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Conserved domains on  [gi|2118010591|ref|XP_044298140|]
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carbonyl reductase [NADPH] 1-like [Varanus komodoensis]

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 ...
 6-276 7.16e-118

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: 336.90  E-value: 7.16e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQFSGDVYLTSRNIERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLNV 85
Cdd:cd05324     2 VALVTGANRGIGFEIVRQLAKSGPGTVILTARDVERGQAAVEKLRAEGLSVRFHQLDVTDDASIEAAADFVEEKYGGLDI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  86 LVNNAGIAFKVADTA-PFAVQAEVTMKTNFFATRNVCKELLPLLKP--NGRVVNISSMCAISALakcsqdlqqkfrsdti 162
Cdd:cd05324    82 LVNNAGIAFKGFDDStPTREQARETMKTNFFGTVDVTQALLPLLKKspAGRIVNVSSGLGSLTS---------------- 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591 163 teeelvklmekfvedtkkgvhekegwpnhAYGVTKIGVTVLSRIQARMLNEtrkgDGILLNACCPGWVRTDMAGPRATKS 242
Cdd:cd05324   146 -----------------------------AYGVSKAALNALTRILAKELKE----TGIKVNACCPGWVKTDMGGGKAPKT 192

                         250       260       270
                  ....*....|....*....|....*....|....
gi 2118010591 243 PDEGAETPVYLALLPPGAdGPHGQHVSEKKVQKW 276
Cdd:cd05324   193 PEEGAETPVYLALLPPDG-EPTGKFFSDKKVVPW 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 ...
 6-276 7.16e-118

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: 336.90  E-value: 7.16e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQFSGDVYLTSRNIERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLNV 85
Cdd:cd05324     2 VALVTGANRGIGFEIVRQLAKSGPGTVILTARDVERGQAAVEKLRAEGLSVRFHQLDVTDDASIEAAADFVEEKYGGLDI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  86 LVNNAGIAFKVADTA-PFAVQAEVTMKTNFFATRNVCKELLPLLKP--NGRVVNISSMCAISALakcsqdlqqkfrsdti 162
Cdd:cd05324    82 LVNNAGIAFKGFDDStPTREQARETMKTNFFGTVDVTQALLPLLKKspAGRIVNVSSGLGSLTS---------------- 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591 163 teeelvklmekfvedtkkgvhekegwpnhAYGVTKIGVTVLSRIQARMLNEtrkgDGILLNACCPGWVRTDMAGPRATKS 242
Cdd:cd05324   146 -----------------------------AYGVSKAALNALTRILAKELKE----TGIKVNACCPGWVKTDMGGGKAPKT 192

                         250       260       270
                  ....*....|....*....|....*....|....
gi 2118010591 243 PDEGAETPVYLALLPPGAdGPHGQHVSEKKVQKW 276
Cdd:cd05324   193 PEEGAETPVYLALLPPDG-EPTGKFFSDKKVVPW 225
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 6-254 1.06e-42

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: 146.08  E-value: 1.06e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQfsG-DVYLTSRNIERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLN 84
Cdd:COG1028     8 VALVTGGSSGIGRAIARALAAE--GaRVVITDRDAEALEAAAAELRAAGGRALAVAADVTDEAAVEALVAAAVAAFGRLD 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  85 VLVNNAGIafkvADTAPFavqAEVT-------MKTNFFATRNVCKELLPLLKPN--GRVVNISSMCAISALAkcsqdlqq 155
Cdd:COG1028    86 ILVNNAGI----TPPGPL---EELTeedwdrvLDVNLKGPFLLTRAALPHMRERggGRIVNISSIAGLRGSP-------- 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591 156 kfrsdtiteeelvklmekfvedtkkgvhekeGWPnhAYGVTKIGVTVLSRIQARMLnetrKGDGILLNACCPGWVRTDMA 235
Cdd:COG1028   151 -------------------------------GQA--AYAASKAAVVGLTRSLALEL----APRGIRVNAVAPGPIDTPMT 193

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 2118010591 236 GPRATK-----------------SPDEGAETPVYLA 254
Cdd:COG1028   194 RALLGAeevrealaariplgrlgTPEEVAAAVLFLA 229
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 6-238 2.43e-37

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 130.81  E-value: 2.43e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNIERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLNV 85
Cdd:pfam00106   2 VALVTGASSGIGRAIAKRLAKE-GAKVVLVDRSEEKLEAVAKELGALGGKALFIQGDVTDRAQVKALVEQAVERLGRLDI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  86 LVNNAGIAfKVADTAPFAVQA-EVTMKTNFFATRNVCKELLPLLK--PNGRVVNISSMcaisalakcsqdlqqkfrsdti 162
Cdd:pfam00106  81 LVNNAGIT-GLGPFSELSDEDwERVIDVNLTGVFNLTRAVLPAMIkgSGGRIVNISSV---------------------- 137

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2118010591 163 teeelvklmekfvedtkkgvHEKEGWPNH-AYGVTKIGVTVLSRIQARMLNETrkgdGILLNACCPGWVRTDMAGPR 238
Cdd:pfam00106 138 --------------------AGLVPYPGGsAYSASKAAVIGFTRSLALELAPH----GIRVNAVAPGGVDTDMTKEL 190
PRK12939 PRK12939
short chain dehydrogenase; Provisional
 6-266 1.11e-29

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 112.37  E-value: 1.11e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNIERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLNV 85
Cdd:PRK12939    9 RALVTGAARGLGAAFAEALAEA-GATVAFNDGLAAEARELAAALEAAGGRAHAIAADLADPASVQRFFDAAAAALGGLDG 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  86 LVNNAGIAfKVADTAPFAVQA-EVTMKTNFFATRNVCKELLPLLK--PNGRVVNISSMCAISALAkcsqdlqqkfrsdti 162
Cdd:PRK12939   88 LVNNAGIT-NSKSATELDIDTwDAVMNVNVRGTFLMLRAALPHLRdsGRGRIVNLASDTALWGAP--------------- 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591 163 teeelvKLMekfvedtkkgvhekegwpnhAYGVTKIGVTVLSRIQARMLnetrKGDGILLNACCPGWVRTDM--AGPR-- 238
Cdd:PRK12939  152 ------KLG--------------------AYVASKGAVIGMTRSLAREL----GGRGITVNAIAPGLTATEAtaYVPAde 201

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 2118010591 239 -----ATKSPDEGAETP-----VYLALLPPGADGPHGQ 266
Cdd:PRK12939  202 rhayyLKGRALERLQVPddvagAVLFLLSDAARFVTGQ 239
3oxo_ACP_reduc TIGR01830
3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, ...
 7-234 9.88e-20

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: 85.34  E-value: 9.88e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   7 AVVTGSNKGIGFAIVRALCKQFSgDVYLTSRNIERGKAAVAK-LQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLNV 85
Cdd:TIGR01830   1 ALVTGASRGIGRAIALKLAKEGA-KVIITYRSSEEGAEEVVEeLKALGVKALGVVLDVSDREDVKAVVEEIEEELGTIDI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  86 LVNNAGI-----AFKVADTAPFAVqaevtMKTNFFATRNVCKELLPLL--KPNGRVVNISSMCAISalakcsqdlqqkfr 158
Cdd:TIGR01830  80 LVNNAGItrdnlLMRMKEEDWDAV-----IDTNLTGVFNLTQAVLRIMikQRSGRIINISSVVGLM-------------- 140

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2118010591 159 sdtiteeelvklmekfvedtkkgvhekeGWPNHA-YGVTKIGVTVLSRIQARMLNeTRkgdGILLNACCPGWVRTDM 234
Cdd:TIGR01830 141 ----------------------------GNAGQAnYAASKAGVIGFTKSLAKELA-SR---NITVNAVAPGFIDTDM 185
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 8-103 2.42e-05

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: 44.01  E-value: 2.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591    8 VVTGSNKGIGFAIVRALCKQFSGDVYLTSRN--IERGKAA-VAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLN 84
Cdd:smart00822   4 LITGGLGGLGRALARWLAERGARRLVLLSRSgpDAPGAAAlLAELEAAGARVTVVACDVADRDALAAVLAAIPAVEGPLT 83

                           90
                   ....*....|....*....
gi 2118010591   85 VLVNNAGiafkVADTAPFA 103
Cdd:smart00822  84 GVIHAAG----VLDDGVLA 98
 
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 ...
 6-276 7.16e-118

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: 336.90  E-value: 7.16e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQFSGDVYLTSRNIERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLNV 85
Cdd:cd05324     2 VALVTGANRGIGFEIVRQLAKSGPGTVILTARDVERGQAAVEKLRAEGLSVRFHQLDVTDDASIEAAADFVEEKYGGLDI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  86 LVNNAGIAFKVADTA-PFAVQAEVTMKTNFFATRNVCKELLPLLKP--NGRVVNISSMCAISALakcsqdlqqkfrsdti 162
Cdd:cd05324    82 LVNNAGIAFKGFDDStPTREQARETMKTNFFGTVDVTQALLPLLKKspAGRIVNVSSGLGSLTS---------------- 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591 163 teeelvklmekfvedtkkgvhekegwpnhAYGVTKIGVTVLSRIQARMLNEtrkgDGILLNACCPGWVRTDMAGPRATKS 242
Cdd:cd05324   146 -----------------------------AYGVSKAALNALTRILAKELKE----TGIKVNACCPGWVKTDMGGGKAPKT 192

                         250       260       270
                  ....*....|....*....|....*....|....
gi 2118010591 243 PDEGAETPVYLALLPPGAdGPHGQHVSEKKVQKW 276
Cdd:cd05324   193 PEEGAETPVYLALLPPDG-EPTGKFFSDKKVVPW 225
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 6-254 1.06e-42

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: 146.08  E-value: 1.06e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQfsG-DVYLTSRNIERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLN 84
Cdd:COG1028     8 VALVTGGSSGIGRAIARALAAE--GaRVVITDRDAEALEAAAAELRAAGGRALAVAADVTDEAAVEALVAAAVAAFGRLD 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  85 VLVNNAGIafkvADTAPFavqAEVT-------MKTNFFATRNVCKELLPLLKPN--GRVVNISSMCAISALAkcsqdlqq 155
Cdd:COG1028    86 ILVNNAGI----TPPGPL---EELTeedwdrvLDVNLKGPFLLTRAALPHMRERggGRIVNISSIAGLRGSP-------- 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591 156 kfrsdtiteeelvklmekfvedtkkgvhekeGWPnhAYGVTKIGVTVLSRIQARMLnetrKGDGILLNACCPGWVRTDMA 235
Cdd:COG1028   151 -------------------------------GQA--AYAASKAAVVGLTRSLALEL----APRGIRVNAVAPGPIDTPMT 193

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 2118010591 236 GPRATK-----------------SPDEGAETPVYLA 254
Cdd:COG1028   194 RALLGAeevrealaariplgrlgTPEEVAAAVLFLA 229
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 7-268 1.07e-42

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: 145.89  E-value: 1.07e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   7 AVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNiERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLNVL 86
Cdd:cd05233     1 ALVTGASSGIGRAIARRLARE-GAKVVLADRN-EEALAELAAIEALGGNAVAVQADVSDEEDVEALVEEALEEFGRLDIL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  87 VNNAGIAFKVADTAPFAVQAEVTMKTNFFATRNVCKELLPLLK--PNGRVVNISSMCAISALAKcsqdlqqkfrsdtite 164
Cdd:cd05233    79 VNNAGIARPGPLEELTDEDWDRVLDVNLTGVFLLTRAALPHMKkqGGGRIVNISSVAGLRPLPG---------------- 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591 165 eelvklmekfvedtkkgvhekegwpNHAYGVTKIGVTVLSRIQARMLnetrKGDGILLNACCPGWVRTDMAGPRATK--- 241
Cdd:cd05233   143 -------------------------QAAYAASKAALEGLTRSLALEL----APYGIRVNAVAPGLVDTPMLAKLGPEeae 193

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 2118010591 242 -------------SPDEGAETPVYLALlpPGADGPHGQHV 268
Cdd:cd05233   194 kelaaaiplgrlgTPEEVAEAVVFLAS--DEASYITGQVI 231
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
1-249 3.17e-39

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 137.31  E-value: 3.17e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   1 MSNT-PVAVVTGSNKGIGFAIVRALCKQfsG-DVYLTSRNIERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKE 78
Cdd:COG0300     1 MSLTgKTVLITGASSGIGRALARALAAR--GaRVVLVARDAERLEALAAELRAAGARVEVVALDVTDPDAVAALAEAVLA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  79 KYGGLNVLVNNAGIA-FKVADTAPFAVQAEVtMKTNFFATRNVCKELLPLLK--PNGRVVNISSMCAISALAKCSqdlqq 155
Cdd:COG0300    79 RFGPIDVLVNNAGVGgGGPFEELDLEDLRRV-FEVNVFGPVRLTRALLPLMRarGRGRIVNVSSVAGLRGLPGMA----- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591 156 kfrsdtiteeelvklmekfvedtkkgvhekegwpnhAYGVTKIGVTVLSRIQARMLnetrKGDGILLNACCPGWVRTDMA 235
Cdd:COG0300   153 ------------------------------------AYAASKAALEGFSESLRAEL----APTGVRVTAVCPGPVDTPFT 192

                         250       260
                  ....*....|....*....|
gi 2118010591 236 GPRATK------SPDEGAET 249
Cdd:COG0300   193 ARAGAPagrpllSPEEVARA 212
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 6-238 2.43e-37

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 130.81  E-value: 2.43e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNIERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLNV 85
Cdd:pfam00106   2 VALVTGASSGIGRAIAKRLAKE-GAKVVLVDRSEEKLEAVAKELGALGGKALFIQGDVTDRAQVKALVEQAVERLGRLDI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  86 LVNNAGIAfKVADTAPFAVQA-EVTMKTNFFATRNVCKELLPLLK--PNGRVVNISSMcaisalakcsqdlqqkfrsdti 162
Cdd:pfam00106  81 LVNNAGIT-GLGPFSELSDEDwERVIDVNLTGVFNLTRAVLPAMIkgSGGRIVNISSV---------------------- 137

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2118010591 163 teeelvklmekfvedtkkgvHEKEGWPNH-AYGVTKIGVTVLSRIQARMLNETrkgdGILLNACCPGWVRTDMAGPR 238
Cdd:pfam00106 138 --------------------AGLVPYPGGsAYSASKAAVIGFTRSLALELAPH----GIRVNAVAPGGVDTDMTKEL 190
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 1-261 6.58e-33

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: 120.29  E-value: 6.58e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   1 MSNT-PVAVVTGSNKGIGFAIVRALCKQfsG-DVYLTSRNIERGKAAVAKLqeeGLKPLFHQLDIDDQQSIQTLRDFLKE 78
Cdd:COG4221     1 MSDKgKVALITGASSGIGAATARALAAA--GaRVVLAARRAERLEALAAEL---GGRALAVPLDVTDEAAVEAAVAAAVA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  79 KYGGLNVLVNNAGIA-FKVADTAPFAvQAEVTMKTNFFATRNVCKELLPLLKPN--GRVVNISSMCAISALAkcsqdlqq 155
Cdd:COG4221    76 EFGRLDVLVNNAGVAlLGPLEELDPE-DWDRMIDVNVKGVLYVTRAALPAMRARgsGHIVNISSIAGLRPYP-------- 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591 156 kfrsdtiteeelvklmekfvedtkkgvhekeGWPnhAYGVTKIGVTVLSRIQARmlnETRkGDGILLNACCPGWVRTDMA 235
Cdd:COG4221   147 -------------------------------GGA--VYAATKAAVRGLSESLRA---ELR-PTGIRVTVIEPGAVDTEFL 189

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 2118010591 236 GPRATK---------------SPDEGAETPVYLALLPPGAD 261
Cdd:COG4221   190 DSVFDGdaeaaaavyegleplTPEDVAEAVLFALTQPAHVN 230
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
 6-257 6.80e-33

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: 121.18  E-value: 6.80e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNIERGKAAVAKLQEEGLKPL--FHQLDIDDQQSIQTLRDFLKEKYGGL 83
Cdd:cd05327     3 VVVITGANSGIGKETARELAKR-GAHVIIACRNEEKGEEAAAEIKKETGNAKveVIQLDLSSLASVRQFAEEFLARFPRL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  84 NVLVNNAGIAfkvadTAPFAVQA---EVTMKTNFFATRNVCKELLPLLK--PNGRVVNISSMcaisalakcsqdLQQKFR 158
Cdd:cd05327    82 DILINNAGIM-----APPRRLTKdgfELQFAVNYLGHFLLTNLLLPVLKasAPSRIVNVSSI------------AHRAGP 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591 159 SDtiteeelvklmekFVEDTKKGVHEKEGWPnhAYGVTKIGVTVLSRIQARMLnetrKGDGILLNACCPGWVRTDM---- 234
Cdd:cd05327   145 ID-------------FNDLDLENNKEYSPYK--AYGQSKLANILFTRELARRL----EGTGVTVNALHPGVVRTELlrrn 205

                         250       260       270
                  ....*....|....*....|....*....|..
gi 2118010591 235 ---------AGPRATKSPDEGAETPVYLALLP 257
Cdd:cd05327   206 gsffllyklLRPFLKKSPEQGAQTALYAATSP 237
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 12-235 2.52e-30

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: 113.68  E-value: 2.52e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  12 SNKGIGFAIVRALCKQfsG-DVYLTSRNiERGKAAVAKLQEEgLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLNVLVNNA 90
Cdd:pfam13561   4 NESGIGWAIARALAEE--GaEVVLTDLN-EALAKRVEELAEE-LGAAVLPCDVTDEEQVEALVAAAVEKFGRLDILVNNA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  91 GIAFK----VADTAPFAVQAevTMKTNFFATRNVCKELLPLLKPNGRVVNISSMCAIsalakcsqdlqqkfrsdtiteee 166
Cdd:pfam13561  80 GFAPKlkgpFLDTSREDFDR--ALDVNLYSLFLLAKAALPLMKEGGSIVNLSSIGAE----------------------- 134

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591 167 lvklmekfvedtkkgvhekEGWPNH-AYGVTKIGVTVLSRIQARMLnetrKGDGILLNACCPGWVRTDMA 235
Cdd:pfam13561 135 -------------------RVVPNYnAYGAAKAALEALTRYLAVEL----GPRGIRVNAISPGPIKTLAA 181
PRK12939 PRK12939
short chain dehydrogenase; Provisional
 6-266 1.11e-29

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 112.37  E-value: 1.11e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNIERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLNV 85
Cdd:PRK12939    9 RALVTGAARGLGAAFAEALAEA-GATVAFNDGLAAEARELAAALEAAGGRAHAIAADLADPASVQRFFDAAAAALGGLDG 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  86 LVNNAGIAfKVADTAPFAVQA-EVTMKTNFFATRNVCKELLPLLK--PNGRVVNISSMCAISALAkcsqdlqqkfrsdti 162
Cdd:PRK12939   88 LVNNAGIT-NSKSATELDIDTwDAVMNVNVRGTFLMLRAALPHLRdsGRGRIVNLASDTALWGAP--------------- 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591 163 teeelvKLMekfvedtkkgvhekegwpnhAYGVTKIGVTVLSRIQARMLnetrKGDGILLNACCPGWVRTDM--AGPR-- 238
Cdd:PRK12939  152 ------KLG--------------------AYVASKGAVIGMTRSLAREL----GGRGITVNAIAPGLTATEAtaYVPAde 201

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 2118010591 239 -----ATKSPDEGAETP-----VYLALLPPGADGPHGQ 266
Cdd:PRK12939  202 rhayyLKGRALERLQVPddvagAVLFLLSDAARFVTGQ 239
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
 6-143 4.30e-28

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: 108.09  E-value: 4.30e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQfsGD-VYLTSRNIERGKAAvAKLQEEGLKPLfhQLDIDDQQSIQTLRDFLKEKYGGLN 84
Cdd:cd05374     2 VVLITGCSSGIGLALALALAAQ--GYrVIATARNPDKLESL-GELLNDNLEVL--ELDVTDEESIKAAVKEVIERFGRID 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2118010591  85 VLVNNAGIAFK--VADTAPFAVQAevTMKTNFFATRNVCKELLPLLK--PNGRVVNISSMCAI 143
Cdd:cd05374    77 VLVNNAGYGLFgpLEETSIEEVRE--LFEVNVFGPLRVTRAFLPLMRkqGSGRIVNVSSVAGL 137
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
 9-147 4.49e-26

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: 102.55  E-value: 4.49e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   9 VTGSNKGIGFAIVRALCKQfsG-DVYLTSRNIERGKAAVAKLqeeglkPLFH--QLDIDDQQSIQTLRDFLKEKYGGLNV 85
Cdd:COG3967    10 ITGGTSGIGLALAKRLHAR--GnTVIITGRREEKLEEAAAAN------PGLHtiVLDVADPASIAALAEQVTAEFPDLNV 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2118010591  86 LVNNAGI--AFKVADTAPFAVQAEVTMKTNFFATRNVCKELLPLLK--PNGRVVNISSMCAISALA 147
Cdd:COG3967    82 LINNAGImrAEDLLDEAEDLADAEREITTNLLGPIRLTAAFLPHLKaqPEAAIVNVSSGLAFVPLA 147
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
6-234 1.25e-25

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 101.39  E-value: 1.25e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQfsG-DVYLTSRNIERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLN 84
Cdd:PRK05653    7 TALVTGASRGIGRAIALRLAAD--GaKVVIYDSNEEAAEALAAELRAAGGEARVLVFDVSDEAAVRALIEAAVEAFGALD 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  85 VLVNNAGIafkvADTAPFAvqaevTMK---------TNFFATRNVCKELLPLLKPN--GRVVNISSMCAISALAkcsqdl 153
Cdd:PRK05653   85 ILVNNAGI----TRDALLP-----RMSeedwdrvidVNLTGTFNVVRAALPPMIKAryGRIVNISSVSGVTGNP------ 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591 154 qqkfrsdtiteeelvklmekfvedtkkgvhekeGWPNhaYGVTKIGVTVLSRIQARMLnetrKGDGILLNACCPGWVRTD 233
Cdd:PRK05653  150 ---------------------------------GQTN--YSAAKAGVIGFTKALALEL----ASRGITVNAVAPGFIDTD 190


                  .
gi 2118010591 234 M 234
Cdd:PRK05653  191 M 191
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
 6-237 6.23e-25

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: 99.74  E-value: 6.23e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNIERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLNV 85
Cdd:cd05347     7 VALVTGASRGIGFGIASGLAEA-GANIVINSRNEEKAEEAQQLIEKEGVEATAFTCDVSDEEAIKAAVEAIEEDFGKIDI 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  86 LVNNAGIAFKVADTAPFAVQAEVTMKTNFFATRNVCKELLPLLKP--NGRVVNISSMcaisalakcsqdlqQKFRSdtit 163
Cdd:cd05347    86 LVNNAGIIRRHPAEEFPEAEWRDVIDVNLNGVFFVSQAVARHMIKqgHGKIINICSL--------------LSELG---- 147

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2118010591 164 eeelvklmekfvedtkkgvhekeGWPNHAYGVTKIGVTVLSRIQArmlNETRKgDGILLNACCPGWVRTDMAGP 237
Cdd:cd05347   148 -----------------------GPPVPAYAASKGGVAGLTKALA---TEWAR-HGIQVNAIAPGYFATEMTEA 194
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
 7-252 6.54e-25

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: 99.29  E-value: 6.54e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   7 AVVTGSNKGIGFAIVRALCKQFSGDVYLTSRNiERGKAAVAKLQEEGLKPLFHQLDIDD--QQSIQTLRDFLKEkyGGLN 84
Cdd:cd05325     1 VLITGASRGIGLELVRQLLARGNNTVIATCRD-PSAATELAALGASHSRLHILELDVTDeiAESAEAVAERLGD--AGLD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  85 VLVNNAGIA--FKVADTAPFAVQAEvTMKTNFFATRNVCKELLPLLKPNGR--VVNISSmcaisalakcsqdlqqkfRSD 160
Cdd:cd05325    78 VLINNAGILhsYGPASEVDSEDLLE-VFQVNVLGPLLLTQAFLPLLLKGARakIINISS------------------RVG 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591 161 TITeeelvklmekfveDTKKGvhekegwPNHAYGVTKIGVTVLSRIQARMLnetrKGDGILLNACCPGWVRTDMAGPRAT 240
Cdd:cd05325   139 SIG-------------DNTSG-------GWYSYRASKAALNMLTKSLAVEL----KRDGITVVSLHPGWVRTDMGGPFAK 194

                         250
                  ....*....|..
gi 2118010591 241 kspDEGAETPVY 252
Cdd:cd05325   195 ---NKGPITPEE 203
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
 5-235 1.38e-23

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: 95.51  E-value: 1.38e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   5 PVAVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNIERGKAAVAklqeEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLN 84
Cdd:cd08932     1 KVALVTGASRGIGIEIARALARD-GYRVSLGLRNPEDLAALSA----SGGDVEAVPYDARDPEDARALVDALRDRFGRID 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  85 VLVNNAGIAFKVADTAPFAVQAEVTMKTNFFATRNVCKELLPLL--KPNGRVVNISSMCAisalakcsqdlqqkfrsdti 162
Cdd:cd08932    76 VLVHNAGIGRPTTLREGSDAELEAHFSINVIAPAELTRALLPALreAGSGRVVFLNSLSG-------------------- 135

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2118010591 163 teeelvklmekfvedtkKGVHEKegwpNHAYGVTKIGVTVLSRIQARMLNETrkgdGILLNACCPGWVRTDMA 235
Cdd:cd08932   136 -----------------KRVLAG----NAGYSASKFALRALAHALRQEGWDH----GVRVSAVCPGFVDTPMA 183
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 6-254 5.59e-23

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 94.49  E-value: 5.59e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQFSGDVYLTSRNIERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLNV 85
Cdd:PRK05557    7 VALVTGASRGIGRAIAERLAAQGANVVINYASSEAGAEALVAEIGALGGKALAVQGDVSDAESVERAVDEAKAEFGGVDI 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  86 LVNNAGIA-------FKVADtapFavqaEVTMKTNFFATRNVCKELLPLL--KPNGRVVNISSMcaisalakcsqdlqqk 156
Cdd:PRK05557   87 LVNNAGITrdnllmrMKEED---W----DRVIDTNLTGVFNLTKAVARPMmkQRSGRIINISSV---------------- 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591 157 frsdtiteeelVKLMekfvedtkkgvhekeGWPNHA-YGVTKIGVTVLSRIQARMLnetrKGDGILLNACCPGWVRTDM- 234
Cdd:PRK05557  144 -----------VGLM---------------GNPGQAnYAASKAGVIGFTKSLAREL----ASRGITVNAVAPGFIETDMt 193

                         250       260       270
                  ....*....|....*....|....*....|....
gi 2118010591 235 -AGPRATK-------------SPDEGAETPVYLA 254
Cdd:PRK05557  194 dALPEDVKeailaqiplgrlgQPEEIASAVAFLA 227
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
 6-146 2.56e-22

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: 92.47  E-value: 2.56e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQFSGDVYLTSRNIERGKAAVAKLQeEGLKPLfhQLDIDDQQSIQTLRDFLKEkyggLNV 85
Cdd:cd05354     5 TVLVTGANRGIGKAFVESLLAHGAKKVYAAVRDPGSAAHLVAKYG-DKVVPL--RLDVTDPESIKAAAAQAKD----VDV 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2118010591  86 LVNNAGIaFKVAD-TAPFAVQA-EVTMKTNFFATRNVCKELLPLLKPNGR--VVNISSMCAISAL 146
Cdd:cd05354    78 VINNAGV-LKPATlLEEGALEAlKQEMDVNVFGLLRLAQAFAPVLKANGGgaIVNLNSVASLKNF 141
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
 7-146 6.23e-22

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: 91.74  E-value: 6.23e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   7 AVVTGSNKGIGFAIVRALCkQFSGDVYLTSRNIERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGG-LNV 85
Cdd:cd05329     9 ALVTGGTKGIGYAIVEELA-GLGAEVYTCARNQKELDECLTEWREKGFKVEGSVCDVSSRSERQELMDTVASHFGGkLNI 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2118010591  86 LVNNAGIAFKVADTAPFAVQAEVTMKTNFFATRNVCKELLPLLKP--NGRVVNISSMCAISAL 146
Cdd:cd05329    88 LVNNAGTNIRKEAKDYTEEDYSLIMSTNFEAAYHLSRLAHPLLKAsgNGNIVFISSVAGVIAV 150
PRK08264 PRK08264
SDR family oxidoreductase;
6-139 7.18e-22

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 91.10  E-value: 7.18e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQFSGDVYLTSRNIERgkaavAKLQEEGLKPLfhQLDIDDQQSIQTLRDFLKEkyggLNV 85
Cdd:PRK08264    8 VVLVTGANRGIGRAFVEQLLARGAAKVYAAARDPES-----VTDLGPRVVPL--QLDVTDPASVAAAAEAASD----VTI 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2118010591  86 LVNNAGIAFK---VADTAPFAVQAEvtMKTNFFATRNVCKELLPLLKPN--GRVVNISS 139
Cdd:PRK08264   77 LVNNAGIFRTgslLLEGDEDALRAE--METNYFGPLAMARAFAPVLAANggGAIVNVLS 133
PRK12937 PRK12937
short chain dehydrogenase; Provisional
 6-234 2.44e-21

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 89.80  E-value: 2.44e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQFSGDVYLTSRNIERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLNV 85
Cdd:PRK12937    7 VAIVTGASRGIGAAIARRLAADGFAVAVNYAGSAAAADELVAEIEAAGGRAIAVQADVADAAAVTRLFDAAETAFGRIDV 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  86 LVNNAGIAF--KVADT--APFavqaEVTMKTNFFATRNVCKELLPLLKPNGRVVNISSmcaiSALAKcsqdlqqkfrsdt 161
Cdd:PRK12937   87 LVNNAGVMPlgTIADFdlEDF----DRTIATNLRGAFVVLREAARHLGQGGRIINLST----SVIAL------------- 145

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2118010591 162 iteeelvklmekfvedtkkgvhekeGWPNH-AYGVTKIGVTVLSRIQARMLnetrKGDGILLNACCPGWVRTDM 234
Cdd:PRK12937  146 -------------------------PLPGYgPYAASKAAVEGLVHVLANEL----RGRGITVNAVAPGPVATEL 190
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
 3-234 3.47e-21

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: 89.81  E-value: 3.47e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   3 NTPVAVVTGSNKGIGFAIVRALCKQfSGDVYLTS-RNIERGKAAVA-KLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKY 80
Cdd:cd08940     1 KGKVALVTGSTSGIGLGIARALAAA-GANIVLNGfGDAAEIEAVRAgLAAKHGVKVLYHGADLSKPAAIEDMVAYAQRQF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  81 GGLNVLVNNAGIAFkVADTAPFAVQA-----EVTMKTNFFATRNVckelLPLLKPN--GRVVNISSmcaisalakcsqdl 153
Cdd:cd08940    80 GGVDILVNNAGIQH-VAPIEDFPTEKwdaiiALNLSAVFHTTRLA----LPHMKKQgwGRIINIAS-------------- 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591 154 qqkfrsdtiteeelvklmekfvedtkkgVHEKEGWPNH-AYGVTKIGVTVLSRIQARmlnETrKGDGILLNACCPGWVRT 232
Cdd:cd08940   141 ----------------------------VHGLVASANKsAYVAAKHGVVGLTKVVAL---ET-AGTGVTCNAICPGWVLT 188


                  ..
gi 2118010591 233 DM 234
Cdd:cd08940   189 PL 190
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
 6-233 1.78e-20

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: 87.71  E-value: 1.78e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQFSgDVYLTSRNIERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLNV 85
Cdd:cd05344     3 VALVTAASSGIGLAIARALAREGA-RVAICARNRENLERAASELRAGGAGVLAVVADLTDPEDIDRLVEKAGDAFGRVDI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  86 LVNNAGIAFK--VADTAPFAVQAEVTMKtnFFATRNVCKELLPLLKPN--GRVVNISSMCAisalakcsqdlqqkfrsdt 161
Cdd:cd05344    82 LVNNAGGPPPgpFAELTDEDWLEAFDLK--LLSVIRIVRAVLPGMKERgwGRIVNISSLTV------------------- 140

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2118010591 162 iteeelvklmekfvedtkkgvheKEGWPNHAY-GVTKIGVTVLSRIQARMLNEtrkgDGILLNACCPGWVRTD 233
Cdd:cd05344   141 -----------------------KEPEPNLVLsNVARAGLIGLVKTLSRELAP----DGVTVNSVLPGYIDTE 186
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
 6-232 2.05e-20

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 87.63  E-value: 2.05e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNIERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLNV 85
Cdd:PRK12429    6 VALVTGAASGIGLEIALALAKE-GAKVVIADLNDEAAAAAAEALQKAGGKAIGVAMDVTDEEAINAGIDYAVETFGGVDI 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  86 LVNNAGIAFkVADTAPFAVQA-EVTMKTN----FFATRNVckelLPLLKPN--GRVVNISSmcaisalakcsqdlqqkfr 158
Cdd:PRK12429   85 LVNNAGIQH-VAPIEDFPTEKwKKMIAIMldgaFLTTKAA----LPIMKAQggGRIINMAS------------------- 140

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2118010591 159 sdtiteeelvklmekfvedtkkgVHEKEGWP-NHAYGVTKIGVTVLSRIQARmlnETRKgDGILLNACCPGWVRT 232
Cdd:PRK12429  141 -----------------------VHGLVGSAgKAAYVSAKHGLIGLTKVVAL---EGAT-HGVTVNAICPGYVDT 188
PRK12826 PRK12826
SDR family oxidoreductase;
6-240 3.49e-20

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 86.89  E-value: 3.49e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNIERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLNV 85
Cdd:PRK12826    8 VALVTGAARGIGRAIAVRLAAD-GAEVIVVDICGDDAAATAELVEAAGGKARARQVDVRDRAALKAAVAAGVEDFGRLDI 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  86 LVNNAGIafkvADTAPFA----VQAEVTMKTNFFATRNVCKELLPLLKPN--GRVVNISSmcaISALAKcsqdlqqkfrs 159
Cdd:PRK12826   87 LVANAGI----FPLTPFAemddEQWERVIDVNLTGTFLLTQAALPALIRAggGRIVLTSS---VAGPRV----------- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591 160 dtiteeelvklmekfvedtkkgvhekeGWPNHA-YGVTKIGVTVLSRIQARMLNEtrkgDGILLNACCPGWVRTDMAGPR 238
Cdd:PRK12826  149 ---------------------------GYPGLAhYAASKAGLVGFTRALALELAA----RNITVNSVHPGGVDTPMAGNL 197


                  ..
gi 2118010591 239 AT 240
Cdd:PRK12826  198 GD 199
FabG-like PRK07231
SDR family oxidoreductase;
6-235 5.80e-20

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 86.42  E-value: 5.80e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNIERGKAAVAKLQEEGlKPLFHQLDIDDQQSIQTLRDFLKEKYGGLNV 85
Cdd:PRK07231    7 VAIVTGASSGIGEGIARRFAAE-GARVVVTDRNEEAAERVAAEILAGG-RAIAVAADVSDEADVEAAVAAALERFGSVDI 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  86 LVNNAGI--AFKV---ADTAPFAVQAEVTMKTNFFATRnvckELLPLLKPN--GRVVNISSMCAISAlakcSQDLqqkfr 158
Cdd:PRK07231   85 LVNNAGTthRNGPlldVDEAEFDRIFAVNVKSPYLWTQ----AAVPAMRGEggGAIVNVASTAGLRP----RPGL----- 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2118010591 159 sdtiteeelvklmekfvedtkkgvhekeGWpnhaYGVTKIGVTVLSRIQARMLNEtrkgDGILLNACCPGWVRTDMA 235
Cdd:PRK07231  152 ----------------------------GW----YNASKGAVITLTKALAAELGP----DKIRVNAVAPVVVETGLL 192
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
 6-266 7.52e-20

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: 85.90  E-value: 7.52e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNIERGKAAVAKLqeeGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLNV 85
Cdd:cd05341     7 VAIVTGGARGLGLAHARLLVAE-GAKVVLSDILDEEGQAAAAEL---GDAARFFHLDVTDEDGWTAVVDTAREAFGRLDV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  86 LVNNAGIAF--KVADTApfAVQAEVTMKTNFFATRNVCKELLPLLKPNGR--VVNISSmcaISALAkcsqdlqqkfrsdt 161
Cdd:cd05341    83 LVNNAGILTggTVETTT--LEEWRRLLDINLTGVFLGTRAVIPPMKEAGGgsIINMSS---IEGLV-------------- 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591 162 iteeelvklmekfvedtkkgvhekeGWPN-HAYGVTKIGVTVLSRIQArmLNETRKGDGILLNACCPGWVRTDMAgprat 240
Cdd:cd05341   144 -------------------------GDPAlAAYNASKGAVRGLTKSAA--LECATQGYGIRVNSVHPGYIYTPMT----- 191

                         250       260
                  ....*....|....*....|....*.
gi 2118010591 241 kspDEGAETPVYLALLPPGADGPHGQ 266
Cdd:cd05341   192 ---DELLIAQGEMGNYPNTPMGRAGE 214
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
 5-237 7.76e-20

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: 85.98  E-value: 7.76e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   5 PVAVVTGSNKGIGFAIVRALCKqfSGDVYLTSRNIERGKAA--VAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGG 82
Cdd:cd05337     2 PVAIVTGASRGIGRAIATELAA--RGFDIAINDLPDDDQATevVAEVLAAGRRAIYFQADIGELSDHEALLDQAWEDFGR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  83 LNVLVNNAGIAFKVA----DTAP--FAVQAEVTMKTNFFATRNVCKELL----PLLKPNGRVVNISSMCAISALakcsqd 152
Cdd:cd05337    80 LDCLVNNAGIAVRPRgdllDLTEdsFDRLIAINLRGPFFLTQAVARRMVeqpdRFDGPHRSIIFVTSINAYLVS------ 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591 153 lqqkfrsdtiteeelvklmekfvedtkkgvhekegwPNHA-YGVTKIGVTVLSRIQARMLNEtrkgDGILLNACCPGWVR 231
Cdd:cd05337   154 ------------------------------------PNRGeYCISKAGLSMATRLLAYRLAD----EGIAVHEIRPGLIH 193


                  ....*.
gi 2118010591 232 TDMAGP 237
Cdd:cd05337   194 TDMTAP 199
3oxo_ACP_reduc TIGR01830
3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, ...
 7-234 9.88e-20

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: 85.34  E-value: 9.88e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   7 AVVTGSNKGIGFAIVRALCKQFSgDVYLTSRNIERGKAAVAK-LQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLNV 85
Cdd:TIGR01830   1 ALVTGASRGIGRAIALKLAKEGA-KVIITYRSSEEGAEEVVEeLKALGVKALGVVLDVSDREDVKAVVEEIEEELGTIDI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  86 LVNNAGI-----AFKVADTAPFAVqaevtMKTNFFATRNVCKELLPLL--KPNGRVVNISSMCAISalakcsqdlqqkfr 158
Cdd:TIGR01830  80 LVNNAGItrdnlLMRMKEEDWDAV-----IDTNLTGVFNLTQAVLRIMikQRSGRIINISSVVGLM-------------- 140

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2118010591 159 sdtiteeelvklmekfvedtkkgvhekeGWPNHA-YGVTKIGVTVLSRIQARMLNeTRkgdGILLNACCPGWVRTDM 234
Cdd:TIGR01830 141 ----------------------------GNAGQAnYAASKAGVIGFTKSLAKELA-SR---NITVNAVAPGFIDTDM 185
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
 6-234 3.38e-19

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: 83.86  E-value: 3.38e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQ-FSGDV-YLTSRniERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGL 83
Cdd:cd05362     5 VALVTGASRGIGRAIAKRLARDgASVVVnYASSK--AAAEEVVAEIEAAGGKAIAVQADVSDPSQVARLFDAAEKAFGGV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  84 NVLVNNAGIAFK--VADTAP--FAVQAEVTMKTNFFatrnVCKELLPLLKPNGRVVNISSmcaiSALAKcsqdlqqkfrs 159
Cdd:cd05362    83 DILVNNAGVMLKkpIAETSEeeFDRMFTVNTKGAFF----VLQEAAKRLRDGGRIINISS----SLTAA----------- 143

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2118010591 160 dtiteeelvklmekfvedtkkgvhekeGWPNH-AYGVTKIGVTVLSRIQARMLnetrKGDGILLNACCPGWVRTDM 234
Cdd:cd05362   144 ---------------------------YTPNYgAYAGSKAAVEAFTRVLAKEL----GGRGITVNAVAPGPVDTDM 188
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 6-234 5.20e-19

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: 83.37  E-value: 5.20e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNIERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLNV 85
Cdd:cd05333     2 VALVTGASRGIGRAIALRLAAE-GAKVAVTDRSEEAAAETVEEIKALGGNAAALEADVSDREAVEALVEKVEAEFGPVDI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  86 LVNNAGIafkVADTapFAV-----QAEVTMKTNFFATRNVCKELLPLL--KPNGRVVNISSmcaISALAkcsqdlqqkfr 158
Cdd:cd05333    81 LVNNAGI---TRDN--LLMrmseeDWDAVINVNLTGVFNVTQAVIRAMikRRSGRIINISS---VVGLI----------- 141

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2118010591 159 sdtiteeelvklmekfvedtkkgvhekeGWPNHA-YGVTKIGVTVLSRIQARMLnETRkgdGILLNACCPGWVRTDM 234
Cdd:cd05333   142 ----------------------------GNPGQAnYAASKAGVIGFTKSLAKEL-ASR---GITVNAVAPGFIDTDM 186
PRK07454 PRK07454
SDR family oxidoreductase;
1-260 8.70e-19

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 82.70  E-value: 8.70e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   1 MSNTPVAVVTGSNKGIGFAIVRALCKQfsG-DVYLTSRNIERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEK 79
Cdd:PRK07454    3 LNSMPRALITGASSGIGKATALAFAKA--GwDLALVARSQDALEALAAELRSTGVKAAAYSIDLSNPEAIAPGIAELLEQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  80 YGGLNVLVNNAGIAFK--VADTaPFAvQAEVTMKTNFFATRNVCKELLPLLKPN--GRVVNISSMCAISALAkcsqdlqq 155
Cdd:PRK07454   81 FGCPDVLINNAGMAYTgpLLEM-PLS-DWQWVIQLNLTSVFQCCSAVLPGMRARggGLIINVSSIAARNAFP-------- 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591 156 kfrsdtiteeelvklmekfvedtkkgvhekeGWpnHAYGVTKIGVTVLSRIqarmLNETRKGDGILLNACCPGWVRT--- 232
Cdd:PRK07454  151 -------------------------------QW--GAYCVSKAALAAFTKC----LAEEERSHGIRVCTITLGAVNTplw 193

                         250       260       270
                  ....*....|....*....|....*....|....
gi 2118010591 233 --DMAGP----RATKSPDEGAETPVYLALLPPGA 260
Cdd:PRK07454  194 dtETVQAdfdrSAMLSPEQVAQTILHLAQLPPSA 227
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
 6-236 1.18e-18

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: 82.76  E-value: 1.18e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRAlCKQFSGDVYLTSRNIERGKAAVAKLQEE-GLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLN 84
Cdd:cd05352    10 VAIVTGGSRGIGLAIARA-LAEAGADVAIIYNSAPRAEEKAEELAKKyGVKTKAYKCDVSSQESVEKTFKQIQKDFGKID 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  85 VLVNNAGIAF-KVADTAPfAVQAEVTMKTNFFATRNVCKELLPLLKPNGR--VVNISSMcaisalakcsqdlqqkfrSDT 161
Cdd:cd05352    89 ILIANAGITVhKPALDYT-YEQWNKVIDVNLNGVFNCAQAAAKIFKKQGKgsLIITASM------------------SGT 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2118010591 162 ITEeelvklmekfvedtkkgvhekegWPNH--AYGVTKIGVTVLSRIQArmlNETRKgDGILLNACCPGWVRTDMAG 236
Cdd:cd05352   150 IVN-----------------------RPQPqaAYNASKAAVIHLAKSLA---VEWAK-YFIRVNSISPGYIDTDLTD 199
PRK09242 PRK09242
SDR family oxidoreductase;
7-237 1.39e-18

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 82.49  E-value: 1.39e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   7 AVVTGSNKGIGFAIVRALCKqFSGDVYLTSRNIERGKAAVAKLQEEGLKPLFHQL--DIDDQQSIQTLRDFLKEKYGGLN 84
Cdd:PRK09242   12 ALITGASKGIGLAIAREFLG-LGADVLIVARDADALAQARDELAEEFPEREVHGLaaDVSDDEDRRAILDWVEDHWDGLH 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  85 VLVNNAG--IAFKVADTAPFAVQAevTMKTNFFATRNVCKELLPLLK--PNGRVVNISSMCAIsalakcsqdlqqkfrsd 160
Cdd:PRK09242   91 ILVNNAGgnIRKAAIDYTEDEWRG--IFETNLFSAFELSRYAHPLLKqhASSAIVNIGSVSGL----------------- 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591 161 titeeelvklmekfvedtkkgVHEKEGWPnhaYGVTKigvtvlsriqARMLNETRK------GDGILLNACCPGWVRTDM 234
Cdd:PRK09242  152 ---------------------THVRSGAP---YGMTK----------AALLQMTRNlavewaEDGIRVNAVAPWYIRTPL 197


                  ...
gi 2118010591 235 AGP 237
Cdd:PRK09242  198 TSG 200
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 6-251 1.44e-18

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 82.61  E-value: 1.44e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQfsG-DVYLTSR-NIERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGL 83
Cdd:PRK12825    8 VALVTGAARGLGRAIALRLARA--GaDVVVHYRsDEEAAEELVEAVEALGRRAQAVQADVTDKAALEAAVAAAVERFGRI 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  84 NVLVNNAGIafkvADTAPFAV----QAEVTMKTNFFATRNVCKELLPLLKPN--GRVVNISSmcaISALAkcsqdlqqkf 157
Cdd:PRK12825   86 DILVNNAGI----FEDKPLADmsddEWDEVIDVNLSGVFHLLRAVVPPMRKQrgGRIVNISS---VAGLP---------- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591 158 rsdtiteeelvklmekfvedtkkgvhekeGWP-NHAYGVTKIGVTVLSRIQARMLNETrkgdGILLNACCPGWVRTDMAG 236
Cdd:PRK12825  149 -----------------------------GWPgRSNYAAAKAGLVGLTKALARELAEY----GITVNMVAPGDIDTDMKE 195

                         250
                  ....*....|....*...
gi 2118010591 237 ---PRATKSPDegAETPV 251
Cdd:PRK12825  196 atiEEAREAKD--AETPL 211
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
 7-149 1.68e-18

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: 81.97  E-value: 1.68e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   7 AVVTGSNKGIGFAIVRALcKQFSGDVYLTSRNIERGKAAVAKLQEEGLKplfhQLDIDDQQSIQTLRDFLKEKYGGLNVL 86
Cdd:cd05370     8 VLITGGTSGIGLALARKF-LEAGNTVIITGRREERLAEAKKELPNIHTI----VLDVGDAESVEALAEALLSEYPNLDIL 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2118010591  87 VNNAGIA--FKVADTAPFAVQAEVTMKTNFFATRNVCKELLPLLK--PNGRVVNISSMCAISALAKC 149
Cdd:cd05370    83 INNAGIQrpIDLRDPASDLDKADTEIDTNLIGPIRLIKAFLPHLKkqPEATIVNVSSGLAFVPMAAN 149
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 6-142 2.25e-18

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: 81.53  E-value: 2.25e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNIERGKAAVAKLQEEGLKP----LFHQLDIDDQQSIQTLRDFLKEKYG 81
Cdd:cd08939     3 HVLITGGSSGIGKALAKELVKE-GANVIIVARSESKLEEAVEEIEAEANASgqkvSYISADLSDYEEVEQAFAQAVEKGG 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2118010591  82 GLNVLVNNAGIAFkvadTAPF----AVQAEVTMKTNFFATRNVCKELLPLLKPN--GRVVNISSMCA 142
Cdd:cd08939    82 PPDLVVNCAGISI----PGLFedltAEEFERGMDVNYFGSLNVAHAVLPLMKEQrpGHIVFVSSQAA 144
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
 6-150 2.79e-18

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: 81.56  E-value: 2.79e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQ-FSGDVYLTSRNIErgkaAVAKLQEE---GLKPLFHQLDIDDQQSIQTLRDFLKEKYG 81
Cdd:cd05367     1 VIILTGASRGIGRALAEELLKRgSPSVVVLLARSEE----PLQELKEElrpGLRVTTVKADLSDAAGVEQLLEAIRKLDG 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2118010591  82 GLNVLVNNAGIAFKVADTAPFAVQAEVT-MKTNFFATRNVCKELLPLLKP---NGRVVNISSMCAISALAKCS 150
Cdd:cd05367    77 ERDLLINNAGSLGPVSKIEFIDLDELQKyFDLNLTSPVCLTSTLLRAFKKrglKKTVVNVSSGAAVNPFKGWG 149
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 6-140 4.19e-18

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 81.04  E-value: 4.19e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQFSGDVYLTSRNIERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLNV 85
Cdd:PRK05565    7 VAIVTGASGGIGRAIAELLAKEGAKVVIAYDINEEAAQELLEEIKEEGGDAIAVKADVSSEEDVENLVEQIVEKFGKIDI 86

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2118010591  86 LVNNAGIAFkvadtapFAVQAEVT-------MKTNFFATRNVCKELLPLLKPNGR--VVNISSM 140
Cdd:PRK05565   87 LVNNAGISN-------FGLVTDMTdeewdrvIDVNLTGVMLLTRYALPYMIKRKSgvIVNISSI 143
PRK06914 PRK06914
SDR family oxidoreductase;
3-146 5.01e-18

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 81.61  E-value: 5.01e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   3 NTPVAVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNIERGKAAVAKLQEEGLKPLFH--QLDIDDQQSIQTLRDFLKEkY 80
Cdd:PRK06914    2 NKKIAIVTGASSGFGLLTTLELAKK-GYLVIATMRNPEKQENLLSQATQLNLQQNIKvqQLDVTDQNSIHNFQLVLKE-I 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2118010591  81 GGLNVLVNNAGIAFkvadtAPFAvqAEVTM-------KTNFFATRNVCKELLPLLKPN--GRVVNISSmcaISAL 146
Cdd:PRK06914   80 GRIDLLVNNAGYAN-----GGFV--EEIPVeeyrkqfETNVFGAISVTQAVLPYMRKQksGKIINISS---ISGR 144
PRK06198 PRK06198
short chain dehydrogenase; Provisional
 6-142 6.28e-18

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 80.82  E-value: 6.28e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQFSGDVYLTSRNIERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLNV 85
Cdd:PRK06198    8 VALVTGGTQGLGAAIARAFAERGAAGLVICGRNAEKGEAQAAELEALGAKAVFVQADLSDVEDCRRVVAAADEAFGRLDA 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2118010591  86 LVNNAGIAFK--VADTAP--FAVQAEVTMKTNFFATRNVCKELLPLLKPnGRVVNISSMCA 142
Cdd:PRK06198   88 LVNAAGLTDRgtILDTSPelFDRHFAVNVRAPFFLMQEAIKLMRRRKAE-GTIVNIGSMSA 147
PRK05650 PRK05650
SDR family oxidoreductase;
8-235 1.40e-17

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 80.08  E-value: 1.40e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   8 VVTGSNKGIGFAIVRALCKQfSGDVYLTSRNIERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLNVLV 87
Cdd:PRK05650    4 MITGAASGLGRAIALRWARE-GWRLALADVNEEGGEETLKLLREAGGDGFYQRCDVRDYSQLTALAQACEEKWGGIDVIV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  88 NNAGiafkVADTAPFAV----QAEVTMKTNFFATRNVCKELLPLLKP--NGRVVNISSMCAIsalakcsqdLQQKFRSDt 161
Cdd:PRK05650   83 NNAG----VASGGFFEElsleDWDWQIAINLMGVVKGCKAFLPLFKRqkSGRIVNIASMAGL---------MQGPAMSS- 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2118010591 162 iteeelvklmekfvedtkkgvhekegwpnhaYGVTKIGVTVLSRiqaRMLNETRKgDGILLNACCPGWVRTDMA 235
Cdd:PRK05650  149 -------------------------------YNVAKAGVVALSE---TLLVELAD-DEIGVHVVCPSFFQTNLL 187
PRK05693 PRK05693
SDR family oxidoreductase;
5-143 1.54e-17

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 80.22  E-value: 1.54e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   5 PVAVVTGSNKGIGfaivRALCKQFSG---DVYLTSRNIERgkaaVAKLQEEGLKPLfhQLDIDDQQSIQTLRDFLKEKYG 81
Cdd:PRK05693    2 PVVLITGCSSGIG----RALADAFKAagyEVWATARKAED----VEALAAAGFTAV--QLDVNDGAALARLAEELEAEHG 71

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2118010591  82 GLNVLVNNAGIAF--KVADTAPFAVQAEvtMKTNFFATRNVCKELLPLLKPN-GRVVNISSMCAI 143
Cdd:PRK05693   72 GLDVLINNAGYGAmgPLLDGGVEAMRRQ--FETNVFAVVGVTRALFPLLRRSrGLVVNIGSVSGV 134
PRK06484 PRK06484
short chain dehydrogenase; Validated
 6-254 1.80e-17

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 81.82  E-value: 1.80e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQfsGDVYLTsrnIERGKAAVAKLQEE-GLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLN 84
Cdd:PRK06484  271 VVAITGGARGIGRAVADRFAAA--GDRLLI---IDRDAEGAKKLAEAlGDEHLSVQADITDEAAVESAFAQIQARWGRLD 345

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  85 VLVNNAGIAFKVADTAPFAVQA-EVTMKTNFFATRNVCKELLPLLKPNGRVVNISSMCAISALAkcsqdlqqkfrsdtit 163
Cdd:PRK06484  346 VLVNNAGIAEVFKPSLEQSAEDfTRVYDVNLSGAFACARAAARLMSQGGVIVNLGSIASLLALP---------------- 409

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591 164 eeelvklmekfvedtkkgvhekegwPNHAYGVTKIGVTVLSRIQARMLNETrkgdGILLNACCPGWVRT----------- 232
Cdd:PRK06484  410 -------------------------PRNAYCASKAAVTMLSRSLACEWAPA----GIRVNTVAPGYIETpavlalkasgr 460

                         250       260
                  ....*....|....*....|....*....
gi 2118010591 233 -DMAGPRA------TKSPDEGAETPVYLA 254
Cdd:PRK06484  461 aDFDSIRRriplgrLGDPEEVAEAIAFLA 489
PRK07326 PRK07326
SDR family oxidoreductase;
6-258 2.94e-17

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 78.51  E-value: 2.94e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNIERGKAAVAKLQEEGlKPLFHQLDIDDQQSIQTLRDFLKEKYGGLNV 85
Cdd:PRK07326    8 VALITGGSKGIGFAIAEALLAE-GYKVAITARDQKELEEAAAELNNKG-NVLGLAADVRDEADVQRAVDAIVAAFGGLDV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  86 LVNNAGIA-FK-VADTAPfaVQAEVTMKTNFFATRNVCKELLPLLKPN-GRVVNISSMCAISALAKCSqdlqqkfrsdti 162
Cdd:PRK07326   86 LIANAGVGhFApVEELTP--EEWRLVIDTNLTGAFYTIKAAVPALKRGgGYIINISSLAGTNFFAGGA------------ 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591 163 teeelvklmekfvedtkkgvhekegwpnhAYGVTKIGVTVLSriQARMLnETRKgDGILLNACCPGWVRTDMAG--PRAT 240
Cdd:PRK07326  152 -----------------------------AYNASKFGLVGFS--EAAML-DLRQ-YGIKVSTIMPGSVATHFNGhtPSEK 198

                         250       260
                  ....*....|....*....|..
gi 2118010591 241 KS----PDEGAETPVYLALLPP 258
Cdd:PRK07326  199 DAwkiqPEDIAQLVLDLLKMPP 220
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
 6-234 3.12e-17

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: 78.69  E-value: 3.12e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNierGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLNV 85
Cdd:cd08944     5 VAIVTGAGAGIGAACAARLARE-GARVVVADID---GGAAQAVVAQIAGGALALRVDVTDEQQVAALFERAVEEFGGLDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  86 LVNNAGIAF---KVADTaPFAVQAEvTMKTNFFATRNVCKELLPLL--KPNGRVVNISSMCAISAlakcsqdlqqkfrsd 160
Cdd:cd08944    81 LVNNAGAMHltpAIIDT-DLAVWDQ-TMAINLRGTFLCCRHAAPRMiaRGGGSIVNLSSIAGQSG--------------- 143

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2118010591 161 titeeelvklmekfveDTKKGvhekegwpnhAYGVTKIGVTVLSRIQArmlNETRKgDGILLNACCPGWVRTDM 234
Cdd:cd08944   144 ----------------DPGYG----------AYGASKAAIRNLTRTLA---AELRH-AGIRCNALAPGLIDTPL 187
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 6-245 3.69e-17

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 78.67  E-value: 3.69e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGfaivRALCKQFSGDVYLTSRNIERGKAAVAKLQEEGLkpLFHQLDIDDQQSIQTLRDFLKEKYGGLNV 85
Cdd:PRK06463    9 VALITGGTRGIG----RAIAEAFLREGAKVAVLYNSAENEAKELREKGV--FTIKCDVGNRDQVKKSKEVVEKEFGRVDV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  86 LVNNAGIAFkvadTAPF----AVQAEVTMKTNFFATRNVCKELLPLLKP--NGRVVNISSMCAISALAKCSQdlqqkfrs 159
Cdd:PRK06463   83 LVNNAGIMY----LMPFeefdEEKYNKMIKINLNGAIYTTYEFLPLLKLskNGAIVNIASNAGIGTAAEGTT-------- 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591 160 dtiteeelvklmekfvedtkkgvhekegwpnhAYGVTKIGVTVLSRIQARMLNETrkgdGILLNACCPGWVRTDMAgpRA 239
Cdd:PRK06463  151 --------------------------------FYAITKAGIIILTRRLAFELGKY----GIRVNAVAPGWVETDMT--LS 192


                  ....*.
gi 2118010591 240 TKSPDE 245
Cdd:PRK06463  193 GKSQEE 198
PRK06179 PRK06179
short chain dehydrogenase; Provisional
 1-139 4.37e-17

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 78.79  E-value: 4.37e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   1 MSNTPVAVVTGSNKGIGFAIVRALCKQfsG-DVYLTSRNIERGKAAvaklqeEGLKPLfhQLDIDDQQSIQTLRDFLKEK 79
Cdd:PRK06179    1 MSNSKVALVTGASSGIGRATAEKLARA--GyRVFGTSRNPARAAPI------PGVELL--ELDVTDDASVQAAVDEVIAR 70

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2118010591  80 YGGLNVLVNNAGIAFkVADTAPFAV-QAEVTMKTNFFATRNVCKELLPLLKP--NGRVVNISS 139
Cdd:PRK06179   71 AGRIDVLVNNAGVGL-AGAAEESSIaQAQALFDTNVFGILRMTRAVLPHMRAqgSGRIINISS 132
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 3-241 4.41e-17

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 78.46  E-value: 4.41e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   3 NTPVAVVTGSNKGIGFAIVRALCKQ-FsgDVYLTS-RNIERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKY 80
Cdd:PRK12745    1 MRPVALVTGGRRGIGLGIARALAAAgF--DLAINDrPDDEELAATQQELRALGVEVIFFPADVADLSAHEAMLDAAQAAW 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  81 GGLNVLVNNAGIAFKVA----DTAP------FAVQAEVTmktnFFATRNVCKELLPLLKPNGR----VVNISSMCAISAL 146
Cdd:PRK12745   79 GRIDCLVNNAGVGVKVRgdllDLTPesfdrvLAINLRGP----FFLTQAVAKRMLAQPEPEELphrsIVFVSSVNAIMVS 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591 147 AKcsqdlqqkfRSDtiteeelvklmekfvedtkkgvhekegwpnhaYGVTKIGVTVLSRIQARMLNETrkgdGILLNACC 226
Cdd:PRK12745  155 PN---------RGE--------------------------------YCISKAGLSMAAQLFAARLAEE----GIGVYEVR 189

                         250
                  ....*....|....*
gi 2118010591 227 PGWVRTDMAGPRATK 241
Cdd:PRK12745  190 PGLIKTDMTAPVTAK 204
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 5-251 4.75e-17

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: 78.11  E-value: 4.75e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   5 PVAVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNIERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLN 84
Cdd:cd05323     1 KVAIITGGASGIGLATAKLLLKK-GAKVAILDRNENPGAAAELQAINPKVKATFVQCDVTSWEQLAAAFKKAIEKFGRVD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  85 VLVNNAGIA--FKVADTAPFAVQAEVTMKTNFFATRNVCKELLPLLK-----PNGRVVNISSMCAISALAKCSqdlqqkf 157
Cdd:cd05323    80 ILINNAGILdeKSYLFAGKLPPPWEKTIDVNLTGVINTTYLALHYMDknkggKGGVIVNIGSVAGLYPAPQFP------- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591 158 rsdtiteeelvklmekfvedtkkgvhekegwpnhAYGVTKIGVTVLSRIQARMLNEtrkGDGILLNACCPGWVRTDMAGP 237
Cdd:cd05323   153 ----------------------------------VYSASKHGVVGFTRSLADLLEY---KTGVRVNAICPGFTNTPLLPD 195

                         250
                  ....*....|....
gi 2118010591 238 RATKSPDEGAETPV 251
Cdd:cd05323   196 LVAKEAEMLPSAPT 209
PRK06181 PRK06181
SDR family oxidoreductase;
6-147 5.28e-17

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 78.48  E-value: 5.28e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGfaivRALCKQFSG---DVYLTSRNIERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGG 82
Cdd:PRK06181    3 VVIITGASEGIG----RALAVRLARagaQLVLAARNETRLASLAQELADHGGEALVVPTDVSDAEACERLIEAAVARFGG 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2118010591  83 LNVLVNNAGIAF--KVADTAPFAVQAEVtMKTNFFATRNVCKELLPLLKPN-GRVVNISSMCAISALA 147
Cdd:PRK06181   79 IDILVNNAGITMwsRFDELTDLSVFERV-MRVNYLGAVYCTHAALPHLKASrGQIVVVSSLAGLTGVP 145
PRK06182 PRK06182
short chain dehydrogenase; Validated
 2-140 6.08e-17

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 78.46  E-value: 6.08e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   2 SNTPVAVVTGSNKGIGFAIVRALcKQFSGDVYLTSRNIERgkaaVAKLQEEGLKPLfhQLDIDDQQSIQTLRDFLKEKYG 81
Cdd:PRK06182    1 MQKKVALVTGASSGIGKATARRL-AAQGYTVYGAARRVDK----MEDLASLGVHPL--SLDVTDEASIKAAVDTIIAEEG 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2118010591  82 GLNVLVNNAGI-AFKVADTAPFAvQAEVTMKTNFFATRNVCKELLPLL--KPNGRVVNISSM 140
Cdd:PRK06182   74 RIDVLVNNAGYgSYGAIEDVPID-EARRQFEVNLFGAARLTQLVLPHMraQRSGRIINISSM 134
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
 6-235 6.80e-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: 77.96  E-value: 6.80e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNIERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLNV 85
Cdd:cd08945     5 VALVTGATSGIGLAIARRLGKE-GLRVFVCARGEEGLATTVKELREAGVEADGRTCDVRSVPEIEALVAAAVARYGPIDV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  86 LVNNAG------IAfKVADTAPFAVqAEVTMKTNFFATRNVCKELLPLLKPNGRVVNISSMCAisalakcsqdlqqkfrs 159
Cdd:cd08945    84 LVNNAGrsgggaTA-ELADELWLDV-VETNLTGVFRVTKEVLKAGGMLERGTGRIINIASTGG----------------- 144

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2118010591 160 dtiteeelvklmekfvedtKKGVhekegwpNHA--YGVTKIGVTVLSRIQARMLNETrkgdGILLNACCPGWVRTDMA 235
Cdd:cd08945   145 -------------------KQGV-------VHAapYSASKHGVVGFTKALGLELART----GITVNAVCPGFVETPMA 192
PRK06128 PRK06128
SDR family oxidoreductase;
7-250 1.52e-16

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 77.59  E-value: 1.52e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   7 AVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNIERGKAA--VAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLN 84
Cdd:PRK06128   58 ALITGADSGIGRATAIAFARE-GADIALNYLPEEEQDAAevVQLIQAEGRKAVALPGDLKDEAFCRQLVERAVKELGGLD 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  85 VLVNNAGIAFKVADTAPFAV-QAEVTMKTNFFATRNVCKELLPLLKPNGRVVNISSMcaisalakcsQDLQQkfrSDTIT 163
Cdd:PRK06128  137 ILVNIAGKQTAVKDIADITTeQFDATFKTNVYAMFWLCKAAIPHLPPGASIINTGSI----------QSYQP---SPTLL 203

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591 164 EeelvklmekfvedtkkgvhekegwpnhaYGVTKIGVTVLSRIQARMLNETrkgdGILLNACCPGWVRTDM---AGPRAT 240
Cdd:PRK06128  204 D----------------------------YASTKAAIVAFTKALAKQVAEK----GIRVNAVAPGPVWTPLqpsGGQPPE 251

                         250
                  ....*....|
gi 2118010591 241 KSPDEGAETP 250
Cdd:PRK06128  252 KIPDFGSETP 261
PRK06484 PRK06484
short chain dehydrogenase; Validated
 6-254 1.61e-16

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 79.12  E-value: 1.61e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGfaivRALCKQFS--GD-VYLTSRNIERgkaAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGG 82
Cdd:PRK06484    7 VVLVTGAAGGIG----RAACQRFAraGDqVVVADRNVER---ARERADSLGPDHHALAMDVSDEAQIREGFEQLHREFGR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  83 LNVLVNNAGI----AFKVADTAPFAVQAevTMKTNFFATRNVCKELLPLL---KPNGRVVNISSMCAISALAKcsqdlqq 155
Cdd:PRK06484   80 IDVLVNNAGVtdptMTATLDTTLEEFAR--LQAINLTGAYLVAREALRLMieqGHGAAIVNVASGAGLVALPK------- 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591 156 kfRSdtiteeelvklmekfvedtkkgvhekegwpnhAYGVTKIGVTVLSRIQARMLNETrkgdGILLNACCPGWVRTDM- 234
Cdd:PRK06484  151 --RT--------------------------------AYSASKAAVISLTRSLACEWAAK----GIRVNAVLPGYVRTQMv 192

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 2118010591 235 -----AG---PRATKS---------PDEGAETPVYLA 254
Cdd:PRK06484  193 aelerAGkldPSAVRSriplgrlgrPEEIAEAVFFLA 229
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
 5-249 2.18e-16

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: 76.28  E-value: 2.18e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   5 PVAVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNIERGKAAVAK------------LQEEGLKPLFHQLDIDDQQSIQTL 72
Cdd:cd05338     4 KVAFVTGASRGIGRAIALRLAKA-GATVVVAAKTASEGDNGSAKslpgtieetaeeIEAAGGQALPIVVDVRDEDQVRAL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  73 RDFLKEKYGGLNVLVNNAGIAF--KVADTApfAVQAEVTMKTNFFATRNVCKELLPLLKPN--GRVVNISSMCAISAlak 148
Cdd:cd05338    83 VEATVDQFGRLDILVNNAGAIWlsLVEDTP--AKRFDLMQRVNLRGTYLLSQAALPHMVKAgqGHILNISPPLSLRP--- 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591 149 csqdlqqkfrsdtiteeelvklmekfvedtkkgvhekeGWPNHAYGVTKIGVTVLsriqARMLNETRKGDGILLNACcpg 228
Cdd:cd05338   158 --------------------------------------ARGDVAYAAGKAGMSRL----TLGLAAELRRHGIAVNSL--- 192

                         250       260
                  ....*....|....*....|.
gi 2118010591 229 WVRTDMAGPRATKSPDEGAET 249
Cdd:cd05338   193 WPSTAIETPAATELSGGSDPA 213
PRK07774 PRK07774
SDR family oxidoreductase;
6-233 3.18e-16

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 75.94  E-value: 3.18e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNIERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLNV 85
Cdd:PRK07774    8 VAIVTGAAGGIGQAYAEALARE-GASVVVADINAEGAERVAKQIVADGGTAIAVQVDVSDPDSAKAMADATVSAFGGIDY 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  86 LVNNA----GIAFKVADTAPFAVQAEVtMKTNFFATRNVCKELLPLL--KPNGRVVNISSMCAisalakcsqdlqqkfrs 159
Cdd:PRK07774   87 LVNNAaiygGMKLDLLITVPWDYYKKF-MSVNLDGALVCTRAVYKHMakRGGGAIVNQSSTAA----------------- 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2118010591 160 dtiteeelvklmekfvedtkkgvhekegW-PNHAYGVTKIGVTVLSRIQARMLNetrkGDGILLNACCPGWVRTD 233
Cdd:PRK07774  149 ----------------------------WlYSNFYGLAKVGLNGLTQQLARELG----GMNIRVNAIAPGPIDTE 191
PRK06138 PRK06138
SDR family oxidoreductase;
6-254 3.64e-16

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 75.96  E-value: 3.64e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNIErGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLNV 85
Cdd:PRK06138    7 VAIVTGAGSGIGRATAKLFARE-GARVVVADRDAE-AAERVAAAIAAGGRAFARQGDVGSAEAVEALVDFVAARWGRLDV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  86 LVNNAG--IAFKVADTAPFAVQAevTMKTNFFATRNVCKELLPLLKPN--GRVVNISSMCAISALAKcsqdlqqkfrsdt 161
Cdd:PRK06138   85 LVNNAGfgCGGTVVTTDEADWDA--VMRVNVGGVFLWAKYAIPIMQRQggGSIVNTASQLALAGGRG------------- 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591 162 iteeelvklmekfvedtkkgvhekegwpNHAYGVTKIGVTVLSRIQArMLNETrkgDGILLNACCPGWVRTDM------- 234
Cdd:PRK06138  150 ----------------------------RAAYVASKGAIASLTRAMA-LDHAT---DGIRVNAVAPGTIDTPYfrrifar 197

                         250       260       270
                  ....*....|....*....|....*....|....
gi 2118010591 235 -AGPRATKS-------------PDEGAETPVYLA 254
Cdd:PRK06138  198 hADPEALREalrarhpmnrfgtAEEVAQAALFLA 231
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
 6-140 4.07e-16

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: 75.65  E-value: 4.07e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNIERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLNV 85
Cdd:cd08934     5 VALVTGASSGIGEATARALAAE-GAAVAIAARRVDRLEALADELEAEGGKALVLELDVTDEQQVDAAVERTVEALGRLDI 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2118010591  86 LVNNAGI----AFKVADTAPFAVQAEVTMKTNFFATRNVckelLPLLKPN--GRVVNISSM 140
Cdd:cd08934    84 LVNNAGImllgPVEDADTTDWTRMIDTNLLGLMYTTHAA----LPHHLLRnkGTIVNISSV 140
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
 6-234 4.10e-16

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: 75.88  E-value: 4.10e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNIERG-KAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLN 84
Cdd:cd05366     4 VAIITGAAQGIGRAIAERLAAD-GFNIVLADLNLEEAaKSTIQEISEAGYNAVAVGADVTDKDDVEALIDQAVEKFGSFD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  85 VLVNNAGIafkvADTAPFAVQAEVTMKT----NFFATRNVCKELLPLLKP---NGRVVNISSMCAIsalakcsqdlqqkf 157
Cdd:cd05366    83 VMVNNAGI----APITPLLTITEEDLKKvyavNVFGVLFGIQAAARQFKKlghGGKIINASSIAGV-------------- 144

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2118010591 158 rsdtiteeelvklmekfvedtkkgvhekEGWPN-HAYGVTKIGVTVLSRIQARMLnetrKGDGILLNACCPGWVRTDM 234
Cdd:cd05366   145 ----------------------------QGFPNlGAYSASKFAVRGLTQTAAQEL----APKGITVNAYAPGIVKTEM 190
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
 8-268 4.56e-16

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: 75.61  E-value: 4.56e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   8 VVTGSNKGIGFAIVRALckQFSGDVYLtsrNIErgkaavaklqeegLKPLFHQLDIDDQQSIQTL-RDFLKEKYGGLNVL 86
Cdd:cd05328     3 VITGAASGIGAATAELL--EDAGHTVI---GID-------------LREADVIADLSTPEGRAAAiADVLARCSGVLDGL 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  87 VNNAGIafkvadtaPFAVQAEVTMKTNFFATRNVCKELLPLLKPN--GRVVNISSMCAIsalakcsqdlQQKFRSDtite 164
Cdd:cd05328    65 VNCAGV--------GGTTVAGLVLKVNYFGLRALMEALLPRLRKGhgPAAVVVSSIAGA----------GWAQDKL---- 122

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591 165 eELVKLMEKFVEDTKKGVHEKEGWPNH-AYGVTKIGVTVLSRiqaRMLNETRKGDGILLNACCPGWVRT--------DMA 235
Cdd:cd05328   123 -ELAKALAAGTEARAVALAEHAGQPGYlAYAGSKEALTVWTR---RRAATWLYGAGVRVNTVAPGPVETpilqaflqDPR 198

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 2118010591 236 GPRATKS----------PDEGAetPVYLALLPPGADGPHGQHV 268
Cdd:cd05328   199 GGESVDAfvtpmgrraePDEIA--PVIAFLASDAASWINGANL 239
PRK07063 PRK07063
SDR family oxidoreductase;
6-259 8.42e-16

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 75.09  E-value: 8.42e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNIERGKAAVAKLQEE--GLKPLFHQLDIDDQQSIQTLRDFLKEKYGGL 83
Cdd:PRK07063    9 VALVTGAAQGIGAAIARAFARE-GAAVALADLDAALAERAAAAIARDvaGARVLAVPADVTDAASVAAAVAAAEEAFGPL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  84 NVLVNNAGIAFkvadtapFAVQAEVT-------MKTNFFATRNVCKELLPLLKPNGR--VVNISSMCAISALAKCsqdlq 154
Cdd:PRK07063   88 DVLVNNAGINV-------FADPLAMTdedwrrcFAVDLDGAWNGCRAVLPGMVERGRgsIVNIASTHAFKIIPGC----- 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591 155 qkfrsdtiteeelvklmekfvedtkkgvhekegWPnhaYGVTKIGVTVLSR---IQ--ARmlnetrkgdGILLNACCPGW 229
Cdd:PRK07063  156 ---------------------------------FP---YPVAKHGLLGLTRalgIEyaAR---------NVRVNAIAPGY 190

                         250       260       270
                  ....*....|....*....|....*....|
gi 2118010591 230 VRTDMAGPRATKSPDEGAETPVYLALLPPG 259
Cdd:PRK07063  191 IETQLTEDWWNAQPDPAAARAETLALQPMK 220
PRK06124 PRK06124
SDR family oxidoreductase;
6-140 1.55e-15

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 74.36  E-value: 1.55e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKqfSG-DVYLTSRNIERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLN 84
Cdd:PRK06124   13 VALVTGSARGLGFEIARALAG--AGaHVLVNGRNAATLEAAVAALRAAGGAAEALAFDIADEEAVAAAFARIDAEHGRLD 90

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  85 VLVNNAGIAFK--VADTAPFAVQAevTMKTNFFATRNVCKELLPLLKPN--GRVVNISSM 140
Cdd:PRK06124   91 ILVNNVGARDRrpLAELDDAAIRA--LLETDLVAPILLSRLAAQRMKRQgyGRIIAITSI 148
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
 7-235 2.04e-15

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: 73.54  E-value: 2.04e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   7 AVVTGSNKGIGFAIVRALCKQfSGDVYLTSR-NIERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLNV 85
Cdd:cd05359     1 ALVTGGSRGIGKAIALRLAER-GADVVINYRkSKDAAAEVAAEIEELGGKAVVVRADVSQPQDVEEMFAAVKERFGRLDV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  86 LVNNAGI-AFK-VADTAPFAVQAevTMKTNFFATRNVCKELLPLLKPN--GRVVNISSMCAISALAkcsqdlqqkfrsdt 161
Cdd:cd05359    80 LVSNAAAgAFRpLSELTPAHWDA--KMNTNLKALVHCAQQAAKLMRERggGRIVAISSLGSIRALP-------------- 143

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2118010591 162 iteeelvklmekfvedtkkgvhekegwPNHAYGVTKIGVTVLSRIQARMLNEtrkgDGILLNACCPGWVRTDMA 235
Cdd:cd05359   144 ---------------------------NYLAVGTAKAALEALVRYLAVELGP----RGIRVNAVSPGVIDTDAL 186
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
6-234 2.23e-15

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 73.61  E-value: 2.23e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQ-FSgdVYLTSRNIERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLN 84
Cdd:PRK08643    4 VALVTGAGQGIGFAIAKRLVEDgFK--VAIVDYNEETAQAAADKLSKDGGKAIAVKADVSDRDQVFAAVRQVVDTFGDLN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  85 VLVNNAGIafkvADTAPFAVQAE--------VTMKTNFFATRnVCKELLPLLKPNGRVVNissmcaisalaKCSQdlqqk 156
Cdd:PRK08643   82 VVVNNAGV----APTTPIETITEeqfdkvynINVGGVIWGIQ-AAQEAFKKLGHGGKIIN-----------ATSQ----- 140

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2118010591 157 frsdtiteeelvklmekfvedtkKGVhekEGWPNHA-YGVTKIGVTVLSRIQARMLNEtrkgDGILLNACCPGWVRTDM 234
Cdd:PRK08643  141 -----------------------AGV---VGNPELAvYSSTKFAVRGLTQTAARDLAS----EGITVNAYAPGIVKTPM 189
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 6-148 2.75e-15

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: 73.43  E-value: 2.75e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGfaivRALCKQFSGD---VYLTSRNIERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGG 82
Cdd:cd05339     1 IVLITGGGSGIG----RLLALEFAKRgakVVILDINEKGAEETANNVRKAGGKVHYYKCDVSKREEVYEAAKKIKKEVGD 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  83 LNVLVNNAGIA--FKVADTAPFAVqaEVTMKTNFFATRNVCKELLPLL--KPNGRVVNISSMCAISALAK 148
Cdd:cd05339    77 VTILINNAGVVsgKKLLELPDEEI--EKTFEVNTLAHFWTTKAFLPDMleRNHGHIVTIASVAGLISPAG 144
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
 6-228 3.41e-15

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: 73.14  E-value: 3.41e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALcKQFSGDVYLTSRNIERGKAAVAKLQEEGLKP-LFHQLDIDDQQSIQTLRDFLKEKYGGLN 84
Cdd:cd08930     4 IILITGAAGLIGKAFCKAL-LSAGARLILADINAPALEQLKEELTNLYKNRvIALELDITSKESIKELIESYLEKFGRID 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  85 VLVNNAGIAFKVADTAPFAVQAE-------VTMKTNFFATRNVCKELLPllKPNGRVVNISSMCAISAlakcsqdlqQKF 157
Cdd:cd08930    83 ILINNAYPSPKVWGSRFEEFPYEqwnevlnVNLGGAFLCSQAFIKLFKK--QGKGSIINIASIYGVIA---------PDF 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2118010591 158 RSDTITEeelvklMEKFVEdtkkgvhekegwpnhaYGVTKIGVTVLSRIQARMLnetrKGDGILLNACCPG 228
Cdd:cd08930   152 RIYENTQ------MYSPVE----------------YSVIKAGIIHLTKYLAKYY----ADTGIRVNAISPG 196
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 6-139 3.88e-15

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 72.80  E-value: 3.88e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNIERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLNV 85
Cdd:PRK07666    9 NALITGAGRGIGRAVAIALAKE-GVNVGLLARTEENLKAVAEEVEAYGVKVVIATADVSDYEEVTAAIEQLKNELGSIDI 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2118010591  86 LVNNAGIA-F-KVADTAPfaVQAEVTMKTNFFATRNVCKELLPLL--KPNGRVVNISS 139
Cdd:PRK07666   88 LINNAGISkFgKFLELDP--AEWEKIIQVNLMGVYYATRAVLPSMieRQSGDIINISS 143
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
 7-145 5.30e-15

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: 72.15  E-value: 5.30e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   7 AVVTGSNKGIGFAIVRALCKQFSGdVYLTSRNiERGKAAVAKLQEEGLKPLfhQLDIDDQQSIQTLRDFLKEKYGGLNVL 86
Cdd:cd08929     3 ALVTGASRGIGEATARLLHAEGYR-VGICARD-EARLAAAAAQELEGVLGL--AGDVRDEADVRRAVDAMEEAFGGLDAL 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2118010591  87 VNNAGIAF--KVADTAPFAVQAEV--TMKTNFFATRnvcKELLPLL-KPNGRVVNISSMCAISA 145
Cdd:cd08929    79 VNNAGVGVmkPVEELTPEEWRLVLdtNLTGAFYCIH---KAAPALLrRGGGTIVNVGSLAGKNA 139
PRK12829 PRK12829
short chain dehydrogenase; Provisional
 6-235 1.19e-14

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 72.01  E-value: 1.19e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALcKQFSGDVYLTSRNIERGKAAVAKLqeEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLNV 85
Cdd:PRK12829   13 RVLVTGGASGIGRAIAEAF-AEAGARVHVCDVSEAALAATAARL--PGAKVTATVADVADPAQVERVFDTAVERFGGLDV 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  86 LVNNAGIA---FKVADTAPfaVQAEVTMKTNFFATRNVCKELLPLLKPNGR---VVNISSMCAISALAkcsqdlqqkfrs 159
Cdd:PRK12829   90 LVNNAGIAgptGGIDEITP--EQWEQTLAVNLNGQFYFARAAVPLLKASGHggvIIALSSVAGRLGYP------------ 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2118010591 160 dtiteeelvklmekfvedtkkgvhekeGWPNhaYGVTKIGVTVLSRIQARMLNEtrkgDGILLNACCPGWVRTDMA 235
Cdd:PRK12829  156 ---------------------------GRTP--YAASKWAVVGLVKSLAIELGP----LGIRVNAILPGIVRGPRM 198
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
 3-248 1.43e-14

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 71.47  E-value: 1.43e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   3 NTPVAVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNIERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGG 82
Cdd:PRK13394    6 NGKTAVVTGAASGIGKEIALELARA-GAAVAIADLNQDGANAVADEINKAGGKAIGVAMDVTNEDAVNAGIDKVAERFGS 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  83 LNVLVNNAGIAFkVADTAPFAVQ-----AEVTMKTNFFATRNVCKELLPlLKPNGRVVNISSmcaisalakcsqdlqqkf 157
Cdd:PRK13394   85 VDILVSNAGIQI-VNPIENYSFAdwkkmQAIHVDGAFLTTKAALKHMYK-DDRGGVVIYMGS------------------ 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591 158 rsdtiteeelvklmekfvedtkkgVHEKEGWP-NHAYGVTKIGVTVLSRIQARmlnETrKGDGILLNACCPGWVRTdmag 236
Cdd:PRK13394  145 ------------------------VHSHEASPlKSAYVTAKHGLLGLARVLAK---EG-AKHNVRSHVVCPGFVRT---- 192

                         250
                  ....*....|..
gi 2118010591 237 PRATKSPDEGAE 248
Cdd:PRK13394  193 PLVDKQIPEQAK 204
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
 6-146 1.81e-14

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: 71.08  E-value: 1.81e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQfsG-DVYLTSRNIERGKAAVAKLQEEG-LKPLFHQLDIDDQQSIQTLRDFLKEKYGGL 83
Cdd:cd05332     5 VVIITGASSGIGEELAYHLARL--GaRLVLSARREERLEEVKSECLELGaPSPHVVPLDMSDLEDAEQVVEEALKLFGGL 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2118010591  84 NVLVNNAGIA-FKVADTAPFAVQAEVtMKTNFFATRNVCKELLPLLKPN--GRVVNISSMCAISAL 146
Cdd:cd05332    83 DILINNAGISmRSLFHDTSIDVDRKI-MEVNYFGPVALTKAALPHLIERsqGSIVVVSSIAGKIGV 147
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
 6-259 1.92e-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: 71.00  E-value: 1.92e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNIERGKAAVAKLQEEGLKPLF-HQLDIDDQQSIQTLRDFLKEKYGGLN 84
Cdd:cd05343     8 VALVTGASVGIGAAVARALVQH-GMKVVGCARRVDKIEALAAECQSAGYPTLFpYQCDLSNEEQILSMFSAIRTQHQGVD 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  85 VLVNNAGIAFK--VADTAPFAVQAevTMKTNFFATRNVCKELLPLLK----PNGRVVNISSMcaisalakcsqdlqqkfr 158
Cdd:cd05343    87 VCINNAGLARPepLLSGKTEGWKE--MFDVNVLALSICTREAYQSMKernvDDGHIININSM------------------ 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591 159 sdtiteeelvklmekfvedtkKGVHEKEGWPNHAYGVTKIGVTVLSRIQARMLNETRKgdGILLNACCPGWVRTDMAGPR 238
Cdd:cd05343   147 ---------------------SGHRVPPVSVFHFYAATKHAVTALTEGLRQELREAKT--HIRATSISPGLVETEFAFKL 203

                         250       260
                  ....*....|....*....|.
gi 2118010591 239 ATKSPDEGAETPVYLALLPPG 259
Cdd:cd05343   204 HDNDPEKAAATYESIPCLKPE 224
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
 6-139 2.62e-14

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: 70.69  E-value: 2.62e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKqFSGDVYLTSRNIERGKAAVAKLQEEGLKPLF-HQLDIDDQQSIQTLRDFLKEKYGGLN 84
Cdd:cd05369     5 VAFITGGGTGIGKAIAKAFAE-LGASVAIAGRKPEVLEAAAEEISSATGGRAHpIQCDVRDPEAVEAAVDETLKEFGKID 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2118010591  85 VLVNNAGIAFkVADTAPFAVQA-EVTMKTNFFATRNVCKELLPLL---KPNGRVVNISS 139
Cdd:cd05369    84 ILINNAAGNF-LAPAESLSPNGfKTVIDIDLNGTFNTTKAVGKRLieaKHGGSILNISA 141
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
 6-142 4.03e-14

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: 70.40  E-value: 4.03e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNIERGKAAVAK--LQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGL 83
Cdd:cd05355    28 KALITGGDSGIGRAVAIAFARE-GADVAINYLPEEEDDAEETKklIEEEGRKCLLIPGDLGDESFCRDLVKEVVKEFGKL 106

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2118010591  84 NVLVNNAG---IAFKVADTAPfaVQAEVTMKTNFFATRNVCKELLPLLKPNGRVVNISSMCA 142
Cdd:cd05355   107 DILVNNAAyqhPQESIEDITT--EQLEKTFRTNIFSMFYLTKAALPHLKKGSSIINTTSVTA 166
DHRS-12_like_SDR_c-like cd09808
human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like ...
 8-274 4.51e-14

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: 70.32  E-value: 4.51e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   8 VVTGSNKGIGFAIVRALCKQfSGDVYLTSRNIERGKAAVAKLQEE-GLKPLF-HQLDIDDQQSIQTLRDFLKEKYGGLNV 85
Cdd:cd09808     5 LITGANSGIGKAAALAIAKR-GGTVHMVCRNQTRAEEARKEIETEsGNQNIFlHIVDMSDPKQVWEFVEEFKEEGKKLHV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  86 LVNNAGIAFKVADTAPFAVqaEVTMKTNFFATRNVCKELLPLLK--PNGRVVNISSmcaisalakcSQDLQQKFRSDTIT 163
Cdd:cd09808    84 LINNAGCMVNKRELTEDGL--EKNFATNTLGTYILTTHLIPVLEkeEDPRVITVSS----------GGMLVQKLNTNNLQ 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591 164 EEelvklmekfvedtkKGVHEKegwpNHAYGVTKigvtvlsRIQARMLNETRKGD-GILLNACCPGW-----VRTDMAGP 237
Cdd:cd09808   152 SE--------------RTAFDG----TMVYAQNK-------RQQVIMTEQWAKKHpEIHFSVMHPGWadtpaVRNSMPDF 206

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 2118010591 238 RAT-----KSPDEGAETPVYLALLPPGADGPHGQHVSEKKVQ 274
Cdd:cd09808   207 HARfkdrlRSEEQGADTVVWLALSSAAAKAPSGRFYQDRKPV 248
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
 6-262 4.52e-14

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: 70.10  E-value: 4.52e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQFSGDV--YLTSRniERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGL 83
Cdd:cd05358     5 VALVTGASSGIGKAIAIRLATAGANVVvnYRSKE--DAAEEVVEEIKAVGGKAIAVQADVSKEEDVVALFQSAIKEFGTL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  84 NVLVNNAGIAFKVA----DTAPFAVQAEVTMKTNFFATRNVCKEllpLLKPN--GRVVNISSmcaisalakcsqdlqqkf 157
Cdd:cd05358    83 DILVNNAGLQGDASshemTLEDWNKVIDVNLTGQFLCAREAIKR---FRKSKikGKIINMSS------------------ 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591 158 rsdtiteeelvklmekfvedtkkgVHEKEGWPNHA-YGVTKIGVTVLSRIQARMLNEtrkgDGILLNACCPGWVRTDMAG 236
Cdd:cd05358   142 ------------------------VHEKIPWPGHVnYAASKGGVKMMTKTLAQEYAP----KGIRVNAIAPGAINTPINA 193

                         250       260
                  ....*....|....*....|....*.
gi 2118010591 237 PrATKSPDEGAETpvyLALLPPGADG 262
Cdd:cd05358   194 E-AWDDPEQRADL---LSLIPMGRIG 215
PRK06197 PRK06197
short chain dehydrogenase; Provisional
 6-139 5.72e-14

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 70.44  E-value: 5.72e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNIERGKAAVAKLQEE--GLKPLFHQLDIDDQQSIQTLRDFLKEKYGGL 83
Cdd:PRK06197   18 VAVVTGANTGLGYETAAALAAK-GAHVVLAVRNLDKGKAAAARITAAtpGADVTLQELDLTSLASVRAAADALRAAYPRI 96

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2118010591  84 NVLVNNAGIAfkvadTAPFAVQA---EVTMKTN----FFATRNVCKELLPLlkPNGRVVNISS 139
Cdd:PRK06197   97 DLLINNAGVM-----YTPKQTTAdgfELQFGTNhlghFALTGLLLDRLLPV--PGSRVVTVSS 152
PRK07806 PRK07806
SDR family oxidoreductase;
6-139 6.23e-14

SDR family oxidoreductase;


Pssm-ID: 181126 [Multi-domain]  Cd Length: 248  Bit Score: 69.75  E-value: 6.23e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQFSGDVYLTSRNIERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLNV 85
Cdd:PRK07806    8 TALVTGSSRGIGADTAKILAGAGAHVVVNYRQKAPRANKVVAEIEAAGGRASAVGADLTDEESVAALMDTAREEFGGLDA 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2118010591  86 LVNNAGIAFKVADTAPFAvqaevtMKTNFFATRNVCKELLPLLKPNGRVVNISS 139
Cdd:PRK07806   88 LVLNASGGMESGMDEDYA------MRLNRDAQRNLARAALPLMPAGSRVVFVTS 135
PRK06949 PRK06949
SDR family oxidoreductase;
6-234 7.12e-14

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 69.41  E-value: 7.12e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIG--FAIVRAlckQFSGDVYLTSRNIERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGL 83
Cdd:PRK06949   11 VALVTGASSGLGarFAQVLA---QAGAKVVLASRRVERLKELRAEIEAEGGAAHVVSLDVTDYQSIKAAVAHAETEAGTI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  84 NVLVNNAGIAF--KVADTAP--FAVQAEVTMKTNFFATRNVCKELL------PLLKPNGRVVNISSMCAISALAKCSqdl 153
Cdd:PRK06949   88 DILVNNSGVSTtqKLVDVTPadFDFVFDTNTRGAFFVAQEVAKRMIarakgaGNTKPGGRIINIASVAGLRVLPQIG--- 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591 154 qqkfrsdtiteeelvklmekfvedtkkgvhekegwpnhAYGVTKIGVTVLSRIqarMLNETRKgDGILLNACCPGWVRTD 233
Cdd:PRK06949  165 --------------------------------------LYCMSKAAVVHMTRA---MALEWGR-HGINVNAICPGYIDTE 202


                  .
gi 2118010591 234 M 234
Cdd:PRK06949  203 I 203
PRK08628 PRK08628
SDR family oxidoreductase;
6-144 1.24e-13

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 68.83  E-value: 1.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQFSGDVYLtSRNiERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLNV 85
Cdd:PRK08628    9 VVIVTGGASGIGAAISLRLAEEGAIPVIF-GRS-APDDEFAEELRALQPRAEFVQVDLTDDAQCRDAVEQTVAKFGRIDG 86

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2118010591  86 LVNNAGIAFKVA-DTAPFAVQAevTMKTNFFATRNVCKELLPLLK-PNGRVVNISSMCAIS 144
Cdd:PRK08628   87 LVNNAGVNDGVGlEAGREAFVA--SLERNLIHYYVMAHYCLPHLKaSRGAIVNISSKTALT 145
PRK06057 PRK06057
short chain dehydrogenase; Provisional
 6-255 1.34e-13

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 68.60  E-value: 1.34e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNIERGKAAVAKLqeEGLkplFHQLDIDDQQSIQTLRDFLKEKYGGLNV 85
Cdd:PRK06057    9 VAVITGGGSGIGLATARRLAAE-GATVVVGDIDPEAGKAAADEV--GGL---FVPTDVTDEDAVNALFDTAAETYGSVDI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  86 LVNNAGIA----FKVADTAPFA---VQaEVTMKTNFFAtrnvCKELLPLLKPNGR--VVNISSMCAISALAKcSQDlqqk 156
Cdd:PRK06057   83 AFNNAGISppedDSILNTGLDAwqrVQ-DVNLTSVYLC----CKAALPHMVRQGKgsIINTASFVAVMGSAT-SQI---- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591 157 frsdtiteeelvklmekfvedtkkgvhekegwpnhAYGVTKIGVTVLSR---IQ-ARmlnetrkgDGILLNACCPGWVRT 232
Cdd:PRK06057  153 -----------------------------------SYTASKGGVLAMSRelgVQfAR--------QGIRVNALCPGPVNT 189

                         250       260
                  ....*....|....*....|...
gi 2118010591 233 DMAGPRATKSPDEGAETPVYLAL 255
Cdd:PRK06057  190 PLLQELFAKDPERAARRLVHVPM 212
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 9-140 1.44e-13

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: 68.84  E-value: 1.44e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   9 VTGSNKGIGFAIVRALCKQ-FSgdVYLTSRNIERGKAAvaKLQE---EGLKPLfhQLDIDDQQSIQTLRDFLKEKYG--G 82
Cdd:cd09805     5 ITGCDSGFGNLLAKKLDSLgFT--VLAGCLTKNGPGAK--ELRRvcsDRLRTL--QLDVTKPEQIKRAAQWVKEHVGekG 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2118010591  83 LNVLVNNAGIA--FKVADTAPFAVQAEVtMKTNFFATRNVCKELLPLL-KPNGRVVNISSM 140
Cdd:cd09805    79 LWGLVNNAGILgfGGDEELLPMDDYRKC-MEVNLFGTVEVTKAFLPLLrRAKGRVVNVSSM 138
PRK07062 PRK07062
SDR family oxidoreductase;
6-142 2.06e-13

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 68.53  E-value: 2.06e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNIERGKAAVAKLQEE-GLKPLFHQ-LDIDDQQSIQTLRDFLKEKYGGL 83
Cdd:PRK07062   10 VAVVTGGSSGIGLATVELLLEA-GASVAICGRDEERLASAEARLREKfPGARLLAArCDVLDEADVAAFAAAVEARFGGV 88

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2118010591  84 NVLVNNAGIAFKV--ADTAPFAVQAEVTMKtnFFATRNVCKELLPLLK--PNGRVVNISSMCA 142
Cdd:PRK07062   89 DMLVNNAGQGRVStfADTTDDAWRDELELK--YFSVINPTRAFLPLLRasAAASIVCVNSLLA 149
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
 6-233 2.13e-13

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: 67.98  E-value: 2.13e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKqFSGDVYLTSRNIERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLNV 85
Cdd:cd05365     1 VAIVTGGAAGIGKAIAGTLAK-AGASVVIADLKSEGAEAVAAAIQQAGGQAIGLECNVTSEQDLEAVVKATVSQFGGITI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  86 LVNNAGIAFKVADTAPFAV-QAEVTMKTNFFATRNVCKELLPLLKP--NGRVVNISSMCAISalakcsqdlqqkfRSDTI 162
Cdd:cd05365    80 LVNNAGGGGPKPFDMPMTEeDFEWAFKLNLFSAFRLSQLCAPHMQKagGGAILNISSMSSEN-------------KNVRI 146

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2118010591 163 TeeelvklmekfvedtkkgvhekegwpnhAYGVTKIGVTVLSRIQARMLNEtrkgDGILLNACCPGWVRTD 233
Cdd:cd05365   147 A----------------------------AYGSSKAAVNHMTRNLAFDLGP----KGIRVNAVAPGAVKTD 185
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
6-139 2.29e-13

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 69.87  E-value: 2.29e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQfsG-DVYLTSRNIERGKAAVAKLQEEGlKPLFHQLDIDDQQSIQTLRDFLKEKYGGLN 84
Cdd:PRK08324  424 VALVTGAAGGIGKATAKRLAAE--GaCVVLADLDEEAAEAAAAELGGPD-RALGVACDVTDEAAVQAAFEEAALAFGGVD 500

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2118010591  85 VLVNNAGIAFkvadTAPFavqAEVTMKT-------NFFATRNVCKELLPLLKPN---GRVVNISS 139
Cdd:PRK08324  501 IVVSNAGIAI----SGPI---EETSDEDwrrsfdvNATGHFLVAREAVRIMKAQglgGSIVFIAS 558
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
 6-235 3.96e-13

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 67.28  E-value: 3.96e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALcKQFSGDVYLTSRNIERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLNV 85
Cdd:PRK08213   14 TALVTGGSRGLGLQIAEAL-GEAGARVVLSARKAEELEEAAAHLEALGIDALWIAADVADEADIERLAEETLERFGHVDI 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  86 LVNNAGIAFKV-ADTAPFAVQAEVtMKTN----FFATRNVCKELLpLLKPNGRVVNISSmcaISALAKCSQDLQqkfrsD 160
Cdd:PRK08213   93 LVNNAGATWGApAEDHPVEAWDKV-MNLNvrglFLLSQAVAKRSM-IPRGYGRIINVAS---VAGLGGNPPEVM-----D 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2118010591 161 TIteeelvklmekfvedtkkgvhekegwpnhAYGVTKIGVTVLSRIQArmlneTRKGD-GILLNACCPGWVRTDMA 235
Cdd:PRK08213  163 TI-----------------------------AYNTSKGAVINFTRALA-----AEWGPhGIRVNAIAPGFFPTKMT 204
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
6-146 4.04e-13

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 67.44  E-value: 4.04e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQFSGDVYLTSRNIERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLNV 85
Cdd:PRK08063    6 VALVTGSSRGIGKAIALRLAEEGYDIAVNYARSRKAAEETAEEIEALGRKALAVKANVGDVEKIKEMFAQIDEEFGRLDV 85

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2118010591  86 LVNNA--GI---AFKVADTapfavQAEVTMKTNFFATRNVCKELLPLL--KPNGRVVNISSMCAISAL 146
Cdd:PRK08063   86 FVNNAasGVlrpAMELEES-----HWDWTMNINAKALLFCAQEAAKLMekVGGGKIISLSSLGSIRYL 148
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
 7-148 4.99e-13

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 67.10  E-value: 4.99e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   7 AVVTGSNKGIGFAIVRALcKQFSGDVYLTSRNIERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLNVL 86
Cdd:PRK07523   13 ALVTGSSQGIGYALAEGL-AQAGAEVILNGRDPAKLAAAAESLKGQGLSAHALAFDVTDHDAVRAAIDAFEAEIGPIDIL 91

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2118010591  87 VNNAGIAFKvADTAPFAVQA-EVTMKTN----FFATRNVCKELLPllKPNGRVVNISSMcaISALAK 148
Cdd:PRK07523   92 VNNAGMQFR-TPLEDFPADAfERLLRTNissvFYVGQAVARHMIA--RGAGKIINIASV--QSALAR 153
PRK07890 PRK07890
short chain dehydrogenase; Provisional
 6-140 5.11e-13

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 67.29  E-value: 5.11e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRAlCKQFSGDVYLTSRNIERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLNV 85
Cdd:PRK07890    7 VVVVSGVGPGLGRTLAVR-AARAGADVVLAARTAERLDEVAAEIDDLGRRALAVPTDITDEDQCANLVALALERFGRVDA 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2118010591  86 LVNNAGI--AFK-VADTAPFAVQAevTMKTNFFATRNVCKELLPLLKP-NGRVVNISSM 140
Cdd:PRK07890   86 LVNNAFRvpSMKpLADADFAHWRA--VIELNVLGTLRLTQAFTPALAEsGGSIVMINSM 142
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 6-148 5.60e-13

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: 67.10  E-value: 5.60e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNIERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLNV 85
Cdd:cd08935     7 VAVITGGTGVLGGAMARALAQA-GAKVAALGRNQEKGDKVAKEITALGGRAIALAADVLDRASLERAREEIVAQFGTVDI 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  86 LVNNAGIAFKVADTAPFAVQAEVTmkTNFFATRNVCKE----------LLP--------LLKPNGRVVNISSMCAISALA 147
Cdd:cd08935    86 LINGAGGNHPDATTDPEHYEPETE--QNFFDLDEEGWEfvfdlnlngsFLPsqvfgkdmLEQKGGSIINISSMNAFSPLT 163


                  .
gi 2118010591 148 K 148
Cdd:cd08935   164 K 164
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
 6-143 5.62e-13

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: 67.05  E-value: 5.62e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNIERGKAAVAKLQEEGL---KPLFHQLDIDDQQSIQTLRDFLKEKYGG 82
Cdd:cd05364     5 VAIITGSSSGIGAGTAILFARL-GARLALTGRDAERLEETRQSCLQAGVsekKILLVVADLTEEEGQDRIISTTLAKFGR 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2118010591  83 LNVLVNNAGIAFKVADTAPFAVQAEVTMKTNFFATRNVCKELLP-LLKPNGRVVNISSMCAI 143
Cdd:cd05364    84 LDILVNNAGILAKGGGEDQDIEEYDKVMNLNLRAVIYLTKLAVPhLIKTKGEIVNVSSVAGG 145
PRK07035 PRK07035
SDR family oxidoreductase;
6-144 6.31e-13

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 66.96  E-value: 6.31e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCkQFSGDVYLTSRNIERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLNV 85
Cdd:PRK07035   10 IALVTGASRGIGEAIAKLLA-QQGAHVIVSSRKLDGCQAVADAIVAAGGKAEALACHIGEMEQIDALFAHIRERHGRLDI 88

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2118010591  86 LVNNAGIA--F-KVADTAPFAVQ--AEVTMKTNFFatrnVCKELLPLLKPNGR--VVNISSMCAIS 144
Cdd:PRK07035   89 LVNNAAANpyFgHILDTDLGAFQktVDVNIRGYFF----MSVEAGKLMKEQGGgsIVNVASVNGVS 150
PRK07074 PRK07074
SDR family oxidoreductase;
6-244 6.50e-13

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 66.72  E-value: 6.50e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGfaivRALCKQFSGD---VYLTSRNIERGKAAVAKLQEEGLKPLfhQLDIDDQQSIQTLRDFLKEKYGG 82
Cdd:PRK07074    4 TALVTGAAGGIG----QALARRFLAAgdrVLALDIDAAALAAFADALGDARFVPV--ACDLTDAASLAAALANAAAERGP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  83 LNVLVNNAGIAFKV--ADTAPFAVQAEVTMKTN--FFATRNVCKELLPLLKpnGRVVNISSMCAISALakcsqdlqqkfr 158
Cdd:PRK07074   78 VDVLVANAGAARAAslHDTTPASWRADNALNLEaaYLCVEAVLEGMLKRSR--GAVVNIGSVNGMAAL------------ 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591 159 sdtiteeelvklmekfvedtkkgvhekeGWPnhAYGVTKIGVTVLSRIQARMLNEtrkgDGILLNACCPGWVRTDMAGPR 238
Cdd:PRK07074  144 ----------------------------GHP--AYSAAKAGLIHYTKLLAVEYGR----FGIRANAVAPGTVKTQAWEAR 189


                  ....*.
gi 2118010591 239 ATKSPD 244
Cdd:PRK07074  190 VAANPQ 195
PRK07856 PRK07856
SDR family oxidoreductase;
6-143 6.69e-13

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 66.88  E-value: 6.69e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNiergkaavAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLNV 85
Cdd:PRK07856    8 VVLVTGGTRGIGAGIARAFLAA-GATVVVCGRR--------APETVDGRPAEFHAADVRDPDQVAALVDAIVERHGRLDV 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2118010591  86 LVNNAGiafkvadTAPFAVQAEVT-------MKTNFFATRNVCKELLPLLKPN---GRVVNISSMCAI 143
Cdd:PRK07856   79 LVNNAG-------GSPYALAAEASprfhekiVELNLLAPLLVAQAANAVMQQQpggGSIVNIGSVSGR 139
PRK06841 PRK06841
short chain dehydrogenase; Provisional
 6-146 9.38e-13

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 66.22  E-value: 9.38e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNiERGKAAVAKLQEEGLKPlfHQLDIDDQQSIQTLRDFLKEKYGGLNV 85
Cdd:PRK06841   17 VAVVTGGASGIGHAIAELFAAK-GARVALLDRS-EDVAEVAAQLLGGNAKG--LVCDVSDSQSVEAAVAAVISAFGRIDI 92

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2118010591  86 LVNNAGIAF----KVADTAPFAVQAEVTMKTNFFATRNVCKELLPllKPNGRVVNISSMCAISAL 146
Cdd:PRK06841   93 LVNSAGVALlapaEDVSEEDWDKTIDINLKGSFLMAQAVGRHMIA--AGGGKIVNLASQAGVVAL 155
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
 6-276 1.03e-12

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: 66.34  E-value: 1.03e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNIERGKAAVAKLQEEGLKP--LFHQLDIDDQQSIQTLRDFLKEKYGGL 83
Cdd:cd09807     3 TVIITGANTGIGKETARELARR-GARVIMACRDMAKCEEAAAEIRRDTLNHevIVRHLDLASLKSIRAFAAEFLAEEDRL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  84 NVLVNNAGIA----FKVADTapFAVQAEVTMKTNFFATrNVckeLLPLLK--PNGRVVNISSMCAISALAKcSQDLQQKF 157
Cdd:cd09807    82 DVLINNAGVMrcpySKTEDG--FEMQFGVNHLGHFLLT-NL---LLDLLKksAPSRIVNVSSLAHKAGKIN-FDDLNSEK 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591 158 RSDTiteeelvklmeKFvedtkkgvhekegwpnhAYGVTKIGVTVLSRIQARMLnetrKGDGILLNACCPGWVRTDM--- 234
Cdd:cd09807   155 SYNT-----------GF-----------------AYCQSKLANVLFTRELARRL----QGTGVTVNALHPGVVRTELgrh 202

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2118010591 235 AGPRAT--------------KSPDEGAETPVYLAlLPPGADGPHGQHVSEKKvQKW 276
Cdd:cd09807   203 TGIHHLflstllnplfwpfvKTPREGAQTSIYLA-LAEELEGVSGKYFSDCK-LKE 256
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
 6-228 1.58e-12

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: 65.58  E-value: 1.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNIERGKAAVAKLQEEGlKPLFHQLDIDDQQSIQTLRDFLKEKYGGLNV 85
Cdd:cd08942     8 IVLVTGGSRGIGRMIAQGFLEA-GARVIISARKAEACADAAEELSAYG-ECIAIPADLSSEEGIEALVARVAERSDRLDV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  86 LVNNAGIAFKVA-DTAP---FAVQAEVTMKTNFFATrnvcKELLPLLKPNG------RVVNISSMCAISAlakcsqdlqq 155
Cdd:cd08942    86 LVNNAGATWGAPlEAFPesgWDKVMDINVKSVFFLT----QALLPLLRAAAtaenpaRVINIGSIAGIVV---------- 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2118010591 156 kfrsdtiteeelvklmekfvedtkkgvhekEGWPNHAYGVTKIGVTVLSRIQARMLnetrKGDGILLNACCPG 228
Cdd:cd08942   152 ------------------------------SGLENYSYGASKAAVHQLTRKLAKEL----AGEHITVNAIAPG 190
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
 6-144 2.00e-12

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: 65.49  E-value: 2.00e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNIERGKAAVAKLQEEGLkplFHQLDIDDQQSIQTLRDFLKEKYGGLNV 85
Cdd:cd05345     7 VAIVTGAGSGFGEGIARRFAQE-GARVVIADINADGAERVAADIGEAAI---AIQADVTKRADVEAMVEAALSKFGRLDI 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2118010591  86 LVNNAGIAFKVADT-----APFAVQAEVTMKTNFFATRnvckELLPLLKPNGRVV--NISSMCAIS 144
Cdd:cd05345    83 LVNNAGITHRNKPMlevdeEEFDRVFAVNVKSIYLSAQ----ALVPHMEEQGGGViiNIASTAGLR 144
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
 6-143 2.05e-12

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: 65.63  E-value: 2.05e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQFSgDVYLTSRNIERGKAAVAKLQEEGL-KPLFHQLDIDDQQSIQTLRDFLKEKYGGLN 84
Cdd:cd08933    11 VVIVTGGSRGIGRGIVRAFVENGA-KVVFCARGEAAGQALESELNRAGPgSCKFVPCDVTKEEDIKTLISVTVERFGRID 89

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2118010591  85 VLVNNAGIAFKVADTAPFAVQA-EVTMKTNFFATRNVCKELLPLL-KPNGRVVNISSMCAI 143
Cdd:cd08933    90 CLVNNAGWHPPHQTTDETSAQEfRDLLNLNLISYFLASKYALPHLrKSQGNIINLSSLVGS 150
PRK08589 PRK08589
SDR family oxidoreductase;
6-145 2.19e-12

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 65.57  E-value: 2.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQfsGDVYLTSRNIERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLNV 85
Cdd:PRK08589    8 VAVITGASTGIGQASAIALAQE--GAYVLAVDIAEAVSETVDKIKSNGGKAKAYHVDISDEQQVKDFASEIKEQFGRVDV 85

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2118010591  86 LVNNAGIAFKVADTAPFAVQA-----EVTMKTNFFATrnvcKELLPL-LKPNGRVVNISSMCAISA 145
Cdd:PRK08589   86 LFNNAGVDNAAGRIHEYPVDVfdkimAVDMRGTFLMT----KMLLPLmMEQGGSIINTSSFSGQAA 147
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
 6-148 3.06e-12

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 65.31  E-value: 3.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNIERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLNV 85
Cdd:PRK08277   12 VAVITGGGGVLGGAMAKELARA-GAKVAILDRNQEKAEAVVAEIKAAGGEALAVKADVLDKESLEQARQQILEDFGPCDI 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  86 LVNNAGIAFKVADTAPFAVQAEVTMKT---------------NFFATrnvckeLLP--------LLKPNGRVVNISSMCA 142
Cdd:PRK08277   91 LINGAGGNHPKATTDNEFHELIEPTKTffdldeegfefvfdlNLLGT------LLPtqvfakdmVGRKGGNIINISSMNA 164


                  ....*.
gi 2118010591 143 ISALAK 148
Cdd:PRK08277  165 FTPLTK 170
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
 5-139 3.11e-12

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: 64.61  E-value: 3.11e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   5 PVAVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNIERgkaaVAKLQEE-----GLKPLFHQLDIDDQQSIQTLRDFLKEK 79
Cdd:cd05346     1 KTVLITGASSGIGEATARRFAKA-GAKLILTGRRAER----LQELADElgakfPVKVLPLQLDVSDRESIEAALENLPEE 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2118010591  80 YGGLNVLVNNAGIAFKVADTAPFAVQAEVTM-KTNFFATRNVCKELLPLL--KPNGRVVNISS 139
Cdd:cd05346    76 FRDIDILVNNAGLALGLDPAQEADLEDWETMiDTNVKGLLNVTRLILPIMiaRNQGHIINLGS 138
PRK09072 PRK09072
SDR family oxidoreductase;
8-139 3.44e-12

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 64.96  E-value: 3.44e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   8 VVTGSNKGIGFAIVRALCKQfSGDVYLTSRNIERgkaaVAKLQEEGLKPLFHQL---DIDDQQSIQTLRDFLKEkYGGLN 84
Cdd:PRK09072    9 LLTGASGGIGQALAEALAAA-GARLLLVGRNAEK----LEALAARLPYPGRHRWvvaDLTSEAGREAVLARARE-MGGIN 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2118010591  85 VLVNNAGIA-FK-VADTAPFAVQAEVTmkTNFFATRNVCKELLPLLK--PNGRVVNISS 139
Cdd:PRK09072   83 VLINNAGVNhFAlLEDQDPEAIERLLA--LNLTAPMQLTRALLPLLRaqPSAMVVNVGS 139
PRK06172 PRK06172
SDR family oxidoreductase;
6-249 4.03e-12

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 64.39  E-value: 4.03e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNIERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLNV 85
Cdd:PRK06172    9 VALVTGGAAGIGRATALAFARE-GAKVVVADRDAAGGEETVALIREAGGEALFVACDVTRDAEVKALVEQTIAAYGRLDY 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  86 LVNNAGIafkVADTAPFAVQAEvtmkTNFFATRNV-------C-KELLPLLKPN--GRVVNISSMCAISALAKCSqdlqq 155
Cdd:PRK06172   88 AFNNAGI---EIEQGRLAEGSE----AEFDAIMGVnvkgvwlCmKYQIPLMLAQggGAIVNTASVAGLGAAPKMS----- 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591 156 kfrsdtiteeelvklmekfvedtkkgvhekegwpnhAYGVTKIGVTVLSRIQArmLNETRKgdGILLNACCPGWVRTDMA 235
Cdd:PRK06172  156 ------------------------------------IYAASKHAVIGLTKSAA--IEYAKK--GIRVNAVCPAVIDTDMF 195

                         250
                  ....*....|....
gi 2118010591 236 gPRATKSPDEGAET 249
Cdd:PRK06172  196 -RRAYEADPRKAEF 208
PRK12827 PRK12827
short chain dehydrogenase; Provisional
 6-139 4.34e-12

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 64.36  E-value: 4.34e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALcKQFSGDVYLTSRNIERGK----AAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYG 81
Cdd:PRK12827    8 RVLITGGSGGLGRAIAVRL-AADGADVIVLDIHPMRGRaeadAVAAGIEAAGGKALGLAFDVRDFAATRAALDAGVEEFG 86

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2118010591  82 GLNVLVNNAGIafkvADTAPFAV----QAEVTMKTNFFATRNVCKELL-PLLKPN--GRVVNISS 139
Cdd:PRK12827   87 RLDILVNNAGI----ATDAAFAElsieEWDDVIDVNLDGFFNVTQAALpPMIRARrgGRIVNIAS 147
PRK07201 PRK07201
SDR family oxidoreductase;
6-139 5.27e-12

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 65.74  E-value: 5.27e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNIERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLNV 85
Cdd:PRK07201  373 VVLITGASSGIGRATAIKVAEA-GATVFLVARNGEALDELVAEIRAKGGTAHAYTCDLTDSAAVDHTVKDILAEHGHVDY 451

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2118010591  86 LVNNAG--IAFKVADTAPFAVQAEVTMKTNFFATRNVCKELLPLL--KPNGRVVNISS 139
Cdd:PRK07201  452 LVNNAGrsIRRSVENSTDRFHDYERTMAVNYFGAVRLILGLLPHMreRRFGHVVNVSS 509
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 5-144 6.24e-12

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 63.97  E-value: 6.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   5 PVAVVTGSNKGIGFAIVRALCKQFSGDVYLTSRNIERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLN 84
Cdd:PRK06077    7 KVVVVTGSGRGIGRAIAVRLAKEGSLVVVNAKKRAEEMNETLKMVKENGGEGIGVLADVSTREGCETLAKATIDRYGVAD 86

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2118010591  85 VLVNNAGIA----FKVADTAPFAVQAEVTMKTNFFATrnvcKELLPLLKPNGRVVNISSMCAIS 144
Cdd:PRK06077   87 ILVNNAGLGlfspFLNVDDKLIDKHISTDFKSVIYCS----QELAKEMREGGAIVNIASVAGIR 146
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
 7-163 7.41e-12

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 63.62  E-value: 7.41e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   7 AVVTGSNKGIGFAIVRALCkQFSGDVYLTSRNIERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLNVL 86
Cdd:PRK08085   12 ILITGSAQGIGFLLATGLA-EYGAEIIINDITAERAELAVAKLRQEGIKAHAAPFNVTHKQEVEAAIEHIEKDIGPIDVL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  87 VNNAGIAFKVADTApFAVQ-----AEVTMKTNFFATRNVCKELLPllKPNGRVVNISSMcaisalakcsqdlQQKFRSDT 161
Cdd:PRK08085   91 INNAGIQRRHPFTE-FPEQewndvIAVNQTAVFLVSQAVARYMVK--RQAGKIINICSM-------------QSELGRDT 154


                  ..
gi 2118010591 162 IT 163
Cdd:PRK08085  155 IT 156
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
 6-140 8.39e-12

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 63.93  E-value: 8.39e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQFSGDVY--LTSRNIERGKAAvakLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGL 83
Cdd:PRK07097   12 IALITGASYGIGFAIAKAYAKAGATIVFndINQELVDKGLAA---YRELGIEAHGYVCDVTDEDGVQAMVSQIEKEVGVI 88

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2118010591  84 NVLVNNAGIAFKVA----DTAPFAVQAEVTMKTNFFATRNVCKELLPllKPNGRVVNISSM 140
Cdd:PRK07097   89 DILVNNAGIIKRIPmlemSAEDFRQVIDIDLNAPFIVSKAVIPSMIK--KGHGKIINICSM 147
PRK08219 PRK08219
SDR family oxidoreductase;
5-139 8.51e-12

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 63.03  E-value: 8.51e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   5 PVAVVTGSNKGIGFAIVRALCKQFsgDVYLTSRNIERGKAAVAKLqeEGLKPLfhQLDIDDQQSIQTlrdfLKEKYGGLN 84
Cdd:PRK08219    4 PTALITGASRGIGAAIARELAPTH--TLLLGGRPAERLDELAAEL--PGATPF--PVDLTDPEAIAA----AVEQLGRLD 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2118010591  85 VLVNNAGIAF--KVADTAPfaVQAEVTMKTNFFATRNVCKELLPLLKPN-GRVVNISS 139
Cdd:PRK08219   74 VLVHNAGVADlgPVAESTV--DEWRATLEVNVVAPAELTRLLLPALRAAhGHVVFINS 129
PRK07060 PRK07060
short chain dehydrogenase; Provisional
 6-235 8.88e-12

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 63.58  E-value: 8.88e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCkQFSGDVYLTSRNIergkAAVAKLQEE-GLKPLfhQLDIDDQQSIqtlRDFLKEkYGGLN 84
Cdd:PRK07060   11 SVLVTGASSGIGRACAVALA-QRGARVVAAARNA----AALDRLAGEtGCEPL--RLDVGDDAAI---RAALAA-AGAFD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  85 VLVNNAGIAF--KVADTApfAVQAEVTMKTNFFATRNVCKELLPLLKPNGR---VVNISSMCAISALakcsqdlqqkfrs 159
Cdd:PRK07060   80 GLVNCAGIASleSALDMT--AEGFDRVMAVNARGAALVARHVARAMIAAGRggsIVNVSSQAALVGL------------- 144

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2118010591 160 dtiteeelvklmekfvedtkkgvhekegwPNH-AYGVTKIGVTVLSRIQARMLNEtrkgDGILLNACCPGWVRTDMA 235
Cdd:PRK07060  145 -----------------------------PDHlAYCASKAALDAITRVLCVELGP----HGIRVNSVNPTVTLTPMA 188
PRK08263 PRK08263
short chain dehydrogenase; Provisional
 9-145 9.17e-12

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 63.90  E-value: 9.17e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   9 VTGSNKGIGFAIVRALCKqfSGD-VYLTSRNIERGKAAVAKLQEEgLKPLfhQLDIDDQQSIQTLRDFLKEKYGGLNVLV 87
Cdd:PRK08263    8 ITGASRGFGRAWTEAALE--RGDrVVATARDTATLADLAEKYGDR-LLPL--ALDVTDRAAVFAAVETAVEHFGRLDIVV 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2118010591  88 NNAGIA-FKVADTAPFAvQAEVTMKTNFFATRNVCKELLPLLKP--NGRVVNISSMCAISA 145
Cdd:PRK08263   83 NNAGYGlFGMIEEVTES-EARAQIDTNFFGALWVTQAVLPYLREqrSGHIIQISSIGGISA 142
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
6-245 9.90e-12

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 63.67  E-value: 9.90e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKqFSGDVYLTSRNIERGKAAvAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLNV 85
Cdd:PRK08226    8 TALITGALQGIGEGIARVFAR-HGANLILLDISPEIEKLA-DELCGRGHRCTAVVADVRDPASVAAAIKRAKEKEGRIDI 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  86 LVNNAGiafkVADTAPFAVQA----EVTMKTNFFATRNVCKELLP--LLKPNGRVVNISSMCAisalakcsqdlqqkfrs 159
Cdd:PRK08226   86 LVNNAG----VCRLGSFLDMSdedrDFHIDINIKGVWNVTKAVLPemIARKDGRIVMMSSVTG----------------- 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591 160 DTITEEELVklmekfvedtkkgvhekegwpnhAYGVTKIGVTVLSRIQARMLNETrkgdGILLNACCPGWVRTDMAGPRA 239
Cdd:PRK08226  145 DMVADPGET-----------------------AYALTKAAIVGLTKSLAVEYAQS----GIRVNAICPGYVRTPMAESIA 197


                  ....*..
gi 2118010591 240 TKS-PDE 245
Cdd:PRK08226  198 RQSnPED 204
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
6-140 1.01e-11

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 63.60  E-value: 1.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQfSGDVYLTS--RNIERGKAAVaklQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGL 83
Cdd:PRK06935   17 VAIVTGGNTGLGQGYAVALAKA-GADIIITThgTNWDETRRLI---EKEGRKVTFVQVDLTKPESAEKVVKEALEEFGKI 92

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2118010591  84 NVLVNNAGIAFKvadtAPFAVQAE----VTMKTN----FFATRNVCKELLPllKPNGRVVNISSM 140
Cdd:PRK06935   93 DILVNNAGTIRR----APLLEYKDedwnAVMDINlnsvYHLSQAVAKVMAK--QGSGKIINIASM 151
PRK06701 PRK06701
short chain dehydrogenase; Provisional
 6-250 1.07e-11

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 63.90  E-value: 1.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQfSGDV---YLT-SRNIERGKAAVaklQEEGLKPLFHQLDIDDQQSI-----QTLRDFl 76
Cdd:PRK06701   48 VALITGGDSGIGRAVAVLFAKE-GADIaivYLDeHEDANETKQRV---EKEGVKCLLIPGDVSDEAFCkdaveETVREL- 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  77 kekyGGLNVLVNNAGIAFKVADTAPF-AVQAEVTMKTNFFATRNVCKELLPLLKPNGRVVNISSMCAISAlakcsqdlqq 155
Cdd:PRK06701  123 ----GRLDILVNNAAFQYPQQSLEDItAEQLDKTFKTNIYSYFHMTKAALPHLKQGSAIINTGSITGYEG---------- 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591 156 kfrsdtitEEELVKlmekfvedtkkgvhekegwpnhaYGVTKIGVTVLSRIQARMLNEtrkgDGILLNACCPGWVRTDMa 235
Cdd:PRK06701  189 --------NETLID-----------------------YSATKGAIHAFTRSLAQSLVQ----KGIRVNAVAPGPIWTPL- 232

                         250
                  ....*....|....*....
gi 2118010591 236 GPrATKSPDE----GAETP 250
Cdd:PRK06701  233 IP-SDFDEEKvsqfGSNTP 250
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
6-236 1.20e-11

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 63.25  E-value: 1.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQfsgdvYLTSRNIERGKAAVAK--LQEEGLKP----LFhQLDIDDQQSIQTLRDFLKEK 79
Cdd:PRK12824    4 IALVTGAKRGIGSAIARELLND-----GYRVIATYFSGNDCAKdwFEEYGFTEdqvrLK-ELDVTDTEECAEALAEIEEE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  80 YGGLNVLVNNAGIAF-KVADTAPFAVQAEVtMKTNFFATRNVCKELLPLL--KPNGRVVNISSMCAisalakcsqdLQQK 156
Cdd:PRK12824   78 EGPVDILVNNAGITRdSVFKRMSHQEWNDV-INTNLNSVFNVTQPLFAAMceQGYGRIINISSVNG----------LKGQ 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591 157 FrsdtiteeelvklmekfvedtkkgvhekeGWPNhaYGVTKIGVTVLSRIQARmlnET-RKgdGILLNACCPGWVRTDMA 235
Cdd:PRK12824  147 F-----------------------------GQTN--YSAAKAGMIGFTKALAS---EGaRY--GITVNCIAPGYIATPMV 190


                  .
gi 2118010591 236 G 236
Cdd:PRK12824  191 E 191
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
 6-139 1.27e-11

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: 62.86  E-value: 1.27e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQFSGDVYLTSRNIERGKAAVAKLQEeglKPLFHQLDIDDQQSIQTLRDFLKEKYGGLNV 85
Cdd:cd05349     2 VVLVTGASRGLGAAIARSFAREGARVVVNYYRSTESAEAVAAEAGE---RAIAIQADVRDRDQVQAMIEEAKNHFGPVDT 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2118010591  86 LVNNAGIAF-------KVADTAP---FAVQAEVTMKtnffATRNVCKELLPLLKPN--GRVVNISS 139
Cdd:cd05349    79 IVNNALIDFpfdpdqrKTFDTIDwedYQQQLEGAVK----GALNLLQAVLPDFKERgsGRVINIGT 140
PRK07109 PRK07109
short chain dehydrogenase; Provisional
 1-142 1.37e-11

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 63.79  E-value: 1.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   1 MSNTPVAVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNIERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKY 80
Cdd:PRK07109    5 PIGRQVVVITGASAGVGRATARAFARR-GAKVVLLARGEEGLEALAAEIRAAGGEALAVVADVADAEAVQAAADRAEEEL 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2118010591  81 GGLNVLVNNAGIA-FKVADTAPFAVQAEVTmKTNFFATRNVCKELLPLLKPNGR--VVNISSMCA 142
Cdd:PRK07109   84 GPIDTWVNNAMVTvFGPFEDVTPEEFRRVT-EVTYLGVVHGTLAALRHMRPRDRgaIIQVGSALA 147
PRK12828 PRK12828
short chain dehydrogenase; Provisional
 6-254 1.67e-11

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 62.51  E-value: 1.67e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNIERGKAAVAKLQEEGLKplFHQLDIDDQQSIQTLRDFLKEKYGGLNV 85
Cdd:PRK12828    9 VVAITGGFGGLGRATAAWLAAR-GARVALIGRGAAPLSQTLPGVPADALR--IGGIDLVDPQAARRAVDEVNRQFGRLDA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  86 LVNNAGiAF---KVADTAPfaVQAEVTMKTNFFATRNVCKELLPLL--KPNGRVVNISSMCAISALAkcsqdlqqkfrsd 160
Cdd:PRK12828   86 LVNIAG-AFvwgTIADGDA--DTWDRMYGVNVKTTLNASKAALPALtaSGGGRIVNIGAGAALKAGP------------- 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591 161 titeeelvklmekfvedtkkgvhekeGWpnHAYGVTKIGVTVLSRIQARMLNETrkgdGILLNACCPGWV-----RTDMA 235
Cdd:PRK12828  150 --------------------------GM--GAYAAAKAGVARLTEALAAELLDR----GITVNAVLPSIIdtppnRADMP 197

                         250       260
                  ....*....|....*....|.
gi 2118010591 236 GPRATK--SPDEGAETPVYLA 254
Cdd:PRK12828  198 DADFSRwvTPEQIAAVIAFLL 218
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
6-139 2.92e-11

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 61.97  E-value: 2.92e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNIERGKAAVAklqEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLNV 85
Cdd:PRK07067    8 VALLTGAASGIGEAVAERYLAE-GARVVIADIKPARARLAAL---EIGPAAIAVSLDVTRQDSIDRIVAAAVERFGGIDI 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2118010591  86 LVNNAGIaFKVA-----DTAPFAVQAEVTMKTNFFATRNVCKELLPLLKpNGRVVNISS 139
Cdd:PRK07067   84 LFNNAAL-FDMApildiSRDSYDRLFAVNVKGLFFLMQAVARHMVEQGR-GGKIINMAS 140
PRK12743 PRK12743
SDR family oxidoreductase;
4-236 3.26e-11

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 61.97  E-value: 3.26e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   4 TPVAVVTGSNKGIGFAIVRALCKQfsG-DVYLTSRNIERG-KAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYG 81
Cdd:PRK12743    2 AQVAIVTASDSGIGKACALLLAQQ--GfDIGITWHSDEEGaKETAEEVRSHGVRAEIRQLDLSDLPEGAQALDKLIQRLG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  82 GLNVLVNNAGIAFKVA--DTaPFAVQAEV-TMKTN--FFATRNVCKELLPLLKPnGRVVNISSmcaisalakcsqdlqqk 156
Cdd:PRK12743   80 RIDVLVNNAGAMTKAPflDM-DFDEWRKIfTVDVDgaFLCSQIAARHMVKQGQG-GRIINITS----------------- 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591 157 frsdtiteeelvklmekfvedtkkgVHEKEGWPNH-AYGVTKIGVTVLSRIQARMLNEtrkgDGILLNACCPGWVRTDMA 235
Cdd:PRK12743  141 -------------------------VHEHTPLPGAsAYTAAKHALGGLTKAMALELVE----HGILVNAVAPGAIATPMN 191


                  .
gi 2118010591 236 G 236
Cdd:PRK12743  192 G 192
PRK06180 PRK06180
short chain dehydrogenase; Provisional
 1-243 3.49e-11

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 62.24  E-value: 3.49e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   1 MSNTPVAVVTGSNKGIGFAIVRALCKQfsGD-VYLTSRNIERgKAAVAKLQEEGLKPLfhQLDIDDQQSIQTLRDFLKEK 79
Cdd:PRK06180    1 MSSMKTWLITGVSSGFGRALAQAALAA--GHrVVGTVRSEAA-RADFEALHPDRALAR--LLDVTDFDAIDAVVADAEAT 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  80 YGGLNVLVNNAGI----AFKVADTAPFAVQAEVtmktNFFATRNVCKELLPLLKP--NGRVVNISSMCAISALAKCSQDL 153
Cdd:PRK06180   76 FGPIDVLVNNAGYghegAIEESPLAEMRRQFEV----NVFGAVAMTKAVLPGMRArrRGHIVNITSMGGLITMPGIGYYC 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591 154 QQKFRSDTITeEELVKLMEKFvedtkkGVHekegwpnhaygVTkigvtvlsriqarmlnetrkgdgillnACCPGWVRTD 233
Cdd:PRK06180  152 GSKFALEGIS-ESLAKEVAPF------GIH-----------VT---------------------------AVEPGSFRTD 186

                         250
                  ....*....|
gi 2118010591 234 MAGPRATKSP 243
Cdd:PRK06180  187 WAGRSMVRTP 196
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
 3-234 3.62e-11

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 61.94  E-value: 3.62e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   3 NTPVAVVTGSNKGIGFAIVRALCKQFSGDVYLTSRNIERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGG 82
Cdd:PRK12935    5 NGKVAIVTGGAKGIGKAITVALAQEGAKVVINYNSSKEAAENLVNELGKEGHDVYAVQADVSKVEDANRLVEEAVNHFGK 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  83 LNVLVNNAGI----AFKVADTAPFavqaEVTMKTNFFATRNVCKELLPLL--KPNGRVVNISSMcaisalakcsqdlqqk 156
Cdd:PRK12935   85 VDILVNNAGItrdrTFKKLNREDW----ERVIDVNLSSVFNTTSAVLPYIteAEEGRIISISSI---------------- 144

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2118010591 157 frsdtiteeelvklmekfvedtkkgVHEKEGWPNHAYGVTKIGVTVLSRIQARMLNETrkgdGILLNACCPGWVRTDM 234
Cdd:PRK12935  145 -------------------------IGQAGGFGQTNYSAAKAGMLGFTKSLALELAKT----NVTVNAICPGFIDTEM 193
PRK07069 PRK07069
short chain dehydrogenase; Validated
 7-145 4.50e-11

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 61.65  E-value: 4.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   7 AVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNIERGKAAVAKLQEEGLKP---LFHQLDIDDQQSIQTLRDFLKEKYGGL 83
Cdd:PRK07069    2 AFITGAAGGLGRAIARRMAEQ-GAKVFLTDINDAAGLDAFAAEINAAHGEgvaFAAVQDVTDEAQWQALLAQAADAMGGL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2118010591  84 NVLVNNAGIAfkvADTAPFAVQAEV---TMKTNFFATRNVCKELLPLLKPN--GRVVNISSMCAISA 145
Cdd:PRK07069   81 SVLVNNAGVG---SFGAIEQIELDEwrrVMAINVESIFLGCKHALPYLRASqpASIVNISSVAAFKA 144
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
 7-235 5.78e-11

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: 61.19  E-value: 5.78e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   7 AVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNIERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLNVL 86
Cdd:cd05350     1 VLITGASSGIGRALAREFAKA-GYNVALAARRTDRLDELKAELLNPNPSVEVEILDVTDEERNQLVIAELEAELGGLDLV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  87 VNNAGIAFKVADTAPFAVQAEVTMKTNFFATRNVCKELLPLLKPNGR--VVNISSmcaISALAkcsqdlqqkfrsdtite 164
Cdd:cd05350    80 IINAGVGKGTSLGDLSFKAFRETIDTNLLGAAAILEAALPQFRAKGRghLVLISS---VAALR----------------- 139

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2118010591 165 eelvklmekfvedtkkgvhekeGWPNH-AYGVTKIGVTVLsriqARMLNETRKGDGILLNACCPGWVRTDMA 235
Cdd:cd05350   140 ----------------------GLPGAaAYSASKAALSSL----AESLRYDVKKRGIRVTVINPGFIDTPLT 185
PRK07825 PRK07825
short chain dehydrogenase; Provisional
 6-140 6.17e-11

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 61.50  E-value: 6.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNIERGKAAVAKLqeeGLkPLFHQLDIDDQQSIQTLRDFLKEKYGGLNV 85
Cdd:PRK07825    7 VVAITGGARGIGLATARALAAL-GARVAIGDLDEALAKETAAEL---GL-VVGGPLDVTDPASFAAFLDAVEADLGPIDV 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2118010591  86 LVNNAGiafkVADTAPFAVQAE----VTMKTNFFATRNVCKELLPLLKPNGR--VVNISSM 140
Cdd:PRK07825   82 LVNNAG----VMPVGPFLDEPDavtrRILDVNVYGVILGSKLAAPRMVPRGRghVVNVASL 138
PRK05854 PRK05854
SDR family oxidoreductase;
7-142 6.60e-11

SDR family oxidoreductase;


Pssm-ID: 235627 [Multi-domain]  Cd Length: 313  Bit Score: 61.62  E-value: 6.60e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   7 AVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNIERGKAAVAKLQEE--GLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLN 84
Cdd:PRK05854   17 AVVTGASDGLGLGLARRLAAA-GAEVILPVRNRAKGEAAVAAIRTAvpDAKLSLRALDLSSLASVAALGEQLRAEGRPIH 95

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2118010591  85 VLVNNAGIAfkvadTAPFAVQA----EVTMKTNFFATRNVCKELLPLLKP-NGRVVNISSMCA 142
Cdd:PRK05854   96 LLINNAGVM-----TPPERQTTadgfELQFGTNHLGHFALTAHLLPLLRAgRARVTSQSSIAA 153
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
 9-143 1.01e-10

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: 60.16  E-value: 1.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   9 VTGSNKGIGfaivRALCKQFSGD---VYLTSRNIERGKAAVAKLQEEGLkpLFHQLDIDDQQSI-QTLRDFLKEKYGGLN 84
Cdd:cd08931     5 ITGAASGIG----RETALLFARNgwfVGLYDIDEDGLAALAAELGAENV--VAGALDVTDRAAWaAALADFAAATGGRLD 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2118010591  85 VLVNNAGIA-FKVADTAPFAvQAEVTMKTNFFATRNVCKELLPLLK--PNGRVVNISSMCAI 143
Cdd:cd08931    79 ALFNNAGVGrGGPFEDVPLA-AHDRMVDINVKGVLNGAYAALPYLKatPGARVINTASSSAI 139
PRK05993 PRK05993
SDR family oxidoreductase;
1-146 1.13e-10

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 60.43  E-value: 1.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   1 MSNTPVAVVTGSNKGIGFAIVRALcKQFSGDVYLTSRNIERgkaaVAKLQEEGLKPLfhQLDIDDQQSIQTLRDFLKEKY 80
Cdd:PRK05993    1 MDMKRSILITGCSSGIGAYCARAL-QSDGWRVFATCRKEED----VAALEAEGLEAF--QLDYAEPESIAALVAQVLELS 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2118010591  81 GG-LNVLVNNA--GIAFKVADTAPFAVQAEvtMKTNFFATRNVCKELLPLLKPN--GRVVNISSMCAISAL 146
Cdd:PRK05993   74 GGrLDALFNNGayGQPGAVEDLPTEALRAQ--FEANFFGWHDLTRRVIPVMRKQgqGRIVQCSSILGLVPM 142
PRK06114 PRK06114
SDR family oxidoreductase;
6-143 1.17e-10

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 60.18  E-value: 1.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCkQFSGDVYLTSRNIERGKAAVAK-LQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLN 84
Cdd:PRK06114   10 VAFVTGAGSGIGQRIAIGLA-QAGADVALFDLRTDDGLAETAEhIEAAGRRAIQIAADVTSKADLRAAVARTEAELGALT 88

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2118010591  85 VLVNNAGIAFKVADTAPFAVQAEVTMKTNFFATRNVCKELLPLLKPNGR--VVNISSMCAI 143
Cdd:PRK06114   89 LAVNAAGIANANPAEEMEEEQWQTVMDINLTGVFLSCQAEARAMLENGGgsIVNIASMSGI 149
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
 6-142 1.29e-10

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 60.25  E-value: 1.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVrALCKQFSGDVYLTSRNIERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLNV 85
Cdd:PRK06113   13 CAIITGAGAGIGKEIA-ITFATAGASVVVSDINADAANHVVDEIQQLGGQAFACRCDITSEQELSALADFALSKLGKVDI 91

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2118010591  86 LVNNAGiafkVADTAPFAVQAEV---TMKTNFFATRNVCKELLPLLKPN--GRVVNISSMCA 142
Cdd:PRK06113   92 LVNNAG----GGGPKPFDMPMADfrrAYELNVFSFFHLSQLVAPEMEKNggGVILTITSMAA 149
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
 6-92 1.48e-10

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: 60.84  E-value: 1.48e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQFSGDVYLTSR-----NIERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKY 80
Cdd:cd08953   207 VYLVTGGAGGIGRALARALARRYGARLVLLGRsplppEEEWKAQTLAALEALGARVLYISADVTDAAAVRRLLEKVRERY 286

                          90
                  ....*....|..
gi 2118010591  81 GGLNVLVNNAGI 92
Cdd:cd08953   287 GAIDGVIHAAGV 298
3KS_SDR_c cd08941
3-keto steroid reductase, classical (c) SDRs; 3-keto steroid reductase (in concert with other ...
 5-258 1.52e-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: 60.48  E-value: 1.52e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   5 PVAVVTGSNKGIGFAIVRALCKQFSGD----VYLTSRNIERGKAAVAKLQEeglkplFH----------QLDIDDQQSIQ 70
Cdd:cd08941     2 KVVLVTGANSGLGLAICERLLAEDDENpeltLILACRNLQRAEAACRALLA------SHpdarvvfdyvLVDLSNMVSVF 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  71 TLRDFLKEKYGGLNVLVNNAGI----------AFKVADTAPFAVQAEVTMK-----------------------TNFFAT 117
Cdd:cd08941    76 AAAKELKKRYPRLDYLYLNAGImpnpgidwigAIKEVLTNPLFAVTNPTYKiqaegllsqgdkatedglgevfqTNVFGH 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591 118 RNVCKELLPLLK---PNGRVVNISSMCAiSALAKCSQDLQqkfrsdtiteeelvklmekfvedtkkgvHEKEgwpNHAYG 194
Cdd:cd08941   156 YYLIRELEPLLCrsdGGSQIIWTSSLNA-SPKYFSLEDIQ----------------------------HLKG---PAPYS 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591 195 VTKIGVTVLSRIQARMLNETrkgdGILLNACCPGWVRTDM-----------------------AGPRATKSPDEGAETPV 251
Cdd:cd08941   204 SSKYLVDLLSLALNRKFNKL----GVYSYVVHPGICTTNLtygilppftwtlalplfyllrrlGSPWHTISPYNGAEALV 279


                  ....*..
gi 2118010591 252 YLALLPP 258
Cdd:cd08941   280 WLALQKP 286
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
 6-146 2.61e-10

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: 59.40  E-value: 2.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCK--QFSGDVYLTSRNIERGKAAVAKLQEEGLKPL-FHQLDIDDQQSIQTLRDFLKEKYgg 82
Cdd:cd09806     2 VVLITGCSSGIGLHLAVRLASdpSKRFKVYATMRDLKKKGRLWEAAGALAGGTLeTLQLDVCDSKSVAAAVERVTERH-- 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  83 LNVLVNNAGIAFkvadTAPFAVQAEVTMK----TNFFATRNVCKELLPLLKP--NGRVVNISSMCAISAL 146
Cdd:cd09806    80 VDVLVCNAGVGL----LGPLEALSEDAMAsvfdVNVFGTVRMLQAFLPDMKRrgSGRILVTSSVGGLQGL 145
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
 6-252 3.75e-10

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: 59.08  E-value: 3.75e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNiERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLNV 85
Cdd:cd08937     6 VVVVTGAAQGIGRGVAERLAGE-GARVLLVDRS-ELVHEVLAEILAAGDAAHVHTADLETYAGAQGVVRAAVERFGRVDV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  86 LVNNAG--IAFKVADTAPFAvQAEVTMKTNFFATRNVCKELLP--LLKPNGRVVNISSmcaisalakcsqdlqqkfrsdt 161
Cdd:cd08937    84 LINNVGgtIWAKPYEHYEEE-QIEAEIRRSLFPTLWCCRAVLPhmLERQQGVIVNVSS---------------------- 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591 162 iteeelvklmekfveDTKKGVHEKegwpnhAYGVTKIGVTVLSRIQARMLNEtrkgDGILLNACCPGWVRTDMAGPRATK 241
Cdd:cd08937   141 ---------------IATRGIYRI------PYSAAKGGVNALTASLAFEHAR----DGIRVNAVAPGGTEAPPRKIPRNA 195

                         250
                  ....*....|.
gi 2118010591 242 SPDEGAETPVY 252
Cdd:cd08937   196 APMSEQEKVWY 206
PRK07831 PRK07831
SDR family oxidoreductase;
6-139 4.41e-10

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 58.89  E-value: 4.41e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGS-NKGIGFAIVRAlCKQFSGDVYLTSRNIERGKAAVAKLQEE-GLKPLFHQL-DIDDQQSIQTLRDFLKEKYGG 82
Cdd:PRK07831   19 VVLVTAAaGTGIGSATARR-ALEEGARVVISDIHERRLGETADELAAElGLGRVEAVVcDVTSEAQVDALIDAAVERLGR 97

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2118010591  83 LNVLVNNAGIA-------------FKVADtapfavqaeVTMKTNFFATRnvckELLPLLKPNGR---VVNISS 139
Cdd:PRK07831   98 LDVLVNNAGLGgqtpvvdmtddewSRVLD---------VTLTGTFRATR----AALRYMRARGHggvIVNNAS 157
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 6-139 5.03e-10

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 58.56  E-value: 5.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQFSGDV--YLTSRNiergkAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYG-G 82
Cdd:PRK08642    7 TVLVTGGSRGLGAAIARAFAREGARVVvnYHQSED-----AAEALADELGDRAIALQADVTDREQVQAMFATATEHFGkP 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2118010591  83 LNVLVNNAGIAFKV-ADTAP---------FAVQAEVTMKtnffATRNVCKELLPLLKP--NGRVVNISS 139
Cdd:PRK08642   82 ITTVVNNALADFSFdGDARKkadditwedFQQQLEGSVK----GALNTIQAALPGMREqgFGRIINIGT 146
PRK08265 PRK08265
short chain dehydrogenase; Provisional
 6-90 5.43e-10

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 58.48  E-value: 5.43e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALcKQFSGDVYLTSRNIERGKAAVAKLqeeGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLNV 85
Cdd:PRK08265    8 VAIVTGGATLIGAAVARAL-VAAGARVAIVDIDADNGAAVAASL---GERARFIATDITDDAAIERAVATVVARFGRVDI 83


                  ....*
gi 2118010591  86 LVNNA 90
Cdd:PRK08265   84 LVNLA 88
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
 1-266 6.64e-10

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: 57.97  E-value: 6.64e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   1 MSNTPVAVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNIERGKAAVAKLQEEG-LKPLFHQLDIDD--QQSIQTLRDFLK 77
Cdd:cd05340     1 LLNDRIILVTGASDGIGREAALTYARY-GATVILLGRNEEKLRQVADHINEEGgRQPQWFILDLLTctSENCQQLAQRIA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  78 EKYGGLNVLVNNAGIafkVADTAPFAVQAEVTMKT----NFFATRNVCKELLPLLK--PNGRVVnissmcaisalakcsq 151
Cdd:cd05340    80 VNYPRLDGVLHNAGL---LGDVCPLSEQNPQVWQDv*qvNVNATFMLTQALLPLLLksDAGSLV---------------- 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591 152 dlqqkFRSDTIteeelvklmekfvedtkkGVHEKEGWpnHAYGVTKIGVTVLSRIQArmlnETRKGDGILLNACCPGWVR 231
Cdd:cd05340   141 -----FTSSSV------------------GRQGRANW--GAYAVSKFATEGL*QVLA----DEYQQRNLRVNCINPGGTR 191

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 2118010591 232 TDMagpRATKSPDEGAET--------PVYLALLPPGADGPHGQ 266
Cdd:cd05340   192 TAM---RASAFPTEDPQKlktpadimPLYLWLMGDDSRRKTGM 231
PRK08267 PRK08267
SDR family oxidoreductase;
9-143 7.60e-10

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 58.03  E-value: 7.60e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   9 VTGSNKGIGfaivRALCKQFSGD---VYLTSRNiergKAAVAKLQEE--GLKPLFHQLDIDDQQSIQT-LRDFLKEKYGG 82
Cdd:PRK08267    6 ITGAASGIG----RATALLFAAEgwrVGAYDIN----EAGLAALAAElgAGNAWTGALDVTDRAAWDAaLADFAAATGGR 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2118010591  83 LNVLVNNAGIA-FKVADTAPFAvQAEVTMKTNFFATRNVCKELLPLLK--PNGRVVNISSMCAI 143
Cdd:PRK08267   78 LDVLFNNAGILrGGPFEDIPLE-AHDRVIDINVKGVLNGAHAALPYLKatPGARVINTSSASAI 140
PRK07814 PRK07814
SDR family oxidoreductase;
6-140 8.76e-10

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 57.87  E-value: 8.76e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCkQFSGDVYLTSRNIERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLNV 85
Cdd:PRK07814   12 VAVVTGAGRGLGAAIALAFA-EAGADVLIAARTESQLDEVAEQIRAAGRRAHVVAADLAHPEATAGLAGQAVEAFGRLDI 90

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2118010591  86 LVNNAGIAFKVADTAPFAVQAEVTMKTNFFATRNVCKELLPLL---KPNGRVVNISSM 140
Cdd:PRK07814   91 VVNNVGGTMPNPLLSTSTKDLADAFTFNVATAHALTVAAVPLMlehSGGGSVINISST 148
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
 3-143 1.52e-09

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: 56.91  E-value: 1.52e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   3 NTPVAVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNIERGkAAVAKLQEEGLkplFHQLDIDDQQSIQTLRDFLKEKYGG 82
Cdd:cd05371     1 KGLVAVVTGGASGLGLATVERLLAQ-GAKVVILDLPNSPG-ETVAKLGDNCR---FVPVDVTSEKDVKAALALAKAKFGR 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2118010591  83 LNVLVNNAGIA-------FKVADTAPFAVQAEVtMKTNFFATRNVCKELLPLLKPN--------GRVVNISSMCAI 143
Cdd:cd05371    76 LDIVVNCAGIAvaaktynKKGQQPHSLELFQRV-INVNLIGTFNVIRLAAGAMGKNepdqggerGVIINTASVAAF 150
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 6-92 1.63e-09

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 56.89  E-value: 1.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNIERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLNV 85
Cdd:PRK08217    7 VIVITGGAQGLGRAMAEYLAQK-GAKLALIDLNQEKLEEAVAECGALGTEVRGYAANVTDEEDVEATFAQIAEDFGQLNG 85


                  ....*..
gi 2118010591  86 LVNNAGI 92
Cdd:PRK08217   86 LINNAGI 92
PRK05855 PRK05855
SDR family oxidoreductase;
7-249 1.63e-09

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 58.07  E-value: 1.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   7 AVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNIERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLNVL 86
Cdd:PRK05855  318 VVVTGAGSGIGRETALAFARE-GAEVVASDIDEAAAERTAELIRAAGAVAHAYRVDVSDADAMEAFAEWVRAEHGVPDIV 396

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  87 VNNAGI--AFKVADTAPfaVQAEVTMKTNFFATRNVCKELLPLLKPN---GRVVNISSMCAISAlakcSQDLQqkfrsdt 161
Cdd:PRK05855  397 VNNAGIgmAGGFLDTSA--EDWDRVLDVNLWGVIHGCRLFGRQMVERgtgGHIVNVASAAAYAP----SRSLP------- 463

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591 162 iteeelvklmekfvedtkkgvhekegwpnhAYGVTKIGVTVLSR-IQARMlnetrKGDGILLNACCPGWVRTDMAgpRAT 240
Cdd:PRK05855  464 ------------------------------AYATSKAAVLMLSEcLRAEL-----AAAGIGVTAICPGFVDTNIV--ATT 506


                  ....*....
gi 2118010591 241 KSPDEGAET 249
Cdd:PRK05855  507 RFAGADAED 515
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
 6-252 2.26e-09

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: 56.69  E-value: 2.26e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNIERGKAAVA-KLQEEGLKPLFHQLDIDDQQSIQTLRDFL-KEKYGGL 83
Cdd:cd09763     5 IALVTGASRGIGRGIALQLGEA-GATVYITGRTILPQLPGTAeEIEARGGKCIPVRCDHSDDDEVEALFERVaREQQGRL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  84 NVLVNNAGIAFK---VADTAPF------------AVQAEVTMKTNFFATrnvckellPLLKPNGR--VVNISSMCAisal 146
Cdd:cd09763    84 DILVNNAYAAVQlilVGVAKPFweepptiwddinNVGLRAHYACSVYAA--------PLMVKAGKglIVIISSTGG---- 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591 147 akcsqdlqqkfrsdtiteeelvkLMEKFvedtkkgvhekegwpNHAYGVTKIGVtvlSRIQARMLNETRKgDGILLNACC 226
Cdd:cd09763   152 -----------------------LEYLF---------------NVAYGVGKAAI---DRMAADMAHELKP-HGVAVVSLW 189

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 2118010591 227 PGWVRT--------DMAGPRATKSPDEG--AETPVY 252
Cdd:cd09763   190 PGFVRTelvlempeDDEGSWHAKERDAFlnGETTEY 225
fabG PRK07792
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 6-266 2.48e-09

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


Pssm-ID: 181120 [Multi-domain]  Cd Length: 306  Bit Score: 56.71  E-value: 2.48e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQFSGDVYLTSRNIERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDfLKEKYGGLNV 85
Cdd:PRK07792   14 VAVVTGAAAGLGRAEALGLARLGATVVVNDVASALDASDVLDEIRAAGAKAVAVAGDISQRATADELVA-TAVGLGGLDI 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  86 LVNNAGIA-----FKVADTAPFAVQAeVTMKTNFFATRNVCKELLPLLKPN-----GRVVNISSmcaisalakcsqdlqq 155
Cdd:PRK07792   93 VVNNAGITrdrmlFNMSDEEWDAVIA-VHLRGHFLLTRNAAAYWRAKAKAAggpvyGRIVNTSS---------------- 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591 156 kfrsdtiteeelvklmekfvedtKKGVHEKEGWPNhaYGVTKIGVTVLSRIQARMLNETrkgdGILLNACCPGwVRTDM- 234
Cdd:PRK07792  156 -----------------------EAGLVGPVGQAN--YGAAKAGITALTLSAARALGRY----GVRANAICPR-ARTAMt 205

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 2118010591 235 -------AGPRATK----SPDEGAETPVYLAllPPGADGPHGQ 266
Cdd:PRK07792  206 advfgdaPDVEAGGidplSPEHVVPLVQFLA--SPAAAEVNGQ 246
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
 6-138 3.08e-09

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: 56.25  E-value: 3.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNIErGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLNV 85
Cdd:cd08943     3 VALVTGGASGIGLAIAKRLAAE-GAAVVVADIDPE-IAEKVAEAAQGGPRALGVQCDVTSEAQVQSAFEQAVLEFGGLDI 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2118010591  86 LVNNAGIAF--KVADTApfAVQAEVTMKTNFFATRNVCKELLPLLKPNGR----VVNIS 138
Cdd:cd08943    81 VVSNAGIATssPIAETS--LEDWNRSMDINLTGHFLVSREAFRIMKSQGIggniVFNAS 137
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
 7-140 5.62e-09

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: 55.30  E-value: 5.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   7 AVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNIERGKaAVAKLQEE--GLKPLFHQLDIDDQQSI-QTLRDFLKekygGL 83
Cdd:cd05356     4 AVVTGATDGIGKAYAEELAKR-GFNVILISRTQEKLD-AVAKEIEEkyGVETKTIAADFSAGDDIyERIEKELE----GL 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2118010591  84 NV--LVNNAGIAFKVADtaPFA-VQAEV---TMKTNFFATRNVCKELLPLLKPNGR--VVNISSM 140
Cdd:cd05356    78 DIgiLVNNVGISHSIPE--YFLeTPEDElqdIINVNVMATLKMTRLILPGMVKRKKgaIVNISSF 140
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
 6-232 6.39e-09

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: 55.28  E-value: 6.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQfsGDVYLTSRNIERGKAAVAKLqeEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLNV 85
Cdd:cd09761     3 VAIVTGGGHGIGKQICLDFLEA--GDKVVFADIDEERGADFAEA--EGPNLFFVHGDVADETLVKFVVYAMLEKLGRIDV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  86 LVNNAGIAFKVADTAPFAVQAEVTMKTNFFATRNVCKELLP-LLKPNGRVVNISSMCAisalakcsqdlqqkFRSDTITE 164
Cdd:cd09761    79 LVNNAARGSKGILSSLLLEEWDRILSVNLTGPYELSRYCRDeLIKNKGRIINIASTRA--------------FQSEPDSE 144

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2118010591 165 eelvklmekfvedtkkgvhekegwpnhAYGVTKIGVTVLSRIQARMLnetrkGDGILLNACCPGWVRT 232
Cdd:cd09761   145 ---------------------------AYAASKGGLVALTHALAMSL-----GPDIRVNCISPGWINT 180
PRK07985 PRK07985
SDR family oxidoreductase;
7-142 7.65e-09

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 55.39  E-value: 7.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   7 AVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNIERGKAA-VAKLQEE-GLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLN 84
Cdd:PRK07985   52 ALVTGGDSGIGRAAAIAYARE-GADVAISYLPVEEEDAQdVKKIIEEcGRKAVLLPGDLSDEKFARSLVHEAHKALGGLD 130

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2118010591  85 VLVNNAGIAFKVADTAPFAV-QAEVTMKTNFFATRNVCKELLPLLKPNGRVVNISSMCA 142
Cdd:PRK07985  131 IMALVAGKQVAIPDIADLTSeQFQKTFAINVFALFWLTQEAIPLLPKGASIITTSSIQA 189
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 6-143 9.37e-09

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


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 55.61  E-value: 9.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQFSGDVYLtsrNIERGKAAVAKLQEE-GLKPLfhQLDIDDQQSIQTLRDFLKEKYGGLN 84
Cdd:PRK08261  212 VALVTGAARGIGAAIAEVLARDGAHVVCL---DVPAAGEALAAVANRvGGTAL--ALDITAPDAPARIAEHLAERHGGLD 286

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2118010591  85 VLVNNAGI------AfKVADTAPFAVqaevtMKTNFFATRNVCKELLP--LLKPNGRVVNISSMCAI 143
Cdd:PRK08261  287 IVVHNAGItrdktlA-NMDEARWDSV-----LAVNLLAPLRITEALLAagALGDGGRIVGVSSISGI 347
PRK12746 PRK12746
SDR family oxidoreductase;
3-139 1.10e-08

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 54.65  E-value: 1.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   3 NTPVAVVTGSNKGIGFAIVRALCKQFSGDVYLTSRNIERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKY-- 80
Cdd:PRK12746    5 DGKVALVTGASRGIGRAIAMRLANDGALVAIHYGRNKQAADETIREIESNGGKAFLIEADLNSIDGVKKLVEQLKNELqi 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2118010591  81 ----GGLNVLVNNAGIAFK--VADTAP--FAVQAEVTMKTNFFatrnVCKELLPLLKPNGRVVNISS 139
Cdd:PRK12746   85 rvgtSEIDILVNNAGIGTQgtIENTTEeiFDEIMAVNIKAPFF----LIQQTLPLLRAEGRVINISS 147
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
 6-139 1.69e-08

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: 53.93  E-value: 1.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQFSgDVYLTSRNIERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLNV 85
Cdd:cd05360     2 VVVITGASSGIGRATALAFAERGA-KVVLAARSAEALHELAREVRELGGEAIAVVADVADAAQVERAADTAVERFGRIDT 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2118010591  86 LVNNAGIAF--KVADTAPFAvqAEVTMKTNFFATRNVCKELLPLLKPN--GRVVNISS 139
Cdd:cd05360    81 WVNNAGVAVfgRFEDVTPEE--FRRVFDVNYLGHVYGTLAALPHLRRRggGALINVGS 136
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
 6-139 1.71e-08

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 54.25  E-value: 1.71e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQfsgDVYLTSRNIERGKaavaklqEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLNV 85
Cdd:PRK06171   11 IIIVTGGSSGIGLAIVKELLAN---GANVVNADIHGGD-------GQHENYQFVPTDVSSAEEVNHTVAEIIEKFGRIDG 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2118010591  86 LVNNAGIAFK-------------VADTAPFAVQAEVTMKTNFFATRNVCKELLPllKPNGRVVNISS 139
Cdd:PRK06171   81 LVNNAGINIPrllvdekdpagkyELNEAAFDKMFNINQKGVFLMSQAVARQMVK--QHDGVIVNMSS 145
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
 6-146 1.79e-08

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: 54.01  E-value: 1.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQFSGDVYLTsrnieRGKAAVAKLQEE--GLKPLfhQLDIDDQQSIQtlrdFLKEKYGGL 83
Cdd:cd05351     9 RALVTGAGKGIGRATVKALAKAGARVVAVS-----RTQADLDSLVREcpGIEPV--CVDLSDWDATE----EALGSVGPV 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2118010591  84 NVLVNNAGIAFKVADTAPFAVQAEVTMKTNFFATRNVCKELLPLLKPN---GRVVNISSMCAISAL 146
Cdd:cd05351    78 DLLVNNAAVAILQPFLEVTKEAFDRSFDVNVRAVIHVSQIVARGMIARgvpGSIVNVSSQASQRAL 143
PRK09186 PRK09186
flagellin modification protein A; Provisional
 1-145 2.15e-08

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 53.84  E-value: 2.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   1 MSNTPVAVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNIERGKAAVAKLQEE-GLKPL-FHQLDIDDQQSIQTLRDFLKE 78
Cdd:PRK09186    1 MLKGKTILITGAGGLIGSALVKAILEA-GGIVIAADIDKEALNELLESLGKEfKSKKLsLVELDITDQESLEEFLSKSAE 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2118010591  79 KYGGLNVLVNNA-------GIAFKVADTAPFAVQAEVTMKTNFFATRNVCKELLPLLKPNgrVVNISSMCAISA 145
Cdd:PRK09186   80 KYGKIDGAVNCAyprnkdyGKKFFDVSLDDFNENLSLHLGSSFLFSQQFAKYFKKQGGGN--LVNISSIYGVVA 151
PRK06398 PRK06398
aldose dehydrogenase; Validated
 6-140 2.37e-08

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 53.68  E-value: 2.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQFSgDVYLTSRNiERGKAAVAklqeeglkplFHQLDIDDQQSIQTLRDFLKEKYGGLNV 85
Cdd:PRK06398    8 VAIVTGGSQGIGKAVVNRLKEEGS-NVINFDIK-EPSYNDVD----------YFKVDVSNKEQVIKGIDYVISKYGRIDI 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2118010591  86 LVNNAGI----AFKVADTAPFAVQAEVTMKTNFFATRNVCKELLPLLKpnGRVVNISSM 140
Cdd:PRK06398   76 LVNNAGIesygAIHAVEEDEWDRIINVNVNGIFLMSKYTIPYMLKQDK--GVIINIASV 132
PLN02253 PLN02253
xanthoxin dehydrogenase
 6-145 2.59e-08

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 53.67  E-value: 2.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQFSgdvyltsrniergKAAVAKLQEE---------GLKP--LFHQLDIDDQQSIQTLRD 74
Cdd:PLN02253   20 VALVTGGATGIGESIVRLFHKHGA-------------KVCIVDLQDDlgqnvcdslGGEPnvCFFHCDVTVEDDVSRAVD 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2118010591  75 FLKEKYGGLNVLVNNAGIA------FKVADTAPFAVQAEVTMKTNFFATRNVCKELLPLLKpnGRVVnisSMCAISA 145
Cdd:PLN02253   87 FTVDKFGTLDIMVNNAGLTgppcpdIRNVELSEFEKVFDVNVKGVFLGMKHAARIMIPLKK--GSIV---SLCSVAS 158
human_WWOX_like_SDR_c-like cd09809
human WWOX (WW domain-containing oxidoreductase)-like, classical (c)-like SDRs; Classical-like ...
 6-257 3.12e-08

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: 53.37  E-value: 3.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNIERGKAAVAKLQEEGLKPL--FHQLDIDDQQSIQTLRDFLKEKYGGL 83
Cdd:cd09809     3 VIIITGANSGIGFETARSFALH-GAHVILACRNMSRASAAVSRILEEWHKARveAMTLDLASLRSVQRFAEAFKAKNSPL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  84 NVLVNNAGIAfkvadTAPFAVQA---EVTMKTN---FFATRNVCKELLPLLKPnGRVVNISSmcaisalakcsqdlqqkf 157
Cdd:cd09809    82 HVLVCNAAVF-----ALPWTLTEdglETTFQVNhlgHFYLVQLLEDVLRRSAP-ARVIVVSS------------------ 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591 158 RSDTITE--EELVKLMEKFVEDTKkgvheKEGWPNHAYGVTKIGVTVLSRIQARMLnetrKGDGILLNACCPG------- 228
Cdd:cd09809   138 ESHRFTDlpDSCGNLDFSLLSPPK-----KKYWSMLAYNRAKLCNILFSNELHRRL----SPRGITSNSLHPGnmmyssi 208

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 2118010591 229 ----WVRT---DMAGPrATKSPDEGAETPVYLALLP 257
Cdd:cd09809   209 hrnwWVYTllfTLARP-FTKSMQQGAATTVYCATAP 243
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
 6-139 3.28e-08

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


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 53.02  E-value: 3.28e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNiERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLNV 85
Cdd:PRK12823   10 VVVVTGAAQGIGRGVALRAAAE-GARVVLVDRS-ELVHEVAAELRAAGGEALALTADLETYAGAQAAMAAAVEAFGRIDV 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2118010591  86 LVNNAG--IAFKvadtaPFA------VQAEVtmKTNFFATRNVCKELLPLLKPNGR--VVNISS 139
Cdd:PRK12823   88 LINNVGgtIWAK-----PFEeyeeeqIEAEI--RRSLFPTLWCCRAVLPHMLAQGGgaIVNVSS 144
LPOR_like_SDR_c_like cd09810
light-dependent protochlorophyllide reductase (LPOR)-like, classical (c)-like SDRs; Classical ...
 7-139 3.55e-08

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: 53.29  E-value: 3.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   7 AVVTGSNKGIGFAIVRALCKQFSGDVYLTSRNIERGKAAVAKL-QEEGLKPLFHqLDIDDQQSIQTLRDFLKEKYGGLNV 85
Cdd:cd09810     4 VVITGASSGLGLAAAKALARRGEWHVVMACRDFLKAEQAAQEVgMPKDSYSVLH-CDLASLDSVRQFVDNFRRTGRPLDA 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2118010591  86 LVNNAGIAFKVADTAPFAVQA-EVTMKTNFFATRNVCKELLPLLK----PNGRVVNISS 139
Cdd:cd09810    83 LVCNAAVYLPTAKEPRFTADGfELTVGVNHLGHFLLTNLLLEDLQrsenASPRIVIVGS 141
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
 6-139 3.66e-08

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 52.96  E-value: 3.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALckqfsgdvyltsrnIERGkAAV-----AKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKY 80
Cdd:PRK08220   10 TVWVTGAAQGIGYAVALAF--------------VEAG-AKVigfdqAFLTQEDYPFATFVLDVSDAAAVAQVCQRLLAET 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2118010591  81 GGLNVLVNNAGIaFKVADTAPFAVQA-EVTMKTNFFATRNVCKELLPLLKPN--GRVVNISS 139
Cdd:PRK08220   75 GPLDVLVNAAGI-LRMGATDSLSDEDwQQTFAVNAGGAFNLFRAVMPQFRRQrsGAIVTVGS 135
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
 6-244 4.15e-08

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: 52.86  E-value: 4.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNIErgkaavaKLQEEGLKPLFH--QLDIDDQQSIQTlrdfLKEKYGGL 83
Cdd:cd05368     4 VALITAAAQGIGRAIALAFARE-GANVIATDINEE-------KLKELERGPGITtrVLDVTDKEQVAA----LAKEEGRI 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  84 NVLVNNAGI----AFKVADTAPFAVQAEVTMKTNFFATRNVCKELLPllKPNGRVVNISSmcaisalakcsqdlqqkfrs 159
Cdd:cd05368    72 DVLFNCAGFvhhgSILDCEDDDWDFAMNLNVRSMYLMIKAVLPKMLA--RKDGSIINMSS-------------------- 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591 160 dtiteeelvklmekfVEDTKKGVhekegwPNH-AYGVTKIGVTVLSRIQARMLNETrkgdGILLNACCPGWVRTDMAGPR 238
Cdd:cd05368   130 ---------------VASSIKGV------PNRfVYSTTKAAVIGLTKSVAADFAQQ----GIRCNAICPGTVDTPSLEER 184


                  ....*.
gi 2118010591 239 ATKSPD 244
Cdd:cd05368   185 IQAQPD 190
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
 9-142 4.20e-08

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


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 52.84  E-value: 4.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   9 VTGSNKGIGFAIVRALCKQfSGDVYLTSRNIERgkaaVAKLQEE-GLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLNVLV 87
Cdd:PRK10538    5 VTGATAGFGECITRRFIQQ-GHKVIATGRRQER----LQELKDElGDNLYIAQLDVRNRAAIEEMLASLPAEWRNIDVLV 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2118010591  88 NNAGIAFKVADTAPFAVQAEVTM-KTNFFATRNVCKELLP-LLKPN-GRVVNISSMCA 142
Cdd:PRK10538   80 NNAGLALGLEPAHKASVEDWETMiDTNNKGLVYMTRAVLPgMVERNhGHIINIGSTAG 137
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
 7-144 4.57e-08

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 52.61  E-value: 4.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   7 AVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNIERGKAAVAKLqeeGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLNVL 86
Cdd:PRK12936    9 ALVTGASGGIGEEIARLLHAQ-GAIVGLHGTRVEKLEALAAEL---GERVKIFPANLSDRDEVKALGQKAEADLEGVDIL 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2118010591  87 VNNAGIA----FKVADTAPFAVQAEVTMKTNFFATRNVCKELLPllKPNGRVVNISSMCAIS 144
Cdd:PRK12936   85 VNNAGITkdglFVRMSDEDWDSVLEVNLTATFRLTRELTHPMMR--RRYGRIINITSVVGVT 144
ENR_SDR cd05372
Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ...
 7-138 5.13e-08

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: 52.58  E-value: 5.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   7 AVVTG--SNKGIGFAIVRALCKQfSGDVYLTSRNiERGKAAVAKLQEE-GLKPLFHQLDIDDQQSIQTLRDFLKEKYGGL 83
Cdd:cd05372     4 ILITGiaNDRSIAWGIAKALHEA-GAELAFTYQP-EALRKRVEKLAERlGESALVLPCDVSNDEEIKELFAEVKKDWGKL 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2118010591  84 NVLVNNAGIAFKVADTAPFavqAEVTMKtNFFATRN--------VCKELLPLLKPNGRVVNIS 138
Cdd:cd05372    82 DGLVHSIAFAPKVQLKGPF---LDTSRK-GFLKALDisayslvsLAKAALPIMNPGGSIVTLS 140
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
 6-139 5.16e-08

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 52.81  E-value: 5.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQFSGDVYLTSRNIERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLNV 85
Cdd:PRK08936    9 VVVITGGSTGLGRAMAVRFGKEKAKVVINYRSDEEEANDVAEEIKKAGGEAIAVKGDVTVESDVVNLIQTAVKEFGTLDV 88

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2118010591  86 LVNNAGIAFKVADTapfavqaEVTMK-------TNFFATRNVCKELLPLLKPN---GRVVNISS 139
Cdd:PRK08936   89 MINNAGIENAVPSH-------EMSLEdwnkvinTNLTGAFLGSREAIKYFVEHdikGNIINMSS 145
PRK06940 PRK06940
short chain dehydrogenase; Provisional
 6-238 5.71e-08

short chain dehydrogenase; Provisional


Pssm-ID: 180766 [Multi-domain]  Cd Length: 275  Bit Score: 52.71  E-value: 5.71e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNkGIGFAIVRalcKQFSG-DVYLTSRNIERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFlKEKYGGLN 84
Cdd:PRK06940    4 VVVVIGAG-GIGQAIAR---RVGAGkKVLLADYNEENLEAAAKTLREAGFDVSTQEVDVSSRESVKALAAT-AQTLGPVT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  85 VLVNNAGIafkvadtAPFAVQAEVTMKTNFFATRNVCKELLPLLKPNGRVVNISSMcAISALAKCSQDLQQKFRSdTITE 164
Cdd:PRK06940   79 GLVHTAGV-------SPSQASPEAILKVDLYGTALVLEEFGKVIAPGGAGVVIASQ-SGHRLPALTAEQERALAT-TPTE 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591 165 E--ELVKLMEKFVEDtkkgvhekegwPNHAYGVTKIGvTVLsRIQARMLNETRKGDGIllNACCPGWVRTDMA-----GP 237
Cdd:PRK06940  150 EllSLPFLQPDAIED-----------SLHAYQIAKRA-NAL-RVMAEAVKWGERGARI--NSISPGIISTPLAqdelnGP 214


                  .
gi 2118010591 238 R 238
Cdd:PRK06940  215 R 215
PRK09730 PRK09730
SDR family oxidoreductase;
6-142 5.74e-08

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 52.54  E-value: 5.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQFSGDVYLTSRNIERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLNV 85
Cdd:PRK09730    3 IALVTGGSRGIGRATALLLAQEGYTVAVNYQQNLHAAQEVVNLITQAGGKAFVLQADISDENQVVAMFTAIDQHDEPLAA 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2118010591  86 LVNNAGIAFKVADTAPF-AVQAEVTMKTNFFATRNVCKELLPLLKPN-----GRVVNISSMCA 142
Cdd:PRK09730   83 LVNNAGILFTQCTVENLtAERINRVLSTNVTGYFLCCREAVKRMALKhggsgGAIVNVSSAAS 145
PRK07576 PRK07576
short chain dehydrogenase; Provisional
 7-138 6.87e-08

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 52.26  E-value: 6.87e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   7 AVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNIERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLNVL 86
Cdd:PRK07576   12 VVVVGGTSGINLGIAQAFARA-GANVAVASRSQEKVDAAVAQLQQAGPEGLGVSADVRDYAAVEAAFAQIADEFGPIDVL 90

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2118010591  87 VNNAGIAFkVADTAPFAVQA-EVTMKTNFFATRNVCKELLPLL-KPNGRVVNIS 138
Cdd:PRK07576   91 VSGAAGNF-PAPAAGMSANGfKTVVDIDLLGTFNVLKAAYPLLrRPGASIIQIS 143
PRK08017 PRK08017
SDR family oxidoreductase;
8-144 6.92e-08

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 52.40  E-value: 6.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   8 VVTGSNKGIGFAIVRALcKQFSGDVYLTSRniergKAA-VAKLQEEGLKPLfhQLDIDDQQSI-QTLRDFLKEKYGGLNV 85
Cdd:PRK08017    6 LITGCSSGIGLEAALEL-KRRGYRVLAACR-----KPDdVARMNSLGFTGI--LLDLDDPESVeRAADEVIALTDNRLYG 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2118010591  86 LVNNAGIAFKVADTAPFAVQAEVTMKTNFFATRNVCKELLPLLKP--NGRVVNISS-MCAIS 144
Cdd:PRK08017   78 LFNNAGFGVYGPLSTISRQQMEQQFSTNFFGTHQLTMLLLPAMLPhgEGRIVMTSSvMGLIS 139
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
 9-266 9.16e-08

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 51.80  E-value: 9.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   9 VTGSNKGIG--FAIVRAlckQFSGDVYLTSRNiergkaaVAKL--------QEEGLKPLFHQLDID--DQQSIQTLRDFL 76
Cdd:PRK08945   17 VTGAGDGIGreAALTYA---RHGATVILLGRT-------EEKLeavydeieAAGGPQPAIIPLDLLtaTPQNYQQLADTI 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  77 KEKYGGLNVLVNNAGIafkVADTAPFAVQAEVT----MKTNFFATRNVCKELLPLLK--PNGRVVnissmcaisalakcs 150
Cdd:PRK08945   87 EEQFGRLDGVLHNAGL---LGELGPMEQQDPEVwqdvMQVNVNATFMLTQALLPLLLksPAASLV--------------- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591 151 qdlqqkFRSDTIteeelvklmekfvedtkkGVHEKEGWpnHAYGVTKIGVTVLSRIQARMLNETRkgdgILLNACCPGWV 230
Cdd:PRK08945  149 ------FTSSSV------------------GRQGRANW--GAYAVSKFATEGMMQVLADEYQGTN----LRVNCINPGGT 198

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 2118010591 231 RTDMagpRATKSPDEGAET--------PVYLALLPPGADGPHGQ 266
Cdd:PRK08945  199 RTAM---RASAFPGEDPQKlktpedimPLYLYLMGDDSRRKNGQ 239
PRK06123 PRK06123
SDR family oxidoreductase;
6-142 1.09e-07

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 51.70  E-value: 1.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVR-------ALCKQfsgdvYLtsRNIERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKE 78
Cdd:PRK06123    4 VMIITGASRGIGAATALlaaergyAVCLN-----YL--RNRDAAEAVVQAIRRQGGEALAVAADVADEADVLRLFEAVDR 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2118010591  79 KYGGLNVLVNNAGIafkvADTAPFAVQAEVTMKTNFFATRNV-----CKELLPLLKP-----NGRVVNISSMCA 142
Cdd:PRK06123   77 ELGRLDALVNNAGI----LEAQMRLEQMDAARLTRIFATNVVgsflcAREAVKRMSTrhggrGGAIVNVSSMAA 146
PRK05866 PRK05866
SDR family oxidoreductase;
8-139 1.77e-07

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 51.28  E-value: 1.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   8 VVTGSNKGIGFAIVRALCKQfSGDVYLTSRNIERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLNVLV 87
Cdd:PRK05866   44 LLTGASSGIGEAAAEQFARR-GATVVAVARREDLLDAVADRITRAGGDAMAVPCDLSDLDAVDALVADVEKRIGGVDILI 122

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2118010591  88 NNAG--IAFKVADTAPFAVQAEVTMKTNFFATRNVCKELLP--LLKPNGRVVNISS 139
Cdd:PRK05866  123 NNAGrsIRRPLAESLDRWHDVERTMVLNYYAPLRLIRGLAPgmLERGDGHIINVAT 178
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
 6-142 1.88e-07

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: 51.00  E-value: 1.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALcKQFSGDVYLTSRNIERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLNV 85
Cdd:cd08936    12 VALVTASTDGIGLAIARRL-AQDGAHVVVSSRKQQNVDRAVATLQGEGLSVTGTVCHVGKAEDRERLVATAVNLHGGVDI 90

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2118010591  86 LVNNAGI---AFKVADTAPFAVQA--EVTMKTNFFATRNVCKELLPllKPNGRVVNISSMCA 142
Cdd:cd08936    91 LVSNAAVnpfFGNILDSTEEVWDKilDVNVKATALMTKAVVPEMEK--RGGGSVVIVSSVAA 150
PRK06947 PRK06947
SDR family oxidoreductase;
4-142 2.54e-07

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 50.57  E-value: 2.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   4 TPVAVVTGSNKGIGFAIVRaLCKQFSGDVYLT-SRNIERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGG 82
Cdd:PRK06947    2 RKVVLITGASRGIGRATAV-LAAARGWSVGINyARDAAAAEETADAVRAAGGRACVVAGDVANEADVIAMFDAVQSAFGR 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2118010591  83 LNVLVNNAGIafkVADTAPFAVQAEVTMK----TNFFATRNVCKELLPLLKPN-----GRVVNISSMCA 142
Cdd:PRK06947   81 LDALVNNAGI---VAPSMPLADMDAARLRrmfdTNVLGAYLCAREAARRLSTDrggrgGAIVNVSSIAS 146
PRK08340 PRK08340
SDR family oxidoreductase;
8-91 3.92e-07

SDR family oxidoreductase;


Pssm-ID: 169390 [Multi-domain]  Cd Length: 259  Bit Score: 50.19  E-value: 3.92e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   8 VVTGSNKGIGFAIVRALCKQfSGDVYLTSRNIERGKAAVAKLQEEGLKPLFhQLDIDDQQSIQTLRDFLKEKYGGLNVLV 87
Cdd:PRK08340    4 LVTASSRGIGFNVARELLKK-GARVVISSRNEENLEKALKELKEYGEVYAV-KADLSDKDDLKNLVKEAWELLGGIDALV 81


                  ....
gi 2118010591  88 NNAG 91
Cdd:PRK08340   82 WNAG 85
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
 7-142 4.76e-07

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: 49.78  E-value: 4.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   7 AVVTGSNKGIGFAIVRALCKQfsgDVYLTSRNIERGKaavakLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLNVL 86
Cdd:cd05331     1 VIVTGAAQGIGRAVARHLLQA---GATVIALDLPFVL-----LLEYGDPLRLTPLDVADAAAVREVCSRLLAEHGPIDAL 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2118010591  87 VNNAGIaFKVADTAPFAVQA-EVTMKTNFFATRNVCKELLPLLKP--NGRVVNISSMCA 142
Cdd:cd05331    73 VNCAGV-LRPGATDPLSTEDwEQTFAVNVTGVFNLLQAVAPHMKDrrTGAIVTVASNAA 130
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
6-140 5.42e-07

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 49.63  E-value: 5.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQFSGDVYLTSRNIERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLNV 85
Cdd:PRK12938    5 IAYVTGGMGGIGTSICQRLHKDGFKVVAGCGPNSPRRVKWLEDQKALGFDFIASEGNVGDWDSTKAAFDKVKAEVGEIDV 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2118010591  86 LVNNAGIAFKVADTAPFAVQAEVTMKTNFFATRNVCKELLPLLKPN--GRVVNISSM 140
Cdd:PRK12938   85 LVNNAGITRDVVFRKMTREDWTAVIDTNLTSLFNVTKQVIDGMVERgwGRIINISSV 141
PRK08415 PRK08415
enoyl-[acyl-carrier-protein] reductase FabI;
13-138 6.36e-07

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


Pssm-ID: 181416 [Multi-domain]  Cd Length: 274  Bit Score: 49.36  E-value: 6.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  13 NKGIGFAIVRAlCKQFSGDVYLTSRNiERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLNVLVNNAGI 92
Cdd:PRK08415   16 NKSIAYGIAKA-CFEQGAELAFTYLN-EALKKRVEPIAQELGSDYVYELDVSKPEHFKSLAESLKKDLGKIDFIVHSVAF 93

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2118010591  93 AFKVADTAPF---AVQA-EVTMKTNFFATRNVCKELLPLLKPNGRVVNIS 138
Cdd:PRK08415   94 APKEALEGSFletSKEAfNIAMEISVYSLIELTRALLPLLNDGASVLTLS 143
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
 5-138 6.76e-07

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: 49.20  E-value: 6.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   5 PVAVVTGSNKGIGFAIVRALCKQfsG-DVYLTSRNIERG-KAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGG 82
Cdd:cd05357     1 AVALVTGAAKRIGRAIAEALAAE--GyRVVVHYNRSEAEaQRLKDELNALRNSAVLVQADLSDFAACADLVAAAFRAFGR 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2118010591  83 LNVLVNNAGIAFKVADTAPFAVQAEVTMKTN----FFATRNvckeLLPLLKP--NGRVVNIS 138
Cdd:cd05357    79 CDVLVNNASAFYPTPLGQGSEDAWAELFGINlkapYLLIQA----FARRLAGsrNGSIINII 136
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
6-140 7.65e-07

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 49.10  E-value: 7.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKqfsGDVYLTSRNIERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLNV 85
Cdd:PRK08993   12 VAVVTGCDTGLGQGMALGLAE---AGCDIVGINIVEPTETIEQVTALGRRFLSLTADLRKIDGIPALLERAVAEFGHIDI 88

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  86 LVNNAGIaFKVADTAPFAVQ-----AEVTMKTNFFATRNVCKELLPLLKpNGRVVNISSM 140
Cdd:PRK08993   89 LVNNAGL-IRREDAIEFSEKdwddvMNLNIKSVFFMSQAAAKHFIAQGN-GGKIINIASM 146
PRK07832 PRK07832
SDR family oxidoreductase;
7-146 8.27e-07

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 49.27  E-value: 8.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   7 AVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNIERGKAAVAKLQEEGLKPLFHQ-LDIDDQQSIQTLRDFLKEKYGGLNV 85
Cdd:PRK07832    3 CFVTGAASGIGRATALRLAAQ-GAELFLTDRDADGLAQTVADARALGGTVPEHRaLDISDYDAVAAFAADIHAAHGSMDV 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2118010591  86 LVNNAGIA-FKVADTAPFAvQAEVTMKTNFFATRNVCKELLPLLKPNGR---VVNISSMCAISAL 146
Cdd:PRK07832   82 VMNIAGISaWGTVDRLTHE-QWRRMVDVNLMGPIHVIETFVPPMVAAGRgghLVNVSSAAGLVAL 145
PRK06125 PRK06125
short chain dehydrogenase; Provisional
 7-91 9.82e-07

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 48.89  E-value: 9.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   7 AVVTGSNKGIGFAIVRALCKQFSGdVYLTSRNIERGKAAVAKLQEE-GLKPLFHQLDIDDQQSiqtlRDFLKEKYGGLNV 85
Cdd:PRK06125   10 VLITGASKGIGAAAAEAFAAEGCH-LHLVARDADALEALAADLRAAhGVDVAVHALDLSSPEA----REQLAAEAGDIDI 84


                  ....*.
gi 2118010591  86 LVNNAG 91
Cdd:PRK06125   85 LVNNAG 90
PRK06196 PRK06196
oxidoreductase; Provisional
 6-139 1.03e-06

oxidoreductase; Provisional


Pssm-ID: 235736 [Multi-domain]  Cd Length: 315  Bit Score: 48.91  E-value: 1.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNIERGKAAVAKLQEEGLKPlfhqLDIDDQQSIqtlRDFlKEKYGG--- 82
Cdd:PRK06196   28 TAIVTGGYSGLGLETTRALAQA-GAHVIVPARRPDVAREALAGIDGVEVVM----LDLADLESV---RAF-AERFLDsgr 98

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2118010591  83 -LNVLVNNAGI-AFKVADTAPfavQAEVTMKTNFFATRNVCKELLPLLKPNG--RVVNISS 139
Cdd:PRK06196   99 rIDILINNAGVmACPETRVGD---GWEAQFATNHLGHFALVNLLWPALAAGAgaRVVALSS 156
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
6-140 1.39e-06

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 48.36  E-value: 1.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQFSGDVyltsrNIERGKAAVAKLQEEGLKPLFHQL--DIDDQQSIQTLRDFLKEKYGGL 83
Cdd:PRK12481   10 VAIITGCNTGLGQGMAIGLAKAGADIV-----GVGVAEAPETQAQVEALGRKFHFItaDLIQQKDIDSIVSQAVEVMGHI 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2118010591  84 NVLVNNAGIaFKVADTAPFAVQ-----AEVTMKTNFFATRNVCKELLPlLKPNGRVVNISSM 140
Cdd:PRK12481   85 DILINNAGI-IRRQDLLEFGNKdwddvININQKTVFFLSQAVAKQFVK-QGNGGKIINIASM 144
PRK12747 PRK12747
short chain dehydrogenase; Provisional
 1-234 1.51e-06

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 48.15  E-value: 1.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   1 MSNTPVAVVTGSNKGIGfaivRALCKQFSGD-----VYLTSRNiERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDF 75
Cdd:PRK12747    1 MLKGKVALVTGASRGIG----RAIAKRLANDgalvaIHYGNRK-EEAEETVYEIQSNGGSAFSIGANLESLHGVEALYSS 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  76 LK---EKYGG---LNVLVNNAGI---AFKVADTAPFAVQ-AEVTMKTNFFatrnVCKELLPLLKPNGRVVNISsmcaiSA 145
Cdd:PRK12747   76 LDnelQNRTGstkFDILINNAGIgpgAFIEETTEQFFDRmVSVNAKAPFF----IIQQALSRLRDNSRIINIS-----SA 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591 146 LAKCSqdlqqkfrsdtiteeelvklMEKFVedtkkgvhekegwpnhAYGVTKIGVTVLSRIQARMLNetrkGDGILLNAC 225
Cdd:PRK12747  147 ATRIS--------------------LPDFI----------------AYSMTKGAINTMTFTLAKQLG----ARGITVNAI 186


                  ....*....
gi 2118010591 226 CPGWVRTDM 234
Cdd:PRK12747  187 LPGFIKTDM 195
PRK08278 PRK08278
SDR family oxidoreductase;
7-138 1.67e-06

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 48.36  E-value: 1.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   7 AVVTGSNKGIGFAIVRALCKQ----------------FSGDVYLTSRNIErgkaavaklqEEGLKPLFHQLDIDDQQSIQ 70
Cdd:PRK08278    9 LFITGASRGIGLAIALRAARDganiviaaktaephpkLPGTIHTAAEEIE----------AAGGQALPLVGDVRDEDQVA 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2118010591  71 TLRDFLKEKYGGLNVLVNNAGiAFKVADTapfavqAEVTMK-------TNFFATRNVCKELLPLLK--PNGRVVNIS 138
Cdd:PRK08278   79 AAVAKAVERFGGIDICVNNAS-AINLTGT------EDTPMKrfdlmqqINVRGTFLVSQACLPHLKksENPHILTLS 148
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
 6-139 1.98e-06

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: 48.00  E-value: 1.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNIERGKAAVAKLqeeGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLNV 85
Cdd:cd05363     5 TALITGSARGIGRAFAQAYVRE-GARVAIADINLEAARATAAEI---GPAACAISLDVTDQASIDRCVAALVDRWGSIDI 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2118010591  86 LVNNAGiAFkvaDTAPFAVQA--------EVTMKTNFFATRNVCKELLPLLKpNGRVVNISS 139
Cdd:cd05363    81 LVNNAA-LF---DLAPIVDITresydrlfAINVSGTLFMMQAVARAMIAQGR-GGKIINMAS 137
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 4-146 1.98e-06

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 47.65  E-value: 1.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   4 TPVAVVTGSNKGIGFAIVRALCKQfSGDVYltsrniergkaAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEkyggL 83
Cdd:PRK06550    5 TKTVLITGAASGIGLAQARAFLAQ-GAQVY-----------GVDKQDKPDLSGNFHFLQLDLSDDLEPLFDWVPS----V 68

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2118010591  84 NVLVNNAGI--AFK-VADTAPFAVQAevTMKTNFFATRNVCKELLPLLKPNGRVVnISSMCAISAL 146
Cdd:PRK06550   69 DILCNTAGIldDYKpLLDTSLEEWQH--IFDTNLTSTFLLTRAYLPQMLERKSGI-IINMCSIASF 131
PRK06953 PRK06953
SDR family oxidoreductase;
5-245 3.46e-06

SDR family oxidoreductase;


Pssm-ID: 180774 [Multi-domain]  Cd Length: 222  Bit Score: 46.99  E-value: 3.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   5 PVAVVTGSNKGIGFAIVRalckQFSGD---VYLTSRNiergKAAVAKLQEEGLKPlfHQLDIDDQQSIQTlrdfLKEKYG 81
Cdd:PRK06953    2 KTVLIVGASRGIGREFVR----QYRADgwrVIATARD----AAALAALQALGAEA--LALDVADPASVAG----LAWKLD 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  82 G--LNVLVNNAGIAFKVADTAPFAVQAE--VTMKTNFFATRNVCKELLPLLKPNGRVVNI--SSMCAISalakcsqdlqq 155
Cdd:PRK06953   68 GeaLDAAVYVAGVYGPRTEGVEPITREDfdAVMHTNVLGPMQLLPILLPLVEAAGGVLAVlsSRMGSIG----------- 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591 156 kfrsdtiteeelvklmekfvedtkkGVHEKEGWpnhAYGVTKIGVTVLSRI---QARmlnetrkgdgillNACC----PG 228
Cdd:PRK06953  137 -------------------------DATGTTGW---LYRASKAALNDALRAaslQAR-------------HATCialhPG 175

                         250
                  ....*....|....*..
gi 2118010591 229 WVRTDMAGPRATKSPDE 245
Cdd:PRK06953  176 WVRTDMGGAQAALDPAQ 192
PRK05872 PRK05872
short chain dehydrogenase; Provisional
 6-145 4.14e-06

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 47.27  E-value: 4.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNIERGKAAVAKLqEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLNV 85
Cdd:PRK05872   11 VVVVTGAARGIGAELARRLHAR-GAKLALVDLEEAELAALAAEL-GGDDRVLTVVADVTDLAAMQAAAEEAVERFGGIDV 88

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2118010591  86 LVNNAGIA----FKVADTAPFAVQAEVtmktNFFATRNVCKELLP-LLKPNGRVVNISSMCAISA 145
Cdd:PRK05872   89 VVANAGIAsggsVAQVDPDAFRRVIDV----NLLGVFHTVRATLPaLIERRGYVLQVSSLAAFAA 149
PRK12428 PRK12428
coniferyl-alcohol dehydrogenase;
58-142 5.19e-06

coniferyl-alcohol dehydrogenase;


Pssm-ID: 237099 [Multi-domain]  Cd Length: 241  Bit Score: 46.53  E-value: 5.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  58 FHQLDIDDQQSIQTLRDFLKEKyggLNVLVNNAGiafkVADTAPfavqAEVTMKTNFFATRNVCKELLPLLKPNGRVVNI 137
Cdd:PRK12428   27 FIQADLGDPASIDAAVAALPGR---IDALFNIAG----VPGTAP----VELVARVNFLGLRHLTEALLPRMAPGGAIVNV 95


                  ....*
gi 2118010591 138 SSMCA 142
Cdd:PRK12428   96 ASLAG 100
PRK06194 PRK06194
hypothetical protein; Provisional
 6-93 5.20e-06

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 46.93  E-value: 5.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGfaivRALCKQFSG---DVYLTSRNIERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGG 82
Cdd:PRK06194    8 VAVITGAASGFG----LAFARIGAAlgmKLVLADVQQDALDRAVAELRAQGAEVLGVRTDVSDAAQVEALADAALERFGA 83

                          90
                  ....*....|.
gi 2118010591  83 LNVLVNNAGIA 93
Cdd:PRK06194   84 VHLLFNNAGVG 94
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
 6-236 5.59e-06

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: 46.68  E-value: 5.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNIERGKAAVAKLQEEGLKplFHQLDIDDQQSIQTLRDFLKEKYGGLNV 85
Cdd:cd05326     6 VAIITGGASGIGEATARLFAKH-GARVVIADIDDDAGQAVAAELGDPDIS--FVHCDVTVEADVRAAVDTAVARFGRLDI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  86 LVNNAGI----AFKVADT--APFAVQAEVTMKTNFFATRNVCKELLPLLKpnGRVVNISSMCAISAlakcsqdlqqkfrs 159
Cdd:cd05326    83 MFNNAGVlgapCYSILETslEEFERVLDVNVYGAFLGTKHAARVMIPAKK--GSIVSVASVAGVVG-------------- 146

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2118010591 160 dtiteeelvklmekfvedtkkgvhekeGWPNHAYGVTKIGVTVLSRIQARMLNETrkgdGILLNACCPGWVRTDMAG 236
Cdd:cd05326   147 ---------------------------GLGPHAYTASKHAVLGLTRSAATELGEH----GIRVNCVSPYGVATPLLT 192
PRK08177 PRK08177
SDR family oxidoreductase;
7-239 9.97e-06

SDR family oxidoreductase;


Pssm-ID: 236173 [Multi-domain]  Cd Length: 225  Bit Score: 45.41  E-value: 9.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   7 AVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNIERGKA--AVAKLQEEglkplfhQLDIDDQQSIQTLRDFLKEKYggLN 84
Cdd:PRK08177    4 ALIIGASRGLGLGLVDRLLER-GWQVTATVRGPQQDTAlqALPGVHIE-------KLDMNDPASLDQLLQRLQGQR--FD 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  85 VLVNNAGIAFKVADTAPFAVQAEVT--MKTNFFATRNVCKELLPLLKPNGRVVNISSmcaiSALAkcsqdlqqkfrSDTI 162
Cdd:PRK08177   74 LLFVNAGISGPAHQSAADATAAEIGqlFLTNAIAPIRLARRLLGQVRPGQGVLAFMS----SQLG-----------SVEL 138

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2118010591 163 TEEELVKLmekfvedtkkgvhekegwpnhaYGVTKIGVTVLSRIQARMLNETRkgdgILLNACCPGWVRTDMAGPRA 239
Cdd:PRK08177  139 PDGGEMPL----------------------YKASKAALNSMTRSFVAELGEPT----LTVLSMHPGWVKTDMGGDNA 189
PRK06720 PRK06720
hypothetical protein; Provisional
 6-92 1.46e-05

hypothetical protein; Provisional


Pssm-ID: 180669 [Multi-domain]  Cd Length: 169  Bit Score: 44.58  E-value: 1.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNIERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLNV 85
Cdd:PRK06720   18 VAIVTGGGIGIGRNTALLLAKQ-GAKVIVTDIDQESGQATVEEITNLGGEALFVSYDMEKQGDWQRVISITLNAFSRIDM 96


                  ....*..
gi 2118010591  86 LVNNAGI 92
Cdd:PRK06720   97 LFQNAGL 103
PRK07677 PRK07677
short chain dehydrogenase; Provisional
 5-90 1.63e-05

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 45.05  E-value: 1.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   5 PVAVVTGSNKGIGfaivRALCKQFSGD---VYLTSRNIERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYG 81
Cdd:PRK07677    2 KVVIITGGSSGMG----KAMAKRFAEEganVVITGRTKEKLEEAKLEIEQFPGQVLTVQMDVRNPEDVQKMVEQIDEKFG 77


                  ....*....
gi 2118010591  82 GLNVLVNNA 90
Cdd:PRK07677   78 RIDALINNA 86
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
 6-126 1.75e-05

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: 45.07  E-value: 1.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQFSGDVYLTSRNIERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLNV 85
Cdd:cd05373     1 VAAVVGAGDGLGAAIARRFAAEGFSVALAARREAKLEALLVDIIRDAGGSAKAVPTDARDEDEVIALFDLIEEEIGPLEV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2118010591  86 LVNNAG--IAFKVADTAP--FAVQAEVTMKTNFFATRNVCKELLP 126
Cdd:cd05373    81 LVYNAGanVWFPILETTPrvFEKVWEMAAFGGFLAAREAAKRMLA 125
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
 6-139 1.89e-05

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 45.03  E-value: 1.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNIERGKAAVAKLQEE--GLKPLFHQLDIDDQQSIQTLRDFLKEKYGGL 83
Cdd:PRK12384    4 VAVVIGGGQTLGAFLCHGLAEE-GYRVAVADINSEKAANVAQEINAEygEGMAYGFGADATSEQSVLALSRGVDEIFGRV 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2118010591  84 NVLVNNAGIAfKVADTAPFAVQA-EVTMKTN----FFATRNVCKELLPlLKPNGRVVNISS 139
Cdd:PRK12384   83 DLLVYNAGIA-KAAFITDFQLGDfDRSLQVNlvgyFLCAREFSRLMIR-DGIQGRIIQINS 141
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 8-103 2.42e-05

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: 44.01  E-value: 2.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591    8 VVTGSNKGIGFAIVRALCKQFSGDVYLTSRN--IERGKAA-VAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLN 84
Cdd:smart00822   4 LITGGLGGLGRALARWLAERGARRLVLLSRSgpDAPGAAAlLAELEAAGARVTVVACDVADRDALAAVLAAIPAVEGPLT 83

                           90
                   ....*....|....*....
gi 2118010591   85 VLVNNAGiafkVADTAPFA 103
Cdd:smart00822  84 GVIHAAG----VLDDGVLA 98
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
8-142 2.94e-05

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 44.58  E-value: 2.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   8 VVTGSNKGIGFAIVRALCKQfsG-DVYLTSRNIERGKAAVAKLQEEglkplFHQLDIDDqqsiqtlRDFLKEKYGGLNVL 86
Cdd:COG0451     3 LVTGGAGFIGSHLARRLLAR--GhEVVGLDRSPPGAANLAALPGVE-----FVRGDLRD-------PEALAAALAGVDAV 68

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2118010591  87 VNNAGIAfkvadtAPFAVQAEVTMKTNFFATRNVCKellpLLKPNG--RVVNISSMCA 142
Cdd:COG0451    69 VHLAAPA------GVGEEDPDETLEVNVEGTLNLLE----AARAAGvkRFVYASSSSV 116
PRK06500 PRK06500
SDR family oxidoreductase;
7-145 4.27e-05

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 43.79  E-value: 4.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   7 AVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNIERGKAAVAKLQEEGLKPLFHQLDIDDQQSiqtLRDFLKEKYGGLNVL 86
Cdd:PRK06500    9 ALITGGTSGIGLETARQFLAE-GARVAITGRDPASLEAARAELGESALVIRADAGDVAAQKA---LAQALAEAFGRLDAV 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2118010591  87 VNNAGiafkVADTAPFAVQAEV----TMKTN----FFatrnVCKELLPLL-KPNGRVVNISsmcaISA 145
Cdd:PRK06500   85 FINAG----VAKFAPLEDWDEAmfdrSFNTNvkgpYF----LIQALLPLLaNPASIVLNGS----INA 140
RhaD COG3347
Rhamnose utilisation protein RhaD, predicted bifunctional aldolase and dehydrogenase ...
 6-99 4.44e-05

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


Pssm-ID: 442576 [Multi-domain]  Cd Length: 674  Bit Score: 44.52  E-value: 4.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNIERGKAAVAKLQEEGLKplfhqLDIDDQQSIQTLRDFLKE------- 78
Cdd:COG3347   427 VALVTGGAGGIGRATAARLAAE-GAAVVVADLDGEAAEAAAAELGGGYGA-----DAVDATDVDVTAEAAVAAafgfagl 500

                          90       100
                  ....*....|....*....|.
gi 2118010591  79 KYGGLNVLVNNAGIAFKVADT 99
Cdd:COG3347   501 DIGGSDIGVANAGIASSSPEE 521
PRK07478 PRK07478
short chain dehydrogenase; Provisional
 6-92 4.97e-05

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 43.76  E-value: 4.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNIERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLNV 85
Cdd:PRK07478    8 VAIITGASSGIGRAAAKLFARE-GAKVVVGARRQAELDQLVAEIRAEGGEAVALAGDVRDEAYAKALVALAVERFGGLDI 86


                  ....*..
gi 2118010591  86 LVNNAGI 92
Cdd:PRK07478   87 AFNNAGT 93
PRK06523 PRK06523
short chain dehydrogenase; Provisional
 7-139 5.11e-05

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 43.74  E-value: 5.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   7 AVVTGSNKGIGFAIVRALCKqfSGDVYLTSrnierGKAAVAKLQEEGlkpLFHQLDIDDQQSIQTLRDFLKEKYGGLNVL 86
Cdd:PRK06523   12 ALVTGGTKGIGAATVARLLE--AGARVVTT-----ARSRPDDLPEGV---EFVAADLTTAEGCAAVARAVLERLGGVDIL 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2118010591  87 VNNAGiafkvADTAP---FAV------QAEvtMKTNFFATRNVCKELLPLLKPNGR--VVNISS 139
Cdd:PRK06523   82 VHVLG-----GSSAPaggFAAltdeewQDE--LNLNLLAAVRLDRALLPGMIARGSgvIIHVTS 138
PRK07775 PRK07775
SDR family oxidoreductase;
7-143 6.38e-05

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 43.59  E-value: 6.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   7 AVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNIERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLNVL 86
Cdd:PRK07775   13 ALVAGASSGIGAATAIELAAA-GFPVALGARRVEKCEELVDKIRADGGEAVAFPLDVTDPDSVKSFVAQAEEALGEIEVL 91

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2118010591  87 VNNAG-IAF-KVADTAP--FAVQAEVTM-KTNFFATRnvckeLLP--LLKPNGRVVNISSMCAI 143
Cdd:PRK07775   92 VSGAGdTYFgKLHEISTeqFESQVQIHLvGANRLATA-----VLPgmIERRRGDLIFVGSDVAL 150
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
 6-139 6.89e-05

(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: 43.08  E-value: 6.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGfaivRALCKQFS------------GDVYLTSRNIERGKAAVAKLQEEGLKPLFHQLDIDDQQSI-QTL 72
Cdd:cd05353     7 VVLVTGAGGGLG----RAYALAFAergakvvvndlgGDRKGSGKSSSAADKVVDEIKAAGGKAVANYDSVEDGEKIvKTA 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2118010591  73 RDflkeKYGGLNVLVNNAGI----AFKVADTAPFAVQAEVTMKTNFFATRNVckelLPLLKPN--GRVVNISS 139
Cdd:cd05353    83 ID----AFGRVDILVNNAGIlrdrSFAKMSEEDWDLVMRVHLKGSFKVTRAA----WPYMRKQkfGRIINTSS 147
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
 6-146 8.47e-05

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: 42.98  E-value: 8.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQFSG---DVYLTSRNIERGKAAVAKLQEE--GLKPLFHQLDIDDQQSIQTLRDFLKEKY 80
Cdd:TIGR01500   2 VCLVTGASRGFGRTIAQELAKCLKSpgsVLVLSARNDEALRQLKAEIGAErsGLRVVRVSLDLGAEAGLEQLLKALRELP 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2118010591  81 GGLN----VLVNNAGIAF---KVADTAPFAVQAEVTMKTNFFATRNVCKELLPLLKP----NGRVVNISSMCAISAL 146
Cdd:TIGR01500  82 RPKGlqrlLLINNAGTLGdvsKGFVDLSDSTQVQNYWALNLTSMLCLTSSVLKAFKDspglNRTVVNISSLCAIQPF 158
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
 6-234 1.18e-04

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: 42.51  E-value: 1.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNIERGKAAVAKLQE--EGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGL 83
Cdd:cd05330     5 VVLITGGGSGLGLATAVRLAKE-GAKLSLVDLNEEGLEAAKAALLEiaPDAEVLLIKADVSDEAQVEAYVDATVEQFGRI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  84 NVLVNNAGIAFKVADTAPFAVQ-----AEVTMKTNFFATRNVckelLPLLKPN--GRVVNISSMCAIsalakcsqdlqqk 156
Cdd:cd05330    84 DGFFNNAGIEGKQNLTEDFGADefdkvVSINLRGVFYGLEKV----LKVMREQgsGMIVNTASVGGI------------- 146

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2118010591 157 frsdtiteeelvklmekfvedtkKGVHEKEGwpnhaYGVTKIGVTVLSRIQARMLNEtrkgDGILLNACCPGWVRTDM 234
Cdd:cd05330   147 -----------------------RGVGNQSG-----YAAAKHGVVGLTRNSAVEYGQ----YGIRINAIAPGAILTPM 192
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
 7-135 1.48e-04

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: 41.74  E-value: 1.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   7 AVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNiergKAAVAKLQEEglkpLFHQLDIDDQQSIQTLRDfLKEKYGGLNVL 86
Cdd:cd11730     1 ALILGATGGIGRALARALAGR-GWRLLLSGRD----AGALAGLAAE----VGALARPADVAAELEVWA-LAQELGPLDLL 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2118010591  87 VNNAGIAFK--VADTAPFAVqaEVTMKTNFFATRNVCKELLPLLKPNGRVV 135
Cdd:cd11730    71 VYAAGAILGkpLARTKPAAW--RRILDANLTGAALVLKHALALLAAGARLV 119
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
7-139 1.93e-04

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 41.98  E-value: 1.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   7 AVVTGSNKGIGFAIVRALCKqfSGD-VYLTSRNIERGKAAVAklQEEGLKPLFHQLDIDDQQSI-QTLRDFL----KEKY 80
Cdd:PRK06924    4 VIITGTSQGLGEAIANQLLE--KGThVISISRTENKELTKLA--EQYNSNLTFHSLDLQDVHELeTNFNEILssiqEDNV 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2118010591  81 GGLNvLVNNAGIafkVADTAPfAVQAEVTM-----KTNFFA----TRNVCKELLPlLKPNGRVVNISS 139
Cdd:PRK06924   80 SSIH-LINNAGM---VAPIKP-IEKAESEElitnvHLNLLApmilTSTFMKHTKD-WKVDKRVINISS 141
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
 8-103 2.24e-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: 41.01  E-value: 2.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   8 VVTGSNKGIGFAIVRALCKQFSGDVYLTSRNI---ERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLN 84
Cdd:pfam08659   4 LITGGLGGLGRELARWLAERGARHLVLLSRSAaprPDAQALIAELEARGVEVVVVACDVSDPDAVAALLAEIKAEGPPIR 83

                          90
                  ....*....|....*....
gi 2118010591  85 VLVNNAGiafkVADTAPFA 103
Cdd:pfam08659  84 GVIHAAG----VLRDALLE 98
PRK07791 PRK07791
short chain dehydrogenase; Provisional
 6-92 2.90e-04

short chain dehydrogenase; Provisional


Pssm-ID: 236099 [Multi-domain]  Cd Length: 286  Bit Score: 41.58  E-value: 2.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQ--------FSGDVYLTSRNIERGKAAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLK 77
Cdd:PRK07791    8 VVIVTGAGGGIGRAHALAFAAEgarvvvndIGVGLDGSASGGSAAQAVVDEIVAAGGEAVANGDDIADWDGAANLVDAAV 87

                          90
                  ....*....|....*
gi 2118010591  78 EKYGGLNVLVNNAGI 92
Cdd:PRK07791   88 ETFGGLDVLVNNAGI 102
PRK12742 PRK12742
SDR family oxidoreductase;
7-269 3.48e-04

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 40.90  E-value: 3.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   7 AVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNieRGKAAVAKLQEEGLKPLfhQLDIDDQ-QSIQTLRDFlkekyGGLNV 85
Cdd:PRK12742    9 VLVLGGSRGIGAAIVRRFVTD-GANVRFTYAG--SKDAAERLAQETGATAV--QTDSADRdAVIDVVRKS-----GALDI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  86 LVNNAGIA----------------FKVADTAPF--AVQAEVTMktnffatrnvckellpllKPNGRVVNISSMCA----I 143
Cdd:PRK12742   79 LVVNAGIAvfgdaleldaddidrlFKINIHAPYhaSVEAARQM------------------PEGGRIIIIGSVNGdrmpV 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591 144 SALAkcsqdlqqkfrsdtiteeelvklmekfvedtkkgvhekegwpnhAYGVTKIGVTVLSRIQARMLNETrkgdGILLN 223
Cdd:PRK12742  141 AGMA--------------------------------------------AYAASKSALQGMARGLARDFGPR----GITIN 172

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591 224 ACCPGWVRTD-----------MAGPRATK---SPDEGAETPVYLAllppgadGPHGQHVS 269
Cdd:PRK12742  173 VVQPGPIDTDanpangpmkdmMHSFMAIKrhgRPEEVAGMVAWLA-------GPEASFVT 225
PRK07024 PRK07024
SDR family oxidoreductase;
3-146 3.84e-04

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 41.07  E-value: 3.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   3 NTPVAVVTGSNKGIGFAIVRALCKQfsGDVY-LTSRNIERGKAAVAKLQEEGlKPLFHQLDIDDQQSIQTL-RDFLkEKY 80
Cdd:PRK07024    1 MPLKVFITGASSGIGQALAREYARQ--GATLgLVARRTDALQAFAARLPKAA-RVSVYAADVRDADALAAAaADFI-AAH 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2118010591  81 GGLNVLVNNAGIAFKV--ADTAPFAVQAEVtMKTNFFAtrnVCKELLPLLKP-----NGRVVNISSMCAISAL 146
Cdd:PRK07024   77 GLPDVVIANAGISVGTltEEREDLAVFREV-MDTNYFG---MVATFQPFIAPmraarRGTLVGIASVAGVRGL 145
PRK09135 PRK09135
pteridine reductase; Provisional
 1-90 5.12e-04

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 40.68  E-value: 5.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   1 MSNTPVAVVTGSNKGIGFAIVRAL----------CKQFSGDVYLTSRNIERGKAAVAklqeeglkpLFHQLDIDDQQSIQ 70
Cdd:PRK09135    3 TDSAKVALITGGARRIGAAIARTLhaagyrvaihYHRSAAEADALAAELNALRPGSA---------AALQADLLDPDALP 73

                          90       100
                  ....*....|....*....|
gi 2118010591  71 TLRDFLKEKYGGLNVLVNNA 90
Cdd:PRK09135   74 ELVAACVAAFGRLDALVNNA 93
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
 6-92 6.79e-04

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


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 40.32  E-value: 6.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGFAIVRalckqfsgdvyltsRNIERG-KAAVAKLQEEGLKPLFHQL------------DIDDQQSI--Q 70
Cdd:PRK06200    8 VALITGGGSGIGRALVE--------------RFLAEGaRVAVLERSAEKLASLRQRFgdhvlvvegdvtSYADNQRAvdQ 73

                          90       100
                  ....*....|....*....|..
gi 2118010591  71 TLRDFlkekyGGLNVLVNNAGI 92
Cdd:PRK06200   74 TVDAF-----GKLDCFVGNAGI 90
PRK06483 PRK06483
dihydromonapterin reductase; Provisional
 2-90 8.33e-04

dihydromonapterin reductase; Provisional


Pssm-ID: 180586 [Multi-domain]  Cd Length: 236  Bit Score: 39.92  E-value: 8.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   2 SNTPVaVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNiERgkAAVAKLQEEGlkPLFHQLDIDDQQSIQTLRDFLKEKYG 81
Cdd:PRK06483    1 MPAPI-LITGAGQRIGLALAWHLLAQ-GQPVIVSYRT-HY--PAIDGLRQAG--AQCIQADFSTNAGIMAFIDELKQHTD 73


                  ....*....
gi 2118010591  82 GLNVLVNNA 90
Cdd:PRK06483   74 GLRAIIHNA 82
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 6-90 8.90e-04

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 39.77  E-value: 8.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSN--KGIGFAIVRALCKQfSGDVYLT-----SRNIERG--KAAVAKLQEE----GLKPLFHQLDIDDQQSIQTL 72
Cdd:PRK12859    8 VAVVTGVSrlDGIGAAICKELAEA-GADIFFTywtayDKEMPWGvdQDEQIQLQEEllknGVKVSSMELDLTQNDAPKEL 86

                          90
                  ....*....|....*...
gi 2118010591  73 RDFLKEKYGGLNVLVNNA 90
Cdd:PRK12859   87 LNKVTEQLGYPHILVNNA 104
HSDL2_SDR_c cd09762
human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup ...
 9-138 9.82e-04

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: 39.74  E-value: 9.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   9 VTGSNKGIGFAIVRALCKQfSGDVYLTSRNIERGK-------AAVAKLQEEGLKPLFHQLDIDDQQSIQTLRDFLKEKYG 81
Cdd:cd09762     8 ITGASRGIGKAIALKAARD-GANVVIAAKTAEPHPklpgtiyTAAEEIEAAGGKALPCIVDIRDEDQVRAAVEKAVEKFG 86

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2118010591  82 GLNVLVNNAGiAFKVADTapfavqAEVTMK-------TNFFATRNVCKELLPLLK--PNGRVVNIS 138
Cdd:cd09762    87 GIDILVNNAS-AISLTGT------LDTPMKrydlmmgVNTRGTYLCSKACLPYLKksKNPHILNLS 145
PRK07023 PRK07023
SDR family oxidoreductase;
7-147 1.13e-03

SDR family oxidoreductase;


Pssm-ID: 180796 [Multi-domain]  Cd Length: 243  Bit Score: 39.61  E-value: 1.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   7 AVVTGSNKGIGFAIVRALCKQfsGDVYLT---SRNIERGKAAVAKLQEeglkplfHQLDIDDQQSIQ------TLRDFLK 77
Cdd:PRK07023    4 AIVTGHSRGLGAALAEQLLQP--GIAVLGvarSRHPSLAAAAGERLAE-------VELDLSDAAAAAawlagdLLAAFVD 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  78 ekyGGLNV-LVNNAGIafkVADTAPFAVQAEVTMKTNFfaTRNVckeLLPLLKPNG-----------RVVNISSMCAISA 145
Cdd:PRK07023   75 ---GASRVlLINNAGT---VEPIGPLATLDAAAIARAV--GLNV---AAPLMLTAAlaqaasdaaerRILHISSGAARNA 143


                  ..
gi 2118010591 146 LA 147
Cdd:PRK07023  144 YA 145
PRK05717 PRK05717
SDR family oxidoreductase;
2-93 1.66e-03

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 39.10  E-value: 1.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   2 SNTPVAVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNIERGkAAVAKLQeeGLKPLFHQLDI-DDQQSIQTLRDFLKEkY 80
Cdd:PRK05717    8 HNGRVALVTGAARGIGLGIAAWLIAE-GWQVVLADLDRERG-SKVAKAL--GENAWFIAMDVaDEAQVAAGVAEVLGQ-F 82

                          90
                  ....*....|...
gi 2118010591  81 GGLNVLVNNAGIA 93
Cdd:PRK05717   83 GRLDALVCNAAIA 95
PRK07577 PRK07577
SDR family oxidoreductase;
7-139 2.03e-03

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 38.55  E-value: 2.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   7 AVVTGSNKGIGFAivralckqfsgdvyLTSRNIERGKAAV--AKLQEEGLKPLFHQLDI-DDQQSIQTLRDFLKEkyGGL 83
Cdd:PRK07577    6 VLVTGATKGIGLA--------------LSLRLANLGHQVIgiARSAIDDFPGELFACDLaDIEQTAATLAQINEI--HPV 69

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2118010591  84 NVLVNNAGIAF-----KVADTAPFAVqaevtMKTNFFATRNVCKELLPLLK--PNGRVVNISS 139
Cdd:PRK07577   70 DAIVNNVGIALpqplgKIDLAALQDV-----YDLNVRAAVQVTQAFLEGMKlrEQGRIVNICS 127
PRK06482 PRK06482
SDR family oxidoreductase;
9-140 2.20e-03

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 38.94  E-value: 2.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   9 VTGSNKGIGfaivRALckqfsgdvylTSRNIERGKAAVAKLQEEG----LKPLFH------QLDIDDQQSIQTLRDFLKE 78
Cdd:PRK06482    7 ITGASSGFG----RGM----------TERLLARGDRVAATVRRPDalddLKARYGdrlwvlQLDVTDSAAVRAVVDRAFA 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2118010591  79 KYGGLNVLVNNAGIA-FKVADTAPFAvQAEVTMKTNFFATRNVCKELLPLLKPN--GRVVNISSM 140
Cdd:PRK06482   73 ALGRIDVVVSNAGYGlFGAAEELSDA-QIRRQIDTNLIGSIQVIRAALPHLRRQggGRIVQVSSE 136
fabG PRK05786
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 8-243 2.76e-03

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


Pssm-ID: 235608 [Multi-domain]  Cd Length: 238  Bit Score: 38.20  E-value: 2.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   8 VVTGSNKGIGFAIVRALCKQfSGDVYLTSRNIERGKAAVAKLQEEGlKPLFHQLDIDDQQSIQTLRDFLKEKYGGLNVLV 87
Cdd:PRK05786    9 AIIGVSEGLGYAVAYFALKE-GAQVCINSRNENKLKRMKKTLSKYG-NIHYVVGDVSSTESARNVIEKAAKVLNAIDGLV 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591  88 NNAGiaFKVADTAPFAVQAEVTMKTNFFATRNVCKELLPLLKPNGRVVNISSMCAISAlakcsqdlqqkfrsdtiteeel 167
Cdd:PRK05786   87 VTVG--GYVEDTVEEFSGLEEMLTNHIKIPLYAVNASLRFLKEGSSIVLVSSMSGIYK---------------------- 142

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2118010591 168 vklmekfvedtkkgvhekeGWPNH-AYGVTKIGVTVLSRIQARMLnetrKGDGILLNACCPGWVRTDMAGPRATKSP 243
Cdd:PRK05786  143 -------------------ASPDQlSYAVAKAGLAKAVEILASEL----LGRGIRVNGIAPTTISGDFEPERNWKKL 196
PLN00015 PLN00015
protochlorophyllide reductase
 8-113 2.90e-03

protochlorophyllide reductase


Pssm-ID: 177654  Cd Length: 308  Bit Score: 38.53  E-value: 2.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   8 VVTGSNKGIGFAIVRALCKQFSGDVYLTSRNIERG-KAAVAKLQEEGLKPLFHqLDIDDQQSIqtlRDFLKE--KYG-GL 83
Cdd:PLN00015    1 IITGASSGLGLATAKALAETGKWHVVMACRDFLKAeRAAKSAGMPKDSYTVMH-LDLASLDSV---RQFVDNfrRSGrPL 76

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2118010591  84 NVLVNNAGIAFKVADTAPFAVQA-EVTMKTN 113
Cdd:PLN00015   77 DVLVCNAAVYLPTAKEPTFTADGfELSVGTN 107
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
 6-139 3.14e-03

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: 38.21  E-value: 3.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   6 VAVVTGSNKGIGfaivRALCKQFSGDVYltsrniergKAAVAKLQEE-------------GLKPLFHQLDIDDQQSIQTL 72
Cdd:cd05322     4 VAVVIGGGQTLG----EFLCHGLAEAGY---------DVAVADINSEnaekvadeinaeyGEKAYGFGADATNEQSVIAL 70

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2118010591  73 RDFLKEKYGGLNVLVNNAGIAfKVADTAPFAVQA-EVTMKTN----FFATRNVCKeLLPLLKPNGRVVNISS 139
Cdd:cd05322    71 SKGVDEIFKRVDLLVYSAGIA-KSAKITDFELGDfDRSLQVNlvgyFLCAREFSK-LMIRDGIQGRIIQINS 140
PRK08251 PRK08251
SDR family oxidoreductase;
8-143 3.29e-03

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 37.99  E-value: 3.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118010591   8 VVTGSNKGIGFAIVRALCKQfsG-DVYLTSRNIERGKAAVAKLQEE--GLKPLFHQLDIDDQQSIQTLRDFLKEKYGGLN 84
Cdd:PRK08251    6 LITGASSGLGAGMAREFAAK--GrDLALCARRTDRLEELKAELLARypGIKVAVAALDVNDHDQVFEVFAEFRDELGGLD 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2118010591  85 VLVNNAGIAFKVADTAPFAVQAEVTMKTNFFATRNVCKELLPLLKPNGR--VVNISSMCAI 143
Cdd:PRK08251   84 RVIVNAGIGKGARLGTGKFWANKATAETNFVAALAQCEAAMEIFREQGSghLVLISSVSAV 144
PRK08339 PRK08339
short chain dehydrogenase; Provisional
 6-52 4.11e-03

short chain dehydrogenase; Provisional


Pssm-ID: 169389 [Multi-domain]  Cd Length: 263  Bit Score: 37.91  E-value: 4.11e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2118010591   6 VAVVTGSNKGIGFAIVRALCKQfSGDVYLTSRNIERGKAAVAKLQEE 52
Cdd:PRK08339   10 LAFTTASSKGIGFGVARVLARA-GADVILLSRNEENLKKAREKIKSE 55
 
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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