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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706934   7 KHVCYVADCGGIALETSKVLMTKNiAKLAILQSTENPQAIAQLQSIKPSTQIFFWTYDVTMaREDMKKYFDEVMVQMDYI 86
Cdd:cd05323   1 KVAIITGGASGIGLATAKLLLKKG-AKVAILDRNENPGAAAELQAINPKVKATFVQCDVTS-WEQLAAAFKKAIEKFGRV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706934  87 DVLINGATLCDEN----------NIDATINTNLTGMMNTVATVLPYMDRKMGGTGGLIVNVTSVIGLDPSPVFCAYSASK 156
Cdd:cd05323  79 DILINNAGILDEKsylfagklppPWEKTIDVNLTGVINTTYLALHYMDKNKGGKGGVIVNIGSVAGLYPAPQFPVYSASK 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706934 157 FGVIGFTRSLADPLYYsQNGVAVMAVCCGPTRVFVDRELKAFLeygqsfADRLRRAPCQSTSVCGQNIVNAIERSE-NGQ 235
Cdd:cd05323 159 HGVVGFTRSLADLLEY-KTGVRVNAICPGFTNTPLLPDLVAKE------AEMLPSAPTQSPEVVAKAIVYLIEDDEkNGA 231

                       250
                ....*....|...
gi 78706934 236 IWIADKGGLELVK 248
Cdd:cd05323 232 IWIVDGGKLIEIE 244

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706934   7 KHVCYVADCGGIALETSKVLMTKNiAKLAILQSTENPQAIAQLQSIKPSTQIFFWTYDVTMaREDMKKYFDEVMVQMDYI 86
Cdd:cd05323   1 KVAIITGGASGIGLATAKLLLKKG-AKVAILDRNENPGAAAELQAINPKVKATFVQCDVTS-WEQLAAAFKKAIEKFGRV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706934  87 DVLINGATLCDEN----------NIDATINTNLTGMMNTVATVLPYMDRKMGGTGGLIVNVTSVIGLDPSPVFCAYSASK 156
Cdd:cd05323  79 DILINNAGILDEKsylfagklppPWEKTIDVNLTGVINTTYLALHYMDKNKGGKGGVIVNIGSVAGLYPAPQFPVYSASK 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706934 157 FGVIGFTRSLADPLYYsQNGVAVMAVCCGPTRVFVDRELKAFLeygqsfADRLRRAPCQSTSVCGQNIVNAIERSE-NGQ 235
Cdd:cd05323 159 HGVVGFTRSLADLLEY-KTGVRVNAICPGFTNTPLLPDLVAKE------AEMLPSAPTQSPEVVAKAIVYLIEDDEkNGA 231

                       250
                ....*....|...
gi 78706934 236 IWIADKGGLELVK 248
Cdd:cd05323 232 IWIVDGGKLIEIE 244

Short-chain dehydrogenase [General function prediction only];

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706934  64 DVTmAREDMKKYFDEVMVQMDYIDVLINGA--------TLCDENNIDATINTNLTGMMNTVATVLPYMdRKMGGtgGLIV 135
Cdd:COG0300  62 DVT-DPDAVAALAEAVLARFGPIDVLVNNAgvggggpfEELDLEDLRRVFEVNVFGPVRLTRALLPLM-RARGR--GRIV 137

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 78706934 136 NVTSVIGLDPSPVFCAYSASKFGVIGFTRSLADPLyySQNGVAVMAVCCGPTR 188
Cdd:COG0300 138 NVSSVAGLRGLPGMAAYAASKAALEGFSESLRAEL--APTGVRVTAVCPGPVD 188

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706934   7 KHVCYVADCGGIALETSKVLMTKNiAKLAILQSTENPQAIAQLQSIKPSTQIFFWTYDVTMaREDMKKYFDEVMVQMDYI 86
Cdd:cd05323   1 KVAIITGGASGIGLATAKLLLKKG-AKVAILDRNENPGAAAELQAINPKVKATFVQCDVTS-WEQLAAAFKKAIEKFGRV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706934  87 DVLINGATLCDEN----------NIDATINTNLTGMMNTVATVLPYMDRKMGGTGGLIVNVTSVIGLDPSPVFCAYSASK 156
Cdd:cd05323  79 DILINNAGILDEKsylfagklppPWEKTIDVNLTGVINTTYLALHYMDKNKGGKGGVIVNIGSVAGLYPAPQFPVYSASK 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706934 157 FGVIGFTRSLADPLYYsQNGVAVMAVCCGPTRVFVDRELKAFLeygqsfADRLRRAPCQSTSVCGQNIVNAIERSE-NGQ 235
Cdd:cd05323 159 HGVVGFTRSLADLLEY-KTGVRVNAICPGFTNTPLLPDLVAKE------AEMLPSAPTQSPEVVAKAIVYLIEDDEkNGA 231

                       250
                ....*....|...
gi 78706934 236 IWIADKGGLELVK 248
Cdd:cd05323 232 IWIVDGGKLIEIE 244

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706934  16 GGIALETSKvLMTKNIAKLAIL-QSTENPQAIAQLQsiKPSTQIFFWTYDVTmAREDMKKYFDEVMVQMDYIDVLINGA- 93
Cdd:cd05233   8 SGIGRAIAR-RLAREGAKVVLAdRNEEALAELAAIE--ALGGNAVAVQADVS-DEEDVEALVEEALEEFGRLDILVNNAg 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706934  94 -------TLCDENNIDATINTNLTGMMNTVATVLPYMdrkMGGTGGLIVNVTSVIGLDPSPVFCAYSASKFGVIGFTRSL 166
Cdd:cd05233  84 iarpgplEELTDEDWDRVLDVNLTGVFLLTRAALPHM---KKQGGGRIVNISSVAGLRPLPGQAAYAASKAALEGLTRSL 160

                       170       180
                ....*....|....*....|..
gi 78706934 167 AdpLYYSQNGVAVMAVCCGPTR 188
Cdd:cd05233 161 A--LELAPYGIRVNAVAPGLVD 180

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706934   1 MFDLTGKhVCYV--ADcGGIALETSKVLMTKNiAKLAILQSTENP--QAIAQLQSIkpSTQIFFWTYDVTmAREDMKKYF 76
Cdd:COG1028   1 MTRLKGK-VALVtgGS-SGIGRAIARALAAEG-ARVVITDRDAEAleAAAAELRAA--GGRALAVAADVT-DEAAVEALV 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706934  77 DEVMVQMDYIDVLINGA--------TLCDENNIDATINTNLTGMMNTVATVLPYMdrkMGGTGGLIVNVTSVIGLDPSPV 148
Cdd:COG1028  75 AAAVAAFGRLDILVNNAgitppgplEELTEEDWDRVLDVNLKGPFLLTRAALPHM---RERGGGRIVNISSIAGLRGSPG 151

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 78706934 149 FCAYSASKFGVIGFTRSLAdpLYYSQNGVAVMAVCCGPTR 188
Cdd:COG1028 152 QAAYAASKAAVVGLTRSLA--LELAPRGIRVNAVAPGPID 189

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706934   64 DVTMArEDMKKYFDEVMVQMDYIDVLINGATLCDENNI--------DATINTNLTGMMNTVATVLPYMdrkMGGTGGLIV 135
Cdd:PRK05557  63 DVSDA-ESVERAVDEAKAEFGGVDILVNNAGITRDNLLmrmkeedwDRVIDTNLTGVFNLTKAVARPM---MKQRSGRII 138

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 78706934  136 NVTSVIGLDPSPVFCAYSASKFGVIGFTRSLADPLyySQNGVAVMAVCCGPTRV 189
Cdd:PRK05557 139 NISSVVGLMGNPGQANYAASKAGVIGFTKSLAREL--ASRGITVNAVAPGFIET 190

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 78706934  16 GGIALETSKVLMTKNiAKLAILQSTENPQAIAQLQSIKPSTQIFFWTYDVTmAREDMKKYFDEVMVQMDYIDVLINGATL 95
Cdd:cd05333  10 RGIGRAIALRLAAEG-AKVAVTDRSEEAAAETVEEIKALGGNAAALEADVS-DREAVEALVEKVEAEFGPVDILVNNAGI 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706934  96 C--------DENNIDATINTNLTGMMNTVATVLPYMDRKMGGTgglIVNVTSVIGLDPSPVFCAYSASKFGVIGFTRSLA 167
Cdd:cd05333  88 TrdnllmrmSEEDWDAVINVNLTGVFNVTQAVIRAMIKRRSGR---IINISSVVGLIGNPGQANYAASKAGVIGFTKSLA 164

                       170
                ....*....|....*...
gi 78706934 168 DPLyySQNGVAVMAVCCG 185
Cdd:cd05333 165 KEL--ASRGITVNAVAPG 180

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706934  47 AQLQSIK------PSTQIFFWTYDVTMArEDMKKYFDEVMVQMDYIDVLINGA-----TLCDENNID---ATINTNLTGM 112
Cdd:cd05332  38 ERLEEVKseclelGAPSPHVVPLDMSDL-EDAEQVVEEALKLFGGLDILINNAgismrSLFHDTSIDvdrKIMEVNYFGP 116

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706934 113 MNTVATVLPYMDRKmggTGGLIVNVTSVIGLDPSPVFCAYSASKFGVIGFTRSL-ADplyYSQNGVAVMAVCCGPtrVFV 191
Cdd:cd05332 117 VALTKAALPHLIER---SQGSIVVVSSIAGKIGVPFRTAYAASKHALQGFFDSLrAE---LSEPNISVTVVCPGL--IDT 188

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 78706934 192 DRELKAFLEYGQSFADRLRRAPCQSTSV-CGQNIVNAIERSENgQIWIADKGGLELVklhWYWHMADQFVHYM 263
Cdd:cd05332 189 NIAMNALSGDGSMSAKMDDTTANGMSPEeCALEILKAIALRKR-EVFYARQVPLLAV---YLRQLFPGLFDWL 257

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706934    12 VADCGGIALETSKvLMTKNIAKLAIL-QSTENPQAIAQLQSIKPSTqifFWTYDVTmAREDMKKYFDEVMVQMDYIDVLI 90
Cdd:pfam13561   2 AANESGIGWAIAR-ALAEEGAEVVLTdLNEALAKRVEELAEELGAA---VLPCDVT-DEEQVEALVAAAVEKFGRLDILV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706934    91 NGA----------TLCDENNIDATINTNLTGMMNTVATVLPYMDRkmggtGGLIVNVTSVIGLDPSPVFCAYSASKFGVI 160
Cdd:pfam13561  77 NNAgfapklkgpfLDTSREDFDRALDVNLYSLFLLAKAALPLMKE-----GGSIVNLSSIGAERVVPNYNAYGAAKAALE 151

                         170       180
                  ....*....|....*....|....*...
gi 78706934   161 GFTRSLAdpLYYSQNGVAVMAVCCGPTR 188
Cdd:pfam13561 152 ALTRYLA--VELGPRGIRVNAISPGPIK 177

short chain dehydrogenase; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706934   53 KPSTQIFFWTYDVTmAREDMKKYFDEVMVQMDYIDVLIN--GATL---CDENNID---ATINTNLTGMMNTVATVLPYMd 124
Cdd:PRK06179  42 APIPGVELLELDVT-DDASVQAAVDEVIARAGRIDVLVNnaGVGLagaAEESSIAqaqALFDTNVFGILRMTRAVLPHM- 119

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 78706934  125 RKMGGtgGLIVNVTSVIGLDPSPVFCAYSASKFGVIGFTRSL 166
Cdd:PRK06179 120 RAQGS--GRIINISSVLGFLPAPYMALYAASKHAVEGYSESL 159

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706934  17 GIALETSKVLMTKNIAKLAILQSTENPQAIAQLQSIKPSTQIFFWTYDVTMAREDMKKYFDEVmVQMDyIDVLINGATLC 96
Cdd:cd05356  12 GIGKAYAEELAKRGFNVILISRTQEKLDAVAKEIEEKYGVETKTIAADFSAGDDIYERIEKEL-EGLD-IGILVNNVGIS 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706934  97 ----------DENNIDATINTNLTGMMNTVATVLPYMDRKmggTGGLIVNVTSVIGLDPSPVFCAYSASKFGVIGFTRSL 166
Cdd:cd05356  90 hsipeyfletPEDELQDIINVNVMATLKMTRLILPGMVKR---KKGAIVNISSFAGLIPTPLLATYSASKAFLDFFSRAL 166

                       170
                ....*....|....*..
gi 78706934 167 AdpLYYSQNGVAVMAVC 183
Cdd:cd05356 167 Y--EEYKSQGIDVQSLL 181

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706934  16 GGIALETSKVLMTKNiAKLAILQSTENPQAIAQLQSIKPSTQIFFWTYDVTmAREDMKKYFDEVMVQMDYIDVLINGATL 95
Cdd:cd05339   9 SGIGRLLALEFAKRG-AKVVILDINEKGAEETANNVRKAGGKVHYYKCDVS-KREEVYEAAKKIKKEVGDVTILINNAGV 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706934  96 --------CDENNIDATINTNLTGMMNTVATVLPYM-DRKMGGtgglIVNVTSVIGLDPSPVFCAYSASKFGVIGFTRSL 166
Cdd:cd05339  87 vsgkklleLPDEEIEKTFEVNTLAHFWTTKAFLPDMlERNHGH----IVTIASVAGLISPAGLADYCASKAAAVGFHESL 162

                       170
                ....*....|....*...
gi 78706934 167 ADPL-YYSQNGVAVMAVC 183
Cdd:cd05339 163 RLELkAYGKPGIKTTLVC 180

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).

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706934  73 KKYFDEVMVQMDYIDVLINGATL--------CDENNIDATINTNLTGMMNTVATVLPYMDRKMGGTgglIVNVTSVIG-L 143
Cdd:cd05368  58 KEQVAALAKEEGRIDVLFNCAGFvhhgsildCEDDDWDFAMNLNVRSMYLMIKAVLPKMLARKDGS---IINMSSVASsI 134

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 78706934 144 DPSPVFCAYSASKFGVIGFTRSLAdpLYYSQNGVAVMAVCCGPTRVFVDRE-LKAFLEYGQSFADRLRRAP 213
Cdd:cd05368 135 KGVPNRFVYSTTKAAVIGLTKSVA--ADFAQQGIRCNAICPGTVDTPSLEErIQAQPDPEEALKAFAARQP 203

short chain dehydrogenase; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706934    3 DLTGKHVCYVADCGGIALETSKVLMTKNiAKLAI--LQSTENPQAIAQLqsikpsTQIFFWTYDVTmAREDMKKYFDEVM 80
Cdd:PRK07825   2 DLRGKVVAITGGARGIGLATARALAALG-ARVAIgdLDEALAKETAAEL------GLVVGGPLDVT-DPASFAAFLDAVE 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706934   81 VQMDYIDVLINGATLC--------DENNIDATINTNLTGMMNTVATVLPYMdRKMGGtgGLIVNVTSVIGLDPSPVFCAY 152
Cdd:PRK07825  74 ADLGPIDVLVNNAGVMpvgpfldePDAVTRRILDVNVYGVILGSKLAAPRM-VPRGR--GHVVNVASLAGKIPVPGMATY 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 78706934  153 SASKFGVIGFTRSLADPlyYSQNGVAVMAVCcgPTrvFVDRELKA 197
Cdd:PRK07825 151 CASKHAVVGFTDAARLE--LRGTGVHVSVVL--PS--FVNTELIA 189

SDR family oxidoreductase;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706934   17 GIALetskVLMTKNIAKLAILQstenpqaiAQLQSIKpsTQIFFWTYDVTMAREdMKKYFDEVMVQMDYIDVLINGATLC 96
Cdd:PRK07454  30 GWDL----ALVARSQDALEALA--------AELRSTG--VKAAAYSIDLSNPEA-IAPGIAELLEQFGCPDVLINNAGMA 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706934   97 DENNIDAT--------INTNLTGMMNTVATVLPYMdRKMGGtgGLIVNVTSVIGLDPSPVFCAYSASKFGVIGFTRSLAD 168
Cdd:PRK07454  95 YTGPLLEMplsdwqwvIQLNLTSVFQCCSAVLPGM-RARGG--GLIINVSSIAARNAFPQWGAYCVSKAALAAFTKCLAE 171

                        170
                 ....*....|....*..
gi 78706934  169 PlyYSQNGVAVMAVCCG 185
Cdd:PRK07454 172 E--ERSHGIRVCTITLG 186

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706934   86 IDVLINGATLCDENNID--------ATINTNLTGMMNTVATVLPYMDRKMGGTgglIVNVTSVIGLDPSPVFCAYSASKF 157
Cdd:PRK07666  85 IDILINNAGISKFGKFLeldpaeweKIIQVNLMGVYYATRAVLPSMIERQSGD---IINISSTAGQKGAAVTSAYSASKF 161

                         90
                 ....*....|
gi 78706934  158 GVIGFTRSLA 167
Cdd:PRK07666 162 GVLGLTESLM 171

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706934  15 CGGIALETSKVLmTKNIAKLAILQSTENPQAIAQLQSIKP-STQIFFWTYDVTmAREDMKKYFDEVMVQMDYIDVLINGA 93
Cdd:cd05366  11 AQGIGRAIAERL-AADGFNIVLADLNLEEAAKSTIQEISEaGYNAVAVGADVT-DKDDVEALIDQAVEKFGSFDVMVNNA 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706934  94 TLC--------DENNIDATINTNLTGMMNTVATVLPYMDRKmgGTGGLIVNVTSVIGLDPSPVFCAYSASKFGVIGFTRS 165
Cdd:cd05366  89 GIApitplltiTEEDLKKVYAVNVFGVLFGIQAAARQFKKL--GHGGKIINASSIAGVQGFPNLGAYSASKFAVRGLTQT 166

                       170       180
                ....*....|....*....|
gi 78706934 166 LADPLyySQNGVAVMAVCCG 185
Cdd:cd05366 167 AAQEL--APKGITVNAYAPG 184

short chain dehydrogenase; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706934    1 MFDLTGKHVCYVADCGGIALETSKVLMTKNiAKLAILQSteNPQAIAQLQSIKPSTQIFFWTYDVTmAREDMKKYFDEVM 80
Cdd:PRK12829   6 LKPLDGLRVLVTGGASGIGRAIAEAFAEAG-ARVHVCDV--SEAALAATAARLPGAKVTATVADVA-DPAQVERVFDTAV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706934   81 VQMDYIDVLINGA----------TLCDENnIDATINTNLTGMMNTVATVLPYMdrKMGGTGGLIVNVTSVIGLDPSPVFC 150
Cdd:PRK12829  82 ERFGGLDVLVNNAgiagptggidEITPEQ-WEQTLAVNLNGQFYFARAAVPLL--KASGHGGVIIALSSVAGRLGYPGRT 158

                        170       180       190
                 ....*....|....*....|....*....|..
gi 78706934  151 AYSASKFGVIGFTRSLADPLYYSqnGVAVMAV 182
Cdd:PRK12829 159 PYAASKWAVVGLVKSLAIELGPL--GIRVNAI 188

short chain dehydrogenase; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706934    2 FDLTGKHVCYVADCGGIALETSKVLMTKNiAKLAILQSTENPQAIAQLQSikpSTQIFFWTYDVTMAREdMKKYFDEVMV 81
Cdd:PRK06841  11 FDLSGKVAVVTGGASGIGHAIAELFAAKG-ARVALLDRSEDVAEVAAQLL---GGNAKGLVCDVSDSQS-VEAAVAAVIS 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706934   82 QMDYIDVLINGATLC--------DENNIDATINTNLTGMMNTVATVLPYMdrkMGGTGGLIVNVTS---VIGLDPSpvfC 150
Cdd:PRK06841  86 AFGRIDILVNSAGVAllapaedvSEEDWDKTIDINLKGSFLMAQAVGRHM---IAAGGGKIVNLASqagVVALERH---V 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 78706934  151 AYSASKFGVIGFTRSLAdpLYYSQNGVAVMAVccGPTRVFVDRELKA 197
Cdd:PRK06841 160 AYCASKAGVVGMTKVLA--LEWGPYGITVNAI--SPTVVLTELGKKA 202