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 344030892   1 LKAINPKVTVTFYPYDVTVPIAETtKLLKTIFAKLKTVDILINGAGILDDH----------QIERTIAVNYTGLVNTTTA 70
Cdd:cd05323   42 LQAINPKVKATFVQCDVTSWEQLA-AAFKKAIEKFGRVDILINNAGILDEKsylfagklppPWEKTIDVNLTGVINTTYL 120

                         90       100
                 ....*....|....*....|....*.
gi 344030892  71 IMDFWDKRKGGPGGIICNIGSVTGFN 96
Cdd:cd05323  121 ALHYMDKNKGGKGGVIVNIGSVAGLY 146

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 344030892   1 LKAINPKVTVTFYPYDVTVPIAETtKLLKTIFAKLKTVDILINGAGILDDH----------QIERTIAVNYTGLVNTTTA 70
Cdd:cd05323   42 LQAINPKVKATFVQCDVTSWEQLA-AAFKKAIEKFGRVDILINNAGILDEKsylfagklppPWEKTIDVNLTGVINTTYL 120

                         90       100
                 ....*....|....*....|....*.
gi 344030892  71 IMDFWDKRKGGPGGIICNIGSVTGFN 96
Cdd:cd05323  121 ALHYMDKNKGGKGGVIVNIGSVAGLY 146

Short-chain dehydrogenase [General function prediction only];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344030892   8 VTVTFYPYDVTVPiAETTKLLKTIFAKLKTVDILINGAGI--------LDDHQIERTIAVNYTGLVNTTTAIMDFWDKRK 79
Cdd:COG0300   54 ARVEVVALDVTDP-DAVAALAEAVLARFGPIDVLVNNAGVggggpfeeLDLEDLRRVFEVNVFGPVRLTRALLPLMRARG 132

                         90
                 ....*....|....*.
gi 344030892  80 ggpGGIICNIGSVTGF 95
Cdd:COG0300  133 ---RGRIVNVSSVAGL 145

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 344030892   1 LKAINPKVTVTFYPYDVTVPIAETtKLLKTIFAKLKTVDILINGAGILDDH----------QIERTIAVNYTGLVNTTTA 70
Cdd:cd05323   42 LQAINPKVKATFVQCDVTSWEQLA-AAFKKAIEKFGRVDILINNAGILDEKsylfagklppPWEKTIDVNLTGVINTTYL 120

                         90       100
                 ....*....|....*....|....*.
gi 344030892  71 IMDFWDKRKGGPGGIICNIGSVTGFN 96
Cdd:cd05323  121 ALHYMDKNKGGKGGVIVNIGSVAGLY 146

Short-chain dehydrogenase [General function prediction only];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344030892   8 VTVTFYPYDVTVPiAETTKLLKTIFAKLKTVDILINGAGI--------LDDHQIERTIAVNYTGLVNTTTAIMDFWDKRK 79
Cdd:COG0300   54 ARVEVVALDVTDP-DAVAALAEAVLARFGPIDVLVNNAGVggggpfeeLDLEDLRRVFEVNVFGPVRLTRALLPLMRARG 132

                         90
                 ....*....|....*.
gi 344030892  80 ggpGGIICNIGSVTGF 95
Cdd:COG0300  133 ---RGRIVNVSSVAGL 145

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 344030892  10 VTFYPYDVTVPiAETTKLLKTIFAKLKTVDILINGAGI--------LDDHQIERTIAVNYTGLVNTTTAIMDFWDKRKgg 81
Cdd:COG4221   53 ALAVPLDVTDE-AAVEAAVAAAVAEFGRLDVLVNNAGVallgpleeLDPEDWDRMIDVNVKGVLYVTRAALPAMRARG-- 129

                         90
                 ....*....|....
gi 344030892  82 pGGIICNIGSVTGF 95
Cdd:COG4221  130 -SGHIVNISSIAGL 142

short chain dehydrogenase; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344030892   1 LKAINPKVTVTFYPYDVTVPiAETTKLLKTIFAKLKTVDILINGAGI---------LDDHQIERTIAVNYTGLVNTTTAI 71
Cdd:PRK12829  51 TAARLPGAKVTATVADVADP-AQVERVFDTAVERFGGLDVLVNNAGIagptggideITPEQWEQTLAVNLNGQFYFARAA 129

                         90       100
                 ....*....|....*....|...
gi 344030892  72 MDFWdkRKGGPGGIICNIGSVTG 94
Cdd:PRK12829 130 VPLL--KASGHGGVIIALSSVAG 150

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 344030892   2 KAINPKVTVTFYPYDVTVPIaETTKLLKTIFAKLKTVDILINGAGI--------LDDHQIERTIAVNYTGLVNTTTAIMD 73
Cdd:cd08939   48 EANASGQKVSYISADLSDYE-EVEQAFAQAVEKGGPPDLVVNCAGIsipglfedLTAEEFERGMDVNYFGSLNVAHAVLP 126

                         90       100
                 ....*....|....*....|..
gi 344030892  74 FWDKRKggpGGIICNIGSVTGF 95
Cdd:cd08939  127 LMKEQR---PGHIVFVSSQAAL 145

SDR family oxidoreductase;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344030892  13 YPYDVTVPiAETTKLLKTIFAKLKTVDILINGAG------ILDD----HQIERTIAVNYTGLVNTTTAIMDFWDKRKGGP 82
Cdd:PRK07201 425 YTCDLTDS-AAVDHTVKDILAEHGHVDYLVNNAGrsirrsVENStdrfHDYERTMAVNYFGAVRLILGLLPHMRERRFGH 503

                         90
                 ....*....|
gi 344030892  83 ggiICNIGSV 92
Cdd:PRK07201 504 ---VVNVSSI 510

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 344030892   6 PKVTVTFYPYDVTVPiAETTKLLKTIFAKLKTVDILINGAGI--------LDDHQIERTIAVNYTGLVNTTTAIMDFWDK 77
Cdd:cd05333   47 LGGNAAALEADVSDR-EAVEALVEKVEAEFGPVDILVNNAGItrdnllmrMSEEDWDAVINVNLTGVFNVTQAVIRAMIK 125

                         90
                 ....*....|....*..
gi 344030892  78 RKGGPggiICNIGSVTG 94
Cdd:cd05333  126 RRSGR---IINISSVVG 139

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 344030892  26 KLLKTIFAKLKTVDILINGAGILDDH---------QIERTIAVNYTGLVNTTTAimdFWDKRKGGPGGIICNIGSVTG 94
Cdd:cd05324   67 AAADFVEEKYGGLDILVNNAGIAFKGfddstptreQARETMKTNFFGTVDVTQA---LLPLLKKSPAGRIVNVSSGLG 141

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 344030892   8 VTVTFYPYDVTVPIaETTKLLKTIFAKLKTVDILINGAGI--------LDDHQIERTIAVNYTGLVNTTTAIM-DFWDKR 78
Cdd:cd05339   48 GKVHYYKCDVSKRE-EVYEAAKKIKKEVGDVTILINNAGVvsgkklleLPDEEIEKTFEVNTLAHFWTTKAFLpDMLERN 126

                         90
                 ....*....|....*..
gi 344030892  79 KGGpggiICNIGSVTGF 95
Cdd:cd05339  127 HGH----IVTIASVAGL 139

SDR family oxidoreductase;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344030892  16 DVTVPiAETTKLLKTIFAKLKTVDILINGAGI--------LDDHQIERTIAVNYTGLVNTTTAIMDfWDKRKGgpGGIIC 87
Cdd:PRK12826  63 DVRDR-AALKAAVAAGVEDFGRLDILVANAGIfpltpfaeMDDEQWERVIDVNLTGTFLLTQAALP-ALIRAG--GGRIV 138

                 ....*..
gi 344030892  88 NIGSVTG 94
Cdd:PRK12826 139 LTSSVAG 145

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 344030892   8 VTVTFYPYDVTVPiAETTKLLKTIFAKLKTVDILINGAGILDDHQIER--------TIAVNYTGLVNTTTAIMDFWDKRK 79
Cdd:cd05347   54 VEATAFTCDVSDE-EAIKAAVEAIEEDFGKIDILVNNAGIIRRHPAEEfpeaewrdVIDVNLNGVFFVSQAVARHMIKQG 132

                         90
                 ....*....|....*.
gi 344030892  80 GGPggiICNIGSVTGF 95
Cdd:cd05347  133 HGK---IINICSLLSE 145

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 344030892   2 KAINPKVTVTFYP--YDVTVPiAETTKLLKTIFAKLKTVDILINGAGI-----------LDDhqIERTIAVNYTGLVNTT 68
Cdd:cd05346   42 DELGAKFPVKVLPlqLDVSDR-ESIEAALENLPEEFRDIDILVNNAGLalgldpaqeadLED--WETMIDTNVKGLLNVT 118

                         90       100
                 ....*....|....*....|....*.
gi 344030892  69 TAIMDFWDKRKggpGGIICNIGSVTG 94
Cdd:cd05346  119 RLILPIMIARN---QGHIINLGSIAG 141

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344030892   7 KVTVTFYPYDVTVpIAETTKLLKTIFAKLKTVDILINGAGI--------LDDHQIERTIAVNYTGLVNTTTAIMDFWDKR 78
Cdd:PRK07666  55 GVKVVIATADVSD-YEEVTAAIEQLKNELGSIDILINNAGIskfgkfleLDPAEWEKIIQVNLMGVYYATRAVLPSMIER 133

                         90
                 ....*....|....*.
gi 344030892  79 KGGPggiICNIGSVTG 94
Cdd:PRK07666 134 QSGD---IINISSTAG 146

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 344030892  26 KLLKTIFAKLKTVDILINGAGILDDHQI----------ERTIAVNYTGLVNTTTAIMDFWDKRkggPGGIICNIGSVTGF 95
Cdd:cd05370   67 ALAEALLSEYPNLDILINNAGIQRPIDLrdpasdldkaDTEIDTNLIGPIRLIKAFLPHLKKQ---PEATIVNVSSGLAF 143

                 .
gi 344030892  96 N 96
Cdd:cd05370  144 V 144

3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes members identified as 3beta17beta hydroxysteroid dehydrogenase, 20beta hydroxysteroid dehydrogenase, and R-alcohol dehydrogenase. These proteins exhibit the canonical active site tetrad and glycine rich NAD(P)-binding motif of the classical SDRs. 17beta-dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens, and include members of the SDR family. 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 344030892  11 TFYPYDVTVPiAETTKLLKTIFAKLKTVDILINGAGILDDHQIE--------RTIAVNYTGLVNTTTAIMDfwDKRKGGP 82
Cdd:cd05341   54 RFFHLDVTDE-DGWTAVVDTAREAFGRLDVLVNNAGILTGGTVEtttleewrRLLDINLTGVFLGTRAVIP--PMKEAGG 130

                         90
                 ....*....|...
gi 344030892  83 GGIIcNIGSVTGF 95
Cdd:cd05341  131 GSII-NMSSIEGL 142

short chain dehydrogenase; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344030892   1 LKAINPKVTVTFYPYDVTVPiAETTKLLKTIFAKLKTVDILINGAGI-LDDHQIERTIA-------VNYTGLVNTTTAI- 71
Cdd:PRK06179  38 PARAAPIPGVELLELDVTDD-ASVQAAVDEVIARAGRIDVLVNNAGVgLAGAAEESSIAqaqalfdTNVFGILRMTRAVl 116

                         90       100
                 ....*....|....*....|....*.
gi 344030892  72 --MdfwdkRKGGPGGIIcNIGSVTGF 95
Cdd:PRK06179 117 phM-----RAQGSGRII-NISSVLGF 136

short chain dehydrogenase; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344030892   9 TVTFYPYDVTVPiAETTKLLKTIFAKLKTVDILINGAGIL--------DDHQIERTIAVNYTGLVN-TTTAIMDFWDKRK 79
Cdd:PRK07825  51 LVVGGPLDVTDP-ASFAAFLDAVEADLGPIDVLVNNAGVMpvgpfldePDAVTRRILDVNVYGVILgSKLAAPRMVPRGR 129

                         90
                 ....*....|....*
gi 344030892  80 GGpggiICNIGSVTG 94
Cdd:PRK07825 130 GH----VVNVASLAG 140

classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a canonical active site triad (and also active site Asn) 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 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 344030892  13 YPYDVTVPiAETTKLLKTIFAKLKTVDILINGAGI--------LDDHQIERTIAVNYTGLVNTTTAIMDFWdkRKGGPGG 84
Cdd:cd05360   54 VVADVADA-AQVERAADTAVERFGRIDTWVNNAGVavfgrfedVTPEEFRRVFDVNYLGHVYGTLAALPHL--RRRGGGA 130

                         90
                 ....*....|.
gi 344030892  85 IIcNIGSVTGF 95
Cdd:cd05360  131 LI-NVGSLLGY 140

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

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 344030892  38 VDILINGAGI--------LDDHQIERTIAVNYTGLVNTTTA---IMdfwdkRKGGPGGIIcNIGSVTG 94
Cdd:PRK12825  85 IDILVNNAGIfedkpladMSDDEWDEVIDVNLSGVFHLLRAvvpPM-----RKQRGGRIV-NISSVAG 146

SDR family oxidoreductase;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344030892   1 LKAINPKVTVTFYPYDVTVPiAETTKLLKTIFAKLKTVDILINGAGI--------LDDHQIERTIAVNYTGLVNTTTAIM 72
Cdd:PRK07831  62 LAAELGLGRVEAVVCDVTSE-AQVDALIDAAVERLGRLDVLVNNAGLggqtpvvdMTDDEWSRVLDVTLTGTFRATRAAL 140

                         90       100
                 ....*....|....*....|..
gi 344030892  73 DFWDKRkgGPGGIICNIGSVTG 94
Cdd:PRK07831 141 RYMRAR--GHGGVIVNNASVLG 160

2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 344030892  31 IFAKLKTVDILINGAGIL--------DDHQIERTIAVNYTGLVNTTTAIMDFWDKRKggpGGIICNIGS 91
Cdd:PRK08220  70 LLAETGPLDVLVNAAGILrmgatdslSDEDWQQTFAVNAGGAFNLFRAVMPQFRRQR---SGAIVTVGS 135

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 344030892  12 FYPYDVTvPIAETTKLLKTIFAKLKTVDILINGAGI----------------LDDHQieRTIAVNYTGLVNTT---TAIM 72
Cdd:cd05371   51 FVPVDVT-SEKDVKAALALAKAKFGRLDIVVNCAGIavaaktynkkgqqphsLELFQ--RVINVNLIGTFNVIrlaAGAM 127

                         90       100
                 ....*....|....*....|...
gi 344030892  73 DFWDKRKGGPGGIICNIGSVTGF 95
Cdd:cd05371  128 GKNEPDQGGERGVIINTASVAAF 150

mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes the conversion of fructose to mannitol, an acyclic 6-carbon sugar. MDH is a tetrameric member of the SDR family. This subgroup also includes various other tetrameric SDRs, including Pichia stipitis D-arabinitol dehydrogenase (aka polyol dehydrogenase), Candida albicans Sou1p, a sorbose reductase, and Candida parapsilosis (S)-specific carbonyl reductase (SCR, aka S-specific alcohol dehydrogenase) which catalyzes the enantioselective reduction of 2-hydroxyacetophenone into (S)-1-phenyl-1,2-ethanediol. 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).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344030892   8 VTVTFYPYDVTVPiAETTKLLKTIFAKLKTVDILINGAGI------LDD--HQIERTIAVNYTGLVNTTTAIMDFWdkRK 79
Cdd:cd05352   58 VKTKAYKCDVSSQ-ESVEKTFKQIQKDFGKIDILIANAGItvhkpaLDYtyEQWNKVIDVNLNGVFNCAQAAAKIF--KK 134

                         90
                 ....*....|....*
gi 344030892  80 GGPGGIICnIGSVTG 94
Cdd:cd05352  135 QGKGSLII-TASMSG 148

short chain dehydrogenase; Provisional

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 344030892  38 VDILINGAGI--------LDDHQIERTIAVNYTGLVNTTTAIMDFWDKRKggpGGIICNIGSVTGF 95
Cdd:PRK06180  79 IDVLVNNAGYghegaieeSPLAEMRRQFEVNVFGAVAMTKAVLPGMRARR---RGHIVNITSMGGL 141

SDR family oxidoreductase;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344030892  22 AETTKLLKTIFAKLKTVDILINGAGIL---------DDHQIERTIAVNYTGLVNTTTAIMDFWDKRKGGPGGIICNIGSV 92
Cdd:PRK06123  65 ADVLRLFEAVDRELGRLDALVNNAGILeaqmrleqmDAARLTRIFATNVVGSFLCAREAVKRMSTRHGGRGGAIVNVSSM 144

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344030892   10 VTFYPYDVTVPiAETTKLLKTIFAKLKTVDILINGAGILDDHQI----------ERTIAVNYTGLVNTTTA---IMdfwd 76
Cdd:pfam13561  45 AAVLPCDVTDE-EQVEALVAAAVEKFGRLDILVNNAGFAPKLKGpfldtsredfDRALDVNLYSLFLLAKAalpLM---- 119

                          90
                  ....*....|....*...
gi 344030892   77 krkgGPGGIICNIGSVTG 94
Cdd:pfam13561 120 ----KEGGSIVNLSSIGA 133

short chain dehydrogenase; Provisional

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 344030892  29 KTI--FAKLktvDILINGAGI---------LDDHQIERTIAVNYTGLVNTTTAIMDFWdkrkgGPGGIICNIGSVTGF 95
Cdd:PRK06701 117 ETVreLGRL---DILVNNAAFqypqqsledITAEQLDKTFKTNIYSYFHMTKAALPHL-----KQGSAIINTGSITGY 186

SDR family oxidoreductase;

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 344030892  26 KLLKTIFAKLKTVDILINGAG---------ILDD-HQIERTIAVNYTG 63
Cdd:PRK05866 106 ALVADVEKRIGGVDILINNAGrsirrplaeSLDRwHDVERTMVLNYYA 153

3-ketoacyl-ACP reductase;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344030892  12 FYPYDVTVPIAETTKllkTIFAKLKT----VDILINGAGILDD---HQIERT-----IAVNYTGLVNTTTAIMDFWDKRk 79
Cdd:PRK12938  55 FIASEGNVGDWDSTK---AAFDKVKAevgeIDVLVNNAGITRDvvfRKMTREdwtavIDTNLTSLFNVTKQVIDGMVER- 130

                         90
                 ....*....|....*
gi 344030892  80 gGPGGIIcNIGSVTG 94
Cdd:PRK12938 131 -GWGRII-NISSVNG 143