classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an incomplete match to the canonical glycine rich NAD-binding motif and lacks the typical active site tetrad (instead of the critical active site Tyr, it has Phe, but contains the nearby Lys). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281943681   3 TIAIVGAGPGLGLSIAKKFGEKGFRVATIARNPEKLaiieRKLKELNIETQ-----SFVADVTNLAALKQAIQSAKKAFG 77
Cdd:cd05373     1 VAAVVGAGDGLGAAIARRFAAEGFSVALAARREAKL----EALLVDIIRDAggsakAVPTDARDEDEVIALFDLIEEEIG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281943681  78 SIDVLEFSpyAKEDIFTSVLETKPQSVVDI--MNSYllAGILSVNEVLPDMISNGSGAILFTTGVSTIfpLPYAGNAGIV 155
Cdd:cd05373    77 PLEVLVYN--AGANVWFPILETTPRVFEKVweMAAF--GGFLAAREAAKRMLARGRGTIIFTGATASL--RGRAGFAAFA 150

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2281943681 156 GA--GMRNYALNLHNELKEKGVFIGHLSIGAMIQP-----------GTEG-----DPDLIAEAWYNLY 205
Cdd:cd05373   151 GAkfALRALAQSMARELGPKGIHVAHVIIDGGIDTdfirerfpkrdERKEedgilDPDAIAEAYWQLH 218

3-oxoacyl-ACP reductase FabG;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281943681   1 MKTIAIVGAGPGLGLSIAKKFGEKGFRVATIARNPEKLAIIERKLKELNIETQSFVADVTNLAALKQAIQSAKKAFGSID 80
Cdd:PRK05653    5 GKTALVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEALAAELRAAGGEARVLVFDVSDEAAVRALIEAAVEAFGALD 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281943681  81 VL-------------EFSPyakEDiFTSVLETkpqsvvdimNsyLLAGILSVNEVLPDMISNGSGAILFTTGVSTIFPLP 147
Cdd:PRK05653   85 ILvnnagitrdallpRMSE---ED-WDRVIDV---------N--LTGTFNVVRAALPPMIKARYGRIVNISSVSGVTGNP 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2281943681 148 YAGN-----AGIVGAgMRNYALnlhnELKEKGV--------FI-----------GHLSIGAMIQPGTEGDPDLIAEA 200
Cdd:PRK05653  150 GQTNysaakAGVIGF-TKALAL----ELASRGItvnavapgFIdtdmteglpeeVKAEILKEIPLGRLGQPEEVANA 221

NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; NADP-dependent 3-hydroxy acid dehydrogenase YdfG is part of the Pathway/BioSystem: Pyrimidine degradation

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281943681   2 KTIAIVGAGPGLGLSIAKKFGEKGFRVATIARNPEKLaiiERKLKELNIETQSFVADVTNLAALKQAIQSAKKAFGSIDV 81
Cdd:COG4221     6 KVALITGASSGIGAATARALAAAGARVVLAARRAERL---EALAAELGGRALAVPLDVTDEAAVEAAVAAAVAEFGRLDV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281943681  82 LEFSpyAKEDIFTSVLETKPQSVVDIMNSYLLAGILSVNEVLPDMISNGSGAILFTTGVSTIFPLPyagNAGIVGA---G 158
Cdd:COG4221    83 LVNN--AGVALLGPLEELDPEDWDRMIDVNVKGVLYVTRAALPAMRARGSGHIVNISSIAGLRPYP---GGAVYAAtkaA 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2281943681 159 MRNYALNLHNELKEKGVFIGHLSIGAMIQPGTEGDPDLIAEAWYNLYENNDHFE 212
Cdd:COG4221   158 VRGLSESLRAELRPTGIRVTVIEPGAVDTEFLDSVFDGDAEAAAAVYEGLEPLT 211

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 2281943681   2 KTIAIVGAGPGLGLSIAKKFGEKGFRVATIARNPEKLAIIERKLKELNIETQSFVADVTNLAALKQAIQSAKKAFGSIDV 81
Cdd:COG1028     7 KVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAELRAAGGRALAVAADVTDEAAVEALVAAAVAAFGRLDI 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281943681  82 L-----EFSPyakedifTSVLETKPQSVVDIMNSYLLAGILSVNEVLPDMISNGSGAILFTTGVSTIFPLPYAGNAGIVG 156
Cdd:COG1028    87 LvnnagITPP-------GPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIAGLRGSPGQAAYAASK 159

                         170
                  ....*....|....*....
gi 2281943681 157 AGMRNYALNLHNELKEKGV 175
Cdd:COG1028   160 AAVVGLTRSLALELAPRGI 178

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 2281943681   4 IAIVGAGPGLGLSIAKKFGEKGFRVATIARNPEKLAIIErKLKELNIETQSFVADVTNLAALKQAIQSAKKAFGSIDVLE 83
Cdd:cd05233     1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEALAELA-AIEALGGNAVAVQADVSDEEDVEALVEEALEEFGRLDILV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281943681  84 FSpyAKEDIFTSVLETKPQSVVDIMNSYLLAGILSVNEVLPDMISNGSGAILFTTGVSTIFPLPYAGNAGIVGAGMRNYA 163
Cdd:cd05233    80 NN--AGIARPGPLEELTDEDWDRVLDVNLTGVFLLTRAALPHMKKQGGGRIVNISSVAGLRPLPGQAAYAASKAALEGLT 157

                         170       180
                  ....*....|....*....|..
gi 2281943681 164 LNLHNELKEKGVFIGHLSIGAM 185
Cdd:cd05233   158 RSLALELAPYGIRVNAVAPGLV 179

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 2281943681   2 KTIAIVGAGPGLGLSIAKKFGEKGFRVATIARNPEKLAiIERKLKELNIETqsFVADVTNLAALKQAIQSAKKAFGSIDV 81
Cdd:cd05374     1 KVVLITGCSSGIGLALALALAAQGYRVIATARNPDKLE-SLGELLNDNLEV--LELDVTDEESIKAAVKEVIERFGRIDV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281943681  82 LEFSpyAKEDIFTSVLETKPQSVVDIMNSYLLaGILSVN-EVLPDMISNGSGAILFTTGVSTIFPLPYAG--NAGivGAG 158
Cdd:cd05374    78 LVNN--AGYGLFGPLEETSIEEVRELFEVNVF-GPLRVTrAFLPLMRKQGSGRIVNVSSVAGLVPTPFLGpyCAS--KAA 152

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2281943681 159 MRNYALNLHNELKEKGVfigHLSIgamIQPGT 190
Cdd:cd05374   153 LEALSESLRLELAPFGI---KVTI---IEPGP 178

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 2281943681   2 KTIAIVGAGPGLGLSIAKKFGEKGFRVATIARNPEKLAIIERKLKELNIETQSFVADVTNLAALKQAIQSAKKAFGSIDV 81
Cdd:cd05333     1 KVALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAAETVEEIKALGGNAAALEADVSDREAVEALVEKVEAEFGPVDI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281943681  82 L---------EFSPYAKEDIFTSVLETKpqsvvdimnsylLAGILSVN-EVLPDMISNGSGAILFTTGVSTIfplpyAGN 151
Cdd:cd05333    81 LvnnagitrdNLLMRMSEEDWDAVINVN------------LTGVFNVTqAVIRAMIKRRSGRIINISSVVGL-----IGN 143

                         170
                  ....*....|..
gi 2281943681 152 AGIVgagmrNYA 163
Cdd:cd05333   144 PGQA-----NYA 150

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 2281943681   2 KTIAIVGAGPGLGLSIAKKFGEKGFRVATIARNPEKLAIIERKLKEL-NIETQSFVADVTNLAALKQAIQSAKKAFGSID 80
Cdd:cd05332     4 KVVIITGASSGIGEELAYHLARLGARLVLSARREERLEEVKSECLELgAPSPHVVPLDMSDLEDAEQVVEEALKLFGGLD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281943681  81 VL-------EFSPYAKEDIftsvletkpQSVVDIMNSYLLAGILSVNEVLPDMISNGSGAILFttgVSTIfplpyagnAG 153
Cdd:cd05332    84 ILinnagisMRSLFHDTSI---------DVDRKIMEVNYFGPVALTKAALPHLIERSQGSIVV---VSSI--------AG 143

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2281943681 154 IVGAGMR------NYALN-----LHNELKEKGVFIGHLSIG 183
Cdd:cd05332   144 KIGVPFRtayaasKHALQgffdsLRAELSEPNISVTVVCPG 184

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281943681   1 MKTIAIVGAGPGLGLSIAKKFGEKGFRVATIARNPEKL-AIIERKLKELNIETQS---FVADVTNLAALKQAIQSAKKAF 76
Cdd:cd08939     1 GKHVLITGGSSGIGKALAKELVKEGANVIIVARSESKLeEAVEEIEAEANASGQKvsyISADLSDYEEVEQAFAQAVEKG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281943681  77 GSIDVLEFSpyAKEDIFTSVLETKPQSVVDIMNSYLLAGILSVNEVLPDMISNGSGAILFTTGVSTIFPL----PYAGna 152
Cdd:cd08939    81 GPPDLVVNC--AGISIPGLFEDLTAEEFERGMDVNYFGSLNVAHAVLPLMKEQRPGHIVFVSSQAALVGIygysAYCP-- 156

                         170       180
                  ....*....|....*....|....*
gi 2281943681 153 giVGAGMRNYALNLHNELKEKGVFI 177
Cdd:cd08939   157 --SKFALRGLAESLRQELKPYNIRV 179

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281943681   2 KTIAIVGAGPGLGLSIAKKFGEKGFRVATIARNPEKLAIIERKLKELnietQSFVADVTNLAALKQAIQSAKKAFGSIDV 81
Cdd:cd05370     6 NTVLITGGTSGIGLALARKFLEAGNTVIITGRREERLAEAKKELPNI----HTIVLDVGDAESVEALAEALLSEYPNLDI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281943681  82 LEFSPYAKEDIFTSVLETKPQSVVDIMNSYLLAGILSVNEVLPDMISNGSGAILFTTGVSTIFPLPYAGNAGIVGAGMRN 161
Cdd:cd05370    82 LINNAGIQRPIDLRDPASDLDKADTEIDTNLIGPIRLIKAFLPHLKKQPEATIVNVSSGLAFVPMAANPVYCATKAALHS 161

                         170
                  ....*....|....
gi 2281943681 162 YALNLHNELKEKGV 175
Cdd:cd05370   162 YTLALRHQLKDTGV 175

short chain dehydrogenase; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281943681   1 MKTIAIVGAGPGLGLSIAKKFGEKGFRVATIARNPEKLAIIERKLKELNIETQSFVADVTNLAALKQAIQSAKKAFGSID 80
Cdd:PRK07109    8 RQVVVITGASAGVGRATARAFARRGAKVVLLARGEEGLEALAAEIRAAGGEALAVVADVADAEAVQAAADRAEEELGPID 87

                  .
gi 2281943681  81 V 81
Cdd:PRK07109   88 T 88

classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281943681   2 KTIAIVGAGPGLGLSIAKKFGEKGFRVATIARNPEKL-----AIIERKLKELNIEtqSFVADVTNLAALKQAIQSAKKAF 76
Cdd:cd05364     4 KVAIITGSSSGIGAGTAILFARLGARLALTGRDAERLeetrqSCLQAGVSEKKIL--LVVADLTEEEGQDRIISTTLAKF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281943681  77 GSIDVLEFSpyAKEDIFTSVLETKPQSVVDIMNSYLLAGILSVNEVLPDMISNgSGAILFTTGVSTIFPLPYAGNAGIVG 156
Cdd:cd05364    82 GRLDILVNN--AGILAKGGGEDQDIEEYDKVMNLNLRAVIYLTKLAVPHLIKT-KGEIVNVSSVAGGRSFPGVLYYCISK 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2281943681 157 AGMRNYALNLHNELKEKGVFIGHLSIGAMIQP--GTEGDPDLIAEAWYN 203
Cdd:cd05364   159 AALDQFTRCTALELAPKGVRVNSVSPGVIVTGfhRRMGMPEEQYIKFLS 207

short chain dehydrogenase; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281943681   2 KTIAIVGAGPGLGLSIAKKFGEKGFRVATIARNPEKLAIIERKLKELNIETQSFVADVTNLAALKQAIQSAKKAFGSIDV 81
Cdd:PRK07890    6 KVVVVSGVGPGLGRTLAVRAARAGADVVLAARTAERLDEVAAEIDDLGRRALAVPTDITDEDQCANLVALALERFGRVDA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281943681  82 LEFSPYAkEDIFTSVLETKPQSVVDIMNSYLLAGILSVNEVLPDMISNGsGAILFTTGVSTIFPLP-YAGNAGIVGAgMR 160
Cdd:PRK07890   86 LVNNAFR-VPSMKPLADADFAHWRAVIELNVLGTLRLTQAFTPALAESG-GSIVMINSMVLRHSQPkYGAYKMAKGA-LL 162

                         170
                  ....*....|....*
gi 2281943681 161 NYALNLHNELKEKGV 175
Cdd:PRK07890  163 AASQSLATELGPQGI 177

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281943681   2 KTIAIVGAGPGLGLSIAKKFGEKGFRVATIARNPEKLAIIERKLKElNIETqsFVADVTNLAALKQAIQSAKKAFGSIDV 81
Cdd:PRK06200    7 QVALITGGGSGIGRALVERFLAEGARVAVLERSAEKLASLRQRFGD-HVLV--VEGDVTSYADNQRAVDQTVDAFGKLDC 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2281943681  82 leFSPYAK-EDIFTSVLETKPQSVVD----IMNSYLLAGILSVNEVLPDMISNGsGAILFTTGVSTIFP 145
Cdd:PRK06200   84 --FVGNAGiWDYNTSLVDIPAETLDTafdeIFNVNVKGYLLGAKAALPALKASG-GSMIFTLSNSSFYP 149

putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes the NAD-dependent interconversion of D-mannonate and D-fructuronate. This subgroup includes Bacillus subtitils UxuB/YjmF, a putative D-mannonate oxidoreductase; the B. subtilis UxuB gene is part of a putative ten-gene operon (the Yjm operon) involved in hexuronate catabolism. Escherichia coli UxuB does not belong to this subgroup. This subgroup has a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281943681   2 KTIAIVGAGPGLGLSIAKKFGEKGFRVATIARNPEKLAIIERKLKELNIETQSFVADVTNLAALKQAIQSAKKAFGSIDV 81
Cdd:cd08935     6 KVAVITGGTGVLGGAMARALAQAGAKVAALGRNQEKGDKVAKEITALGGRAIALAADVLDRASLERAREEIVAQFGTVDI 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281943681  82 L---------------EFSPYAKEDIFTSVLETKPQSVVDImnsYLLAGILSVNEVLPDMISNGSGAILFTTGVSTIFPL 146
Cdd:cd08935    86 LingaggnhpdattdpEHYEPETEQNFFDLDEEGWEFVFDL---NLNGSFLPSQVFGKDMLEQKGGSIINISSMNAFSPL 162

                         170       180
                  ....*....|....*....|....*....
gi 2281943681 147 PYAGNAGIVGAGMRNYALNLHNELKEKGV 175
Cdd:cd08935   163 TKVPAYSAAKAAVSNFTQWLAVEFATTGV 191

classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a canonical active site tetrad and a fairly well conserved typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281943681   4 IAIVGAGPGLGLSIAKKFGEKGFRVATIARNPEKLAIIERKLKELNIETQSFVADVTNLAALKQAIQSAKKAFGSIDVLE 83
Cdd:cd05350     1 VLITGASSGIGRALAREFAKAGYNVALAARRTDRLDELKAELLNPNPSVEVEILDVTDEERNQLVIAELEAELGGLDLVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281943681  84 FSpyAKEDIFTSVLETKPQSVVDIMNSYLLAGILSVNEVLPDMISNGSGAILFTTGVSTIFPLPYAGNAGIVGAGMRNYA 163
Cdd:cd05350    81 IN--AGVGKGTSLGDLSFKAFRETIDTNLLGAAAILEAALPQFRAKGRGHLVLISSVAALRGLPGAAAYSASKAALSSLA 158

                         170       180
                  ....*....|....*....|....*.
gi 2281943681 164 LNLHNELKEKGVFIghlsigAMIQPG 189
Cdd:cd05350   159 ESLRYDVKKRGIRV------TVINPG 178

SDR family oxidoreductase;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281943681   1 MKTIAIVGAGPGLGLSIAKKFGEKGFRVATIARNPEKLAIIERKLKELNIETQSFVADVTNLAALKQAIQSAKKAFGSID 80
Cdd:PRK07454    6 MPRALITGASSGIGKATALAFAKAGWDLALVARSQDALEALAAELRSTGVKAAAYSIDLSNPEAIAPGIAELLEQFGCPD 85

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2281943681  81 VLEFSPYAKediFTSVLETKPQSVVD-IMNSYLLAGILSVNEVLPDMISNGSGAILfttGVSTI-----FP 145
Cdd:PRK07454   86 VLINNAGMA---YTGPLLEMPLSDWQwVIQLNLTSVFQCCSAVLPGMRARGGGLII---NVSSIaarnaFP 150

short chain dehydrogenase; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281943681   2 KTIAIVGAGPGLGLSIAKKFGEKGFRVATIARNPeklAIIERKLKELNIETQSFVADVTNLAALKQAIQSAKKAFGSIDV 81
Cdd:PRK06841   16 KVAVVTGGASGIGHAIAELFAAKGARVALLDRSE---DVAEVAAQLLGGNAKGLVCDVSDSQSVEAAVAAVISAFGRIDI 92

                  .
gi 2281943681  82 L 82
Cdd:PRK06841   93 L 93

SDR family oxidoreductase;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2281943681   1 MKTIAIVGAGPGLGLSIAKKFGEKGFRVATIARNPEKLAIIERKLKELNIETQSFVADVTNLAALKQAIQSAKKAFGSID 80
Cdd:PRK06181    1 GKVVIITGASEGIGRALAVRLARAGAQLVLAARNETRLASLAQELADHGGEALVVPTDVSDAEACERLIEAAVARFGGID 80

                  ..
gi 2281943681  81 VL 82
Cdd:PRK06181   81 IL 82

cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB) is a classical SDR, it is of particular importance for its role in the degradation of biphenyl/polychlorinated biphenyls(PCBs); PCBs are a significant source of environmental contamination. This subgroup also includes Pseudomonas putida F1 cis-biphenyl-1,2-dihydrodiol-1,2-dehydrogenase (aka cis-benzene glycol dehydrogenase, encoded by the bnzE gene), which participates in benzene metabolism. In addition it includes Pseudomonas sp. C18 putative 1,2-dihydroxy-1,2-dihydronaphthalene dehydrogenase (aka dibenzothiophene dihydrodiol dehydrogenase, encoded by the doxE gene) which participates in an upper naphthalene catabolic pathway. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, 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 2281943681   2 KTIAIVGAGPGLGLSIAKKFGEKGFRVATIARNPEKLAIIERKLKElNIETqsFVADVTNLAALKQAIQSAKKAFGSIDV 81
Cdd:cd05348     5 EVALITGGGSGLGRALVERFVAEGAKVAVLDRSAEKVAELRADFGD-AVVG--VEGDVRSLADNERAVARCVERFGKLDC 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2281943681  82 LeFSPYAKEDIFTSVLETKPQSVV----DIMNSYLLAGILSVNEVLPDMISnGSGAILFTTGVSTIFP 145
Cdd:cd05348    82 F-IGNAGIWDYSTSLVDIPEEKLDeafdELFHINVKGYILGAKAALPALYA-TEGSVIFTVSNAGFYP 147