Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a Rossmann-fold NAD(P)H/NAD(P)(+) binding (NADB) domain. The NADB domain is found in numerous dehydrogenases of metabolic pathways such as glycolysis, and many other redox enzymes. NAD binding involves numerous hydrogen-bonds and van der Waals contacts, in particular H-bonding of residues in a turn between the first strand and the subsequent helix of the Rossmann-fold topology. Characteristically, this turn exhibits a consensus binding pattern similar to GXGXXG, in which the first 2 glycines participate in NAD(P)-binding, and the third facilitates close packing of the helix to the beta-strand. Typically, proteins in this family contain a second domain in addition to the NADB domain, which is responsible for specifically binding a substrate and catalyzing a particular enzymatic reaction.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189016132   1 DTSRELVKRDlKNLVILDRIDNPAAIAELKAINPKVTVTFYPYDVTTPlTETTKLLKTIFAQLKTVDVLINGAGILDDH- 79
Cdd:cd05323   15 ATAKLLLKKG-AKVAILDRNENPGAAAELQAINPKVKATFVQCDVTSW-EQLAAAFKKAIEKFGRVDILINNAGILDEKs 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189016132  80 ---------QIERTIAVNFTGLVNTTTAILDFWDKRKGGPGGVICNIGSVTGFNAIYQVPVYSASKAAVVSFTQSIAKLA 150
Cdd:cd05323   93 ylfagklppPWEKTIDVNLTGVINTTYLALHYMDKNKGGKGGVIVNIGSVAGLYPAPQFPVYSASKHGVVGFTRSLADLL 172

                        170
                 ....*....|....*....
gi 189016132 151 NV-TGVTAFTVNPGITKTT 168
Cdd:cd05323  173 EYkTGVRVNAICPGFTNTP 191

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 189016132   1 DTSRELVKRDlKNLVILDRIDNPAAIAELKAINPKVTVTFYPYDVTTPlTETTKLLKTIFAQLKTVDVLINGAGILDDH- 79
Cdd:cd05323   15 ATAKLLLKKG-AKVAILDRNENPGAAAELQAINPKVKATFVQCDVTSW-EQLAAAFKKAIEKFGRVDILINNAGILDEKs 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189016132  80 ---------QIERTIAVNFTGLVNTTTAILDFWDKRKGGPGGVICNIGSVTGFNAIYQVPVYSASKAAVVSFTQSIAKLA 150
Cdd:cd05323   93 ylfagklppPWEKTIDVNLTGVINTTYLALHYMDKNKGGKGGVIVNIGSVAGLYPAPQFPVYSASKHGVVGFTRSLADLL 172

                        170
                 ....*....|....*....
gi 189016132 151 NV-TGVTAFTVNPGITKTT 168
Cdd:cd05323  173 EYkTGVRVNAICPGFTNTP 191

Short-chain dehydrogenase [General function prediction only];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189016132  13 NLVILDRidNPAAIAELKA--INPKVTVTFYPYDVTTPlTETTKLLKTIFAQLKTVDVLINGAGI--------LDDHQIE 82
Cdd:COG0300   31 RVVLVAR--DAERLEALAAelRAAGARVEVVALDVTDP-DAVAALAEAVLARFGPIDVLVNNAGVggggpfeeLDLEDLR 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189016132  83 RTIAVNFTGLVNTTTAILDFWDKRKGGpggVICNIGSVTGFNAIYQVPVYSASKAAVVSFTQSIAKLANVTGVTAFTVNP 162
Cdd:COG0300  108 RVFEVNVFGPVRLTRALLPLMRARGRG---RIVNVSSVAGLRGLPGMAAYAASKAALEGFSESLRAELAPTGVRVTAVCP 184

                 ....*
gi 189016132 163 GITKT 167
Cdd:COG0300  185 GPVDT 189

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 189016132   1 DTSRELVKRDlKNLVILDRIDNPAAIAELKAINPKVTVTFYPYDVTTPlTETTKLLKTIFAQLKTVDVLINGAGILDDH- 79
Cdd:cd05323   15 ATAKLLLKKG-AKVAILDRNENPGAAAELQAINPKVKATFVQCDVTSW-EQLAAAFKKAIEKFGRVDILINNAGILDEKs 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189016132  80 ---------QIERTIAVNFTGLVNTTTAILDFWDKRKGGPGGVICNIGSVTGFNAIYQVPVYSASKAAVVSFTQSIAKLA 150
Cdd:cd05323   93 ylfagklppPWEKTIDVNLTGVINTTYLALHYMDKNKGGKGGVIVNIGSVAGLYPAPQFPVYSASKHGVVGFTRSLADLL 172

                        170
                 ....*....|....*....
gi 189016132 151 NV-TGVTAFTVNPGITKTT 168
Cdd:cd05323  173 EYkTGVRVNAICPGFTNTP 191

Short-chain dehydrogenase [General function prediction only];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189016132  13 NLVILDRidNPAAIAELKA--INPKVTVTFYPYDVTTPlTETTKLLKTIFAQLKTVDVLINGAGI--------LDDHQIE 82
Cdd:COG0300   31 RVVLVAR--DAERLEALAAelRAAGARVEVVALDVTDP-DAVAALAEAVLARFGPIDVLVNNAGVggggpfeeLDLEDLR 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189016132  83 RTIAVNFTGLVNTTTAILDFWDKRKGGpggVICNIGSVTGFNAIYQVPVYSASKAAVVSFTQSIAKLANVTGVTAFTVNP 162
Cdd:COG0300  108 RVFEVNVFGPVRLTRALLPLMRARGRG---RIVNVSSVAGLRGLPGMAAYAASKAALEGFSESLRAELAPTGVRVTAVCP 184

                 ....*
gi 189016132 163 GITKT 167
Cdd:COG0300  185 GPVDT 189

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 189016132  13 NLVILDRIDNPA--AIAELKAINPKVTvtFYPYDVTTPlTETTKLLKTIFAQLKTVDVLINGAGI--------LDDHQIE 82
Cdd:COG1028   32 RVVITDRDAEALeaAAAELRAAGGRAL--AVAADVTDE-AAVEALVAAAVAAFGRLDILVNNAGItppgpleeLTEEDWD 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189016132  83 RTIAVNFTGLVNTTTAILDFWDKRKGGpggVICNIGSVTGFNAIYQVPVYSASKAAVVSFTQSIAK-LANvTGVTAFTVN 161
Cdd:COG1028  109 RVLDVNLKGPFLLTRAALPHMRERGGG---RIVNISSIAGLRGSPGQAAYAASKAAVVGLTRSLALeLAP-RGIRVNAVA 184

                 ....*.
gi 189016132 162 PGITKT 167
Cdd:COG1028  185 PGPIDT 190

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 189016132   4 RELVKRDLK---NLVILDRidNPAAIAELKAINPKVTVTFYPY--DVTTPlTETTKLLKTIFAQLKTVDVLINGAGI--- 75
Cdd:cd05339   13 RLLALEFAKrgaKVVILDI--NEKGAEETANNVRKAGGKVHYYkcDVSKR-EEVYEAAKKIKKEVGDVTILINNAGVvsg 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189016132  76 -----LDDHQIERTIAVNFTGLVNTTTAIL-DFWDKRKGGpggvICNIGSVTGFNAIYQVPVYSASKAAVVSFTQSIA-- 147
Cdd:cd05339   90 kklleLPDEEIEKTFEVNTLAHFWTTKAFLpDMLERNHGH----IVTIASVAGLISPAGLADYCASKAAAVGFHESLRle 165

                        170       180
                 ....*....|....*....|..
gi 189016132 148 -KLANVTGVTAFTVNPGITKTT 168
Cdd:cd05339  166 lKAYGKPGIKTTLVCPYFINTG 187

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 189016132   4 RELVKR--DLKNLVIL-DRidNPAAIAELKAINPKVTVtfYPYDVTTPlTETTKLLKTIFAQLKTVDVLINGAGIL---- 76
Cdd:COG3967   19 LALAKRlhARGNTVIItGR--REEKLEEAAAANPGLHT--IVLDVADP-ASIAALAEQVTAEFPDLNVLINNAGIMraed 93

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 189016132  77 ------DDHQIERTIAVNFTGLVNTTTAILDFWDKRkggPGGVICNIGSVTGFNAIYQVPVYSASKAAVVSFTQSI 146
Cdd:COG3967   94 lldeaeDLADAEREITTNLLGPIRLTAAFLPHLKAQ---PEAAIVNVSSGLAFVPLAVTPTYSATKAALHSYTQSL 166

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189016132  24 AAIAELKAINpkVTVTFYPYDVTTPlTETTKLLKTIFAQLKTVDVLINGAGILDDHQI--------ERTIAVNFTGLVNT 95
Cdd:PRK05557  45 ALVAEIGALG--GKALAVQGDVSDA-ESVERAVDEAKAEFGGVDILVNNAGITRDNLLmrmkeedwDRVIDTNLTGVFNL 121

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 189016132  96 TTAILDfwDKRKGGPGGVIcNIGSVTGFNAIYQVPVYSASKAAVVSFTQSIAKLANVTGVTAFTVNPGITKT 167
Cdd:PRK05557 122 TKAVAR--PMMKQRSGRII-NISSVVGLMGNPGQANYAASKAGVIGFTKSLARELASRGITVNAVAPGFIET 190

3-oxoacyl-ACP reductase;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189016132   2 TSRELVKRDLKnLVILDRIDNPAAIA-ELKAINPKVTVTFYPYDVTTpLTETTKLLKTIFAQLKTVDVLINGAGILDDHQ 80
Cdd:PRK12824  18 IARELLNDGYR-VIATYFSGNDCAKDwFEEYGFTEDQVRLKELDVTD-TEECAEALAEIEEEEGPVDILVNNAGITRDSV 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189016132  81 IERT--------IAVNFTGLVNTTTAILDFWdKRKGGpgGVICNIGSVTGFNAIYQVPVYSASKAAVVSFTQSIAKLANV 152
Cdd:PRK12824  96 FKRMshqewndvINTNLNSVFNVTQPLFAAM-CEQGY--GRIINISSVNGLKGQFGQTNYSAAKAGMIGFTKALASEGAR 172

                        170
                 ....*....|....*
gi 189016132 153 TGVTAFTVNPGITKT 167
Cdd:PRK12824 173 YGITVNCIAPGYIAT 187

Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR which catalyzes the NADPH-dependent reduction of ketones on steroids and prostaglandins. Unlike most SDRs, PTCR functions as a monomer. This subgroup also includes human carbonyl reductase 1 (CBR1) and CBR3. CBR1 is an NADPH-dependent SDR with broad substrate specificity and may be responsible for the in vivo reduction of quinones, prostaglandins, and other carbonyl-containing compounds. In addition it includes poppy NADPH-dependent salutaridine reductase which catalyzes the stereospecific reduction of salutaridine to 7(S)-salutaridinol in the biosynthesis of morphine, and Arabidopsis SDR1,a menthone reductase, which catalyzes the reduction of menthone to neomenthol, a compound with antimicrobial activity; SDR1 can also carry out neomenthol oxidation. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189016132  24 AAIAELKaiNPKVTVTFYPYDVTTPlTETTKLLKTIFAQLKTVDVLINGAGILDDH---------QIERTIAVNFTGLVN 94
Cdd:cd05324   40 AAVEKLR--AEGLSVRFHQLDVTDD-ASIEAAADFVEEKYGGLDILVNNAGIAFKGfddstptreQARETMKTNFFGTVD 116

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 189016132  95 TTTAILDfwdKRKGGPGGVICNIGSVTGfnaIYQVPvYSASKAAVVSFTQSIAKLANVTGVTAFTVNPGITKT 167
Cdd:cd05324  117 VTQALLP---LLKKSPAGRIVNVSSGLG---SLTSA-YGVSKAALNALTRILAKELKETGIKVNACCPGWVKT 182

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 189016132  44 DVTTPlTETTKLLKTIFAQLKTVDVLINGAGI--------LDDHQIERTIAVNFTGLVNTTTAILDFWDKRKGGpggVIC 115
Cdd:cd05374   54 DVTDE-ESIKAAVKEVIERFGRIDVLVNNAGYglfgpleeTSIEEVRELFEVNVFGPLRVTRAFLPLMRKQGSG---RIV 129

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 189016132 116 NIGSVTGFNAIYQVPVYSASKAAVVSFTQSIAKLANVTGVTAFTVNPGITKT 167
Cdd:cd05374  130 NVSSVAGLVPTPFLGPYCASKAALEALSESLRLELAPFGIKVTIIEPGPVRT 181

classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad and domain size of the classical SDRs, but has an atypical NAD-binding motif ([ST]G[GA]XGXXG). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189016132  15 VILDRIDNPAAIAELKAIN--PKVTVTFYPYDVTTPLtETTKLLKTIFAQLKTVDVLINGAGI-----------LDDHQI 81
Cdd:cd08930   29 LILADINAPALEQLKEELTnlYKNRVIALELDITSKE-SIKELIESYLEKFGRIDILINNAYPspkvwgsrfeeFPYEQW 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189016132  82 ERTIAVNFTGLVNTTTAILDFWDKRKGGpggVICNIGSVTGFNA----IYQVP------VYSASKAAVVSFTQSIAKLAN 151
Cdd:cd08930  108 NEVLNVNLGGAFLCSQAFIKLFKKQGKG---SIINIASIYGVIApdfrIYENTqmyspvEYSVIKAGIIHLTKYLAKYYA 184

                        170
                 ....*....|..
gi 189016132 152 VTGVTAFTVNPG 163
Cdd:cd08930  185 DTGIRVNAISPG 196

classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189016132   2 TSRELVKRDLKnlVIL--DRIDNPAAIAelKAINPKVTVTFYP--YDVTTPLtETTKLLKTIFAQLKTVDVLINGAGI-- 75
Cdd:cd05346   16 TARRFAKAGAK--LILtgRRAERLQELA--DELGAKFPVKVLPlqLDVSDRE-SIEAALENLPEEFRDIDILVNNAGLal 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189016132  76 ---------LDDhqIERTIAVNFTGLVNTTTAILDFWDKRKGGpggVICNIGSVTGFNAIYQVPVYSASKAAVVSFTQSI 146
Cdd:cd05346   91 gldpaqeadLED--WETMIDTNVKGLLNVTRLILPIMIARNQG---HIINLGSIAGRYPYAGGNVYCATKAAVRQFSLNL 165

                        170       180
                 ....*....|....*....|...
gi 189016132 147 AK-LANvTGVTAFTVNPGITKTT 168
Cdd:cd05346  166 RKdLIG-TGIRVTNIEPGLVETE 187

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189016132   2 TSRELVKRDLKnLVILDRIDNPAAiAELKAINpkvTVTFYPYDVTTPlTETTKLLKTIFAQLKTVDVLINGAGI------ 75
Cdd:cd05371   18 TVERLLAQGAK-VVILDLPNSPGE-TVAKLGD---NCRFVPVDVTSE-KDVKAALALAKAKFGRLDIVVNCAGIavaakt 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189016132  76 ----------LDDHQieRTIAVNFTGLVNTTTAILDFWDKRK---GGPGGVICNIGSVTGFNAIYQVPVYSASKAAVVSF 142
Cdd:cd05371   92 ynkkgqqphsLELFQ--RVINVNLIGTFNVIRLAAGAMGKNEpdqGGERGVIINTASVAAFEGQIGQAAYSASKGGIVGM 169

                        170       180
                 ....*....|....*....|....*
gi 189016132 143 TQSIAKLANVTGVTAFTVNPGITKT 167
Cdd:cd05371  170 TLPIARDLAPQGIRVVTIAPGLFDT 194

SDR family oxidoreductase;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189016132  22 NPAAIAELKA-INPKVTVTFYpYDVTTPlTETTKLLKTiFAQL--KTVDVLINGAGIL--------DDHQIERTIAVNFT 90
Cdd:PRK08267  34 NEAGLAALAAeLGAGNAWTGA-LDVTDR-AAWDAALAD-FAAAtgGRLDVLFNNAGILrggpfediPLEAHDRVIDINVK 110

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 189016132  91 GLVNTTTAILDFWdkrKGGPGGVICNIGSVTgfnAIYQVP---VYSASKAAVVSFTQS 145
Cdd:PRK08267 111 GVLNGAHAALPYL---KATPGARVINTSSAS---AIYGQPglaVYSATKFAVRGLTEA 162

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189016132  66 VDVLINGAGI--------LDDHQIERTIAVNFTGLVNTTTAILDfwDKRKGGpGGVICNIGSVTGFNA-IYQVPvYSASK 136
Cdd:PRK12825  85 IDILVNNAGIfedkpladMSDDEWDEVIDVNLSGVFHLLRAVVP--PMRKQR-GGRIVNISSVAGLPGwPGRSN-YAAAK 160

                         90       100
                 ....*....|....*....|....*..
gi 189016132 137 AAVVSFTQSIAKLANVTGVTAFTVNPG 163
Cdd:PRK12825 161 AGLVGLTKALARELAEYGITVNMVAPG 187

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 189016132  59 IFAQLKTVDVLINGAGI----------------------LDDHQIERTIAVNFTGlvnTTTAILDFWDKRKGGPGGVICN 116
Cdd:cd08935   76 IVAQFGTVDILINGAGGnhpdattdpehyepeteqnffdLDEEGWEFVFDLNLNG---SFLPSQVFGKDMLEQKGGSIIN 152

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 189016132 117 IGSVTGFNAIYQVPVYSASKAAVVSFTQSIAKLANVTGVTAFTVNPGITKT 167
Cdd:cd08935  153 ISSMNAFSPLTKVPAYSAAKAAVSNFTQWLAVEFATTGVRVNAIAPGFFVT 203

HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC 7120 HetN, a putative oxidoreductase involved in heterocyst differentiation, and related proteins. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189016132  22 NPAAIAELKAINPKVTVtfYPYDVTTPLtETTKLLKTIFAQLKTVDVLINGAGILD--------DHQIERTIAVNFTGLV 93
Cdd:cd08932   33 NPEDLAALSASGGDVEA--VPYDARDPE-DARALVDALRDRFGRIDVLVHNAGIGRpttlregsDAELEAHFSINVIAPA 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189016132  94 NTTTAILDFWdkRKGGPGGVIcNIGSVTG-----FNAiyqvpVYSASKAAVVSFTQSIAKLANVTGVTAFTVNPGITKTT 168
Cdd:cd08932  110 ELTRALLPAL--REAGSGRVV-FLNSLSGkrvlaGNA-----GYSASKFALRALAHALRQEGWDHGVRVSAVCPGFVDTP 181

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189016132   6 LVKRDLKNLvildridnPAAIAELKAInpKVTVTFYPYDVTTpLTETTKLLKTIFAQLKTVDVLINGAGI--------LD 77
Cdd:PRK07666  36 LLARTEENL--------KAVAEEVEAY--GVKVVIATADVSD-YEEVTAAIEQLKNELGSIDILINNAGIskfgkfleLD 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189016132  78 DHQIERTIAVNFTGLVNTTTAILDFWDKRKGGPggvICNIGSVTGFNAIYQVPVYSASKAAVVSFTQSIAKLANVTGVTA 157
Cdd:PRK07666 105 PAEWEKIIQVNLMGVYYATRAVLPSMIERQSGD---IINISSTAGQKGAAVTSAYSASKFGVLGLTESLMQEVRKHNIRV 181

                        170
                 ....*....|
gi 189016132 158 FTVNPGITKT 167
Cdd:PRK07666 182 TALTPSTVAT 191

SDR family oxidoreductase;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189016132  17 LDRIDNPAAIAELKAINPKVTVtfYPYDVTTPlTETTKLLKTIFAQLKTVDVLINGAGI--------LDDHQIERTIAVN 88
Cdd:PRK12826  38 ICGDDAAATAELVEAAGGKARA--RQVDVRDR-AALKAAVAAGVEDFGRLDILVANAGIfpltpfaeMDDEQWERVIDVN 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189016132  89 FTGLVNTTTAILDfWDKRKGGpgGVICNIGSVTGFNAIYQVPV-YSASKAAVVSFTQSIAKLANVTGVTAFTVNPGITKT 167
Cdd:PRK12826 115 LTGTFLLTQAALP-ALIRAGG--GRIVLTSSVAGPRVGYPGLAhYAASKAGLVGFTRALALELAARNITVNSVHPGGVDT 191