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 2366697810  22 KIVMVTGASSGIGWEFCIALAKSGCRIIATARRMNRLkslcdeinnldrqENEGEARNPRVLavAVELDVNADGStIKAS 101
Cdd:cd05374     1 KVVLITGCSSGIGLALALALAAQGYRVIATARNPDKL-------------ESLGELLNDNLE--VLELDVTDEES-IKAA 64

                          90       100
                  ....*....|....*....|
gi 2366697810 102 VRKAWEAFGHIDVLINNAGI 121
Cdd:cd05374    65 VKEVIERFGRIDVLVNNAGY 84

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 2366697810  22 KIVMVTGASSGIGWEFCIALAKSGCRIIATARRMNRLkslcdeinnldrqENEGEARNPRVLavAVELDVNADGStIKAS 101
Cdd:cd05374     1 KVVLITGCSSGIGLALALALAAQGYRVIATARNPDKL-------------ESLGELLNDNLE--VLELDVTDEES-IKAA 64

                          90       100
                  ....*....|....*....|
gi 2366697810 102 VRKAWEAFGHIDVLINNAGI 121
Cdd:cd05374    65 VKEVIERFGRIDVLVNNAGY 84

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2366697810  22 KIVMVTGASSGIGWEFCIALAKSGCRIIATARRMNRLKSLCDEINNLDRQenegearnprvlAVAVELDVnADGSTIKAS 101
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKELGALGGK------------ALFIQGDV-TDRAQVKAL 67

                          90       100
                  ....*....|....*....|
gi 2366697810 102 VRKAWEAFGHIDVLINNAGI 121
Cdd:pfam00106  68 VEQAVERLGRLDILVNNAGI 87

sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain dehydrogenase/reductase family. The enzyme catalyzes the last step in the biosynthesis of tetrahydrobiopterin. A similar enzyme in Bacillus cereus was isolated for its ability to convert benzil to (S)-benzoin, a property sepiapterin reductase also shares. Cutoff scores for this model are set such that benzil reductase scores between trusted and noise cutoffs.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2366697810  23 IVMVTGASSGIGWEFCIALAKS----GCRIIATARRMNRLKSLCDEInnldrqenEGEARNPRVLAVAVELDVNADGSTI 98
Cdd:TIGR01500   2 VCLVTGASRGFGRTIAQELAKClkspGSVLVLSARNDEALRQLKAEI--------GAERSGLRVVRVSLDLGAEAGLEQL 73

                          90       100
                  ....*....|....*....|....*..
gi 2366697810  99 KASVRKA--WEAFGHIdVLINNAGIRG 123
Cdd:TIGR01500  74 LKALRELprPKGLQRL-LLINNAGTLG 99

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 2366697810  22 KIVMVTGASSGIGWEFCIALAKSGCRIIATARRMNRLkslcdeinnldrqENEGEARNPRVLavAVELDVNADGStIKAS 101
Cdd:cd05374     1 KVVLITGCSSGIGLALALALAAQGYRVIATARNPDKL-------------ESLGELLNDNLE--VLELDVTDEES-IKAA 64

                          90       100
                  ....*....|....*....|
gi 2366697810 102 VRKAWEAFGHIDVLINNAGI 121
Cdd:cd05374    65 VKEVIERFGRIDVLVNNAGY 84

Short-chain dehydrogenase [General function prediction only];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2366697810  19 LRGKIVMVTGASSGIGWEFCIALAKSGCRIIATARRMNRLKSLCDEInnldrqenegEARNPRVLAVAveLDVnADGSTI 98
Cdd:COG0300     3 LTGKTVLITGASSGIGRALARALAARGARVVLVARDAERLEALAAEL----------RAAGARVEVVA--LDV-TDPDAV 69

                          90       100
                  ....*....|....*....|...
gi 2366697810  99 KASVRKAWEAFGHIDVLINNAGI 121
Cdd:COG0300    70 AALAEAVLARFGPIDVLVNNAGV 92

11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human 11beta_HSD1 catalyzes the NADP(H)-dependent interconversion of cortisone and cortisol. This subgroup also includes human dehydrogenase/reductase SDR family member 7C (DHRS7C) and DHRS7B. These proteins have the GxxxGxG nucleotide binding motif and S-Y-K catalytic triad characteristic of the SDRs, but have an atypical C-terminal domain that contributes to homodimerization contacts. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2366697810  19 LRGKIVMVTGASSGIGWEFCIALAKSGCRIIATARRMNRLKSLCDEINNLDrqenegearNPRVLAVAveLDVnADGSTI 98
Cdd:cd05332     1 LQGKVVIITGASSGIGEELAYHLARLGARLVLSARREERLEEVKSECLELG---------APSPHVVP--LDM-SDLEDA 68

                          90       100
                  ....*....|....*....|...
gi 2366697810  99 KASVRKAWEAFGHIDVLINNAGI 121
Cdd:cd05332    69 EQVVEEALKLFGGLDILINNAGI 91

SDR family oxidoreductase;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2366697810  18 DLRGKIVMVTGASSGIGWEFCIALAKSGCRIIATARRMNRLKSLCDEInnldrqENEGEArnprvlAVAVELDVnADGST 97
Cdd:PRK06949    6 NLEGKVALVTGASSGLGARFAQVLAQAGAKVVLASRRVERLKELRAEI------EAEGGA------AHVVSLDV-TDYQS 72

                          90       100
                  ....*....|....*....|....*...
gi 2366697810  98 IKASVRKAWEAFGHIDVLINNAGIRGIQ 125
Cdd:PRK06949   73 IKAAVAHAETEAGTIDILVNNSGVSTTQ 100

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2366697810  24 VMVTGASSGIGWEFCIALAKSGCRIIATARRMNRLKSLCDeinnldrqenegeARNPRVLAVAVELDVnADGSTIKASVR 103
Cdd:cd05233     1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEALAELAA-------------IEALGGNAVAVQADV-SDEEDVEALVE 66

                          90
                  ....*....|....*...
gi 2366697810 104 KAWEAFGHIDVLINNAGI 121
Cdd:cd05233    67 EALEEFGRLDILVNNAGI 84

SDR family oxidoreductase;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2366697810  17 QDLRGKIVMVTGASSGIGWEFCIALAKSGCRIIATARRMNRLKSLCDEINNLDRqenegearnprvlAVAVELDVnADGS 96
Cdd:PRK07231    1 MRLEGKVAIVTGASSGIGEGIARRFAAEGARVVVTDRNEEAAERVAAEILAGGR-------------AIAVAADV-SDEA 66

                          90       100
                  ....*....|....*....|....*
gi 2366697810  97 TIKASVRKAWEAFGHIDVLINNAGI 121
Cdd:PRK07231   67 DVEAAVAAALERFGSVDILVNNAGT 91

3-oxoacyl-ACP reductase FabG;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2366697810  17 QDLRGKIVMVTGASSGIGWEFCIALAKSGCRIIATARRMNRLKSLCDEINNLDRQenegearnprvlAVAVELDVnADGS 96
Cdd:PRK05653    1 MSLQGKTALVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEALAAELRAAGGE------------ARVLVFDV-SDEA 67

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2366697810  97 TIKASVRKAWEAFGHIDVLINNAGIRGIQLMM 128
Cdd:PRK05653   68 AVRALIEAAVEAFGALDILVNNAGITRDALLP 99

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 2366697810  18 DLRGKIVMVTGASSGIGWEFCIALAKSGCRIIATARRMNRLKSLCDEInnldrqENEGearnprVLAVAVELDVNADGSt 97
Cdd:cd05347     2 SLKGKVALVTGASRGIGFGIASGLAEAGANIVINSRNEEKAEEAQQLI------EKEG------VEATAFTCDVSDEEA- 68

                          90       100
                  ....*....|....*....|....
gi 2366697810  98 IKASVRKAWEAFGHIDVLINNAGI 121
Cdd:cd05347    69 IKAAVEAIEEDFGKIDILVNNAGI 92

Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER is a peroxisomal protein with a proposed role in fatty acid elongation. Fatty acid synthesis is known to occur in the both endoplasmic reticulum and mitochondria; peroxisomal TER has been proposed as an additional fatty acid elongation system, it reduces the double bond at C-2 as the last step of elongation. This system resembles the mitochondrial system in that acetyl-CoA is used as a carbon donor. TER may also function in phytol metabolism, reducting phytenoyl-CoA to phytanoyl-CoA in peroxisomes. DECR processes double bonds in fatty acids to increase their utility in fatty acid metabolism; it reduces 2,4-dienoyl-CoA to an enoyl-CoA. DECR is active in mitochondria and peroxisomes. This subgroup has the Gly-rich NAD-binding motif of the classical SDR family, but does not display strong identity to the canonical active site tetrad, and lacks the characteristic Tyr at the usual position. 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 2366697810  19 LRGKIVMVTGASSGIGWEFCIALAKSGCRIIATARRMNRLKSLCDEINnldrqenegEARNPRVLAVAVelDVNaDGSTI 98
Cdd:cd05369     1 LKGKVAFITGGGTGIGKAIAKAFAELGASVAIAGRKPEVLEAAAEEIS---------SATGGRAHPIQC--DVR-DPEAV 68

                          90       100
                  ....*....|....*....|..
gi 2366697810  99 KASVRKAWEAFGHIDVLINNAG 120
Cdd:cd05369    69 EAAVDETLKEFGKIDILINNAA 90

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 2366697810  18 DLRGKIVMVTGASSGIGWEFCIALAKSGCRIIATARRMNRLKSLCdeinnldrqenegeARNPRVlaVAVELDVnADGST 97
Cdd:COG3967     2 KLTGNTILITGGTSGIGLALAKRLHARGNTVIITGRREEKLEEAA--------------AANPGL--HTIVLDV-ADPAS 64

                          90       100
                  ....*....|....*....|....
gi 2366697810  98 IKASVRKAWEAFGHIDVLINNAGI 121
Cdd:COG3967    65 IAALAEQVTAEFPDLNVLINNAGI 88

SDR family oxidoreductase;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2366697810  17 QDLRGKIVMVTGASSGIGWEFCIALAKSGCRIIATARRMNRLKSLCDEInnldrqenegEARNPRVLAVAVELdvnADGS 96
Cdd:PRK12826    2 RDLEGRVALVTGAARGIGRAIAVRLAADGAEVIVVDICGDDAAATAELV----------EAAGGKARARQVDV---RDRA 68

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2366697810  97 TIKASVRKAWEAFGHIDVLINNAGIRGIQLMMSL 130
Cdd:PRK12826   69 ALKAAVAAGVEDFGRLDILVANAGIFPLTPFAEM 102

short chain dehydrogenase; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2366697810  22 KIVMVTGASSGIGWEFCIALAKSGCRIIATARRMNRLKSLcdeinnldrqenegearnPRVlaVAVELDVNADGStIKAS 101
Cdd:PRK06179    5 KVALVTGASSGIGRATAEKLARAGYRVFGTSRNPARAAPI------------------PGV--ELLELDVTDDAS-VQAA 63

                          90       100
                  ....*....|....*....|
gi 2366697810 102 VRKAWEAFGHIDVLINNAGI 121
Cdd:PRK06179   64 VDEVIARAGRIDVLVNNAGV 83

SDR family oxidoreductase;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2366697810   5 SEQLAINK-PDPWQDLRGKIVMVTGASSGIGWEFCIALAKSGCRIIATARRMNRLKSLCDEINnldrqENEGEARnprvl 83
Cdd:PRK05866   23 SPQLLINRpPRQPVDLTGKRILLTGASSGIGEAAAEQFARRGATVVAVARREDLLDAVADRIT-----RAGGDAM----- 92

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2366697810  84 AVAVELdvnADGSTIKASVRKAWEAFGHIDVLINNAG--IR 122
Cdd:PRK05866   93 AVPCDL---SDLDAVDALVADVEKRIGGVDILINNAGrsIR 130

glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR family, it catalyzes the NAD(P)-dependent oxidation of beta-D-glucose to D-glucono-delta-lactone. GlcDH has a typical NAD-binding site glycine-rich pattern as well as the canonical active site tetrad (YXXXK motif plus upstream Ser and Asn). 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 2366697810  19 LRGKIVMVTGASSGIGWEFCIALAKSGCRIIATARrmnrlkslcdeiNNLDR-QENEGEARNPRVLAVAVELDVnADGST 97
Cdd:cd05358     1 LKGKVALVTGASSGIGKAIAIRLATAGANVVVNYR------------SKEDAaEEVVEEIKAVGGKAIAVQADV-SKEED 67

                          90       100
                  ....*....|....*....|....*.
gi 2366697810  98 IKASVRKAWEAFGHIDVLINNAGIRG 123
Cdd:cd05358    68 VVALFQSAIKEFGTLDILVNNAGLQG 93

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2366697810  17 QDLRGKIVMVTGASSGIGWEFCIALAKSGCRIIATARrmnrlkSLCDEINNLDRqENEGEARNprvlAVAVELDVNaDGS 96
Cdd:PRK12825    2 GSLMGRVALVTGAARGLGRAIALRLARAGADVVVHYR------SDEEAAEELVE-AVEALGRR----AQAVQADVT-DKA 69

                          90       100
                  ....*....|....*....|....*
gi 2366697810  97 TIKASVRKAWEAFGHIDVLINNAGI 121
Cdd:PRK12825   70 ALEAAVAAAVERFGRIDILVNNAGI 94

gluconate 5-dehydrogenase; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2366697810  18 DLRGKIVMVTGASSGIGWEFCIALAKSGCRIIATARRMNRLKSLCDEINNLDRQenegearnprvlAVAVELDVnADGST 97
Cdd:PRK08213    9 DLSGKTALVTGGSRGLGLQIAEALGEAGARVVLSARKAEELEEAAAHLEALGID------------ALWIAADV-ADEAD 75

                          90       100
                  ....*....|....*....|...
gi 2366697810  98 IKASVRKAWEAFGHIDVLINNAG 120
Cdd:PRK08213   76 IERLAEETLERFGHVDILVNNAG 98

carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl reductase of the classical SDR family. Studies in Drosophila melanogaster implicate Sniffer in the prevention of neurodegeneration due to aging and oxidative-stress. This subgroup also includes Rhodococcus sp. AD45 IsoH, which is an NAD-dependent 1-hydroxy-2-glutathionyl-2-methyl-3-butene dehydrogenase involved in isoprene metabolism, Aspergillus nidulans StcE encoded by a gene which is part of a proposed sterigmatocystin biosynthesis gene cluster, Bacillus circulans SANK 72073 BtrF encoded by a gene found in the butirosin biosynthesis gene cluster, and Aspergillus parasiticus nor-1 involved in the biosynthesis of aflatoxins. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2366697810  24 VMVTGASSGIGWEFCIALAKSGC-RIIATARRMNRLKSLCDEINNLDRqenegearnprvlAVAVELDVNADGSTIKASV 102
Cdd:cd05325     1 VLITGASRGIGLELVRQLLARGNnTVIATCRDPSAATELAALGASHSR-------------LHILELDVTDEIAESAEAV 67

                          90       100
                  ....*....|....*....|....*..
gi 2366697810 103 RKAWEaFGHIDVLINNAGIRGIQLMMS 129
Cdd:cd05325    68 AERLG-DAGLDVLINNAGILHSYGPAS 93

short chain dehydrogenase; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2366697810  21 GKIVMVTGASSGIGWEFCIALAKSGCRIIATARRMNRLKSLcdeinnldrqenegEARNPRvLAVAVELDVNaDGSTIKA 100
Cdd:PRK06180    4 MKTWLITGVSSGFGRALAQAALAAGHRVVGTVRSEAARADF--------------EALHPD-RALARLLDVT-DFDAIDA 67

                          90       100
                  ....*....|....*....|.
gi 2366697810 101 SVRKAWEAFGHIDVLINNAGI 121
Cdd:PRK06180   68 VVADAEATFGPIDVLVNNAGY 88

SDR family oxidoreductase;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2366697810  21 GKIVMVTGASSGIGWEFCIALAKSGCRIIATARRMNRLKSLCDEINNLDRQENegearnprvLAVaVELDVNADGSTikA 100
Cdd:PRK06914    3 KKIAIVTGASSGFGLLTTLELAKKGYLVIATMRNPEKQENLLSQATQLNLQQN---------IKV-QQLDVTDQNSI--H 70

                          90       100
                  ....*....|....*....|
gi 2366697810 101 SVRKAWEAFGHIDVLINNAG 120
Cdd:PRK06914   71 NFQLVLKEIGRIDLLVNNAG 90

SDR family oxidoreductase;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2366697810  18 DLRGKIVMVTGASSGIGWEFCIALAKSGCRIIATARRMNRLKSLCDEINNLDRQEnegearnprvlAVAVELDVNADgst 97
Cdd:PRK09072    2 DLKDKRVLLTGASGGIGQALAEALAAAGARLLLVGRNAEKLEALAARLPYPGRHR-----------WVVADLTSEAG--- 67

                          90       100
                  ....*....|....*....|....
gi 2366697810  98 iKASVRKAWEAFGHIDVLINNAGI 121
Cdd:PRK09072   68 -REAVLARAREMGGINVLINNAGV 90

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 2366697810  22 KIVMVTGASSGIGWEFCIALAKSGCRIIAtarrmnrlkslcdeinnLDRQENEGEAR-----NPRVLAVAVELDVNADGS 96
Cdd:cd05323     1 KVAIITGGASGIGLATAKLLLKKGAKVAI-----------------LDRNENPGAAAelqaiNPKVKATFVQCDVTSWEQ 63

                          90       100
                  ....*....|....*....|....*
gi 2366697810  97 TIKAsVRKAWEAFGHIDVLINNAGI 121
Cdd:cd05323    64 LAAA-FKKAIEKFGRVDILINNAGI 87

putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup resembles the SDR family, but does not have a perfect match to the NAD-binding motif or the catalytic tetrad characteristic of the SDRs. It includes the SDRs, Q9HYA2 from Pseudomonas aeruginosa PAO1 and APE0912 from Aeropyrum pernix K1. 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 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 2366697810  21 GKIVMVTGASSGIGWEFCIALAKSGCRIIATARRmnrlkslcdeINNLDRQENEGEARNPRVLAVAVELdvnADGSTIKA 100
Cdd:cd05344     1 GKVALVTAASSGIGLAIARALAREGARVAICARN----------RENLERAASELRAGGAGVLAVVADL---TDPEDIDR 67

                          90       100
                  ....*....|....*....|
gi 2366697810 101 SVRKAWEAFGHIDVLINNAG 120
Cdd:cd05344    68 LVEKAGDAFGRVDILVNNAG 87

short chain dehydrogenase; Validated

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2366697810  22 KIVMVTGASSGIGWEFCIALAKSGCRIIATARRMNRLKSLCDeinnldrqenEGearnprvlAVAVELDVnADGSTIKAS 101
Cdd:PRK06182    4 KVALVTGASSGIGKATARRLAAQGYTVYGAARRVDKMEDLAS----------LG--------VHPLSLDV-TDEASIKAA 64

                          90
                  ....*....|....*....
gi 2366697810 102 VRKAWEAFGHIDVLINNAG 120
Cdd:PRK06182   65 VDTIIAEEGRIDVLVNNAG 83

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 2366697810  21 GKIVMVTGASSGIGWEFCIALAKSGCRIIATARRMNRLKSLCDEINNLDRQENEgearnprvlavAVELDVNADGStIKA 100
Cdd:cd08930     2 DKIILITGAAGLIGKAFCKALLSAGARLILADINAPALEQLKEELTNLYKNRVI-----------ALELDITSKES-IKE 69

                          90       100
                  ....*....|....*....|...
gi 2366697810 101 SVRKAWEAFGHIDVLINNAGIRG 123
Cdd:cd08930    70 LIESYLEKFGRIDILINNAYPSP 92

SDR family oxidoreductase;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2366697810  17 QDLRGKIVMVTGASSGIGWEFCIALAKSGCRIIATARRMNRLKSLCDEINnldrqeNEGEARnprvlavAVELDVNADGS 96
Cdd:PRK07326    2 MSLKGKVALITGGSKGIGFAIAEALLAEGYKVAITARDQKELEEAAAELN------NKGNVL-------GLAADVRDEAD 68

                          90       100
                  ....*....|....*....|....*
gi 2366697810  97 TIKAsVRKAWEAFGHIDVLINNAGI 121
Cdd:PRK07326   69 VQRA-VDAIVAAFGGLDVLIANAGV 92

xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins identified as L-xylulose reductase (XR) and carbonyl reductase; they are members of the SDR family. XR, catalyzes the NADP-dependent reduction of L-xyulose and other sugars. Tetrameric mouse carbonyl reductase is involved in the metabolism of biogenic and xenobiotic carbonyl compounds. This subgroup also includes tetrameric chicken liver D-erythrulose reductase, which catalyzes the reduction of D-erythrulose to D-threitol. 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 2366697810  15 PWQDLRGKIVMVTGASSGIGWEFCIALAKSGCRIIATARRMNRLKSLCDEinnldrqenegearNPRVLAVAVELDVNad 94
Cdd:cd05351     1 MELDFAGKRALVTGAGKGIGRATVKALAKAGARVVAVSRTQADLDSLVRE--------------CPGIEPVCVDLSDW-- 64

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2366697810  95 gstikASVRKAWEAFGHIDVLINNAGIRGIQ 125
Cdd:cd05351    65 -----DATEEALGSVGPVDLLVNNAAVAILQ 90

SDR family oxidoreductase;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2366697810  22 KIVMVTGASSGIGWEFCIALAKSGCRIIATARRMNRLKSLCDEInnldrqenegeaRNPRVLAVAVELDVnADGSTIKAS 101
Cdd:PRK07454    7 PRALITGASSGIGKATALAFAKAGWDLALVARSQDALEALAAEL------------RSTGVKAAAYSIDL-SNPEAIAPG 73

                          90       100
                  ....*....|....*....|
gi 2366697810 102 VRKAWEAFGHIDVLINNAGI 121
Cdd:PRK07454   74 IAELLEQFGCPDVLINNAGM 93