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Conserved domains on  [gi|699964346|dbj|BAP77015|]
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alcohol dehydrogenase, partial [Drosophila acutilabella]

Protein Classification

SDR family oxidoreductase( domain architecture ID 10143139)

classical SDR (short-chain dehydrogenase/reductase) family NAD(P)-dependent oxidoreductase similar to alcohol dehydrogenase that catalyzes the NAD+-dependent oxidation of alcohols to aldehydes/ketones; 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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 1-234 4.65e-78

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: 234.89  E-value: 4.65e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   1 AALGGVGLATSKEIVKRGpKNFVVLDRIENPKALAELKALNPKVTVSFYLYDVTVPvTETVKLLTTIFGKLKTIDLLING 80
Cdd:cd05323    7 GGASGIGLATAKLLLKKG-AKVAILDRNENPGAAAELQAINPKVKATFVQCDVTSW-EQLAAAFKKAIEKFGRVDILINN 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  81 AGILDDH----------QIERTIAINFTGLVNTTTAIMQFWDKRKGGPGGVIANICSVTGFNAIHQVPVYSASKAAVVSF 150
Cdd:cd05323   85 AGILDEKsylfagklppPWEKTIDVNLTGVINTTYLALHYMDKNKGGKGGVIVNIGSVAGLYPAPQFPVYSASKHGVVGF 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346 151 TSSLAKLAP-ITGITAYSINPGITVTPLTHQFNSWLdveprvAELLNEHPTQTTEECGLNFAKAIEANQ-NGAIWKLDLG 228
Cdd:cd05323  165 TRSLADLLEyKTGVRVNAICPGFTNTPLLPDLVAKE------AEMLPSAPTQSPEVVAKAIVYLIEDDEkNGAIWIVDGG 238


                 ....*.
gi 699964346 229 RLEAVT 234
Cdd:cd05323  239 KLIEIE 244
 
Name Accession Description Interval E-value
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 1-234 4.65e-78

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: 234.89  E-value: 4.65e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   1 AALGGVGLATSKEIVKRGpKNFVVLDRIENPKALAELKALNPKVTVSFYLYDVTVPvTETVKLLTTIFGKLKTIDLLING 80
Cdd:cd05323    7 GGASGIGLATAKLLLKKG-AKVAILDRNENPGAAAELQAINPKVKATFVQCDVTSW-EQLAAAFKKAIEKFGRVDILINN 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  81 AGILDDH----------QIERTIAINFTGLVNTTTAIMQFWDKRKGGPGGVIANICSVTGFNAIHQVPVYSASKAAVVSF 150
Cdd:cd05323   85 AGILDEKsylfagklppPWEKTIDVNLTGVINTTYLALHYMDKNKGGKGGVIVNIGSVAGLYPAPQFPVYSASKHGVVGF 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346 151 TSSLAKLAP-ITGITAYSINPGITVTPLTHQFNSWLdveprvAELLNEHPTQTTEECGLNFAKAIEANQ-NGAIWKLDLG 228
Cdd:cd05323  165 TRSLADLLEyKTGVRVNAICPGFTNTPLLPDLVAKE------AEMLPSAPTQSPEVVAKAIVYLIEDDEkNGAIWIVDGG 238


                 ....*.
gi 699964346 229 RLEAVT 234
Cdd:cd05323  239 KLIEIE 244
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 4-186 1.33e-48

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 158.16  E-value: 1.33e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346    4 GGVGLATSKEIVKRGPKNFVVlDRIENP--KALAELKALNPKVTvsFYLYDVTVPvTETVKLLTTIFGKLKTIDLLINGA 81
Cdd:pfam00106  10 SGIGRAIAKRLAKEGAKVVLV-DRSEEKleAVAKELGALGGKAL--FIQGDVTDR-AQVKALVEQAVERLGRLDILVNNA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   82 GI--------LDDHQIERTIAINFTGLVNTTTAIMQFWDKRKGGpggVIANICSVTGFNAIHQVPVYSASKAAVVSFTSS 153
Cdd:pfam00106  86 GItglgpfseLSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGG---RIVNISSVAGLVPYPGGSAYSASKAAVIGFTRS 162

                         170       180       190
                  ....*....|....*....|....*....|...
gi 699964346  154 LAKLAPITGITAYSINPGITVTPLTHQFNSWLD 186
Cdd:pfam00106 163 LALELAPHGIRVNAVAPGGVDTDMTKELREDEG 195
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
2-193 2.16e-30

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 113.04  E-value: 2.16e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   2 ALGGVGLATSKEIVKRGPkNFVVLDRieNPKALAELKAL--NPKVTVSFYLYDVTVPvtETV-KLLTTIFGKLKTIDLLI 78
Cdd:COG0300   13 ASSGIGRALARALAARGA-RVVLVAR--DAERLEALAAElrAAGARVEVVALDVTDP--DAVaALAEAVLARFGPIDVLV 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  79 NGAGI--------LDDHQIERTIAINFTGLVNTTTAIMQFWDKRKGGpggVIANICSVTGFNAIHQVPVYSASKAAVVSF 150
Cdd:COG0300   88 NNAGVggggpfeeLDLEDLRRVFEVNVFGPVRLTRALLPLMRARGRG---RIVNVSSVAGLRGLPGMAAYAASKAALEGF 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 699964346 151 TSSLAK-LAPiTGITAYSINPGITVTPLTHQF-----NSWLDVEpRVAE 193
Cdd:COG0300  165 SESLRAeLAP-TGVRVTAVCPGPVDTPFTARAgapagRPLLSPE-EVAR 211
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 2-200 9.04e-22

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 89.90  E-value: 9.04e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   2 ALGGVGLATSKEIVKRGPKNFVVLDRIENP--KALAELKALNpkVTVSFYLYDVTVPvTETVKLLTTIFGKLKTIDLLIN 79
Cdd:PRK05565  13 ASGGIGRAIAELLAKEGAKVVIAYDINEEAaqELLEEIKEEG--GDAIAVKADVSSE-EDVENLVEQIVEKFGKIDILVN 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  80 GAGI--------LDDHQIERTIAINFTGLVNTTTAIMQFWDKRKGGpggVIANICSVTGFN-AIHQVPvYSASKAAVVSF 150
Cdd:PRK05565  90 NAGIsnfglvtdMTDEEWDRVIDVNLTGVMLLTRYALPYMIKRKSG---VIVNISSIWGLIgASCEVL-YSASKGAVNAF 165

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 699964346 151 TSSLAK-LAPiTGITAYSINPGITVTPLTHQFNswldvEPRVAELLNEHPT 200
Cdd:PRK05565 166 TKALAKeLAP-SGIRVNAVAPGAIDTEMWSSFS-----EEDKEGLAEEIPL 210
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 2-86 3.29e-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: 43.24  E-value: 3.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346     2 ALGGVGLATSKEIVKRGPKNFVVLDR--IENPKA---LAELKALNPKVTVsfYLYDVTVPVtETVKLLTTIFGKLKTIDL 76
Cdd:smart00822   8 GLGGLGRALARWLAERGARRLVLLSRsgPDAPGAaalLAELEAAGARVTV--VACDVADRD-ALAAVLAAIPAVEGPLTG 84

                           90
                   ....*....|
gi 699964346    77 LINGAGILDD 86
Cdd:smart00822  85 VIHAAGVLDD 94
 
Name Accession Description Interval E-value
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 1-234 4.65e-78

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: 234.89  E-value: 4.65e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   1 AALGGVGLATSKEIVKRGpKNFVVLDRIENPKALAELKALNPKVTVSFYLYDVTVPvTETVKLLTTIFGKLKTIDLLING 80
Cdd:cd05323    7 GGASGIGLATAKLLLKKG-AKVAILDRNENPGAAAELQAINPKVKATFVQCDVTSW-EQLAAAFKKAIEKFGRVDILINN 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  81 AGILDDH----------QIERTIAINFTGLVNTTTAIMQFWDKRKGGPGGVIANICSVTGFNAIHQVPVYSASKAAVVSF 150
Cdd:cd05323   85 AGILDEKsylfagklppPWEKTIDVNLTGVINTTYLALHYMDKNKGGKGGVIVNIGSVAGLYPAPQFPVYSASKHGVVGF 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346 151 TSSLAKLAP-ITGITAYSINPGITVTPLTHQFNSWLdveprvAELLNEHPTQTTEECGLNFAKAIEANQ-NGAIWKLDLG 228
Cdd:cd05323  165 TRSLADLLEyKTGVRVNAICPGFTNTPLLPDLVAKE------AEMLPSAPTQSPEVVAKAIVYLIEDDEkNGAIWIVDGG 238


                 ....*.
gi 699964346 229 RLEAVT 234
Cdd:cd05323  239 KLIEIE 244
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 4-186 1.33e-48

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 158.16  E-value: 1.33e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346    4 GGVGLATSKEIVKRGPKNFVVlDRIENP--KALAELKALNPKVTvsFYLYDVTVPvTETVKLLTTIFGKLKTIDLLINGA 81
Cdd:pfam00106  10 SGIGRAIAKRLAKEGAKVVLV-DRSEEKleAVAKELGALGGKAL--FIQGDVTDR-AQVKALVEQAVERLGRLDILVNNA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   82 GI--------LDDHQIERTIAINFTGLVNTTTAIMQFWDKRKGGpggVIANICSVTGFNAIHQVPVYSASKAAVVSFTSS 153
Cdd:pfam00106  86 GItglgpfseLSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGG---RIVNISSVAGLVPYPGGSAYSASKAAVIGFTRS 162

                         170       180       190
                  ....*....|....*....|....*....|...
gi 699964346  154 LAKLAPITGITAYSINPGITVTPLTHQFNSWLD 186
Cdd:pfam00106 163 LALELAPHGIRVNAVAPGGVDTDMTKELREDEG 195
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 2-181 5.83e-35

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: 124.32  E-value: 5.83e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   2 ALGGVGLATSKEIVKRGpKNFVVLDRieNPKALAELKALN-PKVTVSFYLYDVTVPvtETV-KLLTTIFGKLKTIDLLIN 79
Cdd:cd05233    6 ASSGIGRAIARRLAREG-AKVVLADR--NEEALAELAAIEaLGGNAVAVQADVSDE--EDVeALVEEALEEFGRLDILVN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  80 GAGI--------LDDHQIERTIAINFTGLVNTTTAIMQFWDKRKGGpggVIANICSVTGFNAIHQVPVYSASKAAVVSFT 151
Cdd:cd05233   81 NAGIarpgpleeLTDEDWDRVLDVNLTGVFLLTRAALPHMKKQGGG---RIVNISSVAGLRPLPGQAAYAASKAALEGLT 157

                        170       180       190
                 ....*....|....*....|....*....|
gi 699964346 152 SSLAKLAPITGITAYSINPGITVTPLTHQF 181
Cdd:cd05233  158 RSLALELAPYGIRVNAVAPGLVDTPMLAKL 187
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
2-193 2.16e-30

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 113.04  E-value: 2.16e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   2 ALGGVGLATSKEIVKRGPkNFVVLDRieNPKALAELKAL--NPKVTVSFYLYDVTVPvtETV-KLLTTIFGKLKTIDLLI 78
Cdd:COG0300   13 ASSGIGRALARALAARGA-RVVLVAR--DAERLEALAAElrAAGARVEVVALDVTDP--DAVaALAEAVLARFGPIDVLV 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  79 NGAGI--------LDDHQIERTIAINFTGLVNTTTAIMQFWDKRKGGpggVIANICSVTGFNAIHQVPVYSASKAAVVSF 150
Cdd:COG0300   88 NNAGVggggpfeeLDLEDLRRVFEVNVFGPVRLTRALLPLMRARGRG---RIVNVSSVAGLRGLPGMAAYAASKAALEGF 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 699964346 151 TSSLAK-LAPiTGITAYSINPGITVTPLTHQF-----NSWLDVEpRVAE 193
Cdd:COG0300  165 SESLRAeLAP-TGVRVTAVCPGPVDTPFTARAgapagRPLLSPE-EVAR 211
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 4-199 1.95e-28

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: 107.95  E-value: 1.95e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   4 GGVGLATSKEIVKRGPkNFVVLDRIENP--KALAELKALNPKVTvsFYLYDVTVPvtETVK-LLTTIFGKLKTIDLLING 80
Cdd:COG1028   16 SGIGRAIARALAAEGA-RVVITDRDAEAleAAAAELRAAGGRAL--AVAADVTDE--AAVEaLVAAAVAAFGRLDILVNN 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  81 AGI--------LDDHQIERTIAINFTGLVNTTTAimqFWDKRKGGPGGVIANICSVTGFNAIHQVPVYSASKAAVVSFTS 152
Cdd:COG1028   91 AGItppgpleeLTEEDWDRVLDVNLKGPFLLTRA---ALPHMRERGGGRIVNISSIAGLRGSPGQAAYAASKAAVVGLTR 167

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 699964346 153 SLAK-LAPiTGITAYSINPGITVTPLTHqfnSWLDVEPRVAELLNEHP 199
Cdd:COG1028  168 SLALeLAP-RGIRVNAVAPGPIDTPMTR---ALLGAEEVREALAARIP 211
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 4-179 1.47e-25

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: 99.87  E-value: 1.47e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   4 GGVGLATSKEIVKRGPKnfVVL-DRieNPKALAELKA-LNPKVTVsfYLYDVTVP--VTETVKLLTTIFGKlktIDLLIN 79
Cdd:COG4221   15 SGIGAATARALAAAGAR--VVLaAR--RAERLEALAAeLGGRALA--VPLDVTDEaaVEAAVAAAVAEFGR---LDVLVN 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  80 GAGI--------LDDHQIERTIAINFTGLVNTTTAIMQFWDKRKGGpggVIANICSVTGFNAIHQVPVYSASKAAVVSFT 151
Cdd:COG4221   86 NAGVallgpleeLDPEDWDRMIDVNVKGVLYVTRAALPAMRARGSG---HIVNISSIAGLRPYPGGAVYAATKAAVRGLS 162

                        170       180
                 ....*....|....*....|....*....
gi 699964346 152 SSLAK-LAPiTGITAYSINPGITVTPLTH 179
Cdd:COG4221  163 ESLRAeLRP-TGIRVTVIEPGAVDTEFLD 190
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 2-200 9.04e-22

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 89.90  E-value: 9.04e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   2 ALGGVGLATSKEIVKRGPKNFVVLDRIENP--KALAELKALNpkVTVSFYLYDVTVPvTETVKLLTTIFGKLKTIDLLIN 79
Cdd:PRK05565  13 ASGGIGRAIAELLAKEGAKVVIAYDINEEAaqELLEEIKEEG--GDAIAVKADVSSE-EDVENLVEQIVEKFGKIDILVN 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  80 GAGI--------LDDHQIERTIAINFTGLVNTTTAIMQFWDKRKGGpggVIANICSVTGFN-AIHQVPvYSASKAAVVSF 150
Cdd:PRK05565  90 NAGIsnfglvtdMTDEEWDRVIDVNLTGVMLLTRYALPYMIKRKSG---VIVNISSIWGLIgASCEVL-YSASKGAVNAF 165

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 699964346 151 TSSLAK-LAPiTGITAYSINPGITVTPLTHQFNswldvEPRVAELLNEHPT 200
Cdd:PRK05565 166 TKALAKeLAP-SGIRVNAVAPGAIDTEMWSSFS-----EEDKEGLAEEIPL 210
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 5-214 8.38e-21

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: 87.31  E-value: 8.38e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   5 GVGLATSKEIVKRGPKNFVV---LDRIENPKALAELKALNPKVTVSFYLYDVTVPVtETVKLLTTIFGKLKTIDLLINGA 81
Cdd:cd08939   12 GIGKALAKELVKEGANVIIVarsESKLEEAVEEIEAEANASGQKVSYISADLSDYE-EVEQAFAQAVEKGGPPDLVVNCA 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  82 GI--------LDDHQIERTIAINFTGLVNTTTAIMQFWDKRKGGpggVIANICSVTGFNAIHQVPVYSASKAAVVSFTSS 153
Cdd:cd08939   91 GIsipglfedLTAEEFERGMDVNYFGSLNVAHAVLPLMKEQRPG---HIVFVSSQAALVGIYGYSAYCPSKFALRGLAES 167

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 699964346 154 LAKLAPITGITAYSINPGITVTPlthQFNSWLDVEPRVAELLNE-HPTQTTEECglnfAKAI 214
Cdd:cd08939  168 LRQELKPYNIRVSVVYPPDTDTP---GFEEENKTKPEETKAIEGsSGPITPEEA----ARII 222
PRK12829 PRK12829
short chain dehydrogenase; Provisional
 4-176 2.47e-20

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 86.65  E-value: 2.47e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   4 GGVGLATSKEIVKRGpKNFVVLDRieNPKALAELKALNPKVTVSFYLYDVTVPvTETVKLLTTIFGKLKTIDLLINGAGI 83
Cdd:PRK12829  21 SGIGRAIAEAFAEAG-ARVHVCDV--SEAALAATAARLPGAKVTATVADVADP-AQVERVFDTAVERFGGLDVLVNNAGI 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  84 ---------LDDHQIERTIAINFTGLVNTTTAIMQFWdkRKGGPGGVIANICSVTGFNAIHQVPVYSASKAAVVSFTSSL 154
Cdd:PRK12829  97 agptggideITPEQWEQTLAVNLNGQFYFARAAVPLL--KASGHGGVIIALSSVAGRLGYPGRTPYAASKWAVVGLVKSL 174

                        170       180
                 ....*....|....*....|...
gi 699964346 155 AK-LAPiTGITAYSINPGITVTP 176
Cdd:PRK12829 175 AIeLGP-LGIRVNAILPGIVRGP 196
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 2-218 2.21e-19

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: 83.45  E-value: 2.21e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   2 ALGGVGLATSKEIVKRGPKnFVVLDRieNPKALAELKALNPKVTVSFYLY--DVTVP--VTETVKLLTTIFGKlktIDLL 77
Cdd:cd05339    7 GGSGIGRLLALEFAKRGAK-VVILDI--NEKGAEETANNVRKAGGKVHYYkcDVSKReeVYEAAKKIKKEVGD---VTIL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  78 INGAGI--------LDDHQIERTIAINFTGLVNTTTAIMQFWDKRKGGPggvIANICSVTGFNAIHQVPVYSASKAAVVS 149
Cdd:cd05339   81 INNAGVvsgkklleLPDEEIEKTFEVNTLAHFWTTKAFLPDMLERNHGH---IVTIASVAGLISPAGLADYCASKAAAVG 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 699964346 150 FTSSLA---KLAPITGITAYSINPGITVTPLTHqfnswlDVEPRVAELLnehPTQTTEECGLNFAKAIEANQ 218
Cdd:cd05339  158 FHESLRlelKAYGKPGIKTTLVCPYFINTGMFQ------GVKTPRPLLA---PILEPEYVAEKIVRAILTNQ 220
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
2-180 2.39e-19

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 83.66  E-value: 2.39e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   2 ALGGVGLATSKEIVKRGPKnFVVLDRIENPKALA-ELKALNPKVTVSFYLYDVTvPVTETVKLLTTIFGKLKTIDLLING 80
Cdd:PRK12824  10 AKRGIGSAIARELLNDGYR-VIATYFSGNDCAKDwFEEYGFTEDQVRLKELDVT-DTEECAEALAEIEEEEGPVDILVNN 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  81 AGILDDHQIERT--------IAINFTGLVNTTTAIMQFWdKRKGGpgGVIANICSVTGFNAIHQVPVYSASKAAVVSFTS 152
Cdd:PRK12824  88 AGITRDSVFKRMshqewndvINTNLNSVFNVTQPLFAAM-CEQGY--GRIINISSVNGLKGQFGQTNYSAAKAGMIGFTK 164

                        170       180
                 ....*....|....*....|....*...
gi 699964346 153 SLAKLAPITGITAYSINPGITVTPLTHQ 180
Cdd:PRK12824 165 ALASEGARYGITVNCIAPGYIATPMVEQ 192
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 2-182 7.32e-19

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 82.16  E-value: 7.32e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   2 ALGGVGLATSKEIVKRGpKNFVVLDRIENPKA---LAELKALNPKVTVSfyLYDVTVPvTETVKLLTTIFGKLKTIDLLI 78
Cdd:PRK05557  13 ASRGIGRAIAERLAAQG-ANVVINYASSEAGAealVAEIGALGGKALAV--QGDVSDA-ESVERAVDEAKAEFGGVDILV 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  79 NGAGILDDHQI--------ERTIAINFTGLVNTTTAIMQfwDKRKGGPGGVIaNICSVTGF-NAIHQVPvYSASKAAVVS 149
Cdd:PRK05557  89 NNAGITRDNLLmrmkeedwDRVIDTNLTGVFNLTKAVAR--PMMKQRSGRII-NISSVVGLmGNPGQAN-YAASKAGVIG 164

                        170       180       190
                 ....*....|....*....|....*....|....
gi 699964346 150 FTSSLAK-LAPiTGITAYSINPGITVTPLTHQFN 182
Cdd:PRK05557 165 FTKSLAReLAS-RGITVNAVAPGFIETDMTDALP 197
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
 4-179 7.73e-19

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: 82.28  E-value: 7.73e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   4 GGVGLATSKEIVKRGpknFVVLDRIENPKALAELKALNPKVTVSFYLyDVTVP--VTETVKLLTTIFGKlktIDLLINGA 81
Cdd:cd05374   10 SGIGLALALALAAQG---YRVIATARNPDKLESLGELLNDNLEVLEL-DVTDEesIKAAVKEVIERFGR---IDVLVNNA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  82 GI--------LDDHQIERTIAINFTGLVNTTTAIMQFWDKRKGGpggVIANICSVTGFNAIHQVPVYSASKAAVVSFTSS 153
Cdd:cd05374   83 GYglfgpleeTSIEEVRELFEVNVFGPLRVTRAFLPLMRKQGSG---RIVNVSSVAGLVPTPFLGPYCASKAALEALSES 159

                        170       180
                 ....*....|....*....|....*..
gi 699964346 154 LAK-LAPiTGITAYSINPGITVTPLTH 179
Cdd:cd05374  160 LRLeLAP-FGIKVTIIEPGPVRTGFAD 185
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
 5-154 3.69e-18

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: 80.21  E-value: 3.69e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   5 GVGLATSKEIVKRGpkNFV-VLDRieNPKALAELKALNPKVTVsfYLYDVTVP--VTETVKLLTTIFGKLktiDLLINGA 81
Cdd:COG3967   16 GIGLALAKRLHARG--NTViITGR--REEKLEEAAAANPGLHT--IVLDVADPasIAALAEQVTAEFPDL---NVLINNA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  82 GIL----------DDHQIERTIAINFTGLVNTTTAIMQFWDKRkggPGGVIANICSVTGFNAIHQVPVYSASKAAVVSFT 151
Cdd:COG3967   87 GIMraedlldeaeDLADAEREITTNLLGPIRLTAAFLPHLKAQ---PEAAIVNVSSGLAFVPLAVTPTYSATKAALHSYT 163


                 ...
gi 699964346 152 SSL 154
Cdd:COG3967  164 QSL 166
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 2-178 4.14e-18

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: 80.28  E-value: 4.14e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   2 ALGGVGLATSKEIVKRGPKnFVVLDRIENPKALAELKALNPKVTVSFYLYDVTVPvTETVKLLTTIFGKLKTIDLLINGA 81
Cdd:cd05333    8 ASRGIGRAIALRLAAEGAK-VAVTDRSEEAAAETVEEIKALGGNAAALEADVSDR-EAVEALVEKVEAEFGPVDILVNNA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  82 GI--------LDDHQIERTIAINFTGLVNTTTAIMQFWDKRKGGPggvIANICSVTGF-NAIHQVPvYSASKAAVVSFTS 152
Cdd:cd05333   86 GItrdnllmrMSEEDWDAVINVNLTGVFNVTQAVIRAMIKRRSGR---IINISSVVGLiGNPGQAN-YAASKAGVIGFTK 161

                        170       180
                 ....*....|....*....|....*..
gi 699964346 153 SLAK-LAPiTGITAYSINPGITVTPLT 178
Cdd:cd05333  162 SLAKeLAS-RGITVNAVAPGFIDTDMT 187
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-176 9.80e-18

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 79.14  E-value: 9.80e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   1 AALGGVGLATSKEIVKRGPKnfVVLDRIENPKALAELKALNP--KVTVSFYLYDVTVP------VTETVKLlttiFGKlk 72
Cdd:PRK12825  13 GAARGLGRAIALRLARAGAD--VVVHYRSDEEAAEELVEAVEalGRRAQAVQADVTDKaaleaaVAAAVER----FGR-- 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  73 tIDLLINGAGI--------LDDHQIERTIAINFTGLVNTTTA---IMqfwdKRKGGpgGVIANICSVTGFNA-IHQVPvY 140
Cdd:PRK12825  85 -IDILVNNAGIfedkpladMSDDEWDEVIDVNLSGVFHLLRAvvpPM----RKQRG--GRIVNISSVAGLPGwPGRSN-Y 156

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 699964346 141 SASKAAVVSFTSSLAK-LAPiTGITAYSINPGITVTP 176
Cdd:PRK12825 157 AAAKAGLVGLTKALAReLAE-YGITVNMVAPGDIDTD 192
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
 5-178 2.19e-17

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


Pssm-ID: 187629 [Multi-domain]  Cd Length: 252  Bit Score: 78.48  E-value: 2.19e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   5 GVGLATSKEIVKRGPKnFVVLDRiENPKALAELKALNpkvTVSFYLYDVTvPVTETVKLLTTIFGKLKTIDLLINGAGI- 83
Cdd:cd05371   13 GLGLATVERLLAQGAK-VVILDL-PNSPGETVAKLGD---NCRFVPVDVT-SEKDVKAALALAKAKFGRLDIVVNCAGIa 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  84 ---------------LDDHQieRTIAINFTGLVNTT---TAIMQFWDKRKGGPGGVIANICSVTGFNAIHQVPVYSASKA 145
Cdd:cd05371   87 vaaktynkkgqqphsLELFQ--RVINVNLIGTFNVIrlaAGAMGKNEPDQGGERGVIINTASVAAFEGQIGQAAYSASKG 164

                        170       180       190
                 ....*....|....*....|....*....|....
gi 699964346 146 AVVSFTSSLAK-LAPItGITAYSINPGITVTPLT 178
Cdd:cd05371  165 GIVGMTLPIARdLAPQ-GIRVVTIAPGLFDTPLL 197
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
 4-197 3.43e-17

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: 77.35  E-value: 3.43e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   4 GGVGLATSKEIVKRGpKNFVVLDRieNPKALAELKALNPkvTVSFYLYDVTVPvTETVKLLTTIFGKLKTIDLLINGAGI 83
Cdd:cd05370   15 SGIGLALARKFLEAG-NTVIITGR--REERLAEAKKELP--NIHTIVLDVGDA-ESVEALAEALLSEYPNLDILINNAGI 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  84 LDDHQI----------ERTIAINFTGLVNTTTAIMQFWDKRkggPGGVIANICSVTGFNAIHQVPVYSASKAAVVSFTSS 153
Cdd:cd05370   89 QRPIDLrdpasdldkaDTEIDTNLIGPIRLIKAFLPHLKKQ---PEATIVNVSSGLAFVPMAANPVYCATKAALHSYTLA 165

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 699964346 154 LAKLAPITGITAYSINPGITVTPLTHQFNSWLDVEPR---VAELLNE 197
Cdd:cd05370  166 LRHQLKDTGVEVVEIVPPAVDTELHEERRNPDGGTPRkmpLDEFVDE 212
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 2-199 3.67e-17

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: 78.27  E-value: 3.67e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   2 ALGGVGLATSKEIVKRGPKnFVVLDRIENP--KALAELKALNPkvTVSFYLYDVtVPVTETVKLLTTIFGKLKTIDLLIN 79
Cdd:cd08935   13 GTGVLGGAMARALAQAGAK-VAALGRNQEKgdKVAKEITALGG--RAIALAADV-LDRASLERAREEIVAQFGTVDILIN 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  80 GAGI----------------------LDDHQIERTIAINFTGlvnTTTAIMQFWDKRKGGPGGVIANICSVTGFNAIHQV 137
Cdd:cd08935   89 GAGGnhpdattdpehyepeteqnffdLDEEGWEFVFDLNLNG---SFLPSQVFGKDMLEQKGGSIINISSMNAFSPLTKV 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 699964346 138 PVYSASKAAVVSFTSSLAKLAPITGITAYSINPGITVTPLTHQ--FNSWLDVEPRVAELLNEHP 199
Cdd:cd08935  166 PAYSAAKAAVSNFTQWLAVEFATTGVRVNAIAPGFFVTPQNRKllINPDGSYTDRSNKILGRTP 229
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
 5-181 3.99e-17

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: 77.42  E-value: 3.99e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   5 GVGLATSKEIVKRGPKnFVVLDRIEN--PKALAELKAlnpkvTVSFYLYDVTVPV--TETVKLLTTIFGKLktiDLLING 80
Cdd:cd05341   16 GLGLAHARLLVAEGAK-VVLSDILDEegQAAAAELGD-----AARFFHLDVTDEDgwTAVVDTAREAFGRL---DVLVNN 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  81 AGILDDHQIE--------RTIAINFTGLVNTTTAIMQfwDKRKGGpGGVIANICSVTGFNAIHQVPVYSASKAAVVSFTS 152
Cdd:cd05341   87 AGILTGGTVEtttleewrRLLDINLTGVFLGTRAVIP--PMKEAG-GGSIINMSSIEGLVGDPALAAYNASKGAVRGLTK 163

                        170       180       190
                 ....*....|....*....|....*....|.
gi 699964346 153 SLA-KLAPIT-GITAYSINPGITVTPLTHQF 181
Cdd:cd05341  164 SAAlECATQGyGIRVNSVHPGYIYTPMTDEL 194
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 1-207 5.31e-17

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: 77.09  E-value: 5.31e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346    1 AALGGVGLATSKEIVKRGpKNFVVLDRieNPKALAELKALNPKVTVSFYLYDVTVP--VTETVKLLTTIFGKlktIDLLI 78
Cdd:pfam13561   3 ANESGIGWAIARALAEEG-AEVVLTDL--NEALAKRVEELAEELGAAVLPCDVTDEeqVEALVAAAVEKFGR---LDILV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   79 NGAGILDDHQI----------ERTIAINFTGLVNTTTA---IMQfwdkrkggPGGVIANICSVTGFNAIHQVPVYSASKA 145
Cdd:pfam13561  77 NNAGFAPKLKGpfldtsredfDRALDVNLYSLFLLAKAalpLMK--------EGGSIVNLSSIGAERVVPNYNAYGAAKA 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 699964346  146 AVVSFTSSLAK-LAPiTGITAYSINPGITVTPLTHQFNswlDVEPRVAELLNEHPTQ---TTEECG 207
Cdd:pfam13561 149 ALEALTRYLAVeLGP-RGIRVNAISPGPIKTLAASGIP---GFDELLAAAEARAPLGrlgTPEEVA 210
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
1-178 1.45e-16

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 75.97  E-value: 1.45e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   1 AALGGVGLATSKEIVKRGPKnfVVLDRIeNPKALAELKA--LNPKVTVSFYLYDVTVPvTETVKLLTTIFGKLKTIDLLI 78
Cdd:PRK05653  12 GASRGIGRAIALRLAADGAK--VVIYDS-NEEAAEALAAelRAAGGEARVLVFDVSDE-AAVRALIEAAVEAFGALDILV 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  79 NGAGILDDHQIE--------RTIAINFTGLVNTT-TAIMQFWDKRKGgpggVIANICSVTGFNA-IHQVPvYSASKAAVV 148
Cdd:PRK05653  88 NNAGITRDALLPrmseedwdRVIDVNLTGTFNVVrAALPPMIKARYG----RIVNISSVSGVTGnPGQTN-YSAAKAGVI 162

                        170       180       190
                 ....*....|....*....|....*....|.
gi 699964346 149 SFTSSLAK-LAPiTGITAYSINPGITVTPLT 178
Cdd:PRK05653 163 GFTKALALeLAS-RGITVNAVAPGFIDTDMT 192
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 5-179 2.80e-16

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 75.00  E-value: 2.80e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   5 GVGLATSKEIVKRGPKNFVVlDRIENPKALAELkalnpkvtvSFYLYDVTVPvtetvklLTTIFGKLKTIDLLINGAGIL 84
Cdd:PRK06550  16 GIGLAQARAFLAQGAQVYGV-DKQDKPDLSGNF---------HFLQLDLSDD-------LEPLFDWVPSVDILCNTAGIL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  85 DDHQ---------IERTIAINFTGLVNTTTAIMQFWDKRKggpGGVIANICSVTGFNAIHQVPVYSASKAAVVSFTSSLA 155
Cdd:PRK06550  79 DDYKplldtsleeWQHIFDTNLTSTFLLTRAYLPQMLERK---SGIIINMCSIASFVAGGGGAAYTASKHALAGFTKQLA 155

                        170       180
                 ....*....|....*....|....
gi 699964346 156 KLAPITGITAYSINPGITVTPLTH 179
Cdd:PRK06550 156 LDYAKDGIQVFGIAPGAVKTPMTA 179
FabG-like PRK07231
SDR family oxidoreductase;
2-181 4.31e-16

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 74.87  E-value: 4.31e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   2 ALGGVGLATSKEIVKRGpKNFVVLDRieNPKALAEL-KALNPKVTVSFYLYDVTVP--VTETVKLLTTIFGKLktiDLLI 78
Cdd:PRK07231  13 ASSGIGEGIARRFAAEG-ARVVVTDR--NEEAAERVaAEILAGGRAIAVAADVSDEadVEAAVAAALERFGSV---DILV 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  79 NGAGI---------LDDHQIERTIAINFTGLVNTTTAIMQFWDKRKGGpggVIANICSVTGfnaIHQVP---VYSASKAA 146
Cdd:PRK07231  87 NNAGTthrngplldVDEAEFDRIFAVNVKSPYLWTQAAVPAMRGEGGG---AIVNVASTAG---LRPRPglgWYNASKGA 160

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 699964346 147 VVSFTSSLA-KLAPiTGITAYSINPGITVTPLTHQF 181
Cdd:PRK07231 161 VITLTKALAaELGP-DKIRVNAVAPVVVETGLLEAF 195
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
 5-185 8.71e-16

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: 73.93  E-value: 8.71e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   5 GVGLATSKEIVKRGpKNFVVLDRIENPKALAELKALNPKVTVSFYLYDVTVPvTETVKLLTTIFGKLKTIDLLINGAGIL 84
Cdd:cd05347   16 GIGFGIASGLAEAG-ANIVINSRNEEKAEEAQQLIEKEGVEATAFTCDVSDE-EAIKAAVEAIEEDFGKIDILVNNAGII 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  85 DDHQIER--------TIAINFTGLVNTTTAIMQFWDKRKGGPggvIANICSVTGFNAIHQVPVYSASKAAVVSFTSSLAK 156
Cdd:cd05347   94 RRHPAEEfpeaewrdVIDVNLNGVFFVSQAVARHMIKQGHGK---IINICSLLSELGGPPVPAYAASKGGVAGLTKALAT 170

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 699964346 157 LAPITGITAYSINPGITVTPLT------HQFNSWL 185
Cdd:cd05347  171 EWARHGIQVNAIAPGYFATEMTeavvadPEFNDDI 205
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 5-178 2.22e-15

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: 72.27  E-value: 2.22e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   5 GVGLATSKEIVKRGPkNFVVL---DRIENPKALAELKALnpKVTVSFYLYDVTVPVTeTVKLLTTIFGKLKTIDLLINGA 81
Cdd:cd05324   11 GIGFEIVRQLAKSGP-GTVILtarDVERGQAAVEKLRAE--GLSVRFHQLDVTDDAS-IEAAADFVEEKYGGLDILVNNA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  82 GILDDH---------QIERTIAINFTGLVNTTTAimqFWDKRKGGPGGVIANICSVTGfnaiHQVPVYSASKAAVVSFTS 152
Cdd:cd05324   87 GIAFKGfddstptreQARETMKTNFFGTVDVTQA---LLPLLKKSPAGRIVNVSSGLG----SLTSAYGVSKAALNALTR 159

                        170       180
                 ....*....|....*....|....*.
gi 699964346 153 SLAKLAPITGITAYSINPGITVTPLT 178
Cdd:cd05324  160 ILAKELKETGIKVNACCPGWVKTDMG 185
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
 2-178 4.66e-15

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: 71.98  E-value: 4.66e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   2 ALGGVGLATSKEIVKRGPKNFVVLDRIENPKAL-AELKALNPKVTVSfyLYDVTVPvtETVKLLTTIFGK-LKTIDLLIN 79
Cdd:cd05350    6 ASSGIGRALAREFAKAGYNVALAARRTDRLDELkAELLNPNPSVEVE--ILDVTDE--ERNQLVIAELEAeLGGLDLVII 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  80 GAGI-----LDDHQIE---RTIAINFTGLVNT-TTAIMQFWDKRKGGpggvIANICSVTGFNAIHQVPVYSASKAAVVSF 150
Cdd:cd05350   82 NAGVgkgtsLGDLSFKafrETIDTNLLGAAAIlEAALPQFRAKGRGH----LVLISSVAALRGLPGAAAYSASKAALSSL 157

                        170       180
                 ....*....|....*....|....*....
gi 699964346 151 TSSL-AKLAPiTGITAYSINPGITVTPLT 178
Cdd:cd05350  158 AESLrYDVKK-RGIRVTVINPGFIDTPLT 185
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
 2-172 5.38e-15

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: 71.93  E-value: 5.38e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   2 ALGGVGLATSKEIVKRGPKNFVVLDRIENPKALA-ELKALNPKVTVSFYLyDVTVPVtETVKLLTTIFGKLKTIDLLING 80
Cdd:cd05346    8 ASSGIGEATARRFAKAGAKLILTGRRAERLQELAdELGAKFPVKVLPLQL-DVSDRE-SIEAALENLPEEFRDIDILVNN 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  81 AGI-----------LDDhqIERTIAINFTGLVNTTTAIMQFWDKRKGGpggVIANICSVTGFNAIHQVPVYSASKAAVVS 149
Cdd:cd05346   86 AGLalgldpaqeadLED--WETMIDTNVKGLLNVTRLILPIMIARNQG---HIINLGSIAGRYPYAGGNVYCATKAAVRQ 160

                        170       180
                 ....*....|....*....|...
gi 699964346 150 FTSSLAKLAPITGITAYSINPGI 172
Cdd:cd05346  161 FSLNLRKDLIGTGIRVTNIEPGL 183
PRK12828 PRK12828
short chain dehydrogenase; Provisional
 2-188 7.49e-15

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 71.37  E-value: 7.49e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   2 ALGGVGLATSKEIVKRGPKnFVVLDRIENP--KALAELKALNPKVTVSfylyDVTVPvTETVKLLTTIFGKLKTIDLLIN 79
Cdd:PRK12828  15 GFGGLGRATAAWLAARGAR-VALIGRGAAPlsQTLPGVPADALRIGGI----DLVDP-QAARRAVDEVNRQFGRLDALVN 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  80 GAGI--------LDDHQIERTIAINFTGLVNTTTAIMQFWDKrkgGPGGVIANICSVTGFNAIHQVPVYSASKAAVVSFT 151
Cdd:PRK12828  89 IAGAfvwgtiadGDADTWDRMYGVNVKTTLNASKAALPALTA---SGGGRIVNIGAGAALKAGPGMGAYAAAKAGVARLT 165

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 699964346 152 SSLAKLAPITGITAYSINPGITVTPLTHQ------FNSWLDVE 188
Cdd:PRK12828 166 EALAAELLDRGITVNAVLPSIIDTPPNRAdmpdadFSRWVTPE 208
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
 4-228 4.21e-14

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: 69.40  E-value: 4.21e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   4 GGVGLATSKEIVKRGPKnfVVLDRIENP---KALAELKALNPKVTVSFYLYDVTVP--VTETVKLLTTIFGKLktiDLLI 78
Cdd:cd08940   12 SGIGLGIARALAAAGAN--IVLNGFGDAaeiEAVRAGLAAKHGVKVLYHGADLSKPaaIEDMVAYAQRQFGGV---DILV 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  79 NGAGILDDHQIE--------RTIAINFTGLVNTTTAIMQFWDKRKGGPggvIANICSVTGFNAIHQVPVYSASKAAVVSF 150
Cdd:cd08940   87 NNAGIQHVAPIEdfptekwdAIIALNLSAVFHTTRLALPHMKKQGWGR---IINIASVHGLVASANKSAYVAAKHGVVGL 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346 151 TSSLAKLAPITGITAYSINPGITVTPLTHQ------FNSWLDVEPRVAELLNE-HPTQ---TTEECG---LNFAKAIEAN 217
Cdd:cd08940  164 TKVVALETAGTGVTCNAICPGWVLTPLVEKqisalaQKNGVPQEQAARELLLEkQPSKqfvTPEQLGdtaVFLASDAASQ 243

                        250
                 ....*....|.
gi 699964346 218 QNGAIWKLDLG 228
Cdd:cd08940  244 ITGTAVSVDGG 254
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
 2-177 6.01e-14

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: 68.94  E-value: 6.01e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   2 ALGGVGLATSKEIVKRGpKNFVVLDRIENPKALAELKALNPK-VTVSFYLYDVTVP--VTETVKLLTTIFGklkTIDLLI 78
Cdd:cd05366   10 AAQGIGRAIAERLAADG-FNIVLADLNLEEAAKSTIQEISEAgYNAVAVGADVTDKddVEALIDQAVEKFG---SFDVMV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  79 NGAGI-----LDD---HQIERTIAINFTGLVNTTTAIMQFWDKRKGGpgGVIANICSVTGFNAIHQVPVYSASKAAVVSF 150
Cdd:cd05366   86 NNAGIapitpLLTiteEDLKKVYAVNVFGVLFGIQAAARQFKKLGHG--GKIINASSIAGVQGFPNLGAYSASKFAVRGL 163

                        170       180
                 ....*....|....*....|....*...
gi 699964346 151 TSSLAK-LAPiTGITAYSINPGITVTPL 177
Cdd:cd05366  164 TQTAAQeLAP-KGITVNAYAPGIVKTEM 190
PRK07825 PRK07825
short chain dehydrogenase; Provisional
 5-178 6.55e-14

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 69.20  E-value: 6.55e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   5 GVGLATSKEIVKRGPKnfVV---LDRIENPKALAELKalnpkvTVSFYLYDVTVPVTETvKLLTTIFGKLKTIDLLINGA 81
Cdd:PRK07825  16 GIGLATARALAALGAR--VAigdLDEALAKETAAELG------LVVGGPLDVTDPASFA-AFLDAVEADLGPIDVLVNNA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  82 GIL--------DDHQIERTIAINFTGLVNTTTAIMQfwDKRKGGPGGVIaNICSVTGFNAIHQVPVYSASKAAVVSFTSS 153
Cdd:PRK07825  87 GVMpvgpfldePDAVTRRILDVNVYGVILGSKLAAP--RMVPRGRGHVV-NVASLAGKIPVPGMATYCASKHAVVGFTDA 163

                        170       180
                 ....*....|....*....|....*.
gi 699964346 154 LAK-LAPiTGITAYSINPGITVTPLT 178
Cdd:PRK07825 164 ARLeLRG-TGVHVSVVLPSFVNTELI 188
PRK12826 PRK12826
SDR family oxidoreductase;
1-176 1.10e-13

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 68.02  E-value: 1.10e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   1 AALGGVGLATSKEIVKRGPKNFVV-LDRIENPKALAELKALNPKVTVsfYLYDVTVP--VTETVKLLTTIFGKLktiDLL 77
Cdd:PRK12826  13 GAARGIGRAIAVRLAADGAEVIVVdICGDDAAATAELVEAAGGKARA--RQVDVRDRaaLKAAVAAGVEDFGRL---DIL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  78 INGAGI--------LDDHQIERTIAINFTGLVNTTTAIMQfWDKRKGGpgGVIANICSVTGF-----NAIHqvpvYSASK 144
Cdd:PRK12826  88 VANAGIfpltpfaeMDDEQWERVIDVNLTGTFLLTQAALP-ALIRAGG--GRIVLTSSVAGPrvgypGLAH----YAASK 160

                        170       180       190
                 ....*....|....*....|....*....|...
gi 699964346 145 AAVVSFTSSLAK-LAPiTGITAYSINPGITVTP 176
Cdd:PRK12826 161 AGLVGFTRALALeLAA-RNITVNSVHPGGVDTP 192
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
 4-178 1.13e-13

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: 68.13  E-value: 1.13e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   4 GGVGLATSKEIVKRGpKNFVVLDRIeNPKALAELKALNPK--VTVSFYLYDVTVP--VTETVKLLTTIFGKlktIDLLIN 79
Cdd:cd05352   18 RGIGLAIARALAEAG-ADVAIIYNS-APRAEEKAEELAKKygVKTKAYKCDVSSQesVEKTFKQIQKDFGK---IDILIA 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  80 GAGI------LDD--HQIERTIAINFTGLVNTTTAIMQFWdkRKGGPGGVIAnICSVTGFNA---IHQVPvYSASKAAVV 148
Cdd:cd05352   93 NAGItvhkpaLDYtyEQWNKVIDVNLNGVFNCAQAAAKIF--KKQGKGSLII-TASMSGTIVnrpQPQAA-YNASKAAVI 168

                        170       180       190
                 ....*....|....*....|....*....|
gi 699964346 149 SFTSSLAKLAPITGITAYSINPGITVTPLT 178
Cdd:cd05352  169 HLAKSLAVEWAKYFIRVNSISPGYIDTDLT 198
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
 2-178 1.24e-13

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: 67.95  E-value: 1.24e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   2 ALGGVGLATSKEIVKRGPKNFVVLDRIENPKALA-ELKALNPKVTVsfYLYDVT--VPVTETVKLLTTIFGKLktiDLLI 78
Cdd:cd08934   11 ASSGIGEATARALAAEGAAVAIAARRVDRLEALAdELEAEGGKALV--LELDVTdeQQVDAAVERTVEALGRL---DILV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  79 NGAGIL--------DDHQIERTIAINFTGLVNTTTAIMQFWDKRKGGPggvIANICSVTGFNAIHQVPVYSASKAAVVSF 150
Cdd:cd08934   86 NNAGIMllgpvedaDTTDWTRMIDTNLLGLMYTTHAALPHHLLRNKGT---IVNISSVAGRVAVRNSAVYNATKFGVNAF 162

                        170       180
                 ....*....|....*....|....*...
gi 699964346 151 TSSLAKLAPITGITAYSINPGITVTPLT 178
Cdd:cd08934  163 SEGLRQEVTERGVRVVVIEPGTVDTELR 190
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
 2-178 1.55e-13

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: 67.39  E-value: 1.55e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   2 ALGGVGLATSKEIVKRGpknFVVLDRIENPKALAELKALNPKVTVSFYlyDVTVPVTE--TVKLLTTIFGKlktIDLLIN 79
Cdd:cd08932    8 ASRGIGIEIARALARDG---YRVSLGLRNPEDLAALSASGGDVEAVPY--DARDPEDAraLVDALRDRFGR---IDVLVH 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  80 GAGILD--------DHQIERTIAINFTGLVNTTTAIMQFWdkRKGGPGGVIaNICSVTGFNAIHQVPVYSASKAAVVSFT 151
Cdd:cd08932   80 NAGIGRpttlregsDAELEAHFSINVIAPAELTRALLPAL--REAGSGRVV-FLNSLSGKRVLAGNAGYSASKFALRALA 156

                        170       180
                 ....*....|....*....|....*..
gi 699964346 152 SSLAKLAPITGITAYSINPGITVTPLT 178
Cdd:cd08932  157 HALRQEGWDHGVRVSAVCPGFVDTPMA 183
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
 74-201 2.04e-13

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: 67.49  E-value: 2.04e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  74 IDLLINGAGIL--------DDHQIERTIAINFTGLVNTTTAIMQ-FWDKRkggpGGVIANICSvtgfNAIHQ----VPVY 140
Cdd:cd05331   69 IDALVNCAGVLrpgatdplSTEDWEQTFAVNVTGVFNLLQAVAPhMKDRR----TGAIVTVAS----NAAHVprisMAAY 140

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 699964346 141 SASKAAVVSFTSSLA-KLAPiTGITAYSINPGITVTPLthQFNSWLDvEPRVAELLNEHPTQ 201
Cdd:cd05331  141 GASKAALASLSKCLGlELAP-YGVRCNVVSPGSTDTAM--QRTLWHD-EDGAAQVIAGVPEQ 198
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
 2-179 3.01e-13

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: 66.66  E-value: 3.01e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   2 ALGGVGLATSKEIVKRGPKNFVVLDRieNPKALAELKALNPKVTVSFYLyDVTVPvtETVKLLTTifgKLKTIDLLINGA 81
Cdd:cd05354   11 ANRGIGKAFVESLLAHGAKKVYAAVR--DPGSAAHLVAKYGDKVVPLRL-DVTDP--ESIKAAAA---QAKDVDVVINNA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  82 GIL---------DDHQIERTIAINFTGLVNTTTAimqFWDKRKGGPGGVIANICSVTGFNAIHQVPVYSASKAAVVSFTS 152
Cdd:cd05354   83 GVLkpatlleegALEALKQEMDVNVFGLLRLAQA---FAPVLKANGGGAIVNLNSVASLKNFPAMGTYSASKSAAYSLTQ 159

                        170       180
                 ....*....|....*....|....*...
gi 699964346 153 SL-AKLAPiTGITAYSINPGITVTPLTH 179
Cdd:cd05354  160 GLrAELAA-QGTLVLSVHPGPIDTRMAA 186
PRK08267 PRK08267
SDR family oxidoreductase;
5-178 4.01e-13

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 66.89  E-value: 4.01e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   5 GVGLATSKEIVKRGpkNFV-VLDRieNPKALAELKA-LNPKVTVSFYLyDVTVP--VTETVKLLTTIFGKlkTIDLLING 80
Cdd:PRK08267  12 GIGRATALLFAAEG--WRVgAYDI--NEAGLAALAAeLGAGNAWTGAL-DVTDRaaWDAALADFAAATGG--RLDVLFNN 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  81 AGIL--------DDHQIERTIAINFTGLVNTTTAIMQFWdkrKGGPGGVIANICSVTGFNAIHQVPVYSASKAAVVSFTS 152
Cdd:PRK08267  85 AGILrggpfediPLEAHDRVIDINVKGVLNGAHAALPYL---KATPGARVINTSSASAIYGQPGLAVYSATKFAVRGLTE 161

                        170       180       190
                 ....*....|....*....|....*....|
gi 699964346 153 SL----AKLapitGITAYSINPGITVTPLT 178
Cdd:PRK08267 162 ALdlewRRH----GIRVADVMPLFVDTAML 187
PRK07454 PRK07454
SDR family oxidoreductase;
5-177 9.66e-13

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 65.37  E-value: 9.66e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   5 GVGLATSKEIVKRGpKNFVVLDRieNPKALAELKA--LNPKVTVSFYLYDVTVPvTETVKLLTTIFGKLKTIDLLINGAG 82
Cdd:PRK07454  17 GIGKATALAFAKAG-WDLALVAR--SQDALEALAAelRSTGVKAAAYSIDLSNP-EAIAPGIAELLEQFGCPDVLINNAG 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  83 I----------LDDHQieRTIAINFTGLVNTTTAIMQFWDKRKGGpggVIANICSVTGFNAIHQVPVYSASKAAVVSFTS 152
Cdd:PRK07454  93 MaytgpllempLSDWQ--WVIQLNLTSVFQCCSAVLPGMRARGGG---LIINVSSIAARNAFPQWGAYCVSKAALAAFTK 167

                        170       180
                 ....*....|....*....|....*
gi 699964346 153 SLAKLAPITGITAYSINPGITVTPL 177
Cdd:PRK07454 168 CLAEEERSHGIRVCTITLGAVNTPL 192
PRK06484 PRK06484
short chain dehydrogenase; Validated
 2-177 1.19e-12

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 66.80  E-value: 1.19e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   2 ALGGVGLATSKEIVKRGPKnFVVLDRiENPKALAELKALNPKVTVsfYLYDVT--VPVTETVKLLTTIFGKlktIDLLIN 79
Cdd:PRK06484  13 AAGGIGRAACQRFARAGDQ-VVVADR-NVERARERADSLGPDHHA--LAMDVSdeAQIREGFEQLHREFGR---IDVLVN 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  80 GAGILDD----------HQIERTIAINFTG---LVNTTTAIMQfwdkrKGGPGGVIANICSVTGFNAIHQVPVYSASKAA 146
Cdd:PRK06484  86 NAGVTDPtmtatldttlEEFARLQAINLTGaylVAREALRLMI-----EQGHGAAIVNVASGAGLVALPKRTAYSASKAA 160

                        170       180       190
                 ....*....|....*....|....*....|..
gi 699964346 147 VVSFTSSLA-KLAPiTGITAYSINPGITVTPL 177
Cdd:PRK06484 161 VISLTRSLAcEWAA-KGIRVNAVLPGYVRTQM 191
PRK06841 PRK06841
short chain dehydrogenase; Provisional
 5-180 1.35e-12

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 65.06  E-value: 1.35e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   5 GVGLATSKEIVKRGPKnFVVLDRIENPKALAElkALNPKVTVSFYLyDVTVP--VTETVKLLTTIFGKlktIDLLINGAG 82
Cdd:PRK06841  26 GIGHAIAELFAAKGAR-VALLDRSEDVAEVAA--QLLGGNAKGLVC-DVSDSqsVEAAVAAVISAFGR---IDILVNSAG 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  83 I--------LDDHQIERTIAINFTGLVNTTTAIMQfwDKRKGGpGGVIANICSVTGFNAIHQVPVYSASKAAVVSFTSSL 154
Cdd:PRK06841  99 VallapaedVSEEDWDKTIDINLKGSFLMAQAVGR--HMIAAG-GGKIVNLASQAGVVALERHVAYCASKAGVVGMTKVL 175

                        170       180
                 ....*....|....*....|....*..
gi 699964346 155 A-KLAPiTGITAYSINPGITVTPLTHQ 180
Cdd:PRK06841 176 AlEWGP-YGITVNAISPTVVLTELGKK 201
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
 2-171 1.49e-12

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: 65.05  E-value: 1.49e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   2 ALGGVGLATSKEIVKRGpKNFVVLDR-IENPKALAELKALNPKVTVSFYLYDVTVPvtETVK-LLTTIFGKLKTIDLLIN 79
Cdd:cd08930   10 AAGLIGKAFCKALLSAG-ARLILADInAPALEQLKEELTNLYKNRVIALELDITSK--ESIKeLIESYLEKFGRIDILIN 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  80 GAGI-----------LDDHQIERTIAINFTGLVNTTTAIMQFWDKRKGGpggVIANICSVTGFNA----IHQVP------ 138
Cdd:cd08930   87 NAYPspkvwgsrfeeFPYEQWNEVLNVNLGGAFLCSQAFIKLFKKQGKG---SIINIASIYGVIApdfrIYENTqmyspv 163

                        170       180       190
                 ....*....|....*....|....*....|...
gi 699964346 139 VYSASKAAVVSFTSSLAKLAPITGITAYSINPG 171
Cdd:cd08930  164 EYSVIKAGIIHLTKYLAKYYADTGIRVNAISPG 196
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
 2-177 2.45e-12

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: 64.40  E-value: 2.45e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   2 ALGGVGLATSKEIVKRGPKnfVVLDRIENPKALAELKALNPKvTVSFYLYDVTVP--VTETVKLLTTIFGKLktiDLLIN 79
Cdd:cd05326   12 GASGIGEATARLFAKHGAR--VVIADIDDDAGQAVAAELGDP-DISFVHCDVTVEadVRAAVDTAVARFGRL---DIMFN 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  80 GAGIL----------DDHQIERTIAINFTGLVNTTTAIMQFWDKRKGGPggvIANICSVTGFNAIHQVPVYSASKAAVVS 149
Cdd:cd05326   86 NAGVLgapcysiletSLEEFERVLDVNVYGAFLGTKHAARVMIPAKKGS---IVSVASVAGVVGGLGPHAYTASKHAVLG 162

                        170       180
                 ....*....|....*....|....*....
gi 699964346 150 FTSSLA-KLAPiTGITAYSINPGITVTPL 177
Cdd:cd05326  163 LTRSAAtELGE-HGIRVNCVSPYGVATPL 190
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
5-214 2.50e-12

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 64.36  E-value: 2.50e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   5 GVGLATSKEIVKRGPKNFVVLDRIENPKALAEL------KALNPKVTVSfYLYDVTVPVTETVKllttIFGKLktiDLLI 78
Cdd:PRK08643  13 GIGFAIAKRLVEDGFKVAIVDYNEETAQAAADKlskdggKAIAVKADVS-DRDQVFAAVRQVVD----TFGDL---NVVV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  79 NGAGI-----LDD---HQIERTIAINFTGLV-NTTTAIMQFwdkRKGGPGGVIANICSVTGFNAIHQVPVYSASKAAVVS 149
Cdd:PRK08643  85 NNAGVapttpIETiteEQFDKVYNINVGGVIwGIQAAQEAF---KKLGHGGKIINATSQAGVVGNPELAVYSSTKFAVRG 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 699964346 150 FTSSLAK-LAPItGITAYSINPGITVTPLthqfnsWLDVEPRVAELLNEHPTQTTEEcglnFAKAI 214
Cdd:PRK08643 162 LTQTAARdLASE-GITVNAYAPGIVKTPM------MFDIAHQVGENAGKPDEWGMEQ----FAKDI 216
PRK06180 PRK06180
short chain dehydrogenase; Provisional
 5-171 2.57e-12

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 64.55  E-value: 2.57e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   5 GVGLATSKEIVKRGPKnfvVLDRIENPKALAELKALNPKVTVSFYLyDVTVP--VTETVKLLTTIFGKlktIDLLINGAG 82
Cdd:PRK06180  15 GFGRALAQAALAAGHR---VVGTVRSEAARADFEALHPDRALARLL-DVTDFdaIDAVVADAEATFGP---IDVLVNNAG 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  83 I--------LDDHQIERTIAINFTGLVNTTTAIMQFWDKRKGGPggvIANICSVTGFNAIHQVPVYSASKAAVVSFTSSL 154
Cdd:PRK06180  88 YghegaieeSPLAEMRRQFEVNVFGAVAMTKAVLPGMRARRRGH---IVNITSMGGLITMPGIGYYCGSKFALEGISESL 164

                        170
                 ....*....|....*...
gi 699964346 155 AK-LAPItGITAYSINPG 171
Cdd:PRK06180 165 AKeVAPF-GIHVTAVEPG 181
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
 4-175 3.76e-12

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 64.15  E-value: 3.76e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   4 GGV-GLATSKEIVKRGPKnFVVLDR-IENPKALA-ELKAlnPKVTVSFYLYDVTvPVTETVKLLTTIFGKLKTIDLLING 80
Cdd:PRK08277  19 GGVlGGAMAKELARAGAK-VAILDRnQEKAEAVVaEIKA--AGGEALAVKADVL-DKESLEQARQQILEDFGPCDILING 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  81 AG------ILDDHQ-----------------IERTIAINFTGLVNTTtaiMQFWDKRKGGPGGVIANICSVTGFNAIHQV 137
Cdd:PRK08277  95 AGgnhpkaTTDNEFhelieptktffdldeegFEFVFDLNLLGTLLPT---QVFAKDMVGRKGGNIINISSMNAFTPLTKV 171

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 699964346 138 PVYSASKAAVVSFTSSLAKLAPITGITAYSINPGITVT 175
Cdd:PRK08277 172 PAYSAAKAAISNFTQWLAVHFAKVGIRVNAIAPGFFLT 209
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 5-155 5.55e-12

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 63.17  E-value: 5.55e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   5 GVGLATSKEIVKRGpKNFVVLDRIE-NPKALA-ELKALnpKVTVSFYLYDVTVpVTETVKLLTTIFGKLKTIDLLINGAG 82
Cdd:PRK07666  18 GIGRAVAIALAKEG-VNVGLLARTEeNLKAVAeEVEAY--GVKVVIATADVSD-YEEVTAAIEQLKNELGSIDILINNAG 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  83 I--------LDDHQIERTIAINFTGLVNTTTAIMQFWDKRKGGPggvIANICSVTGFNAIHQVPVYSASKAAVVSFTSSL 154
Cdd:PRK07666  94 IskfgkfleLDPAEWEKIIQVNLMGVYYATRAVLPSMIERQSGD---IINISSTAGQKGAAVTSAYSASKFGVLGLTESL 170


                 .
gi 699964346 155 A 155
Cdd:PRK07666 171 M 171
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
 5-195 6.00e-12

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: 63.08  E-value: 6.00e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   5 GVGLATSKEIVKRGpkNFVVLDRIENPKALAELKALNPKVTVSFYLY-DVTVPVTETVKLLTTIFGKLKtIDLLINGAGI 83
Cdd:cd05325    9 GIGLELVRQLLARG--NNTVIATCRDPSAATELAALGASHSRLHILElDVTDEIAESAEAVAERLGDAG-LDVLINNAGI 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  84 L---------DDHQIERTIAINFTGLVNTTTAimqFWDKRKGGPGGVIANICSVTG---FNAIHQVPVYSASKAAVVSFT 151
Cdd:cd05325   86 LhsygpasevDSEDLLEVFQVNVLGPLLLTQA---FLPLLLKGARAKIINISSRVGsigDNTSGGWYSYRASKAALNMLT 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 699964346 152 SSLAKLAPITGITAYSINPGITVTPLT---HQFNSWLDVEPRVAELL 195
Cdd:cd05325  163 KSLAVELKRDGITVVSLHPGWVRTDMGgpfAKNKGPITPEESVAGLL 209
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
2-176 9.67e-12

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 62.74  E-value: 9.67e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   2 ALGGVGLATSKEIVKRGPKnfVVLDRIENPKALAELKALNPKVtvsfylYDVTVPVTET------VKLLTTIFGKlktID 75
Cdd:PRK07067  14 AASGIGEAVAERYLAEGAR--VVIADIKPARARLAALEIGPAA------IAVSLDVTRQdsidriVAAAVERFGG---ID 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  76 LLINGAGILDDHQI--------ERTIAINFTGLVNTTTAIMQFWDKRkgGPGGVIANICSVTGFNAIHQVPVYSASKAAV 147
Cdd:PRK07067  83 ILFNNAALFDMAPIldisrdsyDRLFAVNVKGLFFLMQAVARHMVEQ--GRGGKIINMASQAGRRGEALVSHYCATKAAV 160

                        170       180       190
                 ....*....|....*....|....*....|
gi 699964346 148 VSFTSSlAKLAPIT-GITAYSINPGITVTP 176
Cdd:PRK07067 161 ISYTQS-AALALIRhGINVNAIAPGVVDTP 189
PRK07831 PRK07831
SDR family oxidoreductase;
1-197 1.23e-11

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 62.74  E-value: 1.23e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   1 AALGGVGLATSKEIVKRGPKnFVVLDRIEN--PKALAELKALNPKVTVSFYLYDVTVpvTETVK-LLTTIFGKLKTIDLL 77
Cdd:PRK07831  25 AAGTGIGSATARRALEEGAR-VVISDIHERrlGETADELAAELGLGRVEAVVCDVTS--EAQVDaLIDAAVERLGRLDVL 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  78 INGAGI--------LDDHQIERTIAINFTGLVNTTTAIMQFWDKRkgGPGGVIANICSVTGFNAIHQVPVYSASKAAVVS 149
Cdd:PRK07831 102 VNNAGLggqtpvvdMTDDEWSRVLDVTLTGTFRATRAALRYMRAR--GHGGVIVNNASVLGWRAQHGQAHYAAAKAGVMA 179

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 699964346 150 FTSSLAKLAPITGITAYSINPGITVTPLTHQFNSwldveprvAELLNE 197
Cdd:PRK07831 180 LTRCSALEAAEYGVRINAVAPSIAMHPFLAKVTS--------AELLDE 219
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
 5-172 1.27e-11

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 62.72  E-value: 1.27e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   5 GVGLATSKEIVKRGpKNFVVLDRIENpkalaELKALNpkvtVSFYLYDVTVP--VTETVKLLTTIFGKlktIDLLINGAG 82
Cdd:PRK06171  20 GIGLAIVKELLANG-ANVVNADIHGG-----DGQHEN----YQFVPTDVSSAeeVNHTVAEIIEKFGR---IDGLVNNAG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  83 I-----------------LDDHQIERTIAINFTGLVNTTTAIMQFWDKRKGGpggVIANICSVTGFNAIHQVPVYSASKA 145
Cdd:PRK06171  87 IniprllvdekdpagkyeLNEAAFDKMFNINQKGVFLMSQAVARQMVKQHDG---VIVNMSSEAGLEGSEGQSCYAATKA 163

                        170       180
                 ....*....|....*....|....*..
gi 699964346 146 AVVSFTSSLAKLAPITGITAYSINPGI 172
Cdd:PRK06171 164 ALNSFTRSWAKELGKHNIRVVGVAPGI 190
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 4-182 1.29e-11

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 62.29  E-value: 1.29e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   4 GGVGLATSKEIVKRGPKnFVVLDRIEN--PKALAELKALNPKVTvsFYLYDVT--VPVTETVKLLTTIFGKlktIDLLIN 79
Cdd:PRK08217  15 QGLGRAMAEYLAQKGAK-LALIDLNQEklEEAVAECGALGTEVR--GYAANVTdeEDVEATFAQIAEDFGQ---LNGLIN 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  80 GAGILDD-----------------HQIERTIAINFTGLVNTT---TAIMQfwdkrKGGPGGVIANICSVTGFNAIHQVPv 139
Cdd:PRK08217  89 NAGILRDgllvkakdgkvtskmslEQFQSVIDVNLTGVFLCGreaAAKMI-----ESGSKGVIINISSIARAGNMGQTN- 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 699964346 140 YSASKAAVVSFTSSLAKLAPITGITAYSINPGITVTPLTHQFN 182
Cdd:PRK08217 163 YSASKAGVAAMTVTWAKELARYGIRVAAIAPGVIETEMTAAMK 205
PRK06484 PRK06484
short chain dehydrogenase; Validated
 5-176 1.38e-11

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 63.33  E-value: 1.38e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   5 GVGLATSKEIVKRGPKnFVVLDR-IENPKALAELKAlNPKVTVSFylyDVTVpVTETVKLLTTIFGKLKTIDLLINGAGI 83
Cdd:PRK06484 280 GIGRAVADRFAAAGDR-LLIIDRdAEGAKKLAEALG-DEHLSVQA---DITD-EAAVESAFAQIQARWGRLDVLVNNAGI 353

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  84 LDD---------HQIERTIAINFTGLVNTTTAIMqfwdkRKGGPGGVIANICSVTGFNAIHQVPVYSASKAAVVSFTSSL 154
Cdd:PRK06484 354 AEVfkpsleqsaEDFTRVYDVNLSGAFACARAAA-----RLMSQGGVIVNLGSIASLLALPPRNAYCASKAAVTMLSRSL 428

                        170       180
                 ....*....|....*....|...
gi 699964346 155 A-KLAPItGITAYSINPGITVTP 176
Cdd:PRK06484 429 AcEWAPA-GIRVNTVAPGYIETP 450
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
 2-178 1.52e-11

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: 61.85  E-value: 1.52e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   2 ALGGVGLATSKEIVKRGPKNFVVLDRIENPKALAELKALNPKVTVSFYLYDVTvpvtetvkLLTTIFGKLKT------ID 75
Cdd:cd05356    9 ATDGIGKAYAEELAKRGFNVILISRTQEKLDAVAKEIEEKYGVETKTIAADFS--------AGDDIYERIEKelegldIG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  76 LLINGAGI----------LDDHQIERTIAINFTGLVNTTTAIMQFWDKRKGGpggVIANICSVTGFNAIHQVPVYSASKA 145
Cdd:cd05356   81 ILVNNVGIshsipeyfleTPEDELQDIINVNVMATLKMTRLILPGMVKRKKG---AIVNISSFAGLIPTPLLATYSASKA 157

                        170       180       190
                 ....*....|....*....|....*....|...
gi 699964346 146 AVVSFTSSLAKLAPITGITAYSINPGITVTPLT 178
Cdd:cd05356  158 FLDFFSRALYEEYKSQGIDVQSLLPYLVATKMS 190
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
 68-177 2.56e-11

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: 61.92  E-value: 2.56e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  68 FGKLktiDLLINGAGI---------LDDHQIERTIAINFTGLVNTTTAIMQFWDkrkggPGGVIANICSVTGFNAIHQVP 138
Cdd:cd05355  103 FGKL---DILVNNAAYqhpqesiedITTEQLEKTFRTNIFSMFYLTKAALPHLK-----KGSSIINTTSVTAYKGSPHLL 174

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 699964346 139 VYSASKAAVVSFTSSLAKLAPITGITAYSINPGITVTPL 177
Cdd:cd05355  175 DYAATKGAIVAFTRGLSLQLAEKGIRVNAVAPGPIWTPL 213
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
 5-176 2.90e-11

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: 61.15  E-value: 2.90e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   5 GVGLATSKEIVKRG-PKNFVVLDRIENPkaLAELKA-LNPKVTVSFYLYDVTVP--VTETVKLLTTIFGKLktiDLLING 80
Cdd:cd05367   10 GIGRALAEELLKRGsPSVVVLLARSEEP--LQELKEeLRPGLRVTTVKADLSDAagVEQLLEAIRKLDGER---DLLINN 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  81 AGIL---------DDHQIERTIAINFTGLVNTTTAIMQfwDKRKGGPGGVIANICSVTGFNAIHQVPVYSASKAAVVSFT 151
Cdd:cd05367   85 AGSLgpvskiefiDLDELQKYFDLNLTSPVCLTSTLLR--AFKKRGLKKTVVNVSSGAAVNPFKGWGLYCSSKAARDMFF 162

                        170       180
                 ....*....|....*....|....*
gi 699964346 152 SSLAKLAPitGITAYSINPGITVTP 176
Cdd:cd05367  163 RVLAAEEP--DVRVLSYAPGVVDTD 185
PRK06701 PRK06701
short chain dehydrogenase; Provisional
 57-177 2.92e-11

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 61.59  E-value: 2.92e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  57 VTETVKLlttiFGKLktiDLLINGAGI---------LDDHQIERTIAINFTGLVNTTTAIMqfwDKRKggPGGVIANICS 127
Cdd:PRK06701 115 VEETVRE----LGRL---DILVNNAAFqypqqsledITAEQLDKTFKTNIYSYFHMTKAAL---PHLK--QGSAIINTGS 182

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 699964346 128 VTGFNAIHQVPVYSASKAAVVSFTSSLAK-LAPiTGITAYSINPGITVTPL 177
Cdd:PRK06701 183 ITGYEGNETLIDYSATKGAIHAFTRSLAQsLVQ-KGIRVNAVAPGPIWTPL 232
PRK07060 PRK07060
short chain dehydrogenase; Provisional
 67-199 4.03e-11

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 60.88  E-value: 4.03e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  67 IFGKLKTIDLLINGAGILD--------DHQIERTIAINFTGLVNTTTAIMQfwdKR-KGGPGGVIANICSVTGFNAIHQV 137
Cdd:PRK07060  71 ALAAAGAFDGLVNCAGIASlesaldmtAEGFDRVMAVNARGAALVARHVAR---AMiAAGRGGSIVNVSSQAALVGLPDH 147

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 699964346 138 PVYSASKAAVVSFTSSLAK-LAPiTGITAYSINPGITVTPLtHQFnSWLDVEPRvAELLNEHP 199
Cdd:PRK07060 148 LAYCASKAALDAITRVLCVeLGP-HGIRVNSVNPTVTLTPM-AAE-AWSDPQKS-GPMLAAIP 206
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
 2-180 4.08e-11

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: 60.75  E-value: 4.08e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   2 ALGGVGLATSKEIVKRGPKnfVVL----DRIENPKALAELKALNPKVTVsfYLYDVTVPvTETVKL---LTTIFGKLkti 74
Cdd:cd05362   11 ASRGIGRAIAKRLARDGAS--VVVnyasSKAAAEEVVAEIEAAGGKAIA--VQADVSDP-SQVARLfdaAEKAFGGV--- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  75 DLLINGAGIL--------DDHQIERTIAINFTGlvntttaimQFWDKRKG----GPGGVIANICSVTGFNAIHQVPVYSA 142
Cdd:cd05362   83 DILVNNAGVMlkkpiaetSEEEFDRMFTVNTKG---------AFFVLQEAakrlRDGGRIINISSSLTAAYTPNYGAYAG 153

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 699964346 143 SKAAVVSFTSSLAKLAPITGITAYSINPGITVTPLTHQ 180
Cdd:cd05362  154 SKAAVEAFTRVLAKELGGRGITVNAVAPGPVDTDMFYA 191
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
2-180 4.35e-11

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 60.97  E-value: 4.35e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   2 ALGGVGLATSKEIVKRGPKnFVVLDRIENPKALAElKALNPKVTVSFYLYDVTVP--VTETVKLLTTIFGKlktIDLLIN 79
Cdd:PRK08226  14 ALQGIGEGIARVFARHGAN-LILLDISPEIEKLAD-ELCGRGHRCTAVVADVRDPasVAAAIKRAKEKEGR---IDILVN 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  80 GAGI--------LDDHQIERTIAINFTGLVNTTTAIMQFWDKRKGGPggvIANICSVTG-FNAIHQVPVYSASKAAVVSF 150
Cdd:PRK08226  89 NAGVcrlgsfldMSDEDRDFHIDINIKGVWNVTKAVLPEMIARKDGR---IVMMSSVTGdMVADPGETAYALTKAAIVGL 165

                        170       180       190
                 ....*....|....*....|....*....|
gi 699964346 151 TSSLAKLAPITGITAYSINPGITVTPLTHQ 180
Cdd:PRK08226 166 TKSLAVEYAQSGIRVNAICPGYVRTPMAES 195
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
 67-186 4.91e-11

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 60.67  E-value: 4.91e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  67 IFGKLKTIDLLINGAGIL--------DDHQIERTIAINFTGLVNTTTAIM-QFWDKRkggpGGVIANICSvtgfNAIHqV 137
Cdd:PRK08220  70 LLAETGPLDVLVNAAGILrmgatdslSDEDWQQTFAVNAGGAFNLFRAVMpQFRRQR----SGAIVTVGS----NAAH-V 140

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 699964346 138 P-----VYSASKAAVVSFTSSLA-KLAPiTGITAYSINPGITVTPLTHQFnsWLD 186
Cdd:PRK08220 141 PrigmaAYGASKAALTSLAKCVGlELAP-YGVRCNVVSPGSTDTDMQRTL--WVD 192
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
4-170 5.28e-11

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 61.79  E-value: 5.28e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   4 GGVGLATSKEIVKRGpKNFVVLDRIENP--KALAELKALNPKVTVSFylyDVTVP--VTETVKLLTTIFGKLktiDLLIN 79
Cdd:PRK08324 432 GGIGKATAKRLAAEG-ACVVLADLDEEAaeAAAAELGGPDRALGVAC---DVTDEaaVQAAFEEAALAFGGV---DIVVS 504

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  80 GAGI--------LDDHQIERTIAINFTGLVNTTTAIMQFWdkRKGGPGGVIANICSVTGFNAIHQVPVYSASKAAVVSFT 151
Cdd:PRK08324 505 NAGIaisgpieeTSDEDWRRSFDVNATGHFLVAREAVRIM--KAQGLGGSIVFIASKNAVNPGPNFGAYGAAKAAELHLV 582

                        170       180
                 ....*....|....*....|
gi 699964346 152 SSLAK-LAPItGITAYSINP 170
Cdd:PRK08324 583 RQLALeLGPD-GIRVNGVNP 601
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
 2-191 7.10e-11

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: 60.09  E-value: 7.10e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   2 ALGGVGLATSKEIVKRGPKnFVVLDRieNPKALAELKAL--NPKVTVSFYLYDVTVP--VTETVKLLTTIFGKlktIDLL 77
Cdd:cd05360    8 ASSGIGRATALAFAERGAK-VVLAAR--SAEALHELAREvrELGGEAIAVVADVADAaqVERAADTAVERFGR---IDTW 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  78 INGAGI--------LDDHQIERTIAINFTGLVNTTTAIMQFWDKRKGGpggVIANICSVTGFNAIHQVPVYSASKAAVVS 149
Cdd:cd05360   82 VNNAGVavfgrfedVTPEEFRRVFDVNYLGHVYGTLAALPHLRRRGGG---ALINVGSLLGYRSAPLQAAYSASKHAVRG 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 699964346 150 FTSSL-AKLA----PITgITaySINPGITVTPLTHQFNSWLDVEPRV 191
Cdd:cd05360  159 FTESLrAELAhdgaPIS-VT--LVQPTAMNTPFFGHARSYMGKKPKP 202
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
 2-177 8.59e-11

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 60.29  E-value: 8.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   2 ALGGVGLATSKEIVKRGpKNFVVLDRIENPKALAELKALNPKVTVSFYLYDVTVP--VTETVKLLTTIFGklkTIDLLIN 79
Cdd:PRK12429  12 AASGIGLEIALALAKEG-AKVVIADLNDEAAAAAAEALQKAGGKAIGVAMDVTDEeaINAGIDYAVETFG---GVDILVN 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  80 GAGI-----LDDHQIER---TIAINFTGLVNTTTAIMQFWDKRKGGpggVIANICSVTGFNAIHQVPVYSASKAAVVSFT 151
Cdd:PRK12429  88 NAGIqhvapIEDFPTEKwkkMIAIMLDGAFLTTKAALPIMKAQGGG---RIINMASVHGLVGSAGKAAYVSAKHGLIGLT 164

                        170       180
                 ....*....|....*....|....*.
gi 699964346 152 SSLAKLAPITGITAYSINPGITVTPL 177
Cdd:PRK12429 165 KVVALEGATHGVTVNAICPGYVDTPL 190
PRK12827 PRK12827
short chain dehydrogenase; Provisional
 2-177 9.11e-11

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 60.12  E-value: 9.11e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   2 ALGGVGLATSKEIVKRGpKNFVVLDRiENPKALAELKALNPKV-----TVSFYLYDVT--VPVTETVKLLTTIFGKLkti 74
Cdd:PRK12827  14 GSGGLGRAIAVRLAADG-ADVIVLDI-HPMRGRAEADAVAAGIeaaggKALGLAFDVRdfAATRAALDAGVEEFGRL--- 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  75 DLLINGAGILDD--------HQIERTIAINFTGLVNTTTAIMQFWDKRKGGpgGVIANICSVTGFNAIH-QVPvYSASKA 145
Cdd:PRK12827  89 DILVNNAGIATDaafaelsiEEWDDVIDVNLDGFFNVTQAALPPMIRARRG--GRIVNIASVAGVRGNRgQVN-YAASKA 165

                        170       180       190
                 ....*....|....*....|....*....|...
gi 699964346 146 AVVSFTSSLA-KLAPiTGITAYSINPGITVTPL 177
Cdd:PRK12827 166 GLIGLTKTLAnELAP-RGITVNAVAPGAINTPM 197
PRK12939 PRK12939
short chain dehydrogenase; Provisional
 74-178 9.61e-11

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 59.99  E-value: 9.61e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  74 IDLLINGAGI--------LDDHQIERTIAINFTGLVNTTTAIMQfwdKRKGGPGGVIANICSVTGFNAIHQVPVYSASKA 145
Cdd:PRK12939  85 LDGLVNNAGItnsksateLDIDTWDAVMNVNVRGTFLMLRAALP---HLRDSGRGRIVNLASDTALWGAPKLGAYVASKG 161

                         90       100       110
                 ....*....|....*....|....*....|...
gi 699964346 146 AVVSFTSSLAKLAPITGITAYSINPGITVTPLT 178
Cdd:PRK12939 162 AVIGMTRSLARELGGRGITVNAIAPGLTATEAT 194
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
 4-180 1.02e-10

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: 59.93  E-value: 1.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   4 GGVGLATSKEIVKRGPKnfVVL-----DRIEnpKALAELKALNPKVTVSFYLYDVTVPvtETVKLLTTIF-GKLKTIDLL 77
Cdd:cd05327   11 SGIGKETARELAKRGAH--VIIacrneEKGE--EAAAEIKKETGNAKVEVIQLDLSSL--ASVRQFAEEFlARFPRLDIL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  78 INGAGI------LDDHQIERTIAINFTGLVNTTT----AIMQFWDKRkggpggvIANICSVT--------------GFNA 133
Cdd:cd05327   85 INNAGImapprrLTKDGFELQFAVNYLGHFLLTNlllpVLKASAPSR-------IVNVSSIAhragpidfndldleNNKE 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 699964346 134 IHQVPVYSASKAAVVSFTSSLAKLAPITGITAYSINPGITVTPLTHQ 180
Cdd:cd05327  158 YSPYKAYGQSKLANILFTRELARRLEGTGVTVNALHPGVVRTELLRR 204
PRK08264 PRK08264
SDR family oxidoreductase;
2-179 1.06e-10

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 59.52  E-value: 1.06e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   2 ALGGVGLATSKEIVKRGPKNFVVLDRieNPKALAELkalNPKVtVSFYLyDVTVPvtETVKLLTTIfgkLKTIDLLINGA 81
Cdd:PRK08264  14 ANRGIGRAFVEQLLARGAAKVYAAAR--DPESVTDL---GPRV-VPLQL-DVTDP--ASVAAAAEA---ASDVTILVNNA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  82 GI------LDDHQIE---RTIAINFTGLVNTTTAimqFWDKRKGGPGGVIANICSVTGFNAIHQVPVYSASKAAVVSFTS 152
Cdd:PRK08264  82 GIfrtgslLLEGDEDalrAEMETNYFGPLAMARA---FAPVLAANGGGAIVNVLSVLSWVNFPNLGTYSASKAAAWSLTQ 158

                        170       180
                 ....*....|....*....|....*...
gi 699964346 153 SL-AKLAPiTGITAYSINPGITVTPLTH 179
Cdd:PRK08264 159 ALrAELAP-QGTRVLGVHPGPIDTDMAA 185
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
 5-199 1.35e-10

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: 59.70  E-value: 1.35e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   5 GVGLATSKEIVKRGPKnfVVLDRIENPKALAELKALNPKVTVSFYLY--DVTVPvTETVKLLTTIFGKLKTIDLLINGAG 82
Cdd:cd05358   14 GIGKAIAIRLATAGAN--VVVNYRSKEDAAEEVVEEIKAVGGKAIAVqaDVSKE-EDVVALFQSAIKEFGTLDILVNNAG 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  83 I----------LDDHQieRTIAINFTG-LVNTTTAIMQFWDKRKGGpggVIANICSVtgfnaiHQV---PV---YSASKA 145
Cdd:cd05358   91 LqgdasshemtLEDWN--KVIDVNLTGqFLCAREAIKRFRKSKIKG---KIINMSSV------HEKipwPGhvnYAASKG 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 699964346 146 AVVSFTSSLA-KLAPiTGITAYSINPGITVTPLThqfNSWLDVEPRVAELLNEHP 199
Cdd:cd05358  160 GVKMMTKTLAqEYAP-KGIRVNAIAPGAINTPIN---AEAWDDPEQRADLLSLIP 210
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
 2-180 1.47e-10

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: 59.47  E-value: 1.47e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   2 ALGGVGLATSKEIVKRGPKNFVVLDRIEnpKALAELKALNPK-VTVSFYLYDVTVPvTETVKLLTTIFGKLKTIDLLING 80
Cdd:cd08945   11 ATSGIGLAIARRLGKEGLRVFVCARGEE--GLATTVKELREAgVEADGRTCDVRSV-PEIEALVAAAVARYGPIDVLVNN 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  81 AG--------ILDDHQIERTIAINFTGLVNTTTAIMQFWDKRKGGPGGVIaNICSVTGFNAIHQVPVYSASKAAVVSFTS 152
Cdd:cd08945   88 AGrsgggataELADELWLDVVETNLTGVFRVTKEVLKAGGMLERGTGRII-NIASTGGKQGVVHAAPYSASKHGVVGFTK 166

                        170       180
                 ....*....|....*....|....*....
gi 699964346 153 SLA-KLAPiTGITAYSINPGITVTPLTHQ 180
Cdd:cd08945  167 ALGlELAR-TGITVNAVCPGFVETPMAAS 194
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
 62-178 2.35e-10

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: 58.96  E-value: 2.35e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  62 KLLTTIFGKLKTIDLLINGAGIL-----DDHQIE---RTIAINFTGLVNTTTAIMQFWDKRKGGpggvIANICSVTGFNA 133
Cdd:cd05364   72 RIISTTLAKFGRLDILVNNAGILakgggEDQDIEeydKVMNLNLRAVIYLTKLAVPHLIKTKGE----IVNVSSVAGGRS 147

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 699964346 134 IHQVPVYSASKAAVVSFTSSLA-KLAPiTGITAYSINPGITVTPLT 178
Cdd:cd05364  148 FPGVLYYCISKAALDQFTRCTAlELAP-KGVRVNSVSPGVIVTGFH 192
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
 5-177 4.34e-10

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 58.09  E-value: 4.34e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   5 GVGLATSKEIVKRGPKnfVVLDRIENPKA----LAELK-----ALNPKVTVSfYLYDVTVPVTETVklltTIFGKLktiD 75
Cdd:PRK12935  17 GIGKAITVALAQEGAK--VVINYNSSKEAaenlVNELGkeghdVYAVQADVS-KVEDANRLVEEAV----NHFGKV---D 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  76 LLINGAGILDDHQI--------ERTIAINFTGLVNTTTAIMQFWDKRKGGPggvIANICSVTGFNAIHQVPVYSASKAAV 147
Cdd:PRK12935  87 ILVNNAGITRDRTFkklnredwERVIDVNLSSVFNTTSAVLPYITEAEEGR---IISISSIIGQAGGFGQTNYSAAKAGM 163

                        170       180       190
                 ....*....|....*....|....*....|
gi 699964346 148 VSFTSSLAKLAPITGITAYSINPGITVTPL 177
Cdd:PRK12935 164 LGFTKSLALELAKTNVTVNAICPGFIDTEM 193
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
 1-181 6.75e-10

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: 57.67  E-value: 6.75e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   1 AALGGVGLATSKEIVKRGPKnfVVL-----DRIEnpKALAELKALNPKVTVSfyLYDVTVP--VTETVKLLTTIFGklkT 73
Cdd:cd05344    8 AASSGIGLAIARALAREGAR--VAIcarnrENLE--RAASELRAGGAGVLAV--VADLTDPedIDRLVEKAGDAFG---R 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  74 IDLLINGAG--------ILDDHQIERTIAINFTGLVNTTTAIMQFWDKRKGGpggVIANICSVTGFNAIHQVPVYSASKA 145
Cdd:cd05344   79 VDILVNNAGgpppgpfaELTDEDWLEAFDLKLLSVIRIVRAVLPGMKERGWG---RIVNISSLTVKEPEPNLVLSNVARA 155

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 699964346 146 AVVSFTSSLAK-LAPiTGITAYSINPGITVTPLTHQF 181
Cdd:cd05344  156 GLIGLVKTLSReLAP-DGVTVNSVLPGYIDTERVRRL 191
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
 1-176 7.45e-10

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: 57.09  E-value: 7.45e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   1 AALGGVGLATSKEIVKRGPKnfVVLDRIeNPKALAELKAlNPKVTVsfylydVTVPVTETvKLLTTIFGKLKTIDLLING 80
Cdd:cd05368    9 AAAQGIGRAIALAFAREGAN--VIATDI-NEEKLKELER-GPGITT------RVLDVTDK-EQVAALAKEEGRIDVLFNC 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  81 AG------ILD--DHQIERTIAINFTGLVNTTTAIMQFWDKRKGGPggvIANICSVTGfnAIHQVP---VYSASKAAVVS 149
Cdd:cd05368   78 AGfvhhgsILDceDDDWDFAMNLNVRSMYLMIKAVLPKMLARKDGS---IINMSSVAS--SIKGVPnrfVYSTTKAAVIG 152

                        170       180
                 ....*....|....*....|....*..
gi 699964346 150 FTSSLAKLAPITGITAYSINPGITVTP 176
Cdd:cd05368  153 LTKSVAADFAQQGIRCNAICPGTVDTP 179
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
 5-177 8.88e-10

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: 57.15  E-value: 8.88e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   5 GVGLATSKEIVKRGPKnFVVLDRIEN--PKALAELKALNPKVTVSFYLYDVT--VPVTETVKLLTTIFGKlktIDLLING 80
Cdd:cd05330   14 GLGLATAVRLAKEGAK-LSLVDLNEEglEAAKAALLEIAPDAEVLLIKADVSdeAQVEAYVDATVEQFGR---IDGFFNN 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  81 AGI---------LDDHQIERTIAINFTGLVNTTTAIMQFWDKRKGGpggVIANICSVTGFNAIHQVPVYSASKAAVVSFT 151
Cdd:cd05330   90 AGIegkqnltedFGADEFDKVVSINLRGVFYGLEKVLKVMREQGSG---MIVNTASVGGIRGVGNQSGYAAAKHGVVGLT 166

                        170       180
                 ....*....|....*....|....*.
gi 699964346 152 SSLAKLAPITGITAYSINPGITVTPL 177
Cdd:cd05330  167 RNSAVEYGQYGIRINAIAPGAILTPM 192
PRK06114 PRK06114
SDR family oxidoreductase;
69-202 1.33e-09

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 56.71  E-value: 1.33e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  69 GKLKTIDLLINGAGI--------LDDHQIERTIAINFTGLVNTTTAIMQFWDKRKGGPggvIANICSVTG------FNAI 134
Cdd:PRK06114  82 AELGALTLAVNAAGIananpaeeMEEEQWQTVMDINLTGVFLSCQAEARAMLENGGGS---IVNIASMSGiivnrgLLQA 158

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 699964346 135 HqvpvYSASKAAVVSFTSSLAKLAPITGITAYSINPGITVTPlthqfnswLDVEPRVAELLNEHPTQT 202
Cdd:PRK06114 159 H----YNASKAGVIHLSKSLAMEWVGRGIRVNSISPGYTATP--------MNTRPEMVHQTKLFEEQT 214
PRK07201 PRK07201
SDR family oxidoreductase;
5-214 1.84e-09

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 57.27  E-value: 1.84e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   5 GVGLATSKEIVKRGPKNFVVldrIENPKALAELKA--LNPKVTVSFYLYDVTVP--VTETVKLLTTIFGKlktIDLLING 80
Cdd:PRK07201 382 GIGRATAIKVAEAGATVFLV---ARNGEALDELVAeiRAKGGTAHAYTCDLTDSaaVDHTVKDILAEHGH---VDYLVNN 455

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  81 AG------ILDD----HQIERTIAINFTGLVNTTTAIMQFWDKRKGGPggvIANICSVtG-------FNAihqvpvYSAS 143
Cdd:PRK07201 456 AGrsirrsVENStdrfHDYERTMAVNYFGAVRLILGLLPHMRERRFGH---VVNVSSI-GvqtnaprFSA------YVAS 525

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 699964346 144 KAAVVSFTSSLAKLAPITGITAYSINPGITVTPLthqfnswldVEPrvAELLNEHPTQTTEECGLNFAKAI 214
Cdd:PRK07201 526 KAALDAFSDVAASETLSDGITFTTIHMPLVRTPM---------IAP--TKRYNNVPTISPEEAADMVVRAI 585
PRK07063 PRK07063
SDR family oxidoreductase;
5-199 2.32e-09

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 56.21  E-value: 2.32e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   5 GVGLATSKEIVKRGPKNFVV-LDRIENPKALAELKALNPKVTVSFYLYDVTVP--VTETVKLLTTIFGKlktIDLLINGA 81
Cdd:PRK07063  18 GIGAAIARAFAREGAAVALAdLDAALAERAAAAIARDVAGARVLAVPADVTDAasVAAAVAAAEEAFGP---LDVLVNNA 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  82 GI--------LDDHQIERTIAINFTGLVNTTTAIMQFWDKRKGGpggVIANICSVTGFNAI-HQVPvYSASKAAVVSFTS 152
Cdd:PRK07063  95 GInvfadplaMTDEDWRRCFAVDLDGAWNGCRAVLPGMVERGRG---SIVNIASTHAFKIIpGCFP-YPVAKHGLLGLTR 170

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 699964346 153 SLA-KLAPiTGITAYSINPGITVTPLTHQ-FNSWLDVEPRVAELLNEHP 199
Cdd:PRK07063 171 ALGiEYAA-RNVRVNAIAPGYIETQLTEDwWNAQPDPAAARAETLALQP 218
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
 5-176 2.43e-09

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: 56.09  E-value: 2.43e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   5 GVGLATSKEIVKRGPKNFVVLDRIENPKALAELkaLNPKVtvsfylYDVTVPVTETV---KLLTTIFGKLKTIDLLINGA 81
Cdd:cd05363   14 GIGRAFAQAYVREGARVAIADINLEAARATAAE--IGPAA------CAISLDVTDQAsidRCVAALVDRWGSIDILVNNA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  82 GILDDHQI--------ERTIAINFTGLVNTTTAIMQfwDKRKGGPGGVIANICSVTGFNAIHQVPVYSASKAAVVSFTSS 153
Cdd:cd05363   86 ALFDLAPIvditresyDRLFAINVSGTLFMMQAVAR--AMIAQGRGGKIINMASQAGRRGEALVGVYCATKAAVISLTQS 163

                        170       180
                 ....*....|....*....|....
gi 699964346 154 LA-KLAPiTGITAYSINPGITVTP 176
Cdd:cd05363  164 AGlNLIR-HGINVNAIAPGVVDGE 186
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
 70-177 2.62e-09

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 56.06  E-value: 2.62e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  70 KLKTIDLLINGAGILDDHQIE--------RTIAINFTGLVNTTTAIMQFWDKRKGGpgGVIANICSVTGFNAIHQVPVYS 141
Cdd:PRK13394  81 RFGSVDILVSNAGIQIVNPIEnysfadwkKMQAIHVDGAFLTTKAALKHMYKDDRG--GVVIYMGSVHSHEASPLKSAYV 158

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 699964346 142 ASKAAVVSFTSSLAKLAPITGITAYSINPGITVTPL 177
Cdd:PRK13394 159 TAKHGLLGLARVLAKEGAKHNVRSHVVCPGFVRTPL 194
PRK07024 PRK07024
SDR family oxidoreductase;
5-178 2.64e-09

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 55.71  E-value: 2.64e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   5 GVGLATSKEIVKRGPKNFVVLDRIEnpkALAELKALNPK-VTVSFYLYDVTVPvtETVKLLTTIF-GKLKTIDLLINGAG 82
Cdd:PRK07024  13 GIGQALAREYARQGATLGLVARRTD---ALQAFAARLPKaARVSVYAADVRDA--DALAAAAADFiAAHGLPDVVIANAG 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  83 IL---------DDHQIERTIAINFTGLVNTttaIMQFWDKRKGGPGGVIANICSVTGFNAIHQVPVYSASKAAVVSFTSS 153
Cdd:PRK07024  88 ISvgtlteereDLAVFREVMDTNYFGMVAT---FQPFIAPMRAARRGTLVGIASVAGVRGLPGAGAYSASKAAAIKYLES 164

                        170       180
                 ....*....|....*....|....*.
gi 699964346 154 L-AKLAPiTGITAYSINPGITVTPLT 178
Cdd:PRK07024 165 LrVELRP-AGVRVVTIAPGYIRTPMT 189
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
 63-181 2.85e-09

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: 55.86  E-value: 2.85e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  63 LLTTIFGKLKTIDLLINGAGI---------LDDHQIERTIAINFTGLVNTTTAIMQFWdkrKGGPGGVIANICSVTGFNA 133
Cdd:cd05345   69 MVEAALSKFGRLDILVNNAGIthrnkpmleVDEEEFDRVFAVNVKSIYLSAQALVPHM---EEQGGGVIINIASTAGLRP 145

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 699964346 134 IHQVPVYSASKAAVVSFTSSLA-KLAPiTGITAYSINPGITVTPLTHQF 181
Cdd:cd05345  146 RPGLTWYNASKGWVVTATKAMAvELAP-RNIRVNCLCPVAGETPLLSMF 193
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
3-177 3.82e-09

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 55.40  E-value: 3.82e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   3 LGGVGLATSKEIVKRGpknFVVL-----DRIENPKALAELKALNpkvtVSFYLYDVTVPVTETVKlltTIFGKLKT---- 73
Cdd:PRK12938  12 MGGIGTSICQRLHKDG---FKVVagcgpNSPRRVKWLEDQKALG----FDFIASEGNVGDWDSTK---AAFDKVKAevge 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  74 IDLLINGAGILDD---HQIERT-----IAINFTGLVNTTTAIMQFWDKRKGGPggvIANICSVTGFNAIHQVPVYSASKA 145
Cdd:PRK12938  82 IDVLVNNAGITRDvvfRKMTREdwtavIDTNLTSLFNVTKQVIDGMVERGWGR---IINISSVNGQKGQFGQTNYSTAKA 158

                        170       180       190
                 ....*....|....*....|....*....|..
gi 699964346 146 AVVSFTSSLAKLAPITGITAYSINPGITVTPL 177
Cdd:PRK12938 159 GIHGFTMSLAQEVATKGVTVNTVSPGYIGTDM 190
PRK07069 PRK07069
short chain dehydrogenase; Validated
 2-155 4.85e-09

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 55.10  E-value: 4.85e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   2 ALGGVGLATSKEIVKRGPKnfVVLDRIENPKALAELKA-LN----PKVTVSFYLyDVTVPVtETVKLLTTIFGKLKTIDL 76
Cdd:PRK07069   7 AAGGLGRAIARRMAEQGAK--VFLTDINDAAGLDAFAAeINaahgEGVAFAAVQ-DVTDEA-QWQALLAQAADAMGGLSV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  77 LINGAGILDDHQIE--------RTIAINFTGLVNTTTAIMQFWdkRKGGPGGVIaNICSVTGFNAIHQVPVYSASKAAVV 148
Cdd:PRK07069  83 LVNNAGVGSFGAIEqieldewrRVMAINVESIFLGCKHALPYL--RASQPASIV-NISSVAAFKAEPDYTAYNASKAAVA 159


                 ....*..
gi 699964346 149 SFTSSLA 155
Cdd:PRK07069 160 SLTKSIA 166
PRK06914 PRK06914
SDR family oxidoreductase;
2-171 6.61e-09

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 55.03  E-value: 6.61e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   2 ALGGVGLATSKEIVKRGpknFVVLDRIENPKA----LAELKALNPKVTVSFYLYDVTVpvTETVKLLTTIFGKLKTIDLL 77
Cdd:PRK06914  11 ASSGFGLLTTLELAKKG---YLVIATMRNPEKqenlLSQATQLNLQQNIKVQQLDVTD--QNSIHNFQLVLKEIGRIDLL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  78 INGA-----GILDDHQIE---RTIAINFTGLVNTTTAIMQFWDKRKGGPggvIANICSVTGFNAIHQVPVYSASKAAVVS 149
Cdd:PRK06914  86 VNNAgyangGFVEEIPVEeyrKQFETNVFGAISVTQAVLPYMRKQKSGK---IINISSISGRVGFPGLSPYVSSKYALEG 162

                        170       180
                 ....*....|....*....|...
gi 699964346 150 FTSSLA-KLAPItGITAYSINPG 171
Cdd:PRK06914 163 FSESLRlELKPF-GIDVALIEPG 184
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
66-199 8.50e-09

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 54.49  E-value: 8.50e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  66 TIFGKlktIDLLINGAGIlddhqIERTIAINFT-----GLVNTTTAIMQFWDKR------KGGPGGVIANICSVTGFNAI 134
Cdd:PRK08993  81 AEFGH---IDILVNNAGL-----IRREDAIEFSekdwdDVMNLNIKSVFFMSQAaakhfiAQGNGGKIINIASMLSFQGG 152

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 699964346 135 HQVPVYSASKAAVVSFTSSLAKLAPITGITAYSINPGITVTPLTHQFNSwldVEPRVAELLNEHP 199
Cdd:PRK08993 153 IRVPSYTASKSGVMGVTRLMANEWAKHNINVNAIAPGYMATNNTQQLRA---DEQRSAEILDRIP 214
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
 33-171 9.26e-09

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 54.18  E-value: 9.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  33 ALAELKALNpkVTVSFYLYDVTVPvtETVKLLT-TIFGKLKTIDLLINGAGI-----LDDHQIE---RTIAINFTGLVNT 103
Cdd:PRK08213  52 AAAHLEALG--IDALWIAADVADE--ADIERLAeETLERFGHVDILVNNAGAtwgapAEDHPVEawdKVMNLNVRGLFLL 127

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 699964346 104 TTAIMQFWDKRKGGpgGVIANICSVTGFNAIH----QVPVYSASKAAVVSFTSSLA-KLAPiTGITAYSINPG 171
Cdd:PRK08213 128 SQAVAKRSMIPRGY--GRIINVASVAGLGGNPpevmDTIAYNTSKGAVINFTRALAaEWGP-HGIRVNAIAPG 197
PRK06398 PRK06398
aldose dehydrogenase; Validated
 5-177 1.06e-08

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 54.07  E-value: 1.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   5 GVGLATSKEIVKRGPKnfVVLDRIENPKalaelkalnpKVTVSFYLYDVTVPvTETVKLLTTIFGKLKTIDLLINGAGI- 83
Cdd:PRK06398  17 GIGKAVVNRLKEEGSN--VINFDIKEPS----------YNDVDYFKVDVSNK-EQVIKGIDYVISKYGRIDILVNNAGIe 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  84 -------LDDHQIERTIAINFTGLVNTTTAIMQFWDKRKggpGGVIANICSVTGFNAIHQVPVYSASKAAVVSFTSSLA- 155
Cdd:PRK06398  84 sygaihaVEEDEWDRIINVNVNGIFLMSKYTIPYMLKQD---KGVIINIASVQSFAVTRNAAAYVTSKHAVLGLTRSIAv 160

                        170       180
                 ....*....|....*....|..
gi 699964346 156 KLAPItgITAYSINPGITVTPL 177
Cdd:PRK06398 161 DYAPT--IRCVAVCPGSIRTPL 180
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
5-199 1.34e-08

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 53.97  E-value: 1.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   5 GVGLATSKEIVKRGPKNFVVL--DRIENPKALAELKALnpkvTVSFYLYDVTVP--VTETVKLLTTIFGKlktIDLLING 80
Cdd:PRK06935  26 GLGQGYAVALAKAGADIIITThgTNWDETRRLIEKEGR----KVTFVQVDLTKPesAEKVVKEALEEFGK---IDILVNN 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  81 AGIL--------DDHQIERTIAINFTGLVNTTTAIMQFWDKRKGGPggvIANICSVTGFNAIHQVPVYSASKAAVVSFTS 152
Cdd:PRK06935  99 AGTIrraplleyKDEDWNAVMDINLNSVYHLSQAVAKVMAKQGSGK---IINIASMLSFQGGKFVPAYTASKHGVAGLTK 175

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 699964346 153 SLAKLAPITGITAYSINPGITVTPLTHQFNswlDVEPRVAELLNEHP 199
Cdd:PRK06935 176 AFANELAAYNIQVNAIAPGYIKTANTAPIR---ADKNRNDEILKRIP 219
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
 5-178 1.38e-08

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: 53.61  E-value: 1.38e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   5 GVGLATSKEIVKRGPKnfvVLDRIENPKALAE-LKALNPK-VTVSFYLYDVTVpVTETVKLLTTIF----GKLktiDLLI 78
Cdd:cd05329   17 GIGYAIVEELAGLGAE---VYTCARNQKELDEcLTEWREKgFKVEGSVCDVSS-RSERQELMDTVAshfgGKL---NILV 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  79 NGAGIlddhqIERTIAINFTglVNTTTAIMQ------------FWDKRKGGPGGVIANICSVTGFNAIHQVPVYSASKAA 146
Cdd:cd05329   90 NNAGT-----NIRKEAKDYT--EEDYSLIMStnfeaayhlsrlAHPLLKASGNGNIVFISSVAGVIAVPSGAPYGATKGA 162

                        170       180       190
                 ....*....|....*....|....*....|..
gi 699964346 147 VVSFTSSLAKLAPITGITAYSINPGITVTPLT 178
Cdd:cd05329  163 LNQLTRSLACEWAKDNIRVNAVAPWVIATPLV 194
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 5-178 1.45e-08

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 53.63  E-value: 1.45e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   5 GVGLATSKEIVKRGPKNFVVLDRIEN-PKALAELKALNPKVTVSfylydvtvPVTETVKLLTTIFGKLKTIDLLINGAGI 83
Cdd:PRK06463  18 GIGRAIAEAFLREGAKVAVLYNSAENeAKELREKGVFTIKCDVG--------NRDQVKKSKEVVEKEFGRVDVLVNNAGI 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  84 L--------DDHQIERTIAINFTGLVNTTtaiMQFWDKRKGGPGGVIANICSVTGF-NAIHQVPVYSASKAAVVSFTSSL 154
Cdd:PRK06463  90 MylmpfeefDEEKYNKMIKINLNGAIYTT---YEFLPLLKLSKNGAIVNIASNAGIgTAAEGTTFYAITKAGIIILTRRL 166

                        170       180
                 ....*....|....*....|....
gi 699964346 155 AKLAPITGITAYSINPGITVTPLT 178
Cdd:PRK06463 167 AFELGKYGIRVNAVAPGWVETDMT 190
PRK06181 PRK06181
SDR family oxidoreductase;
2-175 1.63e-08

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 53.44  E-value: 1.63e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   2 ALGGVGLATSKEIVKRGpKNFVVLDRieNPKALA----ELKALNPKVTVsfYLYDVTVP--VTETVKLLTTIFGKlktID 75
Cdd:PRK06181   9 ASEGIGRALAVRLARAG-AQLVLAAR--NETRLAslaqELADHGGEALV--VPTDVSDAeaCERLIEAAVARFGG---ID 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  76 LLINGAGI--------LDDHQI-ERTIAINFTGLVNTTTAIMQFWDKRKggpgGVIANICSVTGFNAIHQVPVYSASKAA 146
Cdd:PRK06181  81 ILVNNAGItmwsrfdeLTDLSVfERVMRVNYLGAVYCTHAALPHLKASR----GQIVVVSSLAGLTGVPTRSGYAASKHA 156

                        170       180       190
                 ....*....|....*....|....*....|
gi 699964346 147 VVSFTSSL-AKLAPiTGITAYSINPGITVT 175
Cdd:PRK06181 157 LHGFFDSLrIELAD-DGVAVTVVCPGFVAT 185
PRK06949 PRK06949
SDR family oxidoreductase;
73-180 1.83e-08

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 53.61  E-value: 1.83e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  73 TIDLLINGAGILDDHQIERTIAINFTGLVNTTTA----IMQFWDKR-----KGGPG----GVIANICSVTGFNAIHQVPV 139
Cdd:PRK06949  86 TIDILVNNSGVSTTQKLVDVTPADFDFVFDTNTRgaffVAQEVAKRmiaraKGAGNtkpgGRIINIASVAGLRVLPQIGL 165

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 699964346 140 YSASKAAVVSFTSSLAKLAPITGITAYSINPGITVTPLTHQ 180
Cdd:PRK06949 166 YCMSKAAVVHMTRAMALEWGRHGINVNAICPGYIDTEINHH 206
PRK06179 PRK06179
short chain dehydrogenase; Provisional
 5-177 1.89e-08

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 53.37  E-value: 1.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   5 GVGLATSKEIVKRGpknFVVLDRIENPKALAelkalnPKVTVSFYLYDVT--VPVTETVKLLTTIFGKlktIDLLINGAG 82
Cdd:PRK06179  15 GIGRATAEKLARAG---YRVFGTSRNPARAA------PIPGVELLELDVTddASVQAAVDEVIARAGR---IDVLVNNAG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  83 I-----LDDHQIERTIAI---NFTGLVNTTTAI---MqfwdkRKGGpGGVIANICSVTGFnaihqVP-----VYSASKAA 146
Cdd:PRK06179  83 VglagaAEESSIAQAQALfdtNVFGILRMTRAVlphM-----RAQG-SGRIINISSVLGF-----LPapymaLYAASKHA 151

                        170       180       190
                 ....*....|....*....|....*....|.
gi 699964346 147 VVSFTSSLAKLAPITGITAYSINPGITVTPL 177
Cdd:PRK06179 152 VEGYSESLDHEVRQFGIRVSLVEPAYTKTNF 182
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
 2-171 1.96e-08

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: 53.36  E-value: 1.96e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   2 ALGGVGLATSKEIVKRGPKnfVVL-----DRIENPK-ALAELKALNPKVTVSfylyDVTVP------VTETVKLlttiFG 69
Cdd:cd05332   11 ASSGIGEELAYHLARLGAR--LVLsarreERLEEVKsECLELGAPSPHVVPL----DMSDLedaeqvVEEALKL----FG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  70 KlktIDLLINGAGI-----LDDHQIERT---IAINFTGLVNTTTAIMQFWDKRKGGPggvIANICSVTGFNAIHQVPVYS 141
Cdd:cd05332   81 G---LDILINNAGIsmrslFHDTSIDVDrkiMEVNYFGPVALTKAALPHLIERSQGS---IVVVSSIAGKIGVPFRTAYA 154

                        170       180       190
                 ....*....|....*....|....*....|.
gi 699964346 142 ASKAAVVSFTSSL-AKLAPiTGITAYSINPG 171
Cdd:cd05332  155 ASKHALQGFFDSLrAELSE-PNISVTVVCPG 184
PRK05855 PRK05855
SDR family oxidoreductase;
2-178 2.18e-08

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 53.83  E-value: 2.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   2 ALGGVGLATSKEIVKRGPKnFVVLDRieNPKALAELKALNPKVTVSFYLYDVTVPVTETV-KLLTTIFGKLKTIDLLING 80
Cdd:PRK05855 323 AGSGIGRETALAFAREGAE-VVASDI--DEAAAERTAELIRAAGAVAHAYRVDVSDADAMeAFAEWVRAEHGVPDIVVNN 399

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  81 AGI------LD--DHQIERTIAINFTGLVNTTTAIMQFWDKRkgGPGGVIANICSVTGFNAIHQVPVYSASKAAVVSFTS 152
Cdd:PRK05855 400 AGIgmaggfLDtsAEDWDRVLDVNLWGVIHGCRLFGRQMVER--GTGGHIVNVASAAAYAPSRSLPAYATSKAAVLMLSE 477

                        170       180
                 ....*....|....*....|....*..
gi 699964346 153 SL-AKLAPiTGITAYSINPGITVTPLT 178
Cdd:PRK05855 478 CLrAELAA-AGIGVTAICPGFVDTNIV 503
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 69-177 2.37e-08

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 53.19  E-value: 2.37e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  69 GKLKTIDLLINGAGI--------LDDHQIERTIAINFTGLVNTTTAImqfwdKRKGGPGGVIANICSVTGFNAIHQVPVY 140
Cdd:PRK06077  80 DRYGVADILVNNAGLglfspflnVDDKLIDKHISTDFKSVIYCSQEL-----AKEMREGGAIVNIASVAGIRPAYGLSIY 154

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 699964346 141 SASKAAVVSFTSSLA-KLAPitGITAYSINPGITVTPL 177
Cdd:PRK06077 155 GAMKAAVINLTKYLAlELAP--KIRVNAIAPGFVKTKL 190
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
 2-177 3.07e-08

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: 52.45  E-value: 3.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   2 ALGGVGLATSKEIVKRGpkNFVVLDRIeNPKALAELKALNPKVTVSFYLYDVTVPVTETVKL---LTTIFGKLktiDLLI 78
Cdd:cd08931    8 AASGIGRETALLFARNG--WFVGLYDI-DEDGLAALAAELGAENVVAGALDVTDRAAWAAALadfAAATGGRL---DALF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  79 NGAGIL--------DDHQIERTIAINFTGLVNTTTAIMQFWdkrKGGPGGVIANICSVTGFNAIHQVPVYSASKAAVVSF 150
Cdd:cd08931   82 NNAGVGrggpfedvPLAAHDRMVDINVKGVLNGAYAALPYL---KATPGARVINTASSSAIYGQPDLAVYSATKFAVRGL 158

                        170       180
                 ....*....|....*....|....*..
gi 699964346 151 TSSLAKLAPITGITAYSINPGITVTPL 177
Cdd:cd08931  159 TEALDVEWARHGIRVADVWPWFVDTPI 185
PRK05867 PRK05867
SDR family oxidoreductase;
52-191 3.17e-08

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 52.73  E-value: 3.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  52 DVTVPvTETVKLLTTIFGKLKTIDLLINGAGILDDH--------QIERTIAINFTGLVNTTTAIMQFWDKRkgGPGGVIA 123
Cdd:PRK05867  66 DVSQH-QQVTSMLDQVTAELGGIDIAVCNAGIITVTpmldmpleEFQRLQNTNVTGVFLTAQAAAKAMVKQ--GQGGVII 142

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 699964346 124 NICSVTG--FNAIHQVPVYSASKAAVVSFTSSLA-KLAPiTGITAYSINPGIT----VTPLTHQFNSWldvEPRV 191
Cdd:PRK05867 143 NTASMSGhiINVPQQVSHYCASKAAVIHLTKAMAvELAP-HKIRVNSVSPGYIltelVEPYTEYQPLW---EPKI 213
PRK12937 PRK12937
short chain dehydrogenase; Provisional
 62-177 5.70e-08

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 52.05  E-value: 5.70e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  62 KLLTTIFGKLKTIDLLINGAGIL--------DDHQIERTIAINFTGLVNTTTAIMqfwdkRKGGPGGVIANICSVTGFNA 133
Cdd:PRK12937  72 RLFDAAETAFGRIDVLVNNAGVMplgtiadfDLEDFDRTIATNLRGAFVVLREAA-----RHLGQGGRIINLSTSVIALP 146

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 699964346 134 IHQVPVYSASKAAVVSFTSSLAKLAPITGITAYSINPGITVTPL 177
Cdd:PRK12937 147 LPGYGPYAASKAAVEGLVHVLANELRGRGITVNAVAPGPVATEL 190
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 5-178 7.42e-08

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 51.50  E-value: 7.42e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   5 GVGLATSKEIVKRGpKNFVVLDRIENPK---ALAELKALNPKVTvsFYLYDVTvPVTETVKLLTTIFGKLKTIDLLINGA 81
Cdd:PRK12745  13 GIGLGIARALAAAG-FDLAINDRPDDEElaaTQQELRALGVEVI--FFPADVA-DLSAHEAMLDAAQAAWGRIDCLVNNA 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  82 GI-------LDDHQIE---RTIAINFTGLVNTTTAIMQFWDKRKGGPGGVIANICSVTGFNAIHQVPV---YSASKAAVV 148
Cdd:PRK12745  89 GVgvkvrgdLLDLTPEsfdRVLAINLRGPFFLTQAVAKRMLAQPEPEELPHRSIVFVSSVNAIMVSPNrgeYCISKAGLS 168

                        170       180       190
                 ....*....|....*....|....*....|.
gi 699964346 149 SFTSSLA-KLAPiTGITAYSINPGITVTPLT 178
Cdd:PRK12745 169 MAAQLFAaRLAE-EGIGVYEVRPGLIKTDMT 198
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
 2-182 7.69e-08

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 51.45  E-value: 7.69e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   2 ALGGVGLATSKEIVKRGPKNFVVLDRIENPKALAelKALNPKVTvsfyLYDVTVPVTETVKLL-TTIFGKLKTIDLLING 80
Cdd:PRK12936  14 ASGGIGEEIARLLHAQGAIVGLHGTRVEKLEALA--AELGERVK----IFPANLSDRDEVKALgQKAEADLEGVDILVNN 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  81 AGI--------LDDHQIERTIAINFTGLVNTTTAIMQFWDKRKGGPggvIANICSVTGFNAIHQVPVYSASKAAVVSFTS 152
Cdd:PRK12936  88 AGItkdglfvrMSDEDWDSVLEVNLTATFRLTRELTHPMMRRRYGR---IINITSVVGVTGNPGQANYCASKAGMIGFSK 164

                        170       180       190
                 ....*....|....*....|....*....|
gi 699964346 153 SLAKLAPITGITAYSINPGITVTPLTHQFN 182
Cdd:PRK12936 165 SLAQEIATRNVTVNCVAPGFIESAMTGKLN 194
PRK06123 PRK06123
SDR family oxidoreductase;
58-175 7.76e-08

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 51.70  E-value: 7.76e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  58 TETVKLLTTIFGKLKTIDLLINGAGIL---------DDHQIERTIAINFTGLVNTTTAIMQFWDKRKGGPGGVIANICSV 128
Cdd:PRK06123  65 ADVLRLFEAVDRELGRLDALVNNAGILeaqmrleqmDAARLTRIFATNVVGSFLCAREAVKRMSTRHGGRGGAIVNVSSM 144

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 699964346 129 TG-FNAIHQVPVYSASKAAVVSFTSSLAKLAPITGITAYSINPGITVT 175
Cdd:PRK06123 145 AArLGSPGEYIDYAASKGAIDTMTIGLAKEVAAEGIRVNAVRPGVIYT 192
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
74-175 1.09e-07

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 51.06  E-value: 1.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  74 IDLLINGAGIlddhqIERTIAINFT-----GLVNTTTAIMQFWDKR------KGGPGGVIANICSVTGFNAIHQVPVYSA 142
Cdd:PRK12481  84 IDILINNAGI-----IRRQDLLEFGnkdwdDVININQKTVFFLSQAvakqfvKQGNGGKIINIASMLSFQGGIRVPSYTA 158

                         90       100       110
                 ....*....|....*....|....*....|...
gi 699964346 143 SKAAVVSFTSSLAKLAPITGITAYSINPGITVT 175
Cdd:PRK12481 159 SKSAVMGLTRALATELSQYNINVNAIAPGYMAT 191
PRK07035 PRK07035
SDR family oxidoreductase;
68-175 1.11e-07

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 51.17  E-value: 1.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  68 FGKLktiDLLINGAG-------ILDDHQI--ERTIAINFTG--LVNTTTAIMQfwdkRKGGpGGVIANICSVTGFNAIHQ 136
Cdd:PRK07035  83 HGRL---DILVNNAAanpyfghILDTDLGafQKTVDVNIRGyfFMSVEAGKLM----KEQG-GGSIVNVASVNGVSPGDF 154

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 699964346 137 VPVYSASKAAVVSFTSSLAK-LAPItGITAYSINPGITVT 175
Cdd:PRK07035 155 QGIYSITKAAVISMTKAFAKeCAPF-GIRVNALLPGLTDT 193
PRK06482 PRK06482
SDR family oxidoreductase;
5-175 1.15e-07

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 51.27  E-value: 1.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   5 GVGLATSKEIVKRGPKNFVVLDRienPKALAELKALNPKvtvsfYLYDVTVPVTETVKLLTTI---FGKLKTIDLLINGA 81
Cdd:PRK06482  13 GFGRGMTERLLARGDRVAATVRR---PDALDDLKARYGD-----RLWVLQLDVTDSAAVRAVVdraFAALGRIDVVVSNA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  82 GI--------LDDHQIERTIAINFTGLVNTTTAIMQfwDKRKGGpGGVIANICSVTGFNAIHQVPVYSASKAAVVSFTSS 153
Cdd:PRK06482  85 GYglfgaaeeLSDAQIRRQIDTNLIGSIQVIRAALP--HLRRQG-GGRIVQVSSEGGQIAYPGFSLYHATKWGIEGFVEA 161

                        170       180
                 ....*....|....*....|...
gi 699964346 154 LAK-LAPItGITAYSINPGITVT 175
Cdd:PRK06482 162 VAQeVAPF-GIEFTIVEPGPART 183
PRK09242 PRK09242
SDR family oxidoreductase;
5-199 1.30e-07

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 50.90  E-value: 1.30e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   5 GVGLATSKEIVKRGPKNFVV---LDRIEnpKALAELKALNPKVTVSFYLYDVTVPVTETvKLLTTIFGKLKTIDLLINGA 81
Cdd:PRK09242  20 GIGLAIAREFLGLGADVLIVardADALA--QARDELAEEFPEREVHGLAADVSDDEDRR-AILDWVEDHWDGLHILVNNA 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  82 GI------LDDHQIE--RTIAINFTGLVNTTTAIMQFWDKRKGGPggvIANICSVTGFNAIHQVPVYSASKAAVVSFTSS 153
Cdd:PRK09242  97 GGnirkaaIDYTEDEwrGIFETNLFSAFELSRYAHPLLKQHASSA---IVNIGSVSGLTHVRSGAPYGMTKAALLQMTRN 173

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 699964346 154 LAKLAPITGITAYSINPGITVTPLThqfNSWLDVEPRVAELLNEHP 199
Cdd:PRK09242 174 LAVEWAEDGIRVNAVAPWYIRTPLT---SGPLSDPDYYEQVIERTP 216
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
 57-172 1.86e-07

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: 50.28  E-value: 1.86e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  57 VTETVKLLTTIFGKlktIDLLINGAG--------ILDDHQIERTIAINFTGLVNTTTAIMQFWdkRKGGPGGVIANIC-- 126
Cdd:cd05369   68 VEAAVDETLKEFGK---IDILINNAAgnflapaeSLSPNGFKTVIDIDLNGTFNTTKAVGKRL--IEAKHGGSILNISat 142

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 699964346 127 -SVTGFNAihQVPVySASKAAVVSFTSSLA-KLAPiTGITAYSINPGI 172
Cdd:cd05369  143 yAYTGSPF--QVHS-AAAKAGVDALTRSLAvEWGP-YGIRVNAIAPGP 186
PRK06198 PRK06198
short chain dehydrogenase; Provisional
 5-176 2.37e-07

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 50.00  E-value: 2.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   5 GVGLATSKEIVKRGPKNFVVLDRIENP--KALAELKALNPKVTvsFYLYDVTVPVTETVKLLTTI--FGklkTIDLLING 80
Cdd:PRK06198  17 GLGAAIARAFAERGAAGLVICGRNAEKgeAQAAELEALGAKAV--FVQADLSDVEDCRRVVAAADeaFG---RLDALVNA 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  81 AGILDDHQI--------ERTIAINFTG---LVNTTTAIMqfwdKRKGGPGgVIANICSVTGFNAIHQVPVYSASKAAVVS 149
Cdd:PRK06198  92 AGLTDRGTIldtspelfDRHFAVNVRApffLMQEAIKLM----RRRKAEG-TIVNIGSMSAHGGQPFLAAYCASKGALAT 166

                        170       180
                 ....*....|....*....|....*..
gi 699964346 150 FTSSLAKLAPITGITAYSINPGITVTP 176
Cdd:PRK06198 167 LTRNAAYALLRNRIRVNGLNIGWMATE 193
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
 5-178 2.76e-07

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: 49.77  E-value: 2.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   5 GVGLATSKEIVKRGpknFVVL-DRIENPKALAELKALNPK--VTVSFYLYDVTVPVTETvKLLTTIFGKLKTIDLLINGA 81
Cdd:cd05337   12 GIGRAIATELAARG---FDIAiNDLPDDDQATEVVAEVLAagRRAIYFQADIGELSDHE-ALLDQAWEDFGRLDCLVNNA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  82 GI----------LDDHQIERTIAINFTG---LVNTTTAIMQFWDKRKGGPGGVIANICSVTGFNAIHQVPVYSASKAAVV 148
Cdd:cd05337   88 GIavrprgdlldLTEDSFDRLIAINLRGpffLTQAVARRMVEQPDRFDGPHRSIIFVTSINAYLVSPNRGEYCISKAGLS 167

                        170       180       190
                 ....*....|....*....|....*....|.
gi 699964346 149 SFTSSLA-KLAPiTGITAYSINPGITVTPLT 178
Cdd:cd05337  168 MATRLLAyRLAD-EGIAVHEIRPGLIHTDMT 197
PRK05872 PRK05872
short chain dehydrogenase; Provisional
 2-215 3.18e-07

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 49.97  E-value: 3.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   2 ALGGVGLATSKEIVKRGPKnFVVLDRieNPKALAELKA-LNPKVTVSFYLYDVTVP-----VTETVKlltTIFGKlktID 75
Cdd:PRK05872  17 AARGIGAELARRLHARGAK-LALVDL--EEAELAALAAeLGGDDRVLTVVADVTDLaamqaAAEEAV---ERFGG---ID 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  76 LLINGAGIL--------DDHQIERTIAINFTGLVNTTTA-IMQFWDKRkggpgGVIANICSVTGFNAIHQVPVYSASKAA 146
Cdd:PRK05872  88 VVVANAGIAsggsvaqvDPDAFRRVIDVNLLGVFHTVRAtLPALIERR-----GYVLQVSSLAAFAAAPGMAAYCASKAG 162

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 699964346 147 VVSFTSSL-AKLAPiTGITAYSINPGITVTPLThqfNSWLDVEPRVAELLNEHP-----TQTTEECGLNFAKAIE 215
Cdd:PRK05872 163 VEAFANALrLEVAH-HGVTVGSAYLSWIDTDLV---RDADADLPAFRELRARLPwplrrTTSVEKCAAAFVDGIE 233
PRK09730 PRK09730
SDR family oxidoreductase;
58-175 4.23e-07

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 49.46  E-value: 4.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  58 TETVKLLTTIFGKLKTIDLLINGAGIL---------DDHQIERTIAINFTGLVNTTTAIMQFWDKRKGGPGGVIANICSV 128
Cdd:PRK09730  64 NQVVAMFTAIDQHDEPLAALVNNAGILftqctvenlTAERINRVLSTNVTGYFLCCREAVKRMALKHGGSGGAIVNVSSA 143

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 699964346 129 TG-FNAIHQVPVYSASKAAVVSFTSSLAKLAPITGITAYSINPGITVT 175
Cdd:PRK09730 144 ASrLGAPGEYVDYAASKGAIDTLTTGLSLEVAAQGIRVNCVRPGFIYT 191
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
 69-199 4.93e-07

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: 49.01  E-value: 4.93e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  69 GKLKTIDLLINGAGI--------LDDHQIERTIAINFTGLVNTTTAIMQFWDKRkgGPGGVIANICSVTGFNAIHQVPVY 140
Cdd:cd05351   72 GSVGPVDLLVNNAAVailqpfleVTKEAFDRSFDVNVRAVIHVSQIVARGMIAR--GVPGSIVNVSSQASQRALTNHTVY 149

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346 141 SASKAAVVSFTSSLA-KLAPiTGITAYSINPGITVTPLTHqfNSWLDVEpRVAELLNEHP 199
Cdd:cd05351  150 CSTKAALDMLTKVMAlELGP-HKIRVNSVNPTVVMTDMGR--DNWSDPE-KAKKMLNRIP 205
PRK05650 PRK05650
SDR family oxidoreductase;
5-154 5.45e-07

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 49.27  E-value: 5.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   5 GVGLATSKEIVKRGPKnfVVLDRIeNPKALAE-LKALNPKVTVSFYLY-DVTvPVTETVKLLTTIFGKLKTIDLLINGAG 82
Cdd:PRK05650  11 GLGRAIALRWAREGWR--LALADV-NEEGGEEtLKLLREAGGDGFYQRcDVR-DYSQLTALAQACEEKWGGIDVIVNNAG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  83 I-----LDDHQIER---TIAINFTGLVNTTTAIMQFWDKRKGGPggvIANICSVTGFNAIHQVPVYSASKAAVVSFTSSL 154
Cdd:PRK05650  87 VasggfFEELSLEDwdwQIAINLMGVVKGCKAFLPLFKRQKSGR---IVNIASMAGLMQGPAMSSYNVAKAGVVALSETL 163
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
 75-178 8.39e-07

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


Pssm-ID: 187535 [Multi-domain]  Cd Length: 186  Bit Score: 47.90  E-value: 8.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  75 DLLINGAGILDD--------HQIERTIAINFTGLVNTTTAIMQFWDKRkgGPGGVIaNICSVTGFNAIHQVPVYSASKAA 146
Cdd:cd02266   33 DVVVHNAAILDDgrlidltgSRIERAIRANVVGTRRLLEAARELMKAK--RLGRFI-LISSVAGLFGAPGLGGYAASKAA 109

                         90       100       110
                 ....*....|....*....|....*....|..
gi 699964346 147 VVSFTSSLAKLAPITGITAYSINPGITVTPLT 178
Cdd:cd02266  110 LDGLAQQWASEGWGNGLPATAVACGTWAGSGM 141
PRK07109 PRK07109
short chain dehydrogenase; Provisional
 2-190 8.89e-07

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 48.76  E-value: 8.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   2 ALGGVGLATSKEIVKRGPKnFVVLDRieNPKAL----AELKALNPKVTVsfYLYDVTVP--VTETVKLLTTIFGklkTID 75
Cdd:PRK07109  16 ASAGVGRATARAFARRGAK-VVLLAR--GEEGLealaAEIRAAGGEALA--VVADVADAeaVQAAADRAEEELG---PID 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  76 LLINGAGI--------LDDHQIERTIAINFTGLVNTTTAIMQFWdKRKGGpgGVIANICSVTGFNAIHQVPVYSASKAAV 147
Cdd:PRK07109  88 TWVNNAMVtvfgpfedVTPEEFRRVTEVTYLGVVHGTLAALRHM-RPRDR--GAIIQVGSALAYRSIPLQSAYCAAKHAI 164

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 699964346 148 VSFTSSL-AKL----APITgITaySINPGITVTPlthQFN---SWLDVEPR 190
Cdd:PRK07109 165 RGFTDSLrCELlhdgSPVS-VT--MVQPPAVNTP---QFDwarSRLPVEPQ 209
PRK09072 PRK09072
SDR family oxidoreductase;
2-177 1.31e-06

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 48.01  E-value: 1.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   2 ALGGVGLATSKEIVKRGPKnFVVLDRieNPKALAELKALNPK-VTVSFYLYDVTVPvtETVKLLTTIFGKLKTIDLLING 80
Cdd:PRK09072  13 ASGGIGQALAEALAAAGAR-LLLVGR--NAEKLEALAARLPYpGRHRWVVADLTSE--AGREAVLARAREMGGINVLINN 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  81 AGI--------LDDHQIERTIAINFTGLVNTTTAIMQfWDKRKggPGGVIANICSVtgFNAIhQVP---VYSASKAAVVS 149
Cdd:PRK09072  88 AGVnhfalledQDPEAIERLLALNLTAPMQLTRALLP-LLRAQ--PSAMVVNVGST--FGSI-GYPgyaSYCASKFALRG 161

                        170       180
                 ....*....|....*....|....*....
gi 699964346 150 FTSSLAK-LAPiTGITAYSINPGITVTPL 177
Cdd:PRK09072 162 FSEALRReLAD-TGVRVLYLAPRATRTAM 189
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
 2-171 2.11e-06

(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: 47.32  E-value: 2.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   2 ALGGVGLATSKEIVKRGPKnfVVLDRIENP------------KALAELKALNPKVTVSfylYDvtvPVTETVKLLTTIFG 69
Cdd:cd05353   13 AGGGLGRAYALAFAERGAK--VVVNDLGGDrkgsgksssaadKVVDEIKAAGGKAVAN---YD---SVEDGEKIVKTAID 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  70 KLKTIDLLINGAGILDDHQIERT--------IAINFTGLVNTTTAIMQFWDKRKggpGGVIANICSVTG-FNAIHQVPvY 140
Cdd:cd05353   85 AFGRVDILVNNAGILRDRSFAKMseedwdlvMRVHLKGSFKVTRAAWPYMRKQK---FGRIINTSSAAGlYGNFGQAN-Y 160

                        170       180       190
                 ....*....|....*....|....*....|.
gi 699964346 141 SASKAAVVSFTSSLAKLAPITGITAYSINPG 171
Cdd:cd05353  161 SAAKLGLLGLSNTLAIEGAKYNITCNTIAPA 191
PRK06172 PRK06172
SDR family oxidoreductase;
119-199 3.00e-06

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 47.05  E-value: 3.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346 119 GGVIANICSVTGFNAIHQVPVYSASKAAVVSFTSSLAKLAPITGITAYSINPGITVTPLthqFNSWLDVEPRVAELL-NE 197
Cdd:PRK06172 136 GGAIVNTASVAGLGAAPKMSIYAASKHAVIGLTKSAAIEYAKKGIRVNAVCPAVIDTDM---FRRAYEADPRKAEFAaAM 212


                 ..
gi 699964346 198 HP 199
Cdd:PRK06172 213 HP 214
PRK08263 PRK08263
short chain dehydrogenase; Provisional
 5-171 4.06e-06

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 46.57  E-value: 4.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   5 GVGLATSKEIVKRGPKnfvVLDRIENPKALAELKALNPKVTVSFYLyDVT--VPVTETVKLLTTIFGKLktiDLLINGAG 82
Cdd:PRK08263  14 GFGRAWTEAALERGDR---VVATARDTATLADLAEKYGDRLLPLAL-DVTdrAAVFAAVETAVEHFGRL---DIVVNNAG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  83 I--------LDDHQIERTIAINFTGLVNTTTAIMQFWdkRKGGpGGVIANICSVTGFNAIHQVPVYSASKAAVVSFTSSL 154
Cdd:PRK08263  87 YglfgmieeVTESEARAQIDTNFFGALWVTQAVLPYL--REQR-SGHIIQISSIGGISAFPMSGIYHASKWALEGMSEAL 163

                        170
                 ....*....|....*..
gi 699964346 155 AKLAPITGITAYSINPG 171
Cdd:PRK08263 164 AQEVAEFGIKVTLVEPG 180
DHPR_SDR_c_like cd05334
dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an ...
 2-195 5.01e-06

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


Pssm-ID: 187595 [Multi-domain]  Cd Length: 221  Bit Score: 45.78  E-value: 5.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   2 ALGGVGLATSKEIVKRGpKNFVVLDRIENPKALAelkalnpkvtvSFYLYDVTVPVTET---VKLLTTIFGKLktiDLLI 78
Cdd:cd05334    9 GRGALGSAVVQAFKSRG-WWVASIDLAENEEADA-----------SIIVLDSDSFTEQAkqvVASVARLSGKV---DALI 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  79 NGAG------ILDDHQIE---RTIAINftglVNTTTAIMQFWDKRkGGPGGVIANICSVTGFNAIHQVPVYSASKAAVVS 149
Cdd:cd05334   74 CVAGgwaggsAKSKSFVKnwdLMWKQN----LWTSFIASHLATKH-LLSGGLLVLTGAKAALEPTPGMIGYGAAKAAVHQ 148

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 699964346 150 FTSSLA--KLAPITGITAYSINPGITVTPLTHQ------FNSWLDVEpRVAELL 195
Cdd:cd05334  149 LTQSLAaeNSGLPAGSTANAILPVTLDTPANRKampdadFSSWTPLE-FIAELI 201
PRK07074 PRK07074
SDR family oxidoreductase;
2-192 5.24e-06

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 46.30  E-value: 5.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   2 ALGGVGLATSKEIVKRGpKNFVVLDRieNPKALAELKALNPKVTVSFYLYDVTVPvTETVKLLTTIFGKLKTIDLLINGA 81
Cdd:PRK07074  10 AAGGIGQALARRFLAAG-DRVLALDI--DAAALAAFADALGDARFVPVACDLTDA-ASLAAALANAAAERGPVDVLVANA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  82 GI-----LDDHQIE---RTIAINFTGLVNTTTAIMQFWDKRKGGpggVIANICSVTGFNAI-HqvPVYSASKAAVVSFTS 152
Cdd:PRK07074  86 GAaraasLHDTTPAswrADNALNLEAAYLCVEAVLEGMLKRSRG---AVVNIGSVNGMAALgH--PAYSAAKAGLIHYTK 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 699964346 153 SLAKLAPITGITAYSINPGITVTPlthqfnSWldvEPRVA 192
Cdd:PRK07074 161 LLAVEYGRFGIRANAVAPGTVKTQ------AW---EARVA 191
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
 2-197 6.01e-06

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: 45.97  E-value: 6.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   2 ALGGVGLATSKEIVKRGPKNFVVLDRIENPKAL-AELKALNpKVTVSFYLYDVTVPvTETVKLLTTIFGKLKTIDLLING 80
Cdd:cd05343   14 ASVGIGAAVARALVQHGMKVVGCARRVDKIEALaAECQSAG-YPTLFPYQCDLSNE-EQILSMFSAIRTQHQGVDVCINN 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  81 AGIL--------DDHQIERTIAINFTGLVNTTTAIMQFWDKRKGGPGGVIaNICSVTGfnaiHQVP------VYSASKAA 146
Cdd:cd05343   92 AGLArpepllsgKTEGWKEMFDVNVLALSICTREAYQSMKERNVDDGHII-NINSMSG----HRVPpvsvfhFYAATKHA 166

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 699964346 147 VVSFTSSL------AKlapiTGITAYSINPGITVTPLTHQFNswlDVEPRVAELLNE 197
Cdd:cd05343  167 VTALTEGLrqelreAK----THIRATSISPGLVETEFAFKLH---DNDPEKAAATYE 216
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 3-175 7.21e-06

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 45.93  E-value: 7.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   3 LGGVGLATSKEIVKRGPKNFVV------------LDRIENPKALAELKALNPKVTvSFYLyDVTVPvTETVKLLTTIFGK 70
Cdd:PRK12859  17 LDGIGAAICKELAEAGADIFFTywtaydkempwgVDQDEQIQLQEELLKNGVKVS-SMEL-DLTQN-DAPKELLNKVTEQ 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  71 LKTIDLLINGA--------GILDDHQIERTIAINFTGlvnTTTAIMQFWDKRKGGPGGVIANICSVTGFNAIHQVPVYSA 142
Cdd:PRK12859  94 LGYPHILVNNAaystnndfSNLTAEELDKHYMVNVRA---TTLLSSQFARGFDKKSGGRIINMTSGQFQGPMVGELAYAA 170

                        170       180       190
                 ....*....|....*....|....*....|....
gi 699964346 143 SKAAVVSFTSSLA-KLAPItGITAYSINPGITVT 175
Cdd:PRK12859 171 TKGAIDALTSSLAaEVAHL-GITVNAINPGPTDT 203
PRK08589 PRK08589
SDR family oxidoreductase;
51-177 7.88e-06

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 45.92  E-value: 7.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  51 YDVTVPVTETVKLLTT-IFGKLKTIDLLINGAGI------LDDHQIE---RTIAINFTGLVNTTTAIMQFWDKRkggpGG 120
Cdd:PRK08589  59 YHVDISDEQQVKDFASeIKEQFGRVDVLFNNAGVdnaagrIHEYPVDvfdKIMAVDMRGTFLMTKMLLPLMMEQ----GG 134

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 699964346 121 VIANICSVTGFNAIHQVPVYSASKAAVVSFTSSLAKLAPITGITAYSINPGITVTPL 177
Cdd:PRK08589 135 SIINTSSFSGQAADLYRSGYNAAKGAVINFTKSIAIEYGRDGIRANAIAPGTIETPL 191
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
 74-175 1.12e-05

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: 45.14  E-value: 1.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  74 IDLLINGAGI--------LDDHQIERTIAINFTGLVNTTTAIMQFWDKRKGGPGGVIANICSVTG--FNAihqvpVYSAS 143
Cdd:cd09806   80 VDVLVCNAGVgllgpleaLSEDAMASVFDVNVFGTVRMLQAFLPDMKRRGSGRILVTSSVGGLQGlpFND-----VYCAS 154

                         90       100       110
                 ....*....|....*....|....*....|..
gi 699964346 144 KAAVVSFTSSLAKLAPITGITAYSINPGITVT 175
Cdd:cd09806  155 KFALEGLCESLAVQLLPFNVHLSLIECGPVHT 186
PRK07577 PRK07577
SDR family oxidoreductase;
74-177 1.14e-05

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 45.10  E-value: 1.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  74 IDLLINGAGI--------LDDHQIERTIAINFTGLVNTTTAimqFWDKRKGGPGGVIANICSVTGFNAIHQVPvYSASKA 145
Cdd:PRK07577  69 VDAIVNNVGIalpqplgkIDLAALQDVYDLNVRAAVQVTQA---FLEGMKLREQGRIVNICSRAIFGALDRTS-YSAAKS 144

                         90       100       110
                 ....*....|....*....|....*....|...
gi 699964346 146 AVVSFTSSLA-KLAPiTGITAYSINPGITVTPL 177
Cdd:PRK07577 145 ALVGCTRTWAlELAE-YGITVNAVAPGPIETEL 176
PRK06101 PRK06101
SDR family oxidoreductase;
82-178 1.14e-05

SDR family oxidoreductase;


Pssm-ID: 180399 [Multi-domain]  Cd Length: 240  Bit Score: 45.25  E-value: 1.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  82 GILDDHQIERTIAINFTGLVNTTTAIMQFWDkrkggPGGVIANICSVTGFNAIHQVPVYSASKAAVVSFTSSLAKLAPIT 161
Cdd:PRK06101  88 GKVDATLMARVFNVNVLGVANCIEGIQPHLS-----CGHRVVIVGSIASELALPRAEAYGASKAAVAYFARTLQLDLRPK 162

                         90
                 ....*....|....*..
gi 699964346 162 GITAYSINPGITVTPLT 178
Cdd:PRK06101 163 GIEVVTVFPGFVATPLT 179
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
 120-208 1.25e-05

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: 45.13  E-value: 1.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346 120 GVIANICSVTGFNAIHQVPvYSASKAAVVSFTSSLA-KLAPiTGITAYSINPGITVTPLTHQFNSwlDVEPRVAELLNE- 197
Cdd:cd09763  141 GLIVIISSTGGLEYLFNVA-YGVGKAAIDRMAADMAhELKP-HGVAVVSLWPGFVRTELVLEMPE--DDEGSWHAKERDa 216

                         90
                 ....*....|..
gi 699964346 198 -HPTQTTEECGL 208
Cdd:cd09763  217 fLNGETTEYSGR 228
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 5-207 1.73e-05

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: 44.58  E-value: 1.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   5 GVGLATSKEIVKRGpknFVVLDRI--ENPKALAELKALN-PKVTVsfYLYDVTVP-----VTETVKllttifGKLKTIDL 76
Cdd:cd09805   11 GFGNLLAKKLDSLG---FTVLAGCltKNGPGAKELRRVCsDRLRT--LQLDVTKPeqikrAAQWVK------EHVGEKGL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  77 --LINGAGIL-----------DDHQieRTIAINFTGLVNTTTAIMQFWDKRKGGpggvIANICSVTGFNAIHQVPVYSAS 143
Cdd:cd09805   80 wgLVNNAGILgfggdeellpmDDYR--KCMEVNLFGTVEVTKAFLPLLRRAKGR----VVNVSSMGGRVPFPAGGAYCAS 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 699964346 144 KAAVVSFTSSLAK-LAPItGITAYSINPGITVTPLTHQFNSWldvEPRVAELLNEHPTQTTEECG 207
Cdd:cd09805  154 KAAVEAFSDSLRReLQPW-GVKVSIIEPGNFKTGITGNSELW---EKQAKKLWERLPPEVKKDYG 214
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
 2-170 1.74e-05

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: 44.69  E-value: 1.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   2 ALGGVGLATSKEIVKRGpKNFVVLDRIENPKALAELKALNPKVTVSFYLyDVT--VPVTETVKLLTTIFGKlktIDLLIN 79
Cdd:cd08943    9 GASGIGLAIAKRLAAEG-AAVVVADIDPEIAEKVAEAAQGGPRALGVQC-DVTseAQVQSAFEQAVLEFGG---LDIVVS 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  80 GAGILDDHQIE--------RTIAINFTGlvNTTTAIMQFWDKRKGGPGGVIANICSVTGFNAIHQVPVYSASKAAVVSFT 151
Cdd:cd08943   84 NAGIATSSPIAetsledwnRSMDINLTG--HFLVSREAFRIMKSQGIGGNIVFNASKNAVAPGPNAAAYSAAKAAEAHLA 161

                        170
                 ....*....|....*....
gi 699964346 152 SSLAKLAPITGITAYSINP 170
Cdd:cd08943  162 RCLALEGGEDGIRVNTVNP 180
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
 5-171 1.75e-05

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: 44.49  E-value: 1.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   5 GVGLATSKEIVKRGPKnfVVLDRIENPKALAELKALNPKVTvsFYLYDVTvPVTETVKLLTTIFGKLKTIDLLINGAGIL 84
Cdd:cd09761   12 GIGKQICLDFLEAGDK--VVFADIDEERGADFAEAEGPNLF--FVHGDVA-DETLVKFVVYAMLEKLGRIDVLVNNAARG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  85 DDHQI--------ERTIAINFTG---LVNTTTAIMqfwdkRKGGpgGVIANICSVTGFNAIHQVPVYSASKAAVVSFTSS 153
Cdd:cd09761   87 SKGILssllleewDRILSVNLTGpyeLSRYCRDEL-----IKNK--GRIINIASTRAFQSEPDSEAYAASKGGLVALTHA 159

                        170
                 ....*....|....*....
gi 699964346 154 LA-KLAPitGITAYSINPG 171
Cdd:cd09761  160 LAmSLGP--DIRVNCISPG 176
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
 21-171 1.89e-05

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 44.64  E-value: 1.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  21 NFVVLD-RIENPKALA-ELKALNPKVTVSFYLYDVTVP--VTETVKLLTTIFGKlktIDLLINGAGILDDHQI------- 89
Cdd:PRK12384  28 RVAVADiNSEKAANVAqEINAEYGEGMAYGFGADATSEqsVLALSRGVDEIFGR---VDLLVYNAGIAKAAFItdfqlgd 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  90 -ERTIAINFTGLVNTTTAIMQFWDKRkgGPGGVIANICSVTGFNAIHQVPVYSASKAAVVSFTSSLA-KLAPiTGITAYS 167
Cdd:PRK12384 105 fDRSLQVNLVGYFLCAREFSRLMIRD--GIQGRIIQINSKSGKVGSKHNSGYSAAKFGGVGLTQSLAlDLAE-YGITVHS 181


                 ....
gi 699964346 168 INPG 171
Cdd:PRK12384 182 LMLG 185
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 70-175 1.99e-05

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 44.30  E-value: 1.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  70 KLKTIDLLINGA--------GILDDHQIERTIAINftglVNTTTAIMQFWDKR-KGGPGGVIANICSvtgfnAIHQVPV- 139
Cdd:PRK12748  92 RLGDPSILINNAaysthtrlEELTAEQLDKHYAVN----VRATMLLSSAFAKQyDGKAGGRIINLTS-----GQSLGPMp 162

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 699964346 140 ----YSASKAAVVSFTSSLAKLAPITGITAYSINPGITVT 175
Cdd:PRK12748 163 delaYAATKGAIEAFTKSLAPELAEKGITVNAVNPGPTDT 202
PRK08265 PRK08265
short chain dehydrogenase; Provisional
 5-177 2.23e-05

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 44.23  E-value: 2.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   5 GVGLATSKEIVKRGPKnFVVLDR-IENPKALAElkALNPKVTvsFYLYDVT--VPVTETVKLLTTIFGKlktIDLLINGA 81
Cdd:PRK08265  17 LIGAAVARALVAAGAR-VAIVDIdADNGAAVAA--SLGERAR--FIATDITddAAIERAVATVVARFGR---VDILVNLA 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  82 GILDDHQIERTIAINFTGL-VNTTTAIM--QFWDKRKGGPGGVIANICSVTGFNAIHQVPVYSASKAAVVSFTSSLA-KL 157
Cdd:PRK08265  89 CTYLDDGLASSRADWLAALdVNLVSAAMlaQAAHPHLARGGGAIVNFTSISAKFAQTGRWLYPASKAAIRQLTRSMAmDL 168

                        170       180
                 ....*....|....*....|
gi 699964346 158 APiTGITAYSINPGITVTPL 177
Cdd:PRK08265 169 AP-DGIRVNSVSPGWTWSRV 187
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
 74-178 2.92e-05

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: 44.02  E-value: 2.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  74 IDLLINGAGILD-DHQIE--------RTIAINFTGLVNTTtaimqfwdkRKGGP------GGVIANICSVTGFNAIHQVP 138
Cdd:cd08944   78 LDLLVNNAGAMHlTPAIIdtdlavwdQTMAINLRGTFLCC---------RHAAPrmiargGGSIVNLSSIAGQSGDPGYG 148

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 699964346 139 VYSASKAAVVSFTSSLAKLAPITGITAYSINPGITVTPLT 178
Cdd:cd08944  149 AYGASKAAIRNLTRTLAAELRHAGIRCNALAPGLIDTPLL 188
fabG PRK07792
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 68-170 2.94e-05

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


Pssm-ID: 181120 [Multi-domain]  Cd Length: 306  Bit Score: 44.00  E-value: 2.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  68 FGKLktiDLLINGAGILDDHQI--------ERTIAINFTGLVNTTTAIMQFW-DKRKGGPG---GVIANICSVTGFNAIH 135
Cdd:PRK07792  87 LGGL---DIVVNNAGITRDRMLfnmsdeewDAVIAVHLRGHFLLTRNAAAYWrAKAKAAGGpvyGRIVNTSSEAGLVGPV 163

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 699964346 136 QVPVYSASKAAVVSFTSSLAKLAPITGITAYSINP 170
Cdd:PRK07792 164 GQANYGAAKAGITALTLSAARALGRYGVRANAICP 198
PRK08251 PRK08251
SDR family oxidoreductase;
25-171 3.01e-05

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 43.77  E-value: 3.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  25 LDRIENPKAlaELKALNPKVTVSFYLYDVT----VPvtetvklltTIFGKLKT----IDLLINGAGILDDHQI------- 89
Cdd:PRK08251  36 TDRLEELKA--ELLARYPGIKVAVAALDVNdhdqVF---------EVFAEFRDelggLDRVIVNAGIGKGARLgtgkfwa 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  90 -ERTIAINFTGLVNTTTAIMQFWDKRKGGPGGVIANICSVTGFNAihQVPVYSASKAAVVSFTSSLAKLAPITGITAYSI 168
Cdd:PRK08251 105 nKATAETNFVAALAQCEAAMEIFREQGSGHLVLISSVSAVRGLPG--VKAAYAASKAGVASLGEGLRAELAKTPIKVSTI 182


                 ...
gi 699964346 169 NPG 171
Cdd:PRK08251 183 EPG 185
PRK06125 PRK06125
short chain dehydrogenase; Provisional
 73-175 3.10e-05

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 43.88  E-value: 3.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  73 TIDLLINGAG--------ILDDHQIERTIAINFTGLVNTTTAimqFWDKRKGGPGGVIANICSVTGFNAIHQVPVYSASK 144
Cdd:PRK06125  81 DIDILVNNAGaipgggldDVDDAAWRAGWELKVFGYIDLTRL---AYPRMKARGSGVIVNVIGAAGENPDADYICGSAGN 157

                         90       100       110
                 ....*....|....*....|....*....|.
gi 699964346 145 AAVVSFTSSLAKLAPITGITAYSINPGITVT 175
Cdd:PRK06125 158 AALMAFTRALGGKSLDDGVRVVGVNPGPVAT 188
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 2-86 3.29e-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: 43.24  E-value: 3.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346     2 ALGGVGLATSKEIVKRGPKNFVVLDR--IENPKA---LAELKALNPKVTVsfYLYDVTVPVtETVKLLTTIFGKLKTIDL 76
Cdd:smart00822   8 GLGGLGRALARWLAERGARRLVLLSRsgPDAPGAaalLAELEAAGARVTV--VACDVADRD-ALAAVLAAIPAVEGPLTG 84

                           90
                   ....*....|
gi 699964346    77 LINGAGILDD 86
Cdd:smart00822  85 VIHAAGVLDD 94
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
 5-178 3.69e-05

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 43.51  E-value: 3.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   5 GVGLATSKEIVKRGPK---NFVVLDRIEnpKALAELKALNpkVTVSFYLYDVT--VPVTETVKLLTTIFGklkTIDLLIN 79
Cdd:PRK07097  21 GIGFAIAKAYAKAGATivfNDINQELVD--KGLAAYRELG--IEAHGYVCDVTdeDGVQAMVSQIEKEVG---VIDILVN 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  80 GAGIlddhqIERT-------------IAINFTGLVNTTTAIMQFWDKRKGGPggvIANICSVTGFNAIHQVPVYSASKAA 146
Cdd:PRK07097  94 NAGI-----IKRIpmlemsaedfrqvIDIDLNAPFIVSKAVIPSMIKKGHGK---IINICSMMSELGRETVSAYAAAKGG 165

                        170       180       190
                 ....*....|....*....|....*....|..
gi 699964346 147 VVSFTSSLAKLAPITGITAYSINPGITVTPLT 178
Cdd:PRK07097 166 LKMLTKNIASEYGEANIQCNGIGPGYIATPQT 197
PRK06138 PRK06138
SDR family oxidoreductase;
5-177 3.90e-05

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 43.60  E-value: 3.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   5 GVGLATSKEIVKRGPknFVVLDRIENPKALAELKALNPKVTVSFYLYDVTVP--VTETVKLLTTIFGKLktiDLLINGAG 82
Cdd:PRK06138  16 GIGRATAKLFAREGA--RVVVADRDAEAAERVAAAIAAGGRAFARQGDVGSAeaVEALVDFVAARWGRL---DVLVNNAG 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  83 I--------LDDHQIERTIAINFTGL---VNTTTAIMQfwdkRKGGpgGVIANICSVTGFNAIHQVPVYSASKAAVVSFT 151
Cdd:PRK06138  91 FgcggtvvtTDEADWDAVMRVNVGGVflwAKYAIPIMQ----RQGG--GSIVNTASQLALAGGRGRAAYVASKGAIASLT 164

                        170       180
                 ....*....|....*....|....*.
gi 699964346 152 SSLAKLAPITGITAYSINPGITVTPL 177
Cdd:PRK06138 165 RAMALDHATDGIRVNAVAPGTIDTPY 190
PRK12743 PRK12743
SDR family oxidoreductase;
52-189 4.07e-05

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 43.48  E-value: 4.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  52 DVTVPVtETVKLLTTIFGKLKTIDLLINGAGI--------LDDHQIERTIAINftglVNTTTAIMQFWDKR--KGGPGGV 121
Cdd:PRK12743  60 DLSDLP-EGAQALDKLIQRLGRIDVLVNNAGAmtkapfldMDFDEWRKIFTVD----VDGAFLCSQIAARHmvKQGQGGR 134

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 699964346 122 IANICSVTGFNAIHQVPVYSASKAAVVSFTSSLA-KLAPiTGITAYSINPGITVTPLTHQFNSwlDVEP 189
Cdd:PRK12743 135 IINITSVHEHTPLPGASAYTAAKHALGGLTKAMAlELVE-HGILVNAVAPGAIATPMNGMDDS--DVKP 200
PRK06128 PRK06128
SDR family oxidoreductase;
71-177 5.23e-05

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 43.31  E-value: 5.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  71 LKTIDLLINGAGI---------LDDHQIERTIAINFTGLvntttaimqFWDKRKG----GPGGVIANICSVTGFNAIHQV 137
Cdd:PRK06128 132 LGGLDILVNIAGKqtavkdiadITTEQFDATFKTNVYAM---------FWLCKAAiphlPPGASIINTGSIQSYQPSPTL 202

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 699964346 138 PVYSASKAAVVSFTSSLAKLAPITGITAYSINPGITVTPL 177
Cdd:PRK06128 203 LDYASTKAAIVAFTKALAKQVAEKGIRVNAVAPGPVWTPL 242
PRK07856 PRK07856
SDR family oxidoreductase;
63-181 5.26e-05

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 43.00  E-value: 5.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  63 LLTTIFGKLKTIDLLINGAG-----ILDD-----HqiERTIAINFTGLVNTTT---AIMQFWDKrkggpGGVIANICSVT 129
Cdd:PRK07856  65 LVDAIVERHGRLDVLVNNAGgspyaLAAEasprfH--EKIVELNLLAPLLVAQaanAVMQQQPG-----GGSIVNIGSVS 137

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 699964346 130 GFNAIHQVPVYSASKAAVVSFTSSLA-KLAPITGITAysINPGITVTPLTHQF 181
Cdd:PRK07856 138 GRRPSPGTAAYGAAKAGLLNLTRSLAvEWAPKVRVNA--VVVGLVRTEQSELH 188
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
 74-185 7.17e-05

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 42.82  E-value: 7.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  74 IDLLINGAGILDDHQI--------ERTIAINFTGLVNTTTAIMQFWDKRKGGPggvIANICSVTGFNAIHQVPVYSASKA 145
Cdd:PRK08085  87 IDVLINNAGIQRRHPFtefpeqewNDVIAVNQTAVFLVSQAVARYMVKRQAGK---IINICSMQSELGRDTITPYAASKG 163

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 699964346 146 AVVSFTSSLAKLAPITGITAYSINPGITVTPLT------HQFNSWL 185
Cdd:PRK08085 164 AVKMLTRGMCVELARHNIQVNGIAPGYFKTEMTkalvedEAFTAWL 209
PRK06194 PRK06194
hypothetical protein; Provisional
 2-154 7.18e-05

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 43.08  E-value: 7.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   2 ALGGVGLATSKEIVKRGPKnfVVLDRIENP---KALAELKALNPKVtVSFYLyDVTVPvtETVKLLT----TIFGKlktI 74
Cdd:PRK06194  14 AASGFGLAFARIGAALGMK--LVLADVQQDaldRAVAELRAQGAEV-LGVRT-DVSDA--AQVEALAdaalERFGA---V 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  75 DLLINGAGI-----LDDHQI---ERTIAINFTGLVNTT---TAIMQFWDKRKGGPGGVIANICSVTGFNAIHQVPVYSAS 143
Cdd:PRK06194  85 HLLFNNAGVgagglVWENSLadwEWVLGVNLWGVIHGVrafTPLMLAAAEKDPAYEGHIVNTASMAGLLAPPAMGIYNVS 164

                        170
                 ....*....|.
gi 699964346 144 KAAVVSFTSSL 154
Cdd:PRK06194 165 KHAVVSLTETL 175
PRK06947 PRK06947
SDR family oxidoreductase;
64-175 1.18e-04

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 42.10  E-value: 1.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  64 LTTIFGKLktiDLLINGAGI---------LDDHQIERTIAINFTGLVNTTTAIMQFWDKRKGGPGGVIANICSVTG-FNA 133
Cdd:PRK06947  74 VQSAFGRL---DALVNNAGIvapsmpladMDAARLRRMFDTNVLGAYLCAREAARRLSTDRGGRGGAIVNVSSIASrLGS 150

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 699964346 134 IHQVPVYSASKAAVVSFTSSLAK-LAPiTGITAYSINPGITVT 175
Cdd:PRK06947 151 PNEYVDYAGSKGAVDTLTLGLAKeLGP-HGVRVNAVRPGLIET 192
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
 2-91 1.30e-04

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: 42.35  E-value: 1.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   2 ALGGVGLATSKEIVKRGPKNFVVLDR-------IENPKALAELKALNPKVTVsfylydVTVPVTETV---KLLTTIFGKL 71
Cdd:cd08953  213 GAGGIGRALARALARRYGARLVLLGRsplppeeEWKAQTLAALEALGARVLY------ISADVTDAAavrRLLEKVRERY 286

                         90       100
                 ....*....|....*....|
gi 699964346  72 KTIDLLINGAGILDDHQIER 91
Cdd:cd08953  287 GAIDGVIHAAGVLRDALLAQ 306
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
 1-207 1.37e-04

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: 42.14  E-value: 1.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   1 AALGGVGLATSKEIVKRGPKNFVVLDRIEN-PKALAELKALNPKVTVSFylydVTVPVTET-VKLLTTIFGKLKTIDLLI 78
Cdd:cd08936   17 ASTDGIGLAIARRLAQDGAHVVVSSRKQQNvDRAVATLQGEGLSVTGTV----CHVGKAEDrERLVATAVNLHGGVDILV 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  79 NGAG-------ILD--DHQIERTIAINFTGLVNTTTAIMQFWDKRKGGPGGVIAnicSVTGFNAIHQVPVYSASKAAVVS 149
Cdd:cd08936   93 SNAAvnpffgnILDstEEVWDKILDVNVKATALMTKAVVPEMEKRGGGSVVIVS---SVAAFHPFPGLGPYNVSKTALLG 169

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 699964346 150 FTSSLA-KLAPiTGITAYSINPGITVTPLTHQFnsWLD--VEPRVAELLNEHPTQTTEECG 207
Cdd:cd08936  170 LTKNLApELAP-RNIRVNCLAPGLIKTSFSSAL--WMDkaVEESMKETLRIRRLGQPEDCA 227
haloalcohol_DH_SDR_c-like cd05361
haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. ...
 78-170 1.43e-04

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


Pssm-ID: 187619 [Multi-domain]  Cd Length: 242  Bit Score: 41.79  E-value: 1.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  78 INGAGILDDHQIERTIAINFTGLVNTTTAIMQfwdKRKGGPggvIANICSVTGFNAIHQVPVYSASKAAVVSFTSSLAKL 157
Cdd:cd05361   89 IDGTSEADIRQAFEALSIFPFALLQAAIAQMK---KAGGGS---IIFITSAVPKKPLAYNSLYGPARAAAVALAESLAKE 162

                         90
                 ....*....|...
gi 699964346 158 APITGITAYSINP 170
Cdd:cd05361  163 LSRDNILVYAIGP 175
PRK05876 PRK05876
short chain dehydrogenase; Provisional
 5-177 2.18e-04

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 41.48  E-value: 2.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   5 GVGLATSKEIVKRGPKnfVVLDRIENPKALAELKALNPKvtvSFYLYDVTVPV---TETVKLLTTIFGKLKTIDLLINGA 81
Cdd:PRK05876  17 GIGLATGTEFARRGAR--VVLGDVDKPGLRQAVNHLRAE---GFDVHGVMCDVrhrEEVTHLADEAFRLLGHVDVVFSNA 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  82 GIL----------DDHQIerTIAINFTGLVNTTTAIMQFWDKRkgGPGGVIANICSVTGFNAIHQVPVYSASKAAVVSFT 151
Cdd:PRK05876  92 GIVvggpivemthDDWRW--VIDVDLWGSIHTVEAFLPRLLEQ--GTGGHVVFTASFAGLVPNAGLGAYGVAKYGVVGLA 167

                        170       180
                 ....*....|....*....|....*.
gi 699964346 152 SSLAKLAPITGITAYSINPGITVTPL 177
Cdd:PRK05876 168 ETLAREVTADGIGVSVLCPMVVETNL 193
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
 2-91 2.27e-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: 40.62  E-value: 2.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346    2 ALGGVGLATSKEIVKRGPKNFVVLDR--IENPKALAELKALNPK-VTVSFYLYDVTVPvTETVKLLTTIFGKLKTIDLLI 78
Cdd:pfam08659   8 GLGGLGRELARWLAERGARHLVLLSRsaAPRPDAQALIAELEARgVEVVVVACDVSDP-DAVAALLAEIKAEGPPIRGVI 86

                          90
                  ....*....|...
gi 699964346   79 NGAGILDDHQIER 91
Cdd:pfam08659  87 HAAGVLRDALLEN 99
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
 4-177 3.71e-04

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


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 40.71  E-value: 3.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   4 GGVGLATSKEIVKRGPKnFVVLDRieNPKALAELKALNPKVTVSFyLYDVTV------PVTETVklltTIFGKLktiDLL 77
Cdd:PRK06200  16 SGIGRALVERFLAEGAR-VAVLER--SAEKLASLRQRFGDHVLVV-EGDVTSyadnqrAVDQTV----DAFGKL---DCF 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  78 INGAGILD---------DHQIERT----IAINFTGLVNTTTAIMqfwDKRKGGPGGVIANIcSVTGFNAIHQVPVYSASK 144
Cdd:PRK06200  85 VGNAGIWDyntslvdipAETLDTAfdeiFNVNVKGYLLGAKAAL---PALKASGGSMIFTL-SNSSFYPGGGGPLYTASK 160

                        170       180       190
                 ....*....|....*....|....*....|....
gi 699964346 145 AAVVSFTSSLA-KLAPitGITAYSINPGITVTPL 177
Cdd:PRK06200 161 HAVVGLVRQLAyELAP--KIRVNGVAPGGTVTDL 192
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
 23-171 4.49e-04

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: 40.53  E-value: 4.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  23 VVLDrIENPKALAELKALNPKVTVSFYLY--DVT--VPVTETVKLLTTIFgklKTIDLLINGAGILDDHQI--------E 90
Cdd:cd05322   30 AVAD-INSENAEKVADEINAEYGEKAYGFgaDATneQSVIALSKGVDEIF---KRVDLLVYSAGIAKSAKItdfelgdfD 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  91 RTIAINFTG---LVNTTTAIMQfwdkrKGGPGGVIANICSVTGFNAIHQVPVYSASKAAVVSFTSSLAKLAPITGITAYS 167
Cdd:cd05322  106 RSLQVNLVGyflCAREFSKLMI-----RDGIQGRIIQINSKSGKVGSKHNSGYSAAKFGGVGLTQSLALDLAEHGITVNS 180


                 ....
gi 699964346 168 INPG 171
Cdd:cd05322  181 LMLG 184
PRK07985 PRK07985
SDR family oxidoreductase;
63-177 4.59e-04

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 40.36  E-value: 4.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  63 LLTTIFGKLKTIDLLINgagiLDDHQIERTIAINFTGLvntttaimqFWDKRKGGP----GGVIANICSVTGFNAIHQVP 138
Cdd:PRK07985 131 IMALVAGKQVAIPDIAD----LTSEQFQKTFAINVFAL---------FWLTQEAIPllpkGASIITTSSIQAYQPSPHLL 197

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 699964346 139 VYSASKAAVVSFTSSLAKLAPITGITAYSINPGITVTPL 177
Cdd:PRK07985 198 DYAATKAAILNYSRGLAKQVAEKGIRVNIVAPGPIWTAL 236
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
 74-176 5.19e-04

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: 40.20  E-value: 5.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  74 IDLLIN--GAGIL-------DDHQIERTIAIN-FTGLvntttaimqfWDKRKGGPG------GVIANICSVTGFNaIHQV 137
Cdd:cd08937   81 VDVLINnvGGTIWakpyehyEEEQIEAEIRRSlFPTL----------WCCRAVLPHmlerqqGVIVNVSSIATRG-IYRI 149

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 699964346 138 PvYSASKAAVVSFTSSLAKLAPITGITAYSINPGITVTP 176
Cdd:cd08937  150 P-YSAAKGGVNALTASLAFEHARDGIRVNAVAPGGTEAP 187
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
 5-177 8.04e-04

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: 39.76  E-value: 8.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   5 GVGLATSKEIVKRGPKnfVVL---DRIENPKALAEL--KALNPKVTVSfylyDVTVPVTETVK-LLTTIFGKLKTIDLLI 78
Cdd:cd09807   12 GIGKETARELARRGAR--VIMacrDMAKCEEAAAEIrrDTLNHEVIVR----HLDLASLKSIRaFAAEFLAEEDRLDVLI 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  79 NGAGIL------DDHQIERTIAINFTGLVNTTTAIMqfwDKRKGGPGGVIANICSVT-----------GFNAIHQVPV-Y 140
Cdd:cd09807   86 NNAGVMrcpyskTEDGFEMQFGVNHLGHFLLTNLLL---DLLKKSAPSRIVNVSSLAhkagkinfddlNSEKSYNTGFaY 162

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 699964346 141 SASKAAVVSFTSSLAKLAPITGITAYSINPGITVTPL 177
Cdd:cd09807  163 CQSKLANVLFTRELARRLQGTGVTVNALHPGVVRTEL 199
PRK05866 PRK05866
SDR family oxidoreductase;
2-154 8.70e-04

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 39.72  E-value: 8.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   2 ALGGVGLATSKEIVKRGPKNFVVLDRIENPKALAE--LKALNPKVTVSFYLYDVtvpvtETV-KLLTTIFGKLKTIDLLI 78
Cdd:PRK05866  48 ASSGIGEAAAEQFARRGATVVAVARREDLLDAVADriTRAGGDAMAVPCDLSDL-----DAVdALVADVEKRIGGVDILI 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  79 NGAG---------ILDD-HQIERTIAINFTGLVNTTTAIMQFWDKRKGGpggviaNICSVTGFNAIHQVP----VYSASK 144
Cdd:PRK05866 123 NNAGrsirrplaeSLDRwHDVERTMVLNYYAPLRLIRGLAPGMLERGDG------HIINVATWGVLSEASplfsVYNASK 196

                        170
                 ....*....|
gi 699964346 145 AAVVSFTSSL 154
Cdd:PRK05866 197 AALSAVSRVI 206
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
 63-171 8.87e-04

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: 39.39  E-value: 8.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  63 LLTTIFGKLKTIDLLINGAGI-----LDDHQI---ERTIAINFTGLVNTTTAIMQFWDKRK--GGPGGVIaNICSVTGFN 132
Cdd:cd08942   72 LVARVAERSDRLDVLVNNAGAtwgapLEAFPEsgwDKVMDINVKSVFFLTQALLPLLRAAAtaENPARVI-NIGSIAGIV 150

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 699964346 133 AI-HQVPVYSASKAAVVSFTSSLAKLAPITGITAYSINPG 171
Cdd:cd08942  151 VSgLENYSYGASKAAVHQLTRKLAKELAGEHITVNAIAPG 190
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 23-178 1.04e-03

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


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 39.82  E-value: 1.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  23 VVLDRienPKALAELKALNPKVTVSFYLYDVTVP--VTETVKLLTTIFGKLktiDLLINGAGI--------LDDHQIERT 92
Cdd:PRK08261 238 VCLDV---PAAGEALAAVANRVGGTALALDITAPdaPARIAEHLAERHGGL---DIVVHNAGItrdktlanMDEARWDSV 311

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  93 IAINFTGLVNTTTAIMqfwDKRKGGPGGVIANICSVTGF-------NaihqvpvYSASKAAVVSFTSSLAKLAPITGITA 165
Cdd:PRK08261 312 LAVNLLAPLRITEALL---AAGALGDGGRIVGVSSISGIagnrgqtN-------YAASKAGVIGLVQALAPLLAERGITI 381

                        170
                 ....*....|...
gi 699964346 166 YSINPGITVTPLT 178
Cdd:PRK08261 382 NAVAPGFIETQMT 394
PRK05693 PRK05693
SDR family oxidoreductase;
52-171 1.09e-03

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 39.39  E-value: 1.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  52 DVTVPvTETVKLLTTIFGKLKTIDLLINGAG------ILDD--HQIERTIAINFTGLVNTTTAIMQFWDKRKGgpggVIA 123
Cdd:PRK05693  52 DVNDG-AALARLAEELEAEHGGLDVLINNAGygamgpLLDGgvEAMRRQFETNVFAVVGVTRALFPLLRRSRG----LVV 126

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 699964346 124 NICSVTGFNAIHQVPVYSASKAAVVSFTSSL-AKLAPItGITAYSINPG 171
Cdd:PRK05693 127 NIGSVSGVLVTPFAGAYCASKAAVHALSDALrLELAPF-GVQVMEVQPG 174
PRK06139 PRK06139
SDR family oxidoreductase;
2-182 1.10e-03

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 39.32  E-value: 1.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346   2 ALGGVGLATSKEIVKRGPKnFVVLDRieNPKALAEL----KALNPKVTVsfylydVTVPVT--ETVKLLTT----IFGKl 71
Cdd:PRK06139  15 ASSGIGQATAEAFARRGAR-LVLAAR--DEEALQAVaeecRALGAEVLV------VPTDVTdaDQVKALATqaasFGGR- 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  72 ktIDLLINGAGI----------LDDHqiERTIAINFTGLVNTTTAIMQFWDKRKGGpggVIANICSVTGFNAIHQVPVYS 141
Cdd:PRK06139  85 --IDVWVNNVGVgavgrfeetpIEAH--EQVIQTNLIGYMRDAHAALPIFKKQGHG---IFINMISLGGFAAQPYAAAYS 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 699964346 142 ASKAAVVSFTSSL-AKLAPITGITAYSINPGITVTP-LTHQFN 182
Cdd:PRK06139 158 ASKFGLRGFSEALrGELADHPDIHVCDVYPAFMDTPgFRHGAN 200
PLN02253 PLN02253
xanthoxin dehydrogenase
 38-177 1.24e-03

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 39.04  E-value: 1.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  38 KALNPKVTVSFYLYDVTVP--VTETVKLLTTIFGklkTIDLLINGAGI----------LDDHQIERTIAINFTG--LVNT 103
Cdd:PLN02253  60 DSLGGEPNVCFFHCDVTVEddVSRAVDFTVDKFG---TLDIMVNNAGLtgppcpdirnVELSEFEKVFDVNVKGvfLGMK 136

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 699964346 104 TTAIMQFWDKRkggpgGVIANICSVTGFNAIHQVPVYSASKAAVVSFTSSLAKLAPITGITAYSINPGITVTPL 177
Cdd:PLN02253 137 HAARIMIPLKK-----GSIVSLCSVASAIGGLGPHAYTGSKHAVLGLTRSVAAELGKHGIRVNCVSPYAVPTAL 205
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
 62-192 4.00e-03

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: 37.26  E-value: 4.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699964346  62 KLLTTIFGKLKTIDLLINGAGILDDHQIERTIAINFTGL--VNTTTA---IMQFWDKRKGGPGGVIANICS--VTGFNAI 134
Cdd:cd05357   67 DLVAAAFRAFGRCDVLVNNASAFYPTPLGQGSEDAWAELfgINLKAPyllIQAFARRLAGSRNGSIINIIDamTDRPLTG 146

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 699964346 135 HqvPVYSASKAAVVSFTSSLA-KLAPitGITAYSINPGITVTPLTHQFNSWLDVEPRVA 192
Cdd:cd05357  147 Y--FAYCMSKAALEGLTRSAAlELAP--NIRVNGIAPGLILLPEDMDAEYRENALRKVP 201
 
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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