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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007637551   4 RVAVVTGSNKGIGLAIVRALCKQFQGDVYLTARDVGRGQEAVESLVSEGLKPMFHQLDINDLSSITTAAAYFKDKYGGVD 83
Cdd:cd05324     1 KVALVTGANRGIGFEIVRQLAKSGPGTVILTARDVERGQAAVEKLRAEGLSVRFHQLDVTDDASIEAAADFVEEKYGGLD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007637551  84 VLVSNAGIAFKVAD-KTPFAVQAEVTLKTNFFATRDMLTHFLPIIK--SGGRVVNVSSFVGSRTlnqcspalqqrfrsed 160
Cdd:cd05324    81 ILVNNAGIAFKGFDdSTPTREQARETMKTNFFGTVDVTQALLPLLKksPAGRIVNVSSGLGSLT---------------- 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007637551 161 itedelvglmqqfvdetkkdqhkqggwpeTAYGVSKTGLTTLSMILARRLSKerpnDGILLNACCPGWVRTDMAGPKAPR 240
Cdd:cd05324   145 -----------------------------SAYGVSKAALNALTRILAKELKE----TGIKVNACCPGWVKTDMGGGKAPK 191

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 2007637551 241 SPDEGAVTPVYLALLPPGATaPHGKFVNDKEVQPW 275
Cdd:cd05324   192 TPEEGAETPVYLALLPPDGE-PTGKFFSDKKVVPW 225

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007637551   4 RVAVVTGSNKGIGLAIVRALCKQFQGDVYLTARDVGRGQEAVESLVSEGLKPMFHQLDINDLSSITTAAAYFKDKYGGVD 83
Cdd:cd05324     1 KVALVTGANRGIGFEIVRQLAKSGPGTVILTARDVERGQAAVEKLRAEGLSVRFHQLDVTDDASIEAAADFVEEKYGGLD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007637551  84 VLVSNAGIAFKVAD-KTPFAVQAEVTLKTNFFATRDMLTHFLPIIK--SGGRVVNVSSFVGSRTlnqcspalqqrfrsed 160
Cdd:cd05324    81 ILVNNAGIAFKGFDdSTPTREQARETMKTNFFGTVDVTQALLPLLKksPAGRIVNVSSGLGSLT---------------- 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007637551 161 itedelvglmqqfvdetkkdqhkqggwpeTAYGVSKTGLTTLSMILARRLSKerpnDGILLNACCPGWVRTDMAGPKAPR 240
Cdd:cd05324   145 -----------------------------SAYGVSKAALNALTRILAKELKE----TGIKVNACCPGWVKTDMGGGKAPK 191

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 2007637551 241 SPDEGAVTPVYLALLPPGATaPHGKFVNDKEVQPW 275
Cdd:cd05324   192 TPEEGAETPVYLALLPPDGE-PTGKFFSDKKVVPW 225

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007637551   4 RVAVVTGSNKGIGLAIVRALCKQfQGDVYLTARDVGRGQEAVESLVSEGLKPMFHQLDINDLSSITTAAAYFKDKYGGVD 83
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKE-GAKVVLVDRSEEKLEAVAKELGALGGKALFIQGDVTDRAQVKALVEQAVERLGRLD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007637551  84 VLVSNAGIafkvadkTPFAVQAEVTLK-------TNFFATRDMLTHFLP--IIKSGGRVVNVSSfvgsrtlnqcspalqq 154
Cdd:pfam00106  80 ILVNNAGI-------TGLGPFSELSDEdwervidVNLTGVFNLTRAVLPamIKGSGGRIVNISS---------------- 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007637551 155 rfrseditedeLVGLMqqfvdetkkdqhkqgGWPE-TAYGVSKTGLTTLSMILARRLSKerpnDGILLNACCPGWVRTDM 233
Cdd:pfam00106 137 -----------VAGLV---------------PYPGgSAYSASKAAVIGFTRSLALELAP----HGIRVNAVAPGGVDTDM 186

                  ....*.
gi 2007637551 234 AGPKAP 239
Cdd:pfam00106 187 TKELRE 192

acetoacetyl-CoA reductase; This model represent acetoacetyl-CoA reductase, a member of the family short-chain-alcohol dehydrogenases. Note that, despite the precision implied by the enzyme name, the reaction of EC 1.1.1.36 is defined more generally as (R)-3-hydroxyacyl-CoA + NADP+ = 3-oxoacyl-CoA + NADPH. Members of this family may act in the biosynthesis of poly-beta-hydroxybutyrate (e.g. Rhizobium meliloti) and related poly-beta-hydroxyalkanoates. Note that the member of this family from Azospirillum brasilense, designated NodG, appears to lack acetoacetyl-CoA reductase activity and to act instead in the production of nodulation factor. This family is downgraded to subfamily for this NodG. Other proteins designated NodG, as from Rhizobium, belong to related but distinct protein families.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007637551   4 RVAVVTGSNKGIGLAIvralCKQFQGDVYLTARDVG----RGQEAVESLVSEGLKPMFHQLDINDLSSITTAAAYFKDKY 79
Cdd:TIGR01829   1 RIALVTGGMGGIGTAI----CQRLAKDGYRVAANCGpneeRAEAWLQEQGALGFDFRVVEGDVSSFESCKAAVAKVEAEL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007637551  80 GGVDVLVSNAGIA----FKVADKTPFAVQAEVTLKTNFFATRDMLTHFLPiiKSGGRVVNVSSFVGSRtlnqcspalqqr 155
Cdd:TIGR01829  77 GPVDVLVNNAGITrdatFKKMTYEQWDAVIDTNLNSVFNVTQPVIDGMRE--RGWGRIINISSVNGQK------------ 142

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2007637551 156 frseditedelvGLMQQfvdetkkdqhkqggwpeTAYGVSKTGLTTLSMILARRLSKErpndGILLNACCPGWVRTDM 233
Cdd:TIGR01829 143 ------------GQFGQ-----------------TNYSAAKAGMIGFTKALAQEGATK----GVTVNTISPGYIATDM 187

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007637551   4 RVAVVTGSNKGIGLAIVRALCKQFQGDVYLTARDVGRGQEAVESLVSEGLKPMFHQLDINDLSSITTAAAYFKDKYGGVD 83
Cdd:cd05324     1 KVALVTGANRGIGFEIVRQLAKSGPGTVILTARDVERGQAAVEKLRAEGLSVRFHQLDVTDDASIEAAADFVEEKYGGLD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007637551  84 VLVSNAGIAFKVAD-KTPFAVQAEVTLKTNFFATRDMLTHFLPIIK--SGGRVVNVSSFVGSRTlnqcspalqqrfrsed 160
Cdd:cd05324    81 ILVNNAGIAFKGFDdSTPTREQARETMKTNFFGTVDVTQALLPLLKksPAGRIVNVSSGLGSLT---------------- 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007637551 161 itedelvglmqqfvdetkkdqhkqggwpeTAYGVSKTGLTTLSMILARRLSKerpnDGILLNACCPGWVRTDMAGPKAPR 240
Cdd:cd05324   145 -----------------------------SAYGVSKAALNALTRILAKELKE----TGIKVNACCPGWVKTDMGGGKAPK 191

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 2007637551 241 SPDEGAVTPVYLALLPPGATaPHGKFVNDKEVQPW 275
Cdd:cd05324   192 TPEEGAETPVYLALLPPDGE-PTGKFFSDKKVVPW 225

Short-chain dehydrogenase [General function prediction only];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007637551   1 MSTRVAVVTGSNKGIGLAIVRALCKQfqG-DVYLTARDVGRGQEAVESLVSEGLKPMFHQLDINDLSSITTAAAYFKDKY 79
Cdd:COG0300     3 LTGKTVLITGASSGIGRALARALAAR--GaRVVLVARDAERLEALAAELRAAGARVEVVALDVTDPDAVAALAEAVLARF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007637551  80 GGVDVLVSNAGIA-FKVADKTPFAVQAEVtLKTNFFATRDMLTHFLPIIKS--GGRVVNVSSFVGSRTLNQCSpalqqrf 156
Cdd:COG0300    81 GPIDVLVNNAGVGgGGPFEELDLEDLRRV-FEVNVFGPVRLTRALLPLMRArgRGRIVNVSSVAGLRGLPGMA------- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007637551 157 rseditedelvglmqqfvdetkkdqhkqggwpetAYGVSKTGLTTLSMILARRLSKerpnDGILLNACCPGWVRTDMAGp 236
Cdd:COG0300   153 ----------------------------------AYAASKAALEGFSESLRAELAP----TGVRVTAVCPGPVDTPFTA- 193

                         250
                  ....*....|...
gi 2007637551 237 KAPRSPDEGAVTP 249
Cdd:COG0300   194 RAGAPAGRPLLSP 206

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007637551   4 RVAVVTGSNKGIGLAIVRALCKQfQGDVYLTARDVGRGQEAVESLVSEGL--KPMFHQLDINDLSSITTAAAYFKDKYGG 81
Cdd:cd05327     2 KVVVITGANSGIGKETARELAKR-GAHVIIACRNEEKGEEAAAEIKKETGnaKVEVIQLDLSSLASVRQFAEEFLARFPR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007637551  82 VDVLVSNAGIAFKVADKTPFAVqaEVTLKTNFFAtrdmltHFL------PIIK--SGGRVVNVSSfvgsrtlnqcspalq 153
Cdd:cd05327    81 LDILINNAGIMAPPRRLTKDGF--ELQFAVNYLG------HFLltnlllPVLKasAPSRIVNVSS--------------- 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007637551 154 qrfrseditedelvgLMQQFVDETKKDQHKQGG---WPETAYGVSKTGLTTLSMILARRLSKerpnDGILLNACCPGWVR 230
Cdd:cd05327   138 ---------------IAHRAGPIDFNDLDLENNkeySPYKAYGQSKLANILFTRELARRLEG----TGVTVNALHPGVVR 198

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2007637551 231 TDM-------------AGPKAPRSPDEGAVTPVYLALLPPGATAPHGKFVNDKEVQP 274
Cdd:cd05327   199 TELlrrngsffllyklLRPFLKKSPEQGAQTALYAATSPELEGVSGKYFSDCKIKMS 255

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007637551   6 AVVTGSNKGIGLAIVRALCKQFQGDVYLTARDVGRGQEAvESLVSEGLKPMFHQLDINDLssITTAAAYFKDKYG--GVD 83
Cdd:cd05325     1 VLITGASRGIGLELVRQLLARGNNTVIATCRDPSAATEL-AALGASHSRLHILELDVTDE--IAESAEAVAERLGdaGLD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007637551  84 VLVSNAGIA--FKVADKTPFAVQAEvTLKTNFFATRDMLTHFLPIIKSGGR--VVNVSSFVGSRTLNQcspalqqrfrse 159
Cdd:cd05325    78 VLINNAGILhsYGPASEVDSEDLLE-VFQVNVLGPLLLTQAFLPLLLKGARakIINISSRVGSIGDNT------------ 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007637551 160 ditedelvglmqqfvdetkkdqhkQGGWpeTAYGVSKTGLTtlsmILARRLSKERPNDGILLNACCPGWVRTDMAGPKAp 239
Cdd:cd05325   145 ------------------------SGGW--YSYRASKAALN----MLTKSLAVELKRDGITVVSLHPGWVRTDMGGPFA- 193

                         250
                  ....*....|..
gi 2007637551 240 rsPDEGAVTPVY 251
Cdd:cd05325   194 --KNKGPITPEE 203

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007637551   1 MSTRVAVVTGSNKGIGLAIVRALCKQfqG-DVYL-TARDVGRGQEAVESLVSEGLKPMFHQLDINDLSSITTAAAYFKDK 78
Cdd:PRK05557    3 LEGKVALVTGASRGIGRAIAERLAAQ--GaNVVInYASSEAGAEALVAEIGALGGKALAVQGDVSDAESVERAVDEAKAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007637551  79 YGGVDVLVSNAGIA-------FKVADKtpFAVQAeVTLKTNFFATRDMLTHFLPiiKSGGRVVNVSSFvgsrtlnqcspa 151
Cdd:PRK05557   81 FGGVDILVNNAGITrdnllmrMKEEDW--DRVID-TNLTGVFNLTKAVARPMMK--QRSGRIINISSV------------ 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007637551 152 lqqrfrseditedelVGLMQQFvdetkkdqhkqGGwpeTAYGVSKTGLTTLSMILARRL-SKerpndGILLNACCPGWVR 230
Cdd:PRK05557  144 ---------------VGLMGNP-----------GQ---ANYAASKAGVIGFTKSLARELaSR-----GITVNAVAPGFIE 189

                  ...
gi 2007637551 231 TDM 233
Cdd:PRK05557  190 TDM 192

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007637551   4 RVAVVTGSNKGIGLAIVRALCKQfqG-DVYLTARDVGRGQEAVESLVSEGLKPMFHQLDINDLSSITTAAAYFKDKYGGV 82
Cdd:cd05333     1 KVALVTGASRGIGRAIALRLAAE--GaKVAVTDRSEEAAAETVEEIKALGGNAAALEADVSDREAVEALVEKVEAEFGPV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007637551  83 DVLVSNAGIafkVADKTPFAVQAE-------VTLKTNFFATRdMLTHflPIIKSG-GRVVNVSSFVGsrtlnqcspalqq 154
Cdd:cd05333    79 DILVNNAGI---TRDNLLMRMSEEdwdavinVNLTGVFNVTQ-AVIR--AMIKRRsGRIINISSVVG------------- 139

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2007637551 155 rfrseditedeLVGLMQQfvdetkkdqhkqggwpeTAYGVSKTGLTTLSMILARRLSKErpndGILLNACCPGWVRTDM 233
Cdd:cd05333   140 -----------LIGNPGQ-----------------ANYAASKAGVIGFTKSLAKELASR----GITVNAVAPGFIDTDM 186

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007637551  11 SNKGIGLAIVRALCKQfqG-DVYLTARDvGRGQEAVESLVSEgLKPMFHQLDINDLSSITTAAAYFKDKYGGVDVLVSNA 89
Cdd:pfam13561   4 NESGIGWAIARALAEE--GaEVVLTDLN-EALAKRVEELAEE-LGAAVLPCDVTDEEQVEALVAAAVEKFGRLDILVNNA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007637551  90 GIAFKVadKTPFA-VQAE---VTLKTNFFATRDMLTHFLPIIKSGGRVVNVSSFVGSRtlnqcspalqqrfrseditede 165
Cdd:pfam13561  80 GFAPKL--KGPFLdTSREdfdRALDVNLYSLFLLAKAALPLMKEGGSIVNLSSIGAER---------------------- 135

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007637551 166 lvglmqqfvdetkkdqhkqgGWP-ETAYGVSKTGLTTLSMILARRLSKerpnDGILLNACCPGWVRTDMA 234
Cdd:pfam13561 136 --------------------VVPnYNAYGAAKAALEALTRYLAVELGP----RGIRVNAISPGPIKTLAA 181

short chain dehydrogenase; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007637551   1 MSTRVAVVTGSNKGIGLAIVRALCKQfQGDVYLTARDVGRGQEAVESLVSEGLKPMFHQLDINDLSSITTAAAYFKDKYG 80
Cdd:PRK12939    5 LAGKRALVTGAARGLGAAFAEALAEA-GATVAFNDGLAAEARELAAALEAAGGRAHAIAADLADPASVQRFFDAAAAALG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007637551  81 GVDVLVSNAGIAfKVADKTPFAVQA-----EVTLKTNFFATRDMLTHFlpIIKSGGRVVNVSSfvgsrtlnqcSPALQQr 155
Cdd:PRK12939   84 GLDGLVNNAGIT-NSKSATELDIDTwdavmNVNVRGTFLMLRAALPHL--RDSGRGRIVNLAS----------DTALWG- 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007637551 156 frseditedeLVGLMqqfvdetkkdqhkqggwpetAYGVSKTGLTTLSMILARRLSKerpnDGILLNACCPGWVRTDM-- 233
Cdd:PRK12939  150 ----------APKLG--------------------AYVASKGAVIGMTRSLARELGG----RGITVNAIAPGLTATEAta 195

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 2007637551 234 AGPKAPR-------SPDEGAVTP-------VYLAllppgatAPHGKFVN 268
Cdd:PRK12939  196 YVPADERhayylkgRALERLQVPddvagavLFLL-------SDAARFVT 237

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007637551   4 RVAVVTGSNKGIGLAIVRALCKQfqGD-VYLTARDvgrgQEAVESLVSEGLKPMFH-QLDINDLSSITTAAAYFKDKYGG 81
Cdd:cd05374     1 KVVLITGCSSGIGLALALALAAQ--GYrVIATARN----PDKLESLGELLNDNLEVlELDVTDEESIKAAVKEVIERFGR 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2007637551  82 VDVLVSNAGIAFK--VADKTPFAVQAevTLKTNFFATRDMLTHFLPIIKS--GGRVVNVSSFVG 141
Cdd:cd05374    75 IDVLVNNAGYGLFgpLEETSIEEVRE--LFEVNVFGPLRVTRAFLPLMRKqgSGRIVNVSSVAG 136

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007637551   4 RVAVVTGSNKGIGLAIVRALCKQfQGDVYLTARDVGRGQEAVESLVSEGLKPMFHQLDINDLSSITTAAAYFKDKYGGVD 83
Cdd:cd05347     6 KVALVTGASRGIGFGIASGLAEA-GANIVINSRNEEKAEEAQQLIEKEGVEATAFTCDVSDEEAIKAAVEAIEEDFGKID 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007637551  84 VLVSNAGIAFKV-ADKTP---FAVQAEVTLKTNFFATRDMLTHFLPiiKSGGRVVNVSSfvgsrtlnqcspalqqrfrse 159
Cdd:cd05347    85 ILVNNAGIIRRHpAEEFPeaeWRDVIDVNLNGVFFVSQAVARHMIK--QGHGKIINICS--------------------- 141

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2007637551 160 ditedelvglMQQFvdetkkdqhkQGGWPETAYGVSKTGLTTLSMILARRLSKerpnDGILLNACCPGWVRTDMAGP 236
Cdd:cd05347   142 ----------LLSE----------LGGPPVPAYAASKGGVAGLTKALATEWAR----HGIQVNAIAPGYFATEMTEA 194

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007637551   1 MSTRVAVVTGSNKGIGLAIVRALCKQfqG-DVYLTAR-DVGRGQEAVESLVSEGLKPMFHQLDINDLSSITTAAAYFKDK 78
Cdd:PRK12825    4 LMGRVALVTGAARGLGRAIALRLARA--GaDVVVHYRsDEEAAEELVEAVEALGRRAQAVQADVTDKAALEAAVAAAVER 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007637551  79 YGGVDVLVSNAGIAF--KVADKTP--FAVQAEVTLKTNFFATRdmltHFLPIIKS--GGRVVNVSSFVGSRtlnqcspal 152
Cdd:PRK12825   82 FGRIDILVNNAGIFEdkPLADMSDdeWDEVIDVNLSGVFHLLR----AVVPPMRKqrGGRIVNISSVAGLP--------- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007637551 153 qqrfrseditedelvglmqqfvdetkkdqhkqgGWP-ETAYGVSKTGLTTLSMILARRLSKErpndGILLNACCPGWVRT 231
Cdd:PRK12825  149 ---------------------------------GWPgRSNYAAAKAGLVGLTKALARELAEY----GITVNMVAPGDIDT 191

                  ....*
gi 2007637551 232 DMAGP 236
Cdd:PRK12825  192 DMKEA 196

SDR family oxidoreductase;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007637551   4 RVAVVTGSNKGIGLAIVRALCKQfQGDVYLTARDVGRGQEAVESLVSEGlKPMFHQLDINDLSSITTAAAYFKDKYGGVD 83
Cdd:PRK07231    6 KVAIVTGASSGIGEGIARRFAAE-GARVVVTDRNEEAAERVAAEILAGG-RAIAVAADVSDEADVEAAVAAALERFGSVD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007637551  84 VLVSNAGIAFK---VADKTP--FAVQAEVTLKTNFFATRDMLTHFLPiiKSGGRVVNVSSFVGSRTlnqcSPALqqrfrs 158
Cdd:PRK07231   84 ILVNNAGTTHRngpLLDVDEaeFDRIFAVNVKSPYLWTQAAVPAMRG--EGGGAIVNVASTAGLRP----RPGL------ 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2007637551 159 editedelvglmqqfvdetkkdqhkqggwpeTAYGVSKTGLTTLSMILARRLSkerpNDGILLNACCPGWVRTDMA 234
Cdd:PRK07231  152 -------------------------------GWYNASKGAVITLTKALAAELG----PDKIRVNAVAPVVVETGLL 192

short chain dehydrogenase; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007637551   2 STRVAVVTGSNKGIGLAIVRALCKQfQGDVYLTARDVGRGQEAVESLVSEGLKP--MFHQLDINDLSSITTAAAYFKDKY 79
Cdd:PRK06197   15 SGRVAVVTGANTGLGYETAAALAAK-GAHVVLAVRNLDKGKAAAARITAATPGAdvTLQELDLTSLASVRAAADALRAAY 93

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2007637551  80 GGVDVLVSNAGIAFkvadkTPFAVQA---EVTLKTN----FFATRDMLTHFLPIikSGGRVVNVSS 138
Cdd:PRK06197   94 PRIDLLINNAGVMY-----TPKQTTAdgfELQFGTNhlghFALTGLLLDRLLPV--PGSRVVTVSS 152