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 4502601    6 RVALVTGANRGIGLAIARELCRQFSGDVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLN 85
Cdd:cd05324   1 KVALVTGANRGIGFEIVRQLAKSGPGTVILTARDVERGQAAVEKLRAEGLSVRFHQLDVTDDASIEAAADFVEEKYGGLD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502601   86 VLVNNAAVAFKS-DDPMPFDIKAEMTLKTNFFATRNMCNELLPIMKP--HGRVVNISSLQCLRAfencsedlqerfhset 162
Cdd:cd05324  81 ILVNNAGIAFKGfDDSTPTREQARETMKTNFFGTVDVTQALLPLLKKspAGRIVNVSSGLGSLT---------------- 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502601  163 ltegdlvdlmkkfvedtknevheregwpnSPYGVSKLGVTVLSRILARRLDEkrkaDRILVNACCPGPVKTDMDGKDSIR 242
Cdd:cd05324 145 -----------------------------SAYGVSKAALNALTRILAKELKE----TGIKVNACCPGWVKTDMGGGKAPK 191

                       250       260       270
                ....*....|....*....|....*....|....*
gi 4502601  243 TVEEGAETPVYLALLPPDAtEPQGQLVHDKVVQNW 277
Cdd:cd05324 192 TPEEGAETPVYLALLPPDG-EPTGKFFSDKKVVPW 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 4502601    6 RVALVTGANRGIGLAIARELCRQFSGDVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLN 85
Cdd:cd05324   1 KVALVTGANRGIGFEIVRQLAKSGPGTVILTARDVERGQAAVEKLRAEGLSVRFHQLDVTDDASIEAAADFVEEKYGGLD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502601   86 VLVNNAAVAFKS-DDPMPFDIKAEMTLKTNFFATRNMCNELLPIMKP--HGRVVNISSLQCLRAfencsedlqerfhset 162
Cdd:cd05324  81 ILVNNAGIAFKGfDDSTPTREQARETMKTNFFGTVDVTQALLPLLKKspAGRIVNVSSGLGSLT---------------- 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502601  163 ltegdlvdlmkkfvedtknevheregwpnSPYGVSKLGVTVLSRILARRLDEkrkaDRILVNACCPGPVKTDMDGKDSIR 242
Cdd:cd05324 145 -----------------------------SAYGVSKAALNALTRILAKELKE----TGIKVNACCPGWVKTDMGGGKAPK 191

                       250       260       270
                ....*....|....*....|....*....|....*
gi 4502601  243 TVEEGAETPVYLALLPPDAtEPQGQLVHDKVVQNW 277
Cdd:cd05324 192 TPEEGAETPVYLALLPPDG-EPTGKFFSDKKVVPW 225

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502601      6 RVALVTGANRGIGLAIARELCRQfSGDVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLN 85
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKE-GAKVVLVDRSEEKLEAVAKELGALGGKALFIQGDVTDRAQVKALVEQAVERLGRLD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502601     86 VLVNNAAVA----FKSDDPMpfDIKAEMtlKTNFFATRNMCNELLPIMKPH--GRVVNISSlqclrafencsedlqerfh 159
Cdd:pfam00106  80 ILVNNAGITglgpFSELSDE--DWERVI--DVNLTGVFNLTRAVLPAMIKGsgGRIVNISS------------------- 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502601    160 setltegdlvdlmkkfvedtkneVHEREGWPN-SPYGVSKLGVTVLSRILARRLdekrKADRILVNACCPGPVKTDMDGK 238
Cdd:pfam00106 137 -----------------------VAGLVPYPGgSAYSASKAAVIGFTRSLALEL----APHGIRVNAVAPGGVDTDMTKE 189

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502601       9 LVTGANRGIGLAIARELCRQFSGDVVLTAR--DVARGQAA-VQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLN 85
Cdd:smart00822   4 LITGGLGGLGRALARWLAERGARRLVLLSRsgPDAPGAAAlLAELEAAGARVTVVACDVADRDALAAVLAAIPAVEGPLT 83

                   ....*...
gi 4502601      86 VLVNNAAV 93
Cdd:smart00822  84 GVIHAAGV 91

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 4502601    6 RVALVTGANRGIGLAIARELCRQFSGDVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLN 85
Cdd:cd05324   1 KVALVTGANRGIGFEIVRQLAKSGPGTVILTARDVERGQAAVEKLRAEGLSVRFHQLDVTDDASIEAAADFVEEKYGGLD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502601   86 VLVNNAAVAFKS-DDPMPFDIKAEMTLKTNFFATRNMCNELLPIMKP--HGRVVNISSLQCLRAfencsedlqerfhset 162
Cdd:cd05324  81 ILVNNAGIAFKGfDDSTPTREQARETMKTNFFGTVDVTQALLPLLKKspAGRIVNVSSGLGSLT---------------- 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502601  163 ltegdlvdlmkkfvedtknevheregwpnSPYGVSKLGVTVLSRILARRLDEkrkaDRILVNACCPGPVKTDMDGKDSIR 242
Cdd:cd05324 145 -----------------------------SAYGVSKAALNALTRILAKELKE----TGIKVNACCPGWVKTDMGGGKAPK 191

                       250       260       270
                ....*....|....*....|....*....|....*
gi 4502601  243 TVEEGAETPVYLALLPPDAtEPQGQLVHDKVVQNW 277
Cdd:cd05324 192 TPEEGAETPVYLALLPPDG-EPTGKFFSDKKVVPW 225

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 4502601    8 ALVTGANRGIGLAIARELCRQfSGDVVLTARDVARGQAAVQqLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLNVL 87
Cdd:cd05233   1 ALVTGASSGIGRAIARRLARE-GAKVVLADRNEEALAELAA-IEALGGNAVAVQADVSDEEDVEALVEEALEEFGRLDIL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502601   88 VNNAAVAFKSDdpmPFDIKAEM---TLKTNFFATRNMCNELLPIMK--PHGRVVNISSLQCLRAFENcsedlqerfhset 162
Cdd:cd05233  79 VNNAGIARPGP---LEELTDEDwdrVLDVNLTGVFLLTRAALPHMKkqGGGRIVNISSVAGLRPLPG------------- 142

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502601  163 ltegdlvdlmkkfvedtknevheregwpNSPYGVSKLGVTVLSRILARRLdekrKADRILVNACCPGPVKTDMDGKDSIR 242
Cdd:cd05233 143 ----------------------------QAAYAASKAALEGLTRSLALEL----APYGIRVNAVAPGLVDTPMLAKLGPE 190

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 4502601  243 ----------------TVEEGAETPVYLALlpPDATEPQGQLVH 270
Cdd:cd05233 191 eaekelaaaiplgrlgTPEEVAEAVVFLAS--DEASYITGQVIP 232

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502601      6 RVALVTGANRGIGLAIARELCRQfSGDVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLN 85
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKE-GAKVVLVDRSEEKLEAVAKELGALGGKALFIQGDVTDRAQVKALVEQAVERLGRLD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502601     86 VLVNNAAVA----FKSDDPMpfDIKAEMtlKTNFFATRNMCNELLPIMKPH--GRVVNISSlqclrafencsedlqerfh 159
Cdd:pfam00106  80 ILVNNAGITglgpFSELSDE--DWERVI--DVNLTGVFNLTRAVLPAMIKGsgGRIVNISS------------------- 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502601    160 setltegdlvdlmkkfvedtkneVHEREGWPN-SPYGVSKLGVTVLSRILARRLdekrKADRILVNACCPGPVKTDMDGK 238
Cdd:pfam00106 137 -----------------------VAGLVPYPGgSAYSASKAAVIGFTRSLALEL----APHGIRVNAVAPGGVDTDMTKE 189

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 4502601    6 RVALVTGANRGIGLAIARELCRQfSGDVVLTARDVARGQAAVQQLQAEGLSPR--FHQLDIDDLQSIRALRDFLRKEYGG 83
Cdd:cd05327   2 KVVVITGANSGIGKETARELAKR-GAHVIIACRNEEKGEEAAAEIKKETGNAKveVIQLDLSSLASVRQFAEEFLARFPR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502601   84 LNVLVNNAAV----AFKSDDPMpfdikaEMTLKTNFFATRNMCNELLPIMK--PHGRVVNISSLQCLRAFENcsedlqer 157
Cdd:cd05327  81 LDILINNAGImappRRLTKDGF------ELQFAVNYLGHFLLTNLLLPVLKasAPSRIVNVSSIAHRAGPID-------- 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502601  158 fhsetltegdlvdlmkkFVEDTKNEVHEREGWPnsPYGVSKLGVTVLSRILARRLdekrKADRILVNACCPGPVKTDMdG 237
Cdd:cd05327 147 -----------------FNDLDLENNKEYSPYK--AYGQSKLANILFTRELARRL----EGTGVTVNALHPGVVRTEL-L 202

                       250       260       270
                ....*....|....*....|....*....|....*
gi 4502601  238 KDSI--------------RTVEEGAETPVYLALLP 258
Cdd:cd05327 203 RRNGsffllykllrpflkKSPEQGAQTALYAATSP 237

short chain dehydrogenase; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502601     5 SRVALVTGANRGIGLAIARELCRQfSGDVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGL 84
Cdd:PRK12939   7 GKRALVTGAARGLGAAFAEALAEA-GATVAFNDGLAAEARELAAALEAAGGRAHAIAADLADPASVQRFFDAAAAALGGL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502601    85 NVLVNNAAVAfKSDDPMPFDIKA-EMTLKTNFFATRNMCNELLPIMK--PHGRVVNISSLQCLRAFENcsedlqerfhse 161
Cdd:PRK12939  86 DGLVNNAGIT-NSKSATELDIDTwDAVMNVNVRGTFLMLRAALPHLRdsGRGRIVNLASDTALWGAPK------------ 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4502601   162 tltegdlvdLMkkfvedtknevheregwpnsPYGVSKLGVTVLSRILARRLdekrKADRILVNACCPGPVKTDM 235
Cdd:PRK12939 153 ---------LG--------------------AYVASKGAVIGMTRSLAREL----GGRGITVNAIAPGLTATEA 193

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502601     12 GA--NRGIGLAIARELCRQfsG-DVVLTARDvARGQAAVQQLqAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLNVLV 88
Cdd:pfam13561   1 GAanESGIGWAIARALAEE--GaEVVLTDLN-EALAKRVEEL-AEELGAAVLPCDVTDEEQVEALVAAAVEKFGRLDILV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502601     89 NNAAVAFKSDDPMpFDIKAE---MTLKTNFFATRNMCNELLPIMKPHGRVVNISSLQCLRAFENcsedlqerfhsetlte 165
Cdd:pfam13561  77 NNAGFAPKLKGPF-LDTSREdfdRALDVNLYSLFLLAKAALPLMKEGGSIVNLSSIGAERVVPN---------------- 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502601    166 gdlvdlmkkfvedtknevheregwpNSPYGVSKLGVTVLSRILARRLDEKrkadRILVNACCPGPVKTDM----DGKDSI 241
Cdd:pfam13561 140 -------------------------YNAYGAAKAALEALTRYLAVELGPR----GIRVNAISPGPIKTLAasgiPGFDEL 190

                         250       260
                  ....*....|....*....|....*..
gi 4502601    242 R-------------TVEEGAETPVYLA 255
Cdd:pfam13561 191 LaaaearaplgrlgTPEEVANAAAFLA 217

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502601    9 LVTGANRGIGLAIARelcrQFSG---DVVLTARDVARGQAAVQQLqaeglsPRFH--QLDIDDLQSIRALRDFLRKEYGG 83
Cdd:COG3967   9 LITGGTSGIGLALAK----RLHArgnTVIITGRREEKLEEAAAAN------PGLHtiVLDVADPASIAALAEQVTAEFPD 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4502601   84 LNVLVNNAAVA----FKSDDPMPFDIKAEMTlkTNFFATRNMCNELLPIMK--PHGRVVNISS 140
Cdd:COG3967  79 LNVLINNAGIMraedLLDEAEDLADAEREIT--TNLLGPIRLTAAFLPHLKaqPEAAIVNVSS 139

SDR family oxidoreductase;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502601     6 RVALVTGANRGIGLAIARELCRQfSGDVVLTARDVARGQAAVQQLQAEGLSpRFHQLDIDDLQSIRALRDFLRKEYGGLN 85
Cdd:PRK07231   6 KVAIVTGASSGIGEGIARRFAAE-GARVVVTDRNEEAAERVAAEILAGGRA-IAVAADVSDEADVEAAVAAALERFGSVD 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502601    86 VLVNNAAVAFKSD-----DPMPFDIKAEMTLKTNFFATRnmcnELLPIMKPH--GRVVNISSLQCLRAfencsedlqerf 158
Cdd:PRK07231  84 ILVNNAGTTHRNGplldvDEAEFDRIFAVNVKSPYLWTQ----AAVPAMRGEggGAIVNVASTAGLRP------------ 147

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4502601   159 hsetltEGDLvdlmkkfvedtknevhereGWpnspYGVSKLGVTVLSRILARRLdekrKADRILVNACCPGPVKTDM 235
Cdd:PRK07231 148 ------RPGL-------------------GW----YNASKGAVITLTKALAAEL----GPDKIRVNAVAPVVVETGL 191

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 4502601    6 RVALVTGANRGIGLAIARELCRQfSGDVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLN 85
Cdd:cd05333   1 KVALVTGASRGIGRAIALRLAAE-GAKVAVTDRSEEAAAETVEEIKALGGNAAALEADVSDREAVEALVEKVEAEFGPVD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502601   86 VLVNNA-------AVAFKSDDpmpFDikaeMTLKTNFFATRNMCNELLPIM--KPHGRVVNISSlqclrafencsedlqe 156
Cdd:cd05333  80 ILVNNAgitrdnlLMRMSEED---WD----AVINVNLTGVFNVTQAVIRAMikRRSGRIINISS---------------- 136

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502601  157 rfhsetltegdLVDLMKKFvedtknevhereGWPNspYGVSKLGVTVLSRILARRLdekrkADR-ILVNACCPGPVKTDM 235
Cdd:cd05333 137 -----------VVGLIGNP------------GQAN--YAASKAGVIGFTKSLAKEL-----ASRgITVNAVAPGFIDTDM 186

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 4502601    6 RVALVTGANRGIGLAIARELCRQfsGDVVL-TARDvargQAAVQQLQAEgLSPRFH--QLDIDDLQSIRALRDFLRKEYG 82
Cdd:cd05374   1 KVVLITGCSSGIGLALALALAAQ--GYRVIaTARN----PDKLESLGEL-LNDNLEvlELDVTDEESIKAAVKEVIERFG 73

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4502601   83 GLNVLVNNAAVAFKsddpMPF------DIKAEMtlKTNFFATRNMCNELLPIMK--PHGRVVNISSL 141
Cdd:cd05374  74 RIDVLVNNAGYGLF----GPLeetsieEVRELF--EVNVFGPLRVTRAFLPLMRkqGSGRIVNVSSV 134

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 4502601    6 RVALVTGANRGIGLAIARELCRQfSGDVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLN 85
Cdd:cd05347   6 KVALVTGASRGIGFGIASGLAEA-GANIVINSRNEEKAEEAQQLIEKEGVEATAFTCDVSDEEAIKAAVEAIEEDFGKID 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502601   86 VLVNNAAVAFKsdDPMpfdikAEMTLK-------TNFFATRNMCNELLPIMKP--HGRVVNISSLQCLRAFEncsedlqe 156
Cdd:cd05347  85 ILVNNAGIIRR--HPA-----EEFPEAewrdvidVNLNGVFFVSQAVARHMIKqgHGKIINICSLLSELGGP-------- 149

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4502601  157 rfhsetltegdlvdlmkkfvedtknevheregwPNSPYGVSKLGVTVLSRILARRLDEkrkaDRILVNACCPGPVKTDM 235
Cdd:cd05347 150 ---------------------------------PVPAYAASKGGVAGLTKALATEWAR----HGIQVNAIAPGYFATEM 191

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 4502601    8 ALVTGANRGIGLAIARELCRQFSGDVVLTARDvARGQAAVQQLQAEGLSPRFHQLDIDDL--QSIRALRDFLRKeyGGLN 85
Cdd:cd05325   1 VLITGASRGIGLELVRQLLARGNNTVIATCRD-PSAATELAALGASHSRLHILELDVTDEiaESAEAVAERLGD--AGLD 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502601   86 VLVNNAAVAFKSDDPMPFDIKAEM-TLKTNFFATRNMCNELLPIMKP--HGRVVNISSlqclRAfencsedlqerfhset 162
Cdd:cd05325  78 VLINNAGILHSYGPASEVDSEDLLeVFQVNVLGPLLLTQAFLPLLLKgaRAKIINISS----RV---------------- 137

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502601  163 lteGDLVDLmkkfvedtknevhEREGWpnSPYGVSKLGVTVLSRILARRLdekrKADRILVNACCPGPVKTDMDGK---- 238
Cdd:cd05325 138 ---GSIGDN-------------TSGGW--YSYRASKAALNMLTKSLAVEL----KRDGITVVSLHPGWVRTDMGGPfakn 195

                       250
                ....*....|.
gi 4502601  239 DSIRTVEEGAE 249
Cdd:cd05325 196 KGPITPEESVA 206

3-hydroxybutyrate dehydrogenase; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502601     6 RVALVTGANRGIGLAIARELCRQfSGDVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLN 85
Cdd:PRK12429   5 KVALVTGAASGIGLEIALALAKE-GAKVVIADLNDEAAAAAAEALQKAGGKAIGVAMDVTDEEAINAGIDYAVETFGGVD 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502601    86 VLVNNAAVAFKSD-DPMPFDiKAEMTLKTN----FFATRNMcnelLPIMKP--HGRVVNISSlqclrafencsedlqerf 158
Cdd:PRK12429  84 ILVNNAGIQHVAPiEDFPTE-KWKKMIAIMldgaFLTTKAA----LPIMKAqgGGRIINMAS------------------ 140

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4502601   159 hsetltegdlvdlmkkfvedtkneVHEREGWP-NSPYGVSKLGVTVLSRILARrldeKRKADRILVNACCPGPVKT 233
Cdd:PRK12429 141 ------------------------VHGLVGSAgKAAYVSAKHGLIGLTKVVAL----EGATHGVTVNAICPGYVDT 188