-value: 1.02e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  20 MNDRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRG----------LGQRAVEEIGAGARLLVLDVTDLDGIARATTQ 89
Cdd:cd09762   1 LAGKTLFITGASRGIGKAIALKAARDGANVVIAAKTAEphpklpgtiyTAAEEIEAAGGKALPCIVDIRDEDQVRAAVEK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  90 -VDR---LDVLVNNAGiSPSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISsgtasltwstnPNP 165
Cdd:cd09762  81 aVEKfggIDILVNNAS-AISLTGTLDTPMKRYDLMMGVNTRGTYLCSKACLPYLKKSKNPHILNLS-----------PPL 148

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 30267738 166 QFTPG-SGGAAAYRSSKAALNALTVLYAQTLAEDGFKVNALAP 207
Cdd:cd09762 149 NLNPKwFKNHTAYTMAKYGMSMCVLGMAEEFKPGGIAVNALWP 191
ENR_SDR cd05372
Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ...
 24-208 1.45e-12

Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ENRs includes Escherichia coli ENR. ENR catalyzes the NAD(P)H-dependent reduction of enoyl-ACP in the last step of fatty acid biosynthesis. De novo fatty acid biosynthesis is catalyzed by the fatty acid synthetase complex, through the serial addition of 2-carbon subunits. In bacteria and plants,ENR catalyzes one of six synthetic steps in this process. Oilseed rape ENR, and also apparently the NADH-specific form of Escherichia coli ENR, is tetrameric. Although similar to the classical SDRs, this group does not have the canonical catalytic tetrad, nor does it have the typical Gly-rich NAD-binding pattern. Such so-called divergent SDRs have a GXXXXXSXA NAD-binding motif and a YXXMXXXK (or YXXXMXXXK) active site motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187630 [Multi-domain]  Cd Length: 250  Bit Score: 65.30  E-value: 1.45e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  24 TALVTGA--NKGIGKHIARVLVAEGLTV---YVGSRDRGLGQRAVEEIGAGARLLVLDVTDLDGI----ARATTQVDRLD 94
Cdd:cd05372   3 RILITGIanDRSIAWGIAKALHEAGAELaftYQPEALRKRVEKLAERLGESALVLPCDVSNDEEIkelfAEVKKDWGKLD 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  95 VLVNNAGISPSLA---PPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRsphprivnissGTASLTWSTNPNPQFTPGS 171
Cdd:cd05372  83 GLVHSIAFAPKVQlkgPFLDTSRKGFLKALDISAYSLVSLAKAALPIMNP-----------GGSIVTLSYLGSERVVPGY 151

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 30267738 172 GGAAayrSSKAALNALTVLYAQTLAEDGFKVNALAPG 208
Cdd:cd05372 152 NVMG---VAKAALESSVRYLAYELGRKGIRVNAISAG 185
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
 24-196 1.53e-12

classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an incomplete match to the canonical glycine rich NAD-binding motif and lacks the typical active site tetrad (instead of the critical active site Tyr, it has Phe, but contains the nearby Lys). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187631 [Multi-domain]  Cd Length: 238  Bit Score: 65.10  E-value: 1.53e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  24 TALVTGANKGIGKHIARVLVAEGLTV-YVGSRDRGLGQRAVEEI---GAGARLLVLDVTDLDGIARATTQVDR----LDV 95
Cdd:cd05373   1 VAAVVGAGDGLGAAIARRFAAEGFSVaLAARREAKLEALLVDIIrdaGGSAKAVPTDARDEDEVIALFDLIEEeigpLEV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  96 LVNNAGiSPSLAPPADTSVEEFRRTYETNVFGvvavtnAFLPAlrRSPHPRIVNISSGTASLTWSTNPnpqfTPGSGGAA 175
Cdd:cd05373  81 LVYNAG-ANVWFPILETTPRVFEKVWEMAAFG------GFLAA--REAAKRMLARGRGTIIFTGATAS----LRGRAGFA 147

                       170       180
                ....*....|....*....|.
gi 30267738 176 AYRSSKAALNALtvlyAQTLA 196
Cdd:cd05373 148 AFAGAKFALRAL----AQSMA 164
PRK09009 PRK09009
SDR family oxidoreductase;
26-257 1.64e-12

SDR family oxidoreductase;


Pssm-ID: 181609 [Multi-domain]  Cd Length: 235  Bit Score: 65.08  E-value: 1.64e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   26 LVTGANKGIGKhiarVLVAEGLTVYVGSRDRGLGQRAVEEIGA-GARLLVLDVTDLDGIARATTQVDRLDVLVNNAGI-- 102
Cdd:PRK09009   4 LIVGGSGGIGK----AMVKQLLERYPDATVHATYRHHKPDFQHdNVQWHALDVTDEAEIKQLSEQFTQLDWLINCVGMlh 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  103 SPSLAPPADTS---VEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTASLtwSTNpnpQFtpgsGGAAAYRS 179
Cdd:PRK09009  80 TQDKGPEKSLQaldADFFLQNITLNTLPSLLLAKHFTPKLKQSESAKFAVISAKVGSI--SDN---RL----GGWYSYRA 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  180 SKAALN----ALTVLYAQTLaEDGFkVNALAPGMRATDLN-PLAAAAGDD----PAEAAQGAARL--ALLPDDgpTGGFF 248
Cdd:PRK09009 151 SKAALNmflkTLSIEWQRSL-KHGV-VLALHPGTTDTALSkPFQQNVPKGklftPEYVAQCLLGIiaNATPAQ--SGSFL 226


                 ....*....
gi 30267738  249 SWDGTPVPW 257
Cdd:PRK09009 227 AYDGETLPW 235
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
 20-225 1.90e-12

Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related proteins have a canonical classical SDR nucleotide-binding motif and active site tetrad. They are predicted oxoacyl-(acyl carrier protein/ACP) reductases. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187599 [Multi-domain]  Cd Length: 236  Bit Score: 64.91  E-value: 1.90e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  20 MNDRTALVTGANKGIGKHIARVLVAEGLTVYVGSRD----RGLGQRAVEEIGAGARLLVLDVTDLDG------IARATTQ 89
Cdd:cd05340   2 LNDRIILVTGASDGIGREAALTYARYGATVILLGRNeeklRQVADHINEEGGRQPQWFILDLLTCTSencqqlAQRIAVN 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  90 VDRLDVLVNNAGISPSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSgtasltwstnpnpqfTP 169
Cdd:cd05340  82 YPRLDGVLHNAGLLGDVCPLSEQNPQVWQDV*QVNVNATFMLTQALLPLLLKSDAGSLVFTSS---------------SV 146

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738 170 GSGGAA---AYRSSKAALNALTVLYAQTLAEDGFKVNALAPGmrATDLNPLAAA-AGDDP 225
Cdd:cd05340 147 GRQGRAnwgAYAVSKFATEGL*QVLADEYQQRNLRVNCINPG--GTRTAMRASAfPTEDP 204
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
 25-229 2.16e-12

sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain dehydrogenase/reductase family. The enzyme catalyzes the last step in the biosynthesis of tetrahydrobiopterin. A similar enzyme in Bacillus cereus was isolated for its ability to convert benzil to (S)-benzoin, a property sepiapterin reductase also shares. Cutoff scores for this model are set such that benzil reductase scores between trusted and noise cutoffs.


Pssm-ID: 273660 [Multi-domain]  Cd Length: 256  Bit Score: 64.93  E-value: 2.16e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738    25 ALVTGANKGIGKHIARVLV----AEGLTVYVGSRDRGLGQRAVEEIGAGARLLVLDVTDLDGIARATTQ----------- 89
Cdd:TIGR01500   3 CLVTGASRGFGRTIAQELAkclkSPGSVLVLSARNDEALRQLKAEIGAERSGLRVVRVSLDLGAEAGLEqllkalrelpr 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738    90 ---VDRLdVLVNNAGISPSLAPPAD--TSVEEFRRTYETNVFGVVAVTNAFLPALRRSPH-PR-IVNISSGTASLTWStn 162
Cdd:TIGR01500  83 pkgLQRL-LLINNAGTLGDVSKGFVdlSDSTQVQNYWALNLTSMLCLTSSVLKAFKDSPGlNRtVVNISSLCAIQPFK-- 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30267738   163 pnpqftpgsgGAAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDLNPLAAAAGDDPAEAA 229
Cdd:TIGR01500 160 ----------GWALYCAGKAARDMLFQVLALEEKNPNVRVLNYAPGVLDTDMQQQVREESVDPDMRK 216
PRK06483 PRK06483
dihydromonapterin reductase; Provisional
 23-239 2.64e-12

dihydromonapterin reductase; Provisional


Pssm-ID: 180586 [Multi-domain]  Cd Length: 236  Bit Score: 64.57  E-value: 2.64e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   23 RTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEigAGARLLVLDVTDLDG----IARATTQVDRLDVLVN 98
Cdd:PRK06483   3 APILITGAGQRIGLALAWHLLAQGQPVIVSYRTHYPAIDGLRQ--AGAQCIQADFSTNAGimafIDELKQHTDGLRAIIH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   99 NAgiSPSLA-PPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPR--IVNISSGTASltwstnpnpqftPGSGGAA 175
Cdd:PRK06483  81 NA--SDWLAeKPGAPLADVLARMMQIHVNAPYLLNLALEDLLRGHGHAAsdIIHITDYVVE------------KGSDKHI 146

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30267738  176 AYRSSKAALNALTVLYAQTLAEDgFKVNALAPGMraTDLNPlaaaaGDDPAEAAQGAARlALLP 239
Cdd:PRK06483 147 AYAASKAALDNMTLSFAAKLAPE-VKVNSIAPAL--ILFNE-----GDDAAYRQKALAK-SLLK 201
SDR_subfam_2 TIGR04504
SDR family mycofactocin-dependent oxidoreductase; Members of this protein subfamily are ...
 23-221 2.99e-12

SDR family mycofactocin-dependent oxidoreductase; Members of this protein subfamily are putative oxidoreductases belonging to the larger SDR family. All members occur in genomes that encode a cassette for the biosynthesis of mycofactocin, a proposed electron carrier of a novel redox pool. Characterized members of this family are described as NDMA-dependent, meaning that a blue aniline dye serving as an artificial electron acceptor is required for members of this family to cycle in vitro, since the bound NAD residue is not exchangeable. This family resembles TIGR03971 most closely in the N-terminal region, consistent with the published hypothesis of NAD interaction with mycofactocin. See EC 1.1.99.36. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 275297 [Multi-domain]  Cd Length: 259  Bit Score: 64.65  E-value: 2.99e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738    23 RTALVTGANKGIGKHIARVLVAEG---LTVYVGSRDRGLG---------QRAVEEIGAGARLLVLDVTDLDGIARATTQV 90
Cdd:TIGR04504   2 RVALVTGAARGIGAATVRRLAADGwrvVAVDLCADDPAVGyplatraelDAVAAACPDQVLPVIADVRDPAALAAAVALA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738    91 D----RLDVLVNNAGISPSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHP---RIVNISSGTAsltwstnp 163
Cdd:TIGR04504  82 VerwgRLDAAVAAAGVIAGGRPLWETTDAELDLLLDVNLRGVWNLARAAVPAMLARPDPrggRFVAVASAAA-------- 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 30267738   164 npqfTPGSGGAAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDLnpLAAAA 221
Cdd:TIGR04504 154 ----TRGLPHLAAYCAAKHAVVGLVRGLAADLGGTGVTANAVSPGSTRTAM--LAATA 205
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
24-155 3.11e-12

Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 65.00  E-value: 3.11e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  24 TALVTGANKGIGKHIARVLVAEGLTVYVGsrDRGLGQRAVEEIGAGARLLVLDVTDLDGIARATTQVdrlDVLVNnagis 103
Cdd:COG0451   1 RILVTGGAGFIGSHLARRLLARGHEVVGL--DRSPPGAANLAALPGVEFVRGDLRDPEALAAALAGV---DAVVH----- 70

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 30267738 104 psLAPPADTSVEEFRRTYETNVFGVVAVtnafLPALRRSPHPRIVNISSGTA 155
Cdd:COG0451  71 --LAAPAGVGEEDPDETLEVNVEGTLNL----LEAARAAGVKRFVYASSSSV 116
PRK07831 PRK07831
SDR family oxidoreductase;
20-207 3.29e-12

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 64.67  E-value: 3.29e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   20 MNDRTALVTGA-NKGIGKHIARVLVAEGLTVYVGSR-DRGLGQrAVEEIGAGARL-----LVLDVTDLDG----IARATT 88
Cdd:PRK07831  15 LAGKVVLVTAAaGTGIGSATARRALEEGARVVISDIhERRLGE-TADELAAELGLgrveaVVCDVTSEAQvdalIDAAVE 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   89 QVDRLDVLVNNAGISPSlAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHP-RIVNISSgtaSLTWStnpnpqf 167
Cdd:PRK07831  94 RLGRLDVLVNNAGLGGQ-TPVVDMTDDEWSRVLDVTLTGTFRATRAALRYMRARGHGgVIVNNAS---VLGWR------- 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 30267738  168 tpGSGGAAAYRSSKAALNALTVLYAQTLAEDGFKVNALAP 207
Cdd:PRK07831 163 --AQHGQAHYAAAKAGVMALTRCSALEAAEYGVRINAVAP 200
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
 19-214 3.63e-12

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 64.39  E-value: 3.63e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   19 AMNDRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEI---GAGARLLVLDVTDLDGIARATTQVDR--- 92
Cdd:PRK08085   6 SLAGKNILITGSAQGIGFLLATGLAEYGAEIIINDITAERAELAVAKLrqeGIKAHAAPFNVTHKQEVEAAIEHIEKdig 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   93 -LDVLVNNAGISPSlAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTASLTWSTnpnpqFTPgs 171
Cdd:PRK08085  86 pIDVLINNAGIQRR-HPFTEFPEQEWNDVIAVNQTAVFLVSQAVARYMVKRQAGKIINICSMQSELGRDT-----ITP-- 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 30267738  172 ggaaaYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDL 214
Cdd:PRK08085 158 -----YAASKGAVKMLTRGMCVELARHNIQVNGIAPGYFKTEM 195
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
 20-212 3.94e-12

Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine peroxisomal carbonyl reductase and similar proteins. The porcine enzyme efficiently reduces retinals. This subgroup also includes human dehydrogenase/reductase (SDR family) member 4 (DHRS4), and human DHRS4L1. DHRS4 is a peroxisomal enzyme with 3beta-hydroxysteroid dehydrogenase activity; it catalyzes the reduction of 3-keto-C19/C21-steroids into 3beta-hydroxysteroids more efficiently than it does the retinal reduction. The human DHRS4 gene cluster contains DHRS4, DHRS4L2 and DHRS4L1. DHRS4L2 and DHRS4L1 are paralogs of DHRS4, DHRS4L2 being the most recent member. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187641 [Multi-domain]  Cd Length: 256  Bit Score: 64.49  E-value: 3.94e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  20 MNDRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEI-GAGARLL--VLDVTDLDG----IARATTQVDR 92
Cdd:cd08936   8 LANKVALVTASTDGIGLAIARRLAQDGAHVVVSSRKQQNVDRAVATLqGEGLSVTgtVCHVGKAEDrerlVATAVNLHGG 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  93 LDVLVNNAGISPSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTAsltwsTNPNPQFTPgsg 172
Cdd:cd08936  88 VDILVSNAAVNPFFGNILDSTEEVWDKILDVNVKATALMTKAVVPEMEKRGGGSVVIVSSVAA-----FHPFPGLGP--- 159

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 30267738 173 gaaaYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRAT 212
Cdd:cd08936 160 ----YNVSKTALLGLTKNLAPELAPRNIRVNCLAPGLIKT 195
RhaD COG3347
Rhamnose utilisation protein RhaD, predicted bifunctional aldolase and dehydrogenase ...
 23-187 4.96e-12

Rhamnose utilisation protein RhaD, predicted bifunctional aldolase and dehydrogenase [Carbohydrate transport and metabolism];


Pssm-ID: 442576 [Multi-domain]  Cd Length: 674  Bit Score: 65.32  E-value: 4.96e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  23 RTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEIGAGARLLVLDVTDLDGIARATTQVDR---------L 93
Cdd:COG3347 426 RVALVTGGAGGIGRATAARLAAEGAAVVVADLDGEAAEAAAAELGGGYGADAVDATDVDVTAEAAVAAAFgfagldiggS 505

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  94 DVLVNNAGISPSlAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSphpRIVNISSGtasltwstNPNPQFTPGSGG 173
Cdd:COG3347 506 DIGVANAGIASS-SPEEETRLSFWLNNFAHLSTGQFLVARAAFQGTGGQ---GLGGSSVF--------AVSKNAAAAAYG 573

                       170
                ....*....|....
gi 30267738 174 AAAYRSSKAALNAL 187
Cdd:COG3347 574 AAAAATAKAAAQHL 587
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 20-214 8.78e-12

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 63.06  E-value: 8.78e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   20 MNDRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEI---GAGARLLVLDVTDLDGIARATTQV----DR 92
Cdd:PRK08217   3 LKDKVIVITGGAQGLGRAMAEYLAQKGAKLALIDLNQEKLEEAVAECgalGTEVRGYAANVTDEEDVEATFAQIaedfGQ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   93 LDVLVNNAGI-SPSLAPPADT-------SVEEFRRTYETNVFGVVAVT-NAFLPALRRSPHPRIVNISSGTASltwstnp 163
Cdd:PRK08217  83 LNGLINNAGIlRDGLLVKAKDgkvtskmSLEQFQSVIDVNLTGVFLCGrEAAAKMIESGSKGVIINISSIARA------- 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 30267738  164 npqftpGSGGAAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDL 214
Cdd:PRK08217 156 ------GNMGQTNYSASKAGVAAMTVTWAKELARYGIRVAAIAPGVIETEM 200
PRK07023 PRK07023
SDR family oxidoreductase;
25-214 1.21e-11

SDR family oxidoreductase;


Pssm-ID: 180796 [Multi-domain]  Cd Length: 243  Bit Score: 62.72  E-value: 1.21e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   25 ALVTGANKGIGKHIARVLVAEGLTVYVGSRDRG--LGQRAveeigaGARL--LVLDVTDLDGIAR--ATTQVDRLD---- 94
Cdd:PRK07023   4 AIVTGHSRGLGAALAEQLLQPGIAVLGVARSRHpsLAAAA------GERLaeVELDLSDAAAAAAwlAGDLLAAFVdgas 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   95 --VLVNNAGISPSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTASltwstNPNPqftpgsg 172
Cdd:PRK07023  78 rvLLINNAGTVEPIGPLATLDAAAIARAVGLNVAAPLMLTAALAQAASDAAERRILHISSGAAR-----NAYA------- 145

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 30267738  173 GAAAYRSSKAALNaltvLYAQTLAEDG---FKVNALAPGMRATDL 214
Cdd:PRK07023 146 GWSVYCATKAALD----HHARAVALDAnraLRIVSLAPGVVDTGM 186
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
20-239 2.33e-11

2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 62.23  E-value: 2.33e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   20 MNDRTALVTGANKGIGKHIARVLVAEGL-TVYVGSRDRGLGQRAVEEIGAGARLLVLDVTDLDGI----ARATTQVDRLD 94
Cdd:PRK12481   6 LNGKVAIITGCNTGLGQGMAIGLAKAGAdIVGVGVAEAPETQAQVEALGRKFHFITADLIQQKDIdsivSQAVEVMGHID 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   95 VLVNNAGISPSlappadTSVEEFRRTYETNVFGVVAVTNAFLPA------LRRSPHPRIVNISSgtaSLTWStnpnpqft 168
Cdd:PRK12481  86 ILINNAGIIRR------QDLLEFGNKDWDDVININQKTVFFLSQavakqfVKQGNGGKIINIAS---MLSFQ-------- 148

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30267738  169 pGSGGAAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDlNPLAAAagddpAEAAQGAARLALLP 239
Cdd:PRK12481 149 -GGIRVPSYTASKSAVMGLTRALATELSQYNINVNAIAPGYMATD-NTAALR-----ADTARNEAILERIP 212
human_WWOX_like_SDR_c-like cd09809
human WWOX (WW domain-containing oxidoreductase)-like, classical (c)-like SDRs; Classical-like ...
 22-215 4.40e-11

human WWOX (WW domain-containing oxidoreductase)-like, classical (c)-like SDRs; Classical-like SDR domain of human WWOX and related proteins. Proteins in this subfamily share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187669 [Multi-domain]  Cd Length: 284  Bit Score: 61.46  E-value: 4.40e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  22 DRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEIG-----AGARLLVLDVTDLDGIARAT----TQVDR 92
Cdd:cd09809   1 GKVIIITGANSGIGFETARSFALHGAHVILACRNMSRASAAVSRILeewhkARVEAMTLDLASLRSVQRFAeafkAKNSP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  93 LDVLVNNAGIspsLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTASLT--WSTNPNPQFTPG 170
Cdd:cd09809  81 LHVLVCNAAV---FALPWTLTEDGLETTFQVNHLGHFYLVQLLEDVLRRSAPARVIVVSSESHRFTdlPDSCGNLDFSLL 157

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 30267738 171 SGGAAAYRSSKAALNA--LTVLYAQTLAE----DGFKVNALAPG-MRATDLN 215
Cdd:cd09809 158 SPPKKKYWSMLAYNRAklCNILFSNELHRrlspRGITSNSLHPGnMMYSSIH 209
PRK09135 PRK09135
pteridine reductase; Provisional
 20-208 8.19e-11

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 60.33  E-value: 8.19e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   20 MNDRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRA-VEEIGAG----ARLLVLDVTDLDG----IARATTQV 90
Cdd:PRK09135   4 DSAKVALITGGARRIGAAIARTLHAAGYRVAIHYHRSAAEADAlAAELNALrpgsAAALQADLLDPDAlpelVAACVAAF 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   91 DRLDVLVNNAGispSLAPpadTSVEEFRRTYETNVFGVVA-----VTNAFLPALRRSpHPRIVNISSGTAsltwsTNPNP 165
Cdd:PRK09135  84 GRLDALVNNAS---SFYP---TPLGSITEAQWDDLFASNLkapffLSQAAAPQLRKQ-RGAIVNITDIHA-----ERPLK 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 30267738  166 QFTpgsggaaAYRSSKAALNALTVLYAQTLAEDgFKVNALAPG 208
Cdd:PRK09135 152 GYP-------VYCAAKAALEMLTRSLALELAPE-VRVNAVAPG 186
PRK07576 PRK07576
short chain dehydrogenase; Provisional
 23-236 1.19e-10

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 59.97  E-value: 1.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   23 RTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEIG-AGARLL--VLDVTDLDGIARATTQVDR----LDV 95
Cdd:PRK07576  10 KNVVVVGGTSGINLGIAQAFARAGANVAVASRSQEKVDAAVAQLQqAGPEGLgvSADVRDYAAVEAAFAQIADefgpIDV 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   96 LVNNAGiSPSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRsPHPRIVNISSGTAsltwsTNPnpqfTPGSGGAA 175
Cdd:PRK07576  90 LVSGAA-GNFPAPAAGMSANGFKTVVDIDLLGTFNVLKAAYPLLRR-PGASIIQISAPQA-----FVP----MPMQAHVC 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30267738  176 AyrsSKAALNALTvlyaQTLA----EDGFKVNALAPGmratdlnplaaaagddPAEAAQGAARLA 236
Cdd:PRK07576 159 A---AKAGVDMLT----RTLAlewgPEGIRVNSIVPG----------------PIAGTEGMARLA 200
DR_C-13_KR_SDR_c_like cd08951
daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically ...
 26-248 1.40e-10

daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically important therapeutic compound used in some cancer treatments. Daunorubicin C-13 ketoreductase is member of the classical SDR family with a canonical glycine-rich NAD(P)-binding motif, but lacking a complete match to the active site tetrad characteristic of this group. The critical Tyr, plus the Lys and upstream Asn are present, but the catalytic Ser is replaced, generally by Gln. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187654 [Multi-domain]  Cd Length: 260  Bit Score: 59.81  E-value: 1.40e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  26 LVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEIGAGARLLVLDVTDLDGIARATTQVD---RLDVLVNNAGI 102
Cdd:cd08951  11 FITGSSDGLGLAAARTLLHQGHEVVLHARSQKRAADAKAACPGAAGVLIGDLSSLAETRKLADQVNaigRFDAVIHNAGI 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738 103 spslappadtSVEEFRRTYETNVFGVVAVtNAFLP----ALRRSPHpRIVNISS-----GTASLT---WstnpnpqFTPG 170
Cdd:cd08951  91 ----------LSGPNRKTPDTGIPAMVAV-NVLAPyvltALIRRPK-RLIYLSSgmhrgGNASLDdidW-------FNRG 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738 171 SGGAAAYRSSKAAL----NALTVLYAQTLaedgfkVNALAPGMRATDLNplAAAAGDDPAEAAQGAARLALLPDDGP--T 244
Cdd:cd08951 152 ENDSPAYSDSKLHVltlaAAVARRWKDVS------SNAVHPGWVPTKMG--GAGAPDDLEQGHLTQVWLAESDDPQAltS 223


                ....
gi 30267738 245 GGFF 248
Cdd:cd08951 224 GGYF 227
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
 23-208 2.63e-10

Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate dehydrogenase (SDH, aka glucitol 6-phosphate dehydrogenase) catalyzes the NAD-dependent interconversion of D-fructose 6-phosphate to D-sorbitol 6-phosphate. SDH is a member of the classical SDRs, with the characteristic catalytic tetrad, but without a complete match to the typical NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187583 [Multi-domain]  Cd Length: 257  Bit Score: 59.02  E-value: 2.63e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  23 RTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEI----GAGARLLVLDVT---DLDGIARATTQV-DRLD 94
Cdd:cd05322   3 QVAVVIGGGQTLGEFLCHGLAEAGYDVAVADINSENAEKVADEInaeyGEKAYGFGADATneqSVIALSKGVDEIfKRVD 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  95 VLVNNAGISPSlAPPADTSVEEFRRTYETNVFGVvavtnaFLPA-------LRRSPHPRIVNISSGTASLtwstnpnpqf 167
Cdd:cd05322  83 LLVYSAGIAKS-AKITDFELGDFDRSLQVNLVGY------FLCArefsklmIRDGIQGRIIQINSKSGKV---------- 145

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 30267738 168 tpGSGGAAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPG 208
Cdd:cd05322 146 --GSKHNSGYSAAKFGGVGLTQSLALDLAEHGITVNSLMLG 184
3KS_SDR_c cd08941
3-keto steroid reductase, classical (c) SDRs; 3-keto steroid reductase (in concert with other ...
 25-217 7.43e-10

3-keto steroid reductase, classical (c) SDRs; 3-keto steroid reductase (in concert with other enzymes) catalyzes NADP-dependent sterol C-4 demethylation, as part of steroid biosynthesis. 3-keto reductase is a classical SDR, with a well conserved canonical active site tetrad and fairly well conserved characteristic NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187645 [Multi-domain]  Cd Length: 290  Bit Score: 58.17  E-value: 7.43e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  25 ALVTGANKGIGKHIARVLVAE-----GLTVYVGSRDRGLGQRAVEEIGA-------GARLLVLDVTDLDGIARATTQV-- 90
Cdd:cd08941   4 VLVTGANSGLGLAICERLLAEddenpELTLILACRNLQRAEAACRALLAshpdarvVFDYVLVDLSNMVSVFAAAKELkk 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  91 --DRLDVLVNNAGISP------------SLAPP-------------------ADTSVEE-FRRTYETNVFGVVAVTNAFL 136
Cdd:cd08941  84 ryPRLDYLYLNAGIMPnpgidwigaikeVLTNPlfavtnptykiqaegllsqGDKATEDgLGEVFQTNVFGHYYLIRELE 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738 137 PALRRSPHP-RIVNISSGTASLTWSTNPNPQftpGSGGAAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDLN 215
Cdd:cd08941 164 PLLCRSDGGsQIIWTSSLNASPKYFSLEDIQ---HLKGPAPYSSSKYLVDLLSLALNRKFNKLGVYSYVVHPGICTTNLT 240


                ..
gi 30267738 216 PL 217
Cdd:cd08941 241 YG 242
PRK07775 PRK07775
SDR family oxidoreductase;
23-208 1.14e-09

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 57.46  E-value: 1.14e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   23 RTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEI---GAGARLLVLDVTD----LDGIARATTQVDRLDV 95
Cdd:PRK07775  11 RPALVAGASSGIGAATAIELAAAGFPVALGARRVEKCEELVDKIradGGEAVAFPLDVTDpdsvKSFVAQAEEALGEIEV 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   96 LVNNAG-ISPSLAppADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTASLtwstnPNPQFtpgsgga 174
Cdd:PRK07775  91 LVSGAGdTYFGKL--HEISTEQFESQVQIHLVGANRLATAVLPGMIERRRGDLIFVGSDVALR-----QRPHM------- 156

                        170       180       190
                 ....*....|....*....|....*....|....
gi 30267738  175 AAYRSSKAALNALTVLYAQTLAEDGFKVNALAPG 208
Cdd:PRK07775 157 GAYGAAKAGLEAMVTNLQMELEGTGVRASIVHPG 190
PRK06194 PRK06194
hypothetical protein; Provisional
 23-234 1.63e-09

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 56.95  E-value: 1.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   23 RTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEIGA-GARLL--VLDVTD---LDGIARAT-TQVDRLDV 95
Cdd:PRK06194   7 KVAVITGAASGFGLAFARIGAALGMKLVLADVQQDALDRAVAELRAqGAEVLgvRTDVSDaaqVEALADAAlERFGAVHL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   96 LVNNAGISpSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLP----ALRRSPHPR--IVNISSGTASLtwstnpNPQftp 169
Cdd:PRK06194  87 LFNNAGVG-AGGLVWENSLADWEWVLGVNLWGVIHGVRAFTPlmlaAAEKDPAYEghIVNTASMAGLL------APP--- 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30267738  170 gsgGAAAYRSSKAALNALT-VLYAQ-TLAEDGFKVNALAPGMRATDL-----NPLAAAAGDDPAEAAQGAAR 234
Cdd:PRK06194 157 ---AMGIYNVSKHAVVSLTeTLYQDlSLVTDQVGASVLCPYFVPTGIwqserNRPADLANTAPPTRSQLIAQ 225
Epimerase pfam01370
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. ...
 25-193 1.08e-08

NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. The proteins in this family use nucleotide-sugar substrates for a variety of chemical reactions.


Pssm-ID: 396097 [Multi-domain]  Cd Length: 238  Bit Score: 54.23  E-value: 1.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738    25 ALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVeeiGAGARLLVLDVTDLDGIARATTQVdRLDVLVNNAGISp 104
Cdd:pfam01370   1 ILVTGATGFIGSHLVRRLLEKGYEVIGLDRLTSASNTAR---LADLRFVEGDLTDRDALEKLLADV-RPDAVIHLAAVG- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   105 slAPPAdtSVEEFRRTYETNVFGVVAVtnafLPALRRSPHPRIVNISS------GTASLTWSTNPNPQFTPGSggaaAYR 178
Cdd:pfam01370  76 --GVGA--SIEDPEDFIEANVLGTLNL----LEAARKAGVKRFLFASSsevygdGAEIPQEETTLTGPLAPNS----PYA 143

                         170
                  ....*....|....*
gi 30267738   179 SSKAALNALTVLYAQ 193
Cdd:pfam01370 144 AAKLAGEWLVLAYAA 158
PRK07041 PRK07041
SDR family oxidoreductase;
26-235 1.97e-08

SDR family oxidoreductase;


Pssm-ID: 235914 [Multi-domain]  Cd Length: 230  Bit Score: 53.50  E-value: 1.97e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   26 LVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEIGAGARLL--VLDVTDLDGIARATTQVDRLDVLVNNAGIS 103
Cdd:PRK07041   1 LVVGGSSGIGLALARAFAAEGARVTIASRSRDRLAAAARALGGGAPVRtaALDITDEAAVDAFFAEAGPFDHVVITAADT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  104 PSlAPPADTSVEEFRRTYETNVFGvvavtnaflpALRRSPHPRIvnisSGTASLTWSTnpnpqftpgsgGAAAYRSSK-- 181
Cdd:PRK07041  81 PG-GPVRALPLAAAQAAMDSKFWG----------AYRVARAARI----APGGSLTFVS-----------GFAAVRPSAsg 134

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30267738  182 -------AALNALTVLYAQTLAEdgFKVNALAPGMRATdlnPLAAAAGDDPAEA--AQGAARL 235
Cdd:PRK07041 135 vlqgainAALEALARGLALELAP--VRVNTVSPGLVDT---PLWSKLAGDAREAmfAAAAERL 192
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
 22-235 2.03e-08

ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes both KR domains of the Bacillus subtilis Pks J,-L, and PksM, and all three KR domains of PksN, components of the megacomplex bacillaene synthase, which synthesizes the antibiotic bacillaene. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187656 [Multi-domain]  Cd Length: 436  Bit Score: 54.30  E-value: 2.03e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  22 DRTALVTGANKGIGKHIARVLV-AEGLTVYVGSRdRGLG---------QRAVEEIGAGARLLVLDVTDLDGIARATTQVD 91
Cdd:cd08953 205 GGVYLVTGGAGGIGRALARALArRYGARLVLLGR-SPLPpeeewkaqtLAALEALGARVLYISADVTDAAAVRRLLEKVR 283

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  92 ----RLDVLVNNAGISPSlAPPADTSVEEFRRTYETNVFGVVAVtnafLPALRRSPHPRIVNISSGTASLtwstnpnpqf 167
Cdd:cd08953 284 erygAIDGVIHAAGVLRD-ALLAQKTAEDFEAVLAPKVDGLLNL----AQALADEPLDFFVLFSSVSAFF---------- 348

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30267738 168 tpGSGGAAAYrsskAALNALTVLYAQTLAEDGFKVNALA--------PGMRATDLNP-LAAAAGDDPAEAAQGAARL 235
Cdd:cd08953 349 --GGAGQADY----AAANAFLDAFAAYLRQRGPQGRVLSinwpawreGGMAADLGAReLLARAGLLPIEPEEGLQAL 419
fabG PRK05786
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 23-216 2.34e-08

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 235608 [Multi-domain]  Cd Length: 238  Bit Score: 53.23  E-value: 2.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   23 RTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEIG--AGARLLVLDVTDLDGIARATTQVDR----LDVL 96
Cdd:PRK05786   6 KKVAIIGVSEGLGYAVAYFALKEGAQVCINSRNENKLKRMKKTLSkyGNIHYVVGDVSSTESARNVIEKAAKvlnaIDGL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   97 VNNAGispslAPPADTsVEEFRRTYE---TNVFGVVAVTNAFLPALRrsPHPRIVNISS-GTASLTWSTNpnpqftpgsg 172
Cdd:PRK05786  86 VVTVG-----GYVEDT-VEEFSGLEEmltNHIKIPLYAVNASLRFLK--EGSSIVLVSSmSGIYKASPDQ---------- 147

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 30267738  173 gaAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDLNP 216
Cdd:PRK05786 148 --LSYAVAKAGLAKAVEILASELLGRGIRVNGIAPTTISGDFEP 189
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
 25-227 2.43e-08

Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase (KR) domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187535 [Multi-domain]  Cd Length: 186  Bit Score: 52.52  E-value: 2.43e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  25 ALVTGANKGIGKHIARVLVAEGltvyvgsrdrglgqraveeigaGARLLVldvtdldgiarattqVDRLDVLVNNAGIsP 104
Cdd:cd02266   1 VLVTGGSGGIGGAIARWLASRG----------------------SPKVLV---------------VSRRDVVVHNAAI-L 42

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738 105 SLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSgTASLTwstnpnpqftpGSGGAAAYRSSKAAL 184
Cdd:cd02266  43 DDGRLIDLTGSRIERAIRANVVGTRRLLEAARELMKAKRLGRFILISS-VAGLF-----------GAPGLGGYAASKAAL 110

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 30267738 185 NALTVLYAQTLAEDGFKVNALAPGMRATdlnPLAAAAGDDPAE 227
Cdd:cd02266 111 DGLAQQWASEGWGNGLPATAVACGTWAG---SGMAKGPVAPEE 150
PRK07677 PRK07677
short chain dehydrogenase; Provisional
 23-208 3.84e-08

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 52.76  E-value: 3.84e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   23 RTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEIGA-GARLLV--LDVTDLDGIARATTQVD----RLDV 95
Cdd:PRK07677   2 KVVIITGGSSGMGKAMAKRFAEEGANVVITGRTKEKLEEAKLEIEQfPGQVLTvqMDVRNPEDVQKMVEQIDekfgRIDA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   96 LVNNAGiSPSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPA-LRRSPHPRIVNIssgTASLTWSTNPnpqftpgsgGA 174
Cdd:PRK07677  82 LINNAA-GNFICPAEDLSVNGWNSVIDIVLNGTFYCSQAVGKYwIEKGIKGNIINM---VATYAWDAGP---------GV 148

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 30267738  175 AAYRSSKAALNALTvlyaQTLAED-----GFKVNALAPG 208
Cdd:PRK07677 149 IHSAAAKAGVLAMT----RTLAVEwgrkyGIRVNAIAPG 183
PRK05876 PRK05876
short chain dehydrogenase; Provisional
 23-214 1.51e-07

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 51.11  E-value: 1.51e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   23 RTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEI---GAGARLLVLDVTDLDGIARATTQVDRL----DV 95
Cdd:PRK05876   7 RGAVITGGASGIGLATGTEFARRGARVVLGDVDKPGLRQAVNHLraeGFDVHGVMCDVRHREEVTHLADEAFRLlghvDV 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   96 LVNNAGISPSlAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTASLTwstnPNpqftpgsGGAA 175
Cdd:PRK05876  87 VFSNAGIVVG-GPIVEMTHDDWRWVIDVDLWGSIHTVEAFLPRLLEQGTGGHVVFTASFAGLV----PN-------AGLG 154

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 30267738  176 AYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDL 214
Cdd:PRK05876 155 AYGVAKYGVVGLAETLAREVTADGIGVSVLCPMVVETNL 193
PRK09186 PRK09186
flagellin modification protein A; Provisional
 20-208 1.58e-07

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 50.76  E-value: 1.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   20 MNDRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEIGAGAR-----LLVLDVTDLDGIARA----TTQV 90
Cdd:PRK09186   2 LKGKTILITGAGGLIGSALVKAILEAGGIVIAADIDKEALNELLESLGKEFKskklsLVELDITDQESLEEFlsksAEKY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   91 DRLDVLVNNAgispslAPPA--------DTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISS--GTAsltws 160
Cdd:PRK09186  82 GKIDGAVNCA------YPRNkdygkkffDVSLDDFNENLSLHLGSSFLFSQQFAKYFKKQGGGNLVNISSiyGVV----- 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 30267738  161 tnpNPQFTPGSGGAAA----YRSSKAALNALTVLYAQTLAEDGFKVNALAPG 208
Cdd:PRK09186 151 ---APKFEIYEGTSMTspveYAAIKAGIIHLTKYLAKYFKDSNIRVNCVSPG 199
YbjT COG0702
Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General ...
 26-152 1.98e-07

Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General function prediction only];


Pssm-ID: 440466 [Multi-domain]  Cd Length: 215  Bit Score: 50.23  E-value: 1.98e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  26 LVTGANKGIGKHIARVLVAEGLTVYVGSRDRglgQRAVEEIGAGARLLVLDVTDLDGIARATTQVdrlDVLVNNAGISPS 105
Cdd:COG0702   3 LVTGATGFIGRRVVRALLARGHPVRALVRDP---EKAAALAAAGVEVVQGDLDDPESLAAALAGV---DAVFLLVPSGPG 76

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 30267738 106 LAPPADtsveefrrtyetnvfgvVAVTNAFLPALRRSPHPRIVNISS 152
Cdd:COG0702  77 GDFAVD-----------------VEGARNLADAAKAAGVKRIVYLSA 106
fabG PRK07792
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 13-228 2.26e-07

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 181120 [Multi-domain]  Cd Length: 306  Bit Score: 50.94  E-value: 2.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   13 SQGTVVAMNDRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAV-EEI-GAGARLLVL--DVTD---LDGIAR 85
Cdd:PRK07792   3 RTTNTTDLSGKVAVVTGAAAGLGRAEALGLARLGATVVVNDVASALDASDVlDEIrAAGAKAVAVagDISQratADELVA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   86 ATTQVDRLDVLVNNAGISPSLApPADTSVEEFRRTYETNVFGVVAVTNaFLPALRRSP--------HPRIVNISSgtasl 157
Cdd:PRK07792  83 TAVGLGGLDIVVNNAGITRDRM-LFNMSDEEWDAVIAVHLRGHFLLTR-NAAAYWRAKakaaggpvYGRIVNTSS----- 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30267738  158 twstnpnPQFTPGSGGAAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDLNPLAAAAGDDPAEA 228
Cdd:PRK07792 156 -------EAGLVGPVGQANYGAAKAGITALTLSAARALGRYGVRANAICPRARTAMTADVFGDAPDVEAGG 219
PRK06101 PRK06101
SDR family oxidoreductase;
24-214 2.81e-07

SDR family oxidoreductase;


Pssm-ID: 180399 [Multi-domain]  Cd Length: 240  Bit Score: 50.25  E-value: 2.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   24 TALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLgqraVEEIGAGAR---LLVLDVTDLDGIARATTQVDRL-DVLVNN 99
Cdd:PRK06101   3 AVLITGATSGIGKQLALDYAKQGWQVIACGRNQSV----LDELHTQSAnifTLAFDVTDHPGTKAALSQLPFIpELWIFN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  100 AGISPSLaPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIV-NISSGTASltwstnpnPQftpgsggAAAYR 178
Cdd:PRK06101  79 AGDCEYM-DDGKVDATLMARVFNVNVLGVANCIEGIQPHLSCGHRVVIVgSIASELAL--------PR-------AEAYG 142

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 30267738  179 SSKAALNaltvLYAQTLAED----GFKVNALAPGMRATDL 214
Cdd:PRK06101 143 ASKAAVA----YFARTLQLDlrpkGIEVVTVFPGFVATPL 178
Lin1944_like_SDR_c cd11731
Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a ...
 25-232 2.81e-07

Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a classical SDR, it contains a glycine-rich motif similar to the canonical motif of the SDR NAD(P)-binding site. However, the typical SDR active site residues are absent in this subgroup of proteins of undetermined function. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212497 [Multi-domain]  Cd Length: 198  Bit Score: 49.50  E-value: 2.81e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  25 ALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQraveeigagarllvLDVTDLDGIARATTQVDRLDVLVNNAGiSP 104
Cdd:cd11731   1 IIVIGATGTIGLAVAQLLSAHGHEVITAGRSSGDYQ--------------VDITDEASIKALFEKVGHFDAIVSTAG-DA 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738 105 SLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRrsphprivniSSGTASLTwSTNPNPQFTPGSGGAAAyrsSKAAL 184
Cdd:cd11731  66 EFAPLAELTDADFQRGLNSKLLGQINLVRHGLPYLN----------DGGSITLT-SGILAQRPIPGGAAAAT---VNGAL 131

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 30267738 185 NALTVLYAQTLaEDGFKVNALAPGMRATDLNPL-AAAAGDDPAEAAQGA 232
Cdd:cd11731 132 EGFVRAAAIEL-PRGIRINAVSPGVVEESLEAYgDFFPGFEPVPAEDVA 179
PLN02780 PLN02780
ketoreductase/ oxidoreductase
 25-157 3.08e-07

ketoreductase/ oxidoreductase


Pssm-ID: 166421 [Multi-domain]  Cd Length: 320  Bit Score: 50.63  E-value: 3.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   25 ALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEIGAG-----ARLLVLDVT-DLD-GIARATTQVDRLDV-- 95
Cdd:PLN02780  56 ALVTGPTDGIGKGFAFQLARKGLNLVLVARNPDKLKDVSDSIQSKysktqIKTVVVDFSgDIDeGVKRIKETIEGLDVgv 135

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30267738   96 LVNNAGISPSLAPPADTSVEEF-RRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTASL 157
Cdd:PLN02780 136 LINNVGVSYPYARFFHEVDEELlKNLIKVNVEGTTKVTQAVLPGMLKRKKGAIINIGSGAAIV 198
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
23-213 4.68e-07

2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 49.49  E-value: 4.68e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   23 RTALVTGANKGIGKHIARVLVAEGLTV----YVGSRDrglgqrAVEEIGAGARLLV---LDVTDLDGIA----RATTQVD 91
Cdd:PRK08993  11 KVAVVTGCDTGLGQGMALGLAEAGCDIvginIVEPTE------TIEQVTALGRRFLsltADLRKIDGIPalleRAVAEFG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   92 RLDVLVNNAGISPSlAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPH-PRIVNISSgtaSLTWStnpnpqftpG 170
Cdd:PRK08993  85 HIDILVNNAGLIRR-EDAIEFSEKDWDDVMNLNIKSVFFMSQAAAKHFIAQGNgGKIINIAS---MLSFQ---------G 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 30267738  171 SGGAAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATD 213
Cdd:PRK08993 152 GIRVPSYTASKSGVMGVTRLMANEWAKHNINVNAIAPGYMATN 194
PRK08251 PRK08251
SDR family oxidoreductase;
23-228 6.86e-07

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 49.16  E-value: 6.86e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   23 RTALVTGANKGIGKHIARVLVAEGltvyvgsRDRGLGQRAVE-------EIGA---GARLLV--LDVTDLDGIARATTQV 90
Cdd:PRK08251   3 QKILITGASSGLGAGMAREFAAKG-------RDLALCARRTDrleelkaELLArypGIKVAVaaLDVNDHDQVFEVFAEF 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   91 DR----LDVLVNNAGISPSlAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTAsltwstnpnpq 166
Cdd:PRK08251  76 RDelggLDRVIVNAGIGKG-ARLGTGKFWANKATAETNFVAALAQCEAAMEIFREQGSGHLVLISSVSA----------- 143

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30267738  167 FTPGSGGAAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATDLNplaAAAGDDPAEA 228
Cdd:PRK08251 144 VRGLPGVKAAYAASKAGVASLGEGLRAELAKTPIKVSTIEPGYIRSEMN---AKAKSTPFMV 202
SDR_a5 cd05243
atypical (a) SDRs, subgroup 5; This subgroup contains atypical SDRs, some of which are ...
 26-105 7.01e-07

atypical (a) SDRs, subgroup 5; This subgroup contains atypical SDRs, some of which are identified as putative NAD(P)-dependent epimerases, one as a putative NAD-dependent epimerase/dehydratase. Atypical SDRs are distinct from classical SDRs. Members of this subgroup have a glycine-rich NAD(P)-binding motif that is very similar to the extended SDRs, GXXGXXG, and binds NADP. Generally, this subgroup has poor conservation of the active site tetrad; however, individual sequences do contain matches to the YXXXK active site motif, the upstream Ser, and there is a highly conserved Asp in place of the usual active site Asn throughout the subgroup. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187554 [Multi-domain]  Cd Length: 203  Bit Score: 48.39  E-value: 7.01e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  26 LVTGANKGIGKHIARVLVAEGLTVYVGSRDRglgQRAVEEIGAGARLLVLDVTDLDGIARATTQVdrlDVLVNNAGISPS 105
Cdd:cd05243   3 LVVGATGKVGRHVVRELLDRGYQVRALVRDP---SQAEKLEAAGAEVVVGDLTDAESLAAALEGI---DAVISAAGSGGK 76
pter_reduc_Leis TIGR02685
pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including ...
 25-209 8.34e-07

pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including Trypanosoma cruzi and Leishmania major) to obtain reduced pteridines by salvage rather than biosynthetic pathways. Enzymes in T. cruzi described as pteridine reductase 1 (PTR1) and pteridine reductase 2 (PTR2) have different activity profiles. PTR1 is more active with with fully oxidized biopterin and folate than with reduced forms, while PTR2 reduces dihydrobiopterin and dihydrofolate but not oxidized pteridines. T. cruzi PTR1 and PTR2 are more similar to each other in sequence than either is to the pteridine reductase of Leishmania major, and all are included in this family.


Pssm-ID: 131732 [Multi-domain]  Cd Length: 267  Bit Score: 48.77  E-value: 8.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738    25 ALVTGANKGIGKHIARVLVAEGLTVYVG-SRDRGLGQRAVEEIGA----GARLLVLDVTDLDGI-ARATTQVD------- 91
Cdd:TIGR02685   4 AVVTGAAKRIGSSIAVALHQEGYRVVLHyHRSAAAASTLAAELNArrpnSAVTCQADLSNSATLfSRCEAIIDacfrafg 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738    92 RLDVLVNNA-GISPS-LAPPADTSVEEFRRTYETNV---FGVVAVTNAFL-----------PALRRSPHPRIVNISSGTA 155
Cdd:TIGR02685  84 RCDVLVNNAsAFYPTpLLRGDAGEGVGDKKSLEVQVaelFGSNAIAPYFLikafaqrqagtRAEQRSTNLSIVNLCDAMT 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 30267738   156 SLtwstnPNPQFTpgsggaaAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGM 209
Cdd:TIGR02685 164 DQ-----PLLGFT-------MYTMAKHALEGLTRSAALELAPLQIRVNGVAPGL 205
NmrA_TMR_like_1_SDR_a cd05231
NmrA (a transcriptional regulator) and triphenylmethane reductase (TMR) like proteins, ...
 26-163 9.73e-07

NmrA (a transcriptional regulator) and triphenylmethane reductase (TMR) like proteins, subgroup 1, atypical (a) SDRs; Atypical SDRs related to NMRa, TMR, and HSCARG (an NADPH sensor). This subgroup resembles the SDRs and has a partially conserved characteristic [ST]GXXGXXG NAD-binding motif, but lacks the conserved active site residues. NmrA is a negative transcriptional regulator of various fungi, involved in the post-translational modulation of the GATA-type transcription factor AreA. NmrA lacks the canonical GXXGXXG NAD-binding motif and has altered residues at the catalytic triad, including a Met instead of the critical Tyr residue. NmrA may bind nucleotides but appears to lack any dehydrogenase activity. HSCARG has been identified as a putative NADP-sensing molecule, and redistributes and restructures in response to NADPH/NADP ratios. Like NmrA, it lacks most of the active site residues of the SDR family, but has an NAD(P)-binding motif similar to the extended SDR family, GXXGXXG. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Atypical SDRs are distinct from classical SDRs. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187542 [Multi-domain]  Cd Length: 259  Bit Score: 48.48  E-value: 9.73e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  26 LVTGANKGIGKHIARVLVAEGLTVYVGSRDrglGQRAVEEIGAGARLLVLDVTDLDGIARATTQVDRLDVLvnnagisps 105
Cdd:cd05231   2 LVTGATGRIGSKVATTLLEAGRPVRALVRS---DERAAALAARGAEVVVGDLDDPAVLAAALAGVDAVFFL--------- 69

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 30267738 106 lAPPADTSVEEFrrtyetnvfGVVAVTNAFLPALRRSPHPRIVNISSGTASLTWSTNP 163
Cdd:cd05231  70 -APPAPTADARP---------GYVQAAEAFASALREAGVKRVVNLSSVGADPESPSGL 117
PRK12428 PRK12428
coniferyl-alcohol dehydrogenase;
76-242 1.10e-06

coniferyl-alcohol dehydrogenase;


Pssm-ID: 237099 [Multi-domain]  Cd Length: 241  Bit Score: 48.46  E-value: 1.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   76 DVTDLDGIARATTQVD-RLDVLVNNAGISPSLAPPADTSVeefrrtyetNVFGVVAVTNAFLPalRRSPHPRIVNISSgT 154
Cdd:PRK12428  31 DLGDPASIDAAVAALPgRIDALFNIAGVPGTAPVELVARV---------NFLGLRHLTEALLP--RMAPGGAIVNVAS-L 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  155 ASLTWSTN--------PNPQFTPGSGGAAA--------YRSSKAALNALTVLYAQT-LAEDGFKVNALAPGMRATD-LNP 216
Cdd:PRK12428  99 AGAEWPQRlelhkalaATASFDEGAAWLAAhpvalatgYQLSKEALILWTMRQAQPwFGARGIRVNCVAPGPVFTPiLGD 178

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 30267738  217 LAAAAGDD-----------PAEAAQGAARLALLPDDG 242
Cdd:PRK12428 179 FRSMLGQErvdsdakrmgrPATADEQAAVLVFLCSDA 215
PRK08303 PRK08303
short chain dehydrogenase; Provisional
 19-208 1.31e-06

short chain dehydrogenase; Provisional


Pssm-ID: 236229 [Multi-domain]  Cd Length: 305  Bit Score: 48.46  E-value: 1.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   19 AMNDRTALVTGANKGIGKHIARVLVAEGLTVYVGSRD----RGLGQRA--VEEI-----GAGARLLVLDVTDLDG----- 82
Cdd:PRK08303   5 PLRGKVALVAGATRGAGRGIAVELGAAGATVYVTGRStrarRSEYDRPetIEETaelvtAAGGRGIAVQVDHLVPeqvra 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   83 -IARATTQVDRLDVLVNNagI----------SPSLAPPADTSVEEFRRTYETNvfgvvAVTNAF-LPALRRSPHPRIVNI 150
Cdd:PRK08303  85 lVERIDREQGRLDILVND--IwggeklfewgKPVWEHSLDKGLRMLRLAIDTH-----LITSHFaLPLLIRRPGGLVVEI 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30267738  151 SSGTASLTwstnpnpqftpgsggAAAYRSS------KAALNALTVLYAQTLAEDGFKVNALAPG 208
Cdd:PRK08303 158 TDGTAEYN---------------ATHYRLSvfydlaKTSVNRLAFSLAHELAPHGATAVALTPG 206
UDP_AE_SDR_e cd05256
UDP-N-acetylglucosamine 4-epimerase, extended (e) SDRs; This subgroup contains ...
 26-155 1.33e-06

UDP-N-acetylglucosamine 4-epimerase, extended (e) SDRs; This subgroup contains UDP-N-acetylglucosamine 4-epimerase of Pseudomonas aeruginosa, WbpP, an extended SDR, that catalyzes the NAD+ dependent conversion of UDP-GlcNAc and UDPGalNA to UDP-Glc and UDP-Gal. This subgroup has the characteristic active site tetrad and NAD-binding motif of the extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187566 [Multi-domain]  Cd Length: 304  Bit Score: 48.37  E-value: 1.33e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  26 LVTGANKGIGKHIARVLVAEGLTVYV------GSRDRglgqraVEEIGAGARLLVLDVTDLDGIARATTQVDRLDVLVNN 99
Cdd:cd05256   3 LVTGGAGFIGSHLVERLLERGHEVIVldnlstGKKEN------LPEVKPNVKFIEGDIRDDELVEFAFEGVDYVFHQAAQ 76

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 30267738 100 AGISPslappadtSVEEFRRTYETNVFGVVAVtnafLPALRRSPHPRIVNISSGTA 155
Cdd:cd05256  77 ASVPR--------SIEDPIKDHEVNVLGTLNL----LEAARKAGVKRFVYASSSSV 120
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
 25-230 1.96e-06

Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a classical SDR which binds NADP. Members of this subgroup contain the YXXXK active site characteristic of SDRs. Also, an upstream Asn residue of the canonical catalytic tetrad is partially conserved in this subgroup of proteins of undetermined function. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212496 [Multi-domain]  Cd Length: 206  Bit Score: 47.13  E-value: 1.96e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  25 ALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEIGAGARllVLDVTDLDGIARATTQVDRLDVLVNNAGISP 104
Cdd:cd11730   1 ALILGATGGIGRALARALAGRGWRLLLSGRDAGALAGLAAEVGALAR--PADVAAELEVWALAQELGPLDLLVYAAGAIL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738 105 SlAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPH-------PRIVNISsgtasltwstnpnpqftpgsgGAAAY 177
Cdd:cd11730  79 G-KPLARTKPAAWRRILDANLTGAALVLKHALALLAAGARlvflgayPELVMLP---------------------GLSAY 136

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 30267738 178 RSSKAALNALtvLYAQTLAEDGFKVNALAPGMRATDL-NPLAAAAGD--DPAEAAQ 230
Cdd:cd11730 137 AAAKAALEAY--VEVARKEVRGLRLTLVRPPAVDTGLwAPPGRLPKGalSPEDVAA 190
PRK08339 PRK08339
short chain dehydrogenase; Provisional
 18-213 2.04e-06

short chain dehydrogenase; Provisional


Pssm-ID: 169389 [Multi-domain]  Cd Length: 263  Bit Score: 47.54  E-value: 2.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   18 VAMNDRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEIGAGARL----LVLDVT---DLDGIARATTQV 90
Cdd:PRK08339   4 IDLSGKLAFTTASSKGIGFGVARVLARAGADVILLSRNEENLKKAREKIKSESNVdvsyIVADLTkreDLERTVKELKNI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   91 DRLDVLVNNAGiSPSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSGTASltwstNPNPQFtpg 170
Cdd:PRK08339  84 GEPDIFFFSTG-GPKPGYFMEMSMEDWEGAVKLLLYPAVYLTRALVPAMERKGFGRIIYSTSVAIK-----EPIPNI--- 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 30267738  171 sggaAAYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATD 213
Cdd:PRK08339 155 ----ALSNVVRISMAGLVRTLAKELGPKGITVNGIMPGIIRTD 193
PRK07806 PRK07806
SDR family oxidoreductase;
21-100 2.32e-06

SDR family oxidoreductase;


Pssm-ID: 181126 [Multi-domain]  Cd Length: 248  Bit Score: 47.41  E-value: 2.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   21 NDRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDR-GLGQRAVEEI-GAGARLLVL--DVTDLDGIAR----ATTQVDR 92
Cdd:PRK07806   5 PGKTALVTGSSRGIGADTAKILAGAGAHVVVNYRQKaPRANKVVAEIeAAGGRASAVgaDLTDEESVAAlmdtAREEFGG 84


                 ....*...
gi 30267738   93 LDVLVNNA 100
Cdd:PRK07806  85 LDALVLNA 92
DHPR_SDR_c_like cd05334
dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an ...
 23-215 2.36e-06

dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an NAD-binding protein related to the SDRs. It converts dihydrobiopterin into tetrahydrobiopterin, a cofactor necessary in catecholamines synthesis. Dihydropteridine reductase has the YXXXK of these tyrosine-dependent oxidoreductases, but lacks the typical upstream Asn and Ser catalytic residues. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187595 [Multi-domain]  Cd Length: 221  Bit Score: 47.32  E-value: 2.36e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  23 RTALVTGANKGIGKHIARVLVAEGLTVYvgsrdrGLGQRAVEEigAGARLLVLDVTDLDGIAR-----ATTQVDRLDVLV 97
Cdd:cd05334   2 RVVLVYGGRGALGSAVVQAFKSRGWWVA------SIDLAENEE--ADASIIVLDSDSFTEQAKqvvasVARLSGKVDALI 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  98 NNAGISPSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPhpRIVNISSGtASLTwstnpnpqftpGSGGAAAY 177
Cdd:cd05334  74 CVAGGWAGGSAKSKSFVKNWDLMWKQNLWTSFIASHLATKHLLSGG--LLVLTGAK-AALE-----------PTPGMIGY 139

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 30267738 178 RSSKAALNALTvlyaQTLAED------GFKVNALAPGMRATDLN 215
Cdd:cd05334 140 GAAKAAVHQLT----QSLAAEnsglpaGSTANAILPVTLDTPAN 179
GDP_MD_SDR_e cd05260
GDP-mannose 4,6 dehydratase, extended (e) SDRs; GDP-mannose 4,6 dehydratase, a homodimeric SDR, ...
 24-193 2.67e-06

GDP-mannose 4,6 dehydratase, extended (e) SDRs; GDP-mannose 4,6 dehydratase, a homodimeric SDR, catalyzes the NADP(H)-dependent conversion of GDP-(D)-mannose to GDP-4-keto, 6-deoxy-(D)-mannose in the fucose biosynthesis pathway. These proteins have the canonical active site triad and NAD-binding pattern, however the active site Asn is often missing and may be substituted with Asp. A Glu residue has been identified as an important active site base. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187570 [Multi-domain]  Cd Length: 316  Bit Score: 47.59  E-value: 2.67e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  24 TALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEIGAGA----RLLVLDVTDLDGIARATTQVdRLDVLVNN 99
Cdd:cd05260   1 RALITGITGQDGSYLAEFLLEKGYEVHGIVRRSSSFNTDRIDHLYINkdriTLHYGDLTDSSSLRRAIEKV-RPDEIYHL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738 100 AGISpslAPPadTSVEEFRRTYETNVFGvvavTNAFLPALR-RSPHPRIVNISSG-----TASLTWS-TNPnpqFTPGSg 172
Cdd:cd05260  80 AAQS---HVK--VSFDDPEYTAEVNAVG----TLNLLEAIRiLGLDARFYQASSSeeygkVQELPQSeTTP---FRPRS- 146

                       170       180
                ....*....|....*....|.
gi 30267738 173 gaaAYRSSKAALNALTVLYAQ 193
Cdd:cd05260 147 ---PYAVSKLYADWITRNYRE 164
PRK07102 PRK07102
SDR family oxidoreductase;
26-212 3.43e-06

SDR family oxidoreductase;


Pssm-ID: 180838 [Multi-domain]  Cd Length: 243  Bit Score: 46.84  E-value: 3.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   26 LVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEI----GAGARLLVLDVTDLDGIARATTQVD-RLDVLVNNA 100
Cdd:PRK07102   5 LIIGATSDIARACARRYAAAGARLYLAARDVERLERLADDLrargAVAVSTHELDILDTASHAAFLDSLPaLPDIVLIAV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  101 GISPSLApPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVNISSgtasltwstnpnpqfTPGSGGAAA---Y 177
Cdd:PRK07102  85 GTLGDQA-ACEADPALALREFRTNFEGPIALLTLLANRFEARGSGTIVGISS---------------VAGDRGRASnyvY 148

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 30267738  178 RSSKAALNALTVLYAQTLAEDGFKVNALAPGMRAT 212
Cdd:PRK07102 149 GSAKAALTAFLSGLRNRLFKSGVHVLTVKPGFVRT 183
UDP_G4E_2_SDR_e cd05234
UDP-glucose 4 epimerase, subgroup 2, extended (e) SDRs; UDP-glucose 4 epimerase (aka ...
 25-210 3.54e-06

UDP-glucose 4 epimerase, subgroup 2, extended (e) SDRs; UDP-glucose 4 epimerase (aka UDP-galactose-4-epimerase), is a homodimeric extended SDR. It catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. This subgroup is comprised of archaeal and bacterial proteins, and has the characteristic active site tetrad and NAD-binding motif of the extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187545 [Multi-domain]  Cd Length: 305  Bit Score: 47.29  E-value: 3.54e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  25 ALVTGANKGIGKHIARVLVAEGLTVYV------GSRDRGLGQRAVEEigagARLLVLDVTDLDGIARATTqVDRLDVLVN 98
Cdd:cd05234   2 ILVTGGAGFIGSHLVDRLLEEGNEVVVvdnlssGRRENIEPEFENKA----FRFVKRDLLDTADKVAKKD-GDTVFHLAA 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  99 NAGISPSLAPPadtsveefRRTYETNVFGVVAVtnafLPALRRSPHPRIVNISSGTASLTWSTNPNPQ---FTPGSggaa 175
Cdd:cd05234  77 NPDVRLGATDP--------DIDLEENVLATYNV----LEAMRANGVKRIVFASSSTVYGEAKVIPTPEdypPLPIS---- 140

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 30267738 176 AYRSSKAALNALTVLYAQTlaeDGFK------VNALAPGMR 210
Cdd:cd05234 141 VYGASKLAAEALISAYAHL---FGFQawifrfANIVGPRST 178
PRK08415 PRK08415
enoyl-[acyl-carrier-protein] reductase FabI;
20-223 4.72e-06

enoyl-[acyl-carrier-protein] reductase FabI;


Pssm-ID: 181416 [Multi-domain]  Cd Length: 274  Bit Score: 46.66  E-value: 4.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   20 MNDRTALVTGA--NKGIGKHIARVLVAEGLTVYVGSRDRGLGQRaVEEIGA--GARLLV-LDVTD---LDGIARATTQ-V 90
Cdd:PRK08415   3 MKGKKGLIVGVanNKSIAYGIAKACFEQGAELAFTYLNEALKKR-VEPIAQelGSDYVYeLDVSKpehFKSLAESLKKdL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   91 DRLDVLVNNAGISPSLA---PPADTSVEEFRRTYETNVFGVVAVTNAFLPALrrsphprivniSSGTASLTWSTNPNPQF 167
Cdd:PRK08415  82 GKIDFIVHSVAFAPKEAlegSFLETSKEAFNIAMEISVYSLIELTRALLPLL-----------NDGASVLTLSYLGGVKY 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 30267738  168 TPGSG--GAAayrssKAALNALTVLYAQTLAEDGFKVNALAPGMRATdlnpLAAAA-GD 223
Cdd:PRK08415 151 VPHYNvmGVA-----KAALESSVRYLAVDLGKKGIRVNAISAGPIKT----LAASGiGD 200
AR_FR_like_1_SDR_e cd05228
uncharacterized subgroup of aldehyde reductase and flavonoid reductase related proteins, ...
 25-216 4.75e-06

uncharacterized subgroup of aldehyde reductase and flavonoid reductase related proteins, extended (e) SDRs; This subgroup contains proteins of unknown function related to aldehyde reductase and flavonoid reductase of the extended SDR-type. Aldehyde reductase I (aka carbonyl reductase) is an NADP-binding SDR; it has an NADP-binding motif consensus that is slightly different from the canonical SDR form and lacks the Asn of the extended SDR active site tetrad. Aldehyde reductase I catalyzes the NADP-dependent reduction of ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. The related flavonoid reductases act in the NADP-dependent reduction of flavonoids, ketone-containing plant secondary metabolites. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187539 [Multi-domain]  Cd Length: 318  Bit Score: 46.89  E-value: 4.75e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  25 ALVTGANKGIGKHIARVLVAEGLTVYVGSRDrglGQRAVEEIGAGARLLVLDVTDLDGIARATTQVDRldvLVNNAGIsp 104
Cdd:cd05228   1 ILVTGATGFLGSNLVRALLAQGYRVRALVRS---GSDAVLLDGLPVEVVEGDLTDAASLAAAMKGCDR---VFHLAAF-- 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738 105 slAPPADTSVEEFRRtyeTNVFGvvavTNAFLPALRRSPHPRIVNISSGTAsltwstnpnpqFTPGSGGAA---AYRSSK 181
Cdd:cd05228  73 --TSLWAKDRKELYR---TNVEG----TRNVLDAALEAGVRRVVHTSSIAA-----------LGGPPDGRIdetTPWNER 132

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 30267738 182 AALNAltvlYAQT--LAEdgfKV--NALAPGMRATDLNP 216
Cdd:cd05228 133 PFPND----YYRSklLAE---LEvlEAAAEGLDVVIVNP 164
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 23-187 6.42e-06

This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.


Pssm-ID: 214833 [Multi-domain]  Cd Length: 180  Bit Score: 45.55  E-value: 6.42e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738     23 RTALVTGANKGIGKHIARVLVAEG-----LTVYVGSRDRGLGQRAVEEIGAGARLLVL--DVTDLDGIARATTQVD---- 91
Cdd:smart00822   1 GTYLITGGLGGLGRALARWLAERGarrlvLLSRSGPDAPGAAALLAELEAAGARVTVVacDVADRDALAAVLAAIPaveg 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738     92 RLDVLVNNAGIsPSLAPPADTSVEEFRRTYETNVFGVVAVTNAFlpalRRSPHPRIVNISSGTASLtwstnpnpqftpGS 171
Cdd:smart00822  81 PLTGVIHAAGV-LDDGVLASLTPERFAAVLAPKAAGAWNLHELT----ADLPLDFFVLFSSIAGVL------------GS 143

                          170
                   ....*....|....*.
gi 30267738    172 GGAAAYRSSKAALNAL 187
Cdd:smart00822 144 PGQANYAAANAFLDAL 159
PRK05884 PRK05884
SDR family oxidoreductase;
26-237 1.25e-05

SDR family oxidoreductase;


Pssm-ID: 135642 [Multi-domain]  Cd Length: 223  Bit Score: 45.19  E-value: 1.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   26 LVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEIGAGArlLVLDVTDLDGIARATTQVDR-LDVLVNNAGISP 104
Cdd:PRK05884   4 LVTGGDTDLGRTIAEGFRNDGHKVTLVGARRDDLEVAAKELDVDA--IVCDNTDPASLEEARGLFPHhLDTIVNVPAPSW 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  105 SLAPP-----ADTSvEEFRRTYETNVFGVVAVTNAFLPALRrsphprivnisSGTASLtwstNPNPQFTPGSGGAAAyrs 179
Cdd:PRK05884  82 DAGDPrtyslADTA-NAWRNALDATVLSAVLTVQSVGDHLR-----------SGGSII----SVVPENPPAGSAEAA--- 142

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 30267738  180 SKAALNALTVLYAQTLAEDGFKVNALAPGMRAtdlNPLAAAAGDDPAEAAQGAARLAL 237
Cdd:PRK05884 143 IKAALSNWTAGQAAVFGTRGITINAVACGRSV---QPGYDGLSRTPPPVAAEIARLAL 197
Arna_like_SDR_e cd05257
Arna decarboxylase_like, extended (e) SDRs; Decarboxylase domain of ArnA. ArnA, is an enzyme ...
 26-207 1.73e-05

Arna decarboxylase_like, extended (e) SDRs; Decarboxylase domain of ArnA. ArnA, is an enzyme involved in the modification of outer membrane protein lipid A of gram-negative bacteria. It is a bifunctional enzyme that catalyzes the NAD-dependent decarboxylation of UDP-glucuronic acid and N-10-formyltetrahydrofolate-dependent formylation of UDP-4-amino-4-deoxy-l-arabinose; its NAD-dependent decaboxylating activity is in the C-terminal 360 residues. This subgroup belongs to the extended SDR family, however the NAD binding motif is not a perfect match and the upstream Asn of the canonical active site tetrad is not conserved. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187567 [Multi-domain]  Cd Length: 316  Bit Score: 44.98  E-value: 1.73e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  26 LVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEIGAGARLLVL--DVTDLDGIARATTQVDRLDVLVNNAGIS 103
Cdd:cd05257   3 LVTGADGFIGSHLTERLLREGHEVRALDIYNSFNSWGLLDNAVHDRFHFIsgDVRDASEVEYLVKKCDVVFHLAALIAIP 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738 104 PSLAPPadtsveefRRTYETNVFGvvavTNAFLPALRRSPHPRIVNISS----GTASLTW--STNPNPQF-TPGSGgaaa 176
Cdd:cd05257  83 YSYTAP--------LSYVETNVFG----TLNVLEAACVLYRKRVVHTSTsevyGTAQDVPidEDHPLLYInKPRSP---- 146

                       170       180       190
                ....*....|....*....|....*....|.
gi 30267738 177 YRSSKAALNALTVLYAqtlAEDGFKVNALAP 207
Cdd:cd05257 147 YSASKQGADRLAYSYG---RSFGLPVTIIRP 174
PRK06720 PRK06720
hypothetical protein; Provisional
 23-102 3.02e-05

hypothetical protein; Provisional


Pssm-ID: 180669 [Multi-domain]  Cd Length: 169  Bit Score: 43.42  E-value: 3.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   23 RTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEI---GAGARLLVLDVtDLDG-----IARATTQVDRLD 94
Cdd:PRK06720  17 KVAIVTGGGIGIGRNTALLLAKQGAKVIVTDIDQESGQATVEEItnlGGEALFVSYDM-EKQGdwqrvISITLNAFSRID 95


                 ....*...
gi 30267738   95 VLVNNAGI 102
Cdd:PRK06720  96 MLFQNAGL 103
SDR_e cd08946
extended (e) SDRs; Extended SDRs are distinct from classical SDRs. In addition to the Rossmann ...
 26-205 3.50e-05

extended (e) SDRs; Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 212494 [Multi-domain]  Cd Length: 200  Bit Score: 43.44  E-value: 3.50e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  26 LVTGANKGIGKHIARVLVAEGLTVYVgsrdrglgqraveeigagarllvldvtdldgiarattqVDRLDVLVNNAGISps 105
Cdd:cd08946   2 LVTGGAGFIGSHLVRRLLERGHEVVV--------------------------------------IDRLDVVVHLAALV-- 41

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738 106 lAPPAdtSVEEFRRTYETNVFGVVAVTNAflpaLRRSPHPRIVNISS----GTASLTWSTNPNPqFTPGSggaaAYRSSK 181
Cdd:cd08946  42 -GVPA--SWDNPDEDFETNVVGTLNLLEA----ARKAGVKRFVYASSasvyGSPEGLPEEEETP-PRPLS----PYGVSK 109

                       170       180
                ....*....|....*....|....
gi 30267738 182 AALNALTVLYAqtlAEDGFKVNAL 205
Cdd:cd08946 110 LAAEHLLRSYG---ESYGLPVVIL 130
PRK08416 PRK08416
enoyl-ACP reductase;
20-213 6.38e-05

enoyl-ACP reductase;


Pssm-ID: 181417 [Multi-domain]  Cd Length: 260  Bit Score: 43.22  E-value: 6.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   20 MNDRTALVTGANKGIGKHIARVLVAEGLTV-YVGSRDRGLGQRAVEEI----GAGARLLVLDVTDLDGIARATTQVD--- 91
Cdd:PRK08416   6 MKGKTLVISGGTRGIGKAIVYEFAQSGVNIaFTYNSNVEEANKIAEDLeqkyGIKAKAYPLNILEPETYKELFKKIDedf 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   92 -RLDVLVNNAGISPSLAPPADTSVEEFRRTYETNVFgvVAVTNAFLPALRRSPHpRIVNISSGtASLTWSTNPNPQFTPG 170
Cdd:PRK08416  86 dRVDFFISNAIISGRAVVGGYTKFMRLKPKGLNNIY--TATVNAFVVGAQEAAK-RMEKVGGG-SIISLSSTGNLVYIEN 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 30267738  171 SGGaaaYRSSKAALNALTVLYAQTLAEDGFKVNALAPGMRATD 213
Cdd:PRK08416 162 YAG---HGTSKAAVETMVKYAATELGEKNIRVNAVSGGPIDTD 201
PRK06139 PRK06139
SDR family oxidoreductase;
20-188 1.11e-04

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 42.79  E-value: 1.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   20 MNDRTALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEE---IGAGARLLVLDVTDLDGI----ARATTQVDR 92
Cdd:PRK06139   5 LHGAVVVITGASSGIGQATAEAFARRGARLVLAARDEEALQAVAEEcraLGAEVLVVPTDVTDADQVkalaTQAASFGGR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   93 LDVLVNNAGISpSLAPPADTSVEEFRRTYETNVFGVVAVTNAFLPALRRSPHPRIVN-ISSGtaslTWSTNPNpqftpgs 171
Cdd:PRK06139  85 IDVWVNNVGVG-AVGRFEETPIEAHEQVIQTNLIGYMRDAHAALPIFKKQGHGIFINmISLG----GFAAQPY------- 152

                        170
                 ....*....|....*..
gi 30267738  172 ggAAAYRSSKAALNALT 188
Cdd:PRK06139 153 --AAAYSASKFGLRGFS 167
PLN00015 PLN00015
protochlorophyllide reductase
 26-212 1.15e-04

protochlorophyllide reductase


Pssm-ID: 177654  Cd Length: 308  Bit Score: 42.77  E-value: 1.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   26 LVTGANKGIGKHIARVLVAEG-LTVYVGSRDRGLGQRAVEEIGAGAR---LLVLDVTDLDGIARATTQVDR----LDVLV 97
Cdd:PLN00015   1 IITGASSGLGLATAKALAETGkWHVVMACRDFLKAERAAKSAGMPKDsytVMHLDLASLDSVRQFVDNFRRsgrpLDVLV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   98 NNAGI-SPSLAPPADTSvEEFRRTYETNVFGVVAVTNAFLPALRRSPHP--RIVNISSGTASL-TWSTNPNPQFTPG--S 171
Cdd:PLN00015  81 CNAAVyLPTAKEPTFTA-DGFELSVGTNHLGHFLLSRLLLDDLKKSDYPskRLIIVGSITGNTnTLAGNVPPKANLGdlR 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30267738  172 G--------------------GAAAYRSSKAAlNALTV--LYAQTLAEDGFKVNALAPGMRAT 212
Cdd:PLN00015 160 GlagglnglnssamidggefdGAKAYKDSKVC-NMLTMqeFHRRYHEETGITFASLYPGCIAT 221
NDUFA9_like_SDR_a cd05271
NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, subunit 9, 39 kDa, (NDUFA9) -like, ...
 24-102 1.28e-04

NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, subunit 9, 39 kDa, (NDUFA9) -like, atypical (a) SDRs; This subgroup of extended SDR-like proteins are atypical SDRs. They have a glycine-rich NAD(P)-binding motif similar to the typical SDRs, GXXGXXG, and have the YXXXK active site motif (though not the other residues of the SDR tetrad). Members identified include NDUFA9 (mitochondrial) and putative nucleoside-diphosphate-sugar epimerase. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187579 [Multi-domain]  Cd Length: 273  Bit Score: 42.23  E-value: 1.28e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  24 TALVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRA-VEEIGAGARLLVLDVTDLDGIARAttqVDRLDVLVNNAGI 102
Cdd:cd05271   2 VVTVFGATGFIGRYVVNRLAKRGSQVIVPYRCEAYARRLlVMGDLGQVLFVEFDLRDDESIRKA---LEGSDVVINLVGR 78
KR_1_SDR_x cd08952
ketoreductase (KR), subgroup 1, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
 24-187 1.42e-04

ketoreductase (KR), subgroup 1, complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes KR domains found in many multidomain PKSs, including six of seven Sorangium cellulosum PKSs (encoded by spiDEFGHIJ) which participate in the synthesis of the polyketide scaffold of the cytotoxic spiroketal polyketide spirangien. These seven PKSs have either a single PKS module (SpiF), two PKR modules (SpiD,-E,-I,-J), or three PKS modules (SpiG,-H). This subfamily includes the single KR domain of SpiF, the first KR domains of SpiE,-G,H,-I,and #J, the third KR domain of SpiG, and the second KR domain of SpiH. The second KR domains of SpiE,-G, I, and #J, and the KR domains of SpiD, belong to a different KR_FAS_SDR subfamily. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187655 [Multi-domain]  Cd Length: 480  Bit Score: 42.54  E-value: 1.42e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  24 TALVTGANKGIGKHIARVLVAEG-----LTVYVGSRDRGLGQRAVEEIGAGARLLVL--DVTDLDGIARATTQVD---RL 93
Cdd:cd08952 232 TVLVTGGTGALGAHVARWLARRGaehlvLTSRRGPDAPGAAELVAELTALGARVTVAacDVADRDALAALLAALPaghPL 311

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  94 DVLVNNAGIsPSLAPPADTSVEEFRRTyetnVFGVVAVTNAFLPALRRSPHPRIVNISSGTAslTWstnpnpqftpGSGG 173
Cdd:cd08952 312 TAVVHAAGV-LDDGPLDDLTPERLAEV----LRAKVAGARHLDELTRDRDLDAFVLFSSIAG--VW----------GSGG 374

                       170
                ....*....|....
gi 30267738 174 AAAYRSSKAALNAL 187
Cdd:cd08952 375 QGAYAAANAYLDAL 388
UDP_G4E_4_SDR_e cd05232
UDP-glucose 4 epimerase, subgroup 4, extended (e) SDRs; UDP-glucose 4 epimerase (aka ...
 26-209 1.90e-04

UDP-glucose 4 epimerase, subgroup 4, extended (e) SDRs; UDP-glucose 4 epimerase (aka UDP-galactose-4-epimerase), is a homodimeric extended SDR. It catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. This subgroup is comprised of bacterial proteins, and includes the Staphylococcus aureus capsular polysaccharide Cap5N, which may have a role in the synthesis of UDP-N-acetyl-d-fucosamine. This subgroup has the characteristic active site tetrad and NAD-binding motif of the extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187543 [Multi-domain]  Cd Length: 303  Bit Score: 41.95  E-value: 1.90e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  26 LVTGANKGIGKHIARVLVAEGLTVYVGSRDRGlgqraveeiGAGARLLVLDVTDLDGIARATTQVdrlDVLVNNAGISPS 105
Cdd:cd05232   3 LVTGANGFIGRALVDKLLSRGEEVRIAVRNAE---------NAEPSVVLAELPDIDSFTDLFLGV---DAVVHLAARVHV 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738 106 LAPPADTSVEEFRrtyETNVFGvvavTNAFLPALRRSPHPRIVNISS--------GTASLTWSTNPNPQftpgsggaAAY 177
Cdd:cd05232  71 MNDQGADPLSDYR---KVNTEL----TRRLARAAARQGVKRFVFLSSvkvngegtVGAPFDETDPPAPQ--------DAY 135

                       170       180       190
                ....*....|....*....|....*....|...
gi 30267738 178 -RSSKAALNALTVLYaqtlAEDGFKVNALAPGM 209
Cdd:cd05232 136 gRSKLEAERALLELG----ASDGMEVVILRPPM 164
KR_FAS_SDR_x cd05274
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ...
 8-251 2.68e-04

ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. In some instances, such as porcine FAS, an enoyl reductase (ER) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consist of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthase uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-KR, forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-ER. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187582 [Multi-domain]  Cd Length: 375  Bit Score: 41.60  E-value: 2.68e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   8 WQGAHSQGTVVAMNDRTALVTGANKGIGKHIARVLVAEGLT-VYVGSRdRGLGQRAVEEIGA----GARLLVL--DVTDL 80
Cdd:cd05274 136 PAAALELAAAPGGLDGTYLITGGLGGLGLLVARWLAARGARhLVLLSR-RGPAPRAAARAALlragGARVSVVrcDVTDP 214

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  81 DGIARATTQVDR---LDVLVNNAGISPSlAPPADTSVEEFRRTYETNVFGvvavTNAFLPALRRSPHPRIVNISSgtASL 157
Cdd:cd05274 215 AALAALLAELAAggpLAGVIHAAGVLRD-ALLAELTPAAFAAVLAAKVAG----ALNLHELTPDLPLDFFVLFSS--VAA 287

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738 158 TWstnpnpqftpGSGGAAAYrsskAALNALTVLYAQTLAEDGFKVNALAPG-------MRATDLNPLAAAAGDDPAEAAQ 230
Cdd:cd05274 288 LL----------GGAGQAAY----AAANAFLDALAAQRRRRGLPATSVQWGawagggmAAAAALRARLARSGLGPLAPAE 353

                       250       260
                ....*....|....*....|..
gi 30267738 231 G-AARLALLPDDGPTGGFFSWD 251
Cdd:cd05274 354 AlEALEALLASDAPQAVVASVD 375
NAD_binding_10 pfam13460
NAD(P)H-binding;
29-115 2.93e-04

NAD(P)H-binding;


Pssm-ID: 463885 [Multi-domain]  Cd Length: 183  Bit Score: 40.67  E-value: 2.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738    29 GANKGIGKHIARVLVAEGLTVYVGSRDRglGQRAVEEIGAGARLLVLDVTDLDGIARATTQVdrlDVLVNNAGISPSLAP 108
Cdd:pfam13460   1 GATGKIGRLLVKQLLARGHEVTALVRNP--EKLADLEDHPGVEVVDGDVLDPDDLAEALAGQ---DAVISALGGGGTDET 75


                  ....*..
gi 30267738   109 PADTSVE 115
Cdd:pfam13460  76 GAKNIID 82
SDR_e_a cd05226
Extended (e) and atypical (a) SDRs; Extended or atypical short-chain dehydrogenases/reductases ...
 25-226 7.85e-04

Extended (e) and atypical (a) SDRs; Extended or atypical short-chain dehydrogenases/reductases (SDRs, aka tyrosine-dependent oxidoreductases) are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187537 [Multi-domain]  Cd Length: 176  Bit Score: 39.31  E-value: 7.85e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  25 ALVTGANKGIGKHIARVLVAEGLTVYVGSRDRglgQRAVEEIGAGARLLVLDVTDLDGIARAttqVDRLDVLVNNAGISP 104
Cdd:cd05226   1 ILILGATGFIGRALARELLEQGHEVTLLVRNT---KRLSKEDQEPVAVVEGDLRDLDSLSDA---VQGVDVVIHLAGAPR 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738 105 SLAPPADTSVEEFRrtyetNVfgvvavtnafLPALRRSPHPRIVNISSGTA--SLTWSTNPNPQFtpgsggaaAYRSSKA 182
Cdd:cd05226  75 DTRDFCEVDVEGTR-----NV----------LEAAKEAGVKHFIFISSLGAygDLHEETEPSPSS--------PYLAVKA 131

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 30267738 183 ALNALtvlyaqtLAEDGFKVNALAPGMRATDLNPLAAAAGDDPA 226
Cdd:cd05226 132 KTEAV-------LREASLPYTIVRPGVIYGDLARAIANAVVTPG 168
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
 24-92 7.97e-04

KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.


Pssm-ID: 430138 [Multi-domain]  Cd Length: 180  Bit Score: 39.08  E-value: 7.97e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30267738    24 TALVTGANKGIGKHIARVLVAEGLT--VYVgSRDRGLGQRAVEEI------GAGARLLVLDVTDLDGIARATTQVDR 92
Cdd:pfam08659   2 TYLITGGLGGLGRELARWLAERGARhlVLL-SRSAAPRPDAQALIaelearGVEVVVVACDVSDPDAVAALLAEIKA 77
SDR_a1 cd05265
atypical (a) SDRs, subgroup 1; Atypical SDRs in this subgroup are poorly defined and have been ...
 23-104 2.77e-03

atypical (a) SDRs, subgroup 1; Atypical SDRs in this subgroup are poorly defined and have been identified putatively as isoflavones reductase, sugar dehydratase, mRNA binding protein etc. Atypical SDRs are distinct from classical SDRs. Members of this subgroup retain the canonical active site triad (though not the upstream Asn found in most SDRs) but have an unusual putative glycine-rich NAD(P)-binding motif, GGXXXXG, in the usual location. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187575 [Multi-domain]  Cd Length: 250  Bit Score: 38.04  E-value: 2.77e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738  23 RTALVTGANKGIGKHIARVLVAEGLTVYVGSRdrglGQRAVeEIGAGARLLVLDVTDLDGIARATTQVDrLDVLVNNAGI 102
Cdd:cd05265   1 MKILIIGGTRFIGKALVEELLAAGHDVTVFNR----GRTKP-DLPEGVEHIVGDRNDRDALEELLGGED-FDVVVDTIAY 74


                ..
gi 30267738 103 SP 104
Cdd:cd05265  75 TP 76
PRK08340 PRK08340
SDR family oxidoreductase;
26-101 6.33e-03

SDR family oxidoreductase;


Pssm-ID: 169390 [Multi-domain]  Cd Length: 259  Bit Score: 37.09  E-value: 6.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30267738   26 LVTGANKGIGKHIARVLVAEGLTVYVGSRDRGLGQRAVEEIG--AGARLLVLDVTDLDGIAR----ATTQVDRLDVLVNN 99
Cdd:PRK08340   4 LVTASSRGIGFNVARELLKKGARVVISSRNEENLEKALKELKeyGEVYAVKADLSDKDDLKNlvkeAWELLGGIDALVWN 83


                 ..
gi 30267738  100 AG 101
Cdd:PRK08340  84 AG 85
TMR_SDR_a cd05269
triphenylmethane reductase (TMR)-like proteins, NMRa-like, atypical (a) SDRs; TMR is an ...
 26-93 7.28e-03

triphenylmethane reductase (TMR)-like proteins, NMRa-like, atypical (a) SDRs; TMR is an atypical NADP-binding protein of the SDR family. It lacks the active site residues of the SDRs but has a glycine rich NAD(P)-binding motif that matches the extended SDRs. Proteins in this subgroup however, are more similar in length to the classical SDRs. TMR was identified as a reducer of triphenylmethane dyes, important environmental pollutants. This subgroup also includes Escherichia coli NADPH-dependent quinine oxidoreductase (QOR2), which catalyzes two-electron reduction of quinone; but is unlikely to play a major role in protecting against quinone cytotoxicity. Atypical SDRs are distinct from classical SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187578 [Multi-domain]  Cd Length: 272  Bit Score: 36.86  E-value: 7.28e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30267738  26 LVTGANKGIGKHIARVLVAEGLTVYVGSRDrglGQRAVEEIGAGARLLVLDVTDLDGIARATTQVDRL 93
Cdd:cd05269   2 LVTGATGKLGTAVVELLLAKVASVVALVRN---PEKAKAFAADGVEVRQGDYDDPETLERAFEGVDRL 66
dTDP_HR_like_SDR_e cd05254
dTDP-6-deoxy-L-lyxo-4-hexulose reductase and related proteins, extended (e) SDRs; ...
 26-102 8.23e-03

dTDP-6-deoxy-L-lyxo-4-hexulose reductase and related proteins, extended (e) SDRs; dTDP-6-deoxy-L-lyxo-4-hexulose reductase, an extended SDR, synthesizes dTDP-L-rhamnose from alpha-D-glucose-1-phosphate, providing the precursor of L-rhamnose, an essential cell wall component of many pathogenic bacteria. This subgroup has the characteristic active site tetrad and NADP-binding motif. This subgroup also contains human MAT2B, the regulatory subunit of methionine adenosyltransferase (MAT); MAT catalyzes S-adenosylmethionine synthesis. The human gene encoding MAT2B encodes two major splicing variants which are induced in human cell liver cancer and regulate HuR, an mRNA-binding protein which stabilizes the mRNA of several cyclins, to affect cell proliferation. Both MAT2B variants include this extended SDR domain. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187564 [Multi-domain]  Cd Length: 280  Bit Score: 36.84  E-value: 8.23e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30267738  26 LVTGANKGIGKHIARVLVAEGLTVYVGSRDRglgqraveeigagARLLVLDVTDLDGIARATTQVdRLDVLVNNAGI 102
Cdd:cd05254   3 LITGATGMLGRALVRLLKERGYEVIGTGRSR-------------ASLFKLDLTDPDAVEEAIRDY-KPDVIINCAAY 65
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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