Short-chain dehydrogenase [General function prediction only];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368104   1 MRKVVLITGASSGIGLALCKRLLAEDDelHLCLACRNMSKAEAVCAALLASHptAEVTIVQVDVSNLQSVFRASKELKQR 80
Cdd:COG0300    4 TGKTVLITGASSGIGRALARALAARGA--RVVLVARDAERLEALAAELRAAG--ARVEVVALDVTDPDAVAALAEAVLAR 79

                         90
                 ....*....|....*
gi 751368104  81 FQRLDCIYLNAGIMP 95
Cdd:COG0300   80 FGPIDVLVNNAGVGG 94

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368104    3 KVVLITGASSGIGLALCKRLLAEDDELHLCLacRNMSKAEAVCAALLASHPtaEVTIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVD--RSEEKLEAVAKELGALGG--KALFIQGDVTDRAQVKALVEQAVERLG 76

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 751368104   83 RLDCIYLNAGIMPNP--------------QLNIKALFFG 107
Cdd:pfam00106  77 RLDILVNNAGITGLGpfselsdedwerviDVNLTGVFNL 115

SDR family mycofactocin-dependent oxidoreductase; Members of this protein subfamily are putative oxidoreductases belonging to the larger SDR family. All members occur in genomes that encode a cassette for the biosynthesis of mycofactocin, a proposed electron carrier of a novel redox pool. Characterized members of this family are described as NDMA-dependent, meaning that a blue aniline dye serving as an artificial electron acceptor is required for members of this family to cycle in vitro, since the bound NAD residue is not exchangeable. This family resembles TIGR03971 most closely in the N-terminal region, consistent with the published hypothesis of NAD interaction with mycofactocin. See EC 1.1.99.36. [Unknown function, Enzymes of unknown specificity]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368104    2 RKVVLITGASSGIGLALCKRLLAE------------DDELHLCLACRnmskaeAVCAALLASHPtAEVTIVQVDVSNLQS 69
Cdd:TIGR04504   1 GRVALVTGAARGIGAATVRRLAADgwrvvavdlcadDPAVGYPLATR------AELDAVAAACP-DQVLPVIADVRDPAA 73

                          90       100
                  ....*....|....*....|....*
gi 751368104   70 VFRASKELKQRFQRLDCIYLNAGIM 94
Cdd:TIGR04504  74 LAAAVALAVERWGRLDAAVAAAGVI 98

retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) OxidoReductase (LPOR) and related proteins, classical (c) SDRs; Classical SDR subgroup containing retinol-DHs, LPORs, and related proteins. Retinol is processed by a medium chain alcohol dehydrogenase followed by retinol-DHs. Pchlide reductases act in chlorophyll biosynthesis. There are distinct enzymes that catalyze Pchlide reduction in light or dark conditions. Light-dependent reduction is via an NADP-dependent SDR, LPOR. Proteins in this subfamily share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. This subgroup includes the human proteins: retinol dehydrogenase -12, -13 ,and -14, dehydrogenase/reductase SDR family member (DHRS)-12 , -13 and -X (a DHRS on chromosome X), and WWOX (WW domain-containing oxidoreductase), as well as a Neurospora crassa SDR encoded by the blue light inducible bli-4 gene. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368104   3 KVVLITGASSGIGLALCKRLLAEDDELHLclACRNMSKAEAVCAALLASHPTAEVTIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:cd05327    2 KVVVITGANSGIGKETARELAKRGAHVII--ACRNEEKGEEAAAEIKKETGNAKVEVIQLDLSSLASVRQFAEEFLARFP 79

                         90
                 ....*....|....*
gi 751368104  83 RLDCIYLNAGIMPNP 97
Cdd:cd05327   80 RLDILINNAGIMAPP 94

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 751368104   2 RKVVLITGASSGIGLALCKRLLAEDDelHLCLACRNMSKAEAVCAALlashpTAEVTIVQVDVSNLQSVFRASKELKQRF 81
Cdd:COG4221    5 GKVALITGASSGIGAATARALAAAGA--RVVLAARRAERLEALAAEL-----GGRALAVPLDVTDEAAVEAAVAAAVAEF 77

                         90
                 ....*....|....
gi 751368104  82 QRLDCIYLNAGIMP 95
Cdd:COG4221   78 GRLDVLVNNAGVAL 91

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368104    3 KVVLITGASSGIGLALCKRLLAEDDELHLCLacRNMSKAEAVCAALLASHPtaEVTIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVD--RSEEKLEAVAKELGALGG--KALFIQGDVTDRAQVKALVEQAVERLG 76

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 751368104   83 RLDCIYLNAGIMPNP--------------QLNIKALFFG 107
Cdd:pfam00106  77 RLDILVNNAGITGLGpfselsdedwerviDVNLTGVFNL 115

NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and metabolism]; NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family is part of the Pathway/BioSystem: Fatty acid biosynthesis

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368104   3 KVVLITGASSGIGLALCKRLLAEDDelHLCLACRNMSKAEAVCAALLASHptAEVTIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:COG1028    7 KVALVTGGSSGIGRAIARALAAEGA--RVVITDRDAEALEAAAAELRAAG--GRALAVAADVTDEAAVEALVAAAVAAFG 82

                         90
                 ....*....|...
gi 751368104  83 RLDCIYLNAGIMP 95
Cdd:COG1028   83 RLDILVNNAGITP 95

SDR family oxidoreductase;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368104   1 MRKVVLITGASSGIGLALCKRLLAEDDELHLClaCRNMSKAEAVCAALLASHPTAEVTIVQVDVSNLQSVFRASKELKQR 80
Cdd:PRK08251   1 TRQKILITGASSGLGAGMAREFAAKGRDLALC--ARRTDRLEELKAELLARYPGIKVAVAALDVNDHDQVFEVFAEFRDE 78

                         90
                 ....*....|...
gi 751368104  81 FQRLDCIYLNAGI 93
Cdd:PRK08251  79 LGGLDRVIVNAGI 91

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 751368104   3 KVVLITGASSGIGLALCKRLLAEDDELHLClaCRNMSKAEAVCAALLAShptaeVTIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:cd05374    1 KVVLITGCSSGIGLALALALAAQGYRVIAT--ARNPDKLESLGELLNDN-----LEVLELDVTDEESIKAAVKEVIERFG 73

                         90
                 ....*....|..
gi 751368104  83 RLDCIYLNAGIM 94
Cdd:cd05374   74 RIDVLVNNAGYG 85

light-dependent protochlorophyllide reductase (LPOR)-like, classical (c)-like SDRs; Classical SDR-like subgroup containing LPOR and related proteins. Protochlorophyllide (Pchlide) reductases act in chlorophyll biosynthesis. There are distinct enzymes that catalyze Pchlide reduction in light or dark conditions. Light-dependent reduction is via an NADP-dependent SDR, LPOR. Proteins in this subfamily share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. 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 751368104   2 RKVVLITGASSGIGLAlCKRLLAEDDELHLCLACRNMSKAEAvcAALLASHPTAEVTIVQVDVSNLQSVFRASKELKQRF 81
Cdd:cd09810    1 KGTVVITGASSGLGLA-AAKALARRGEWHVVMACRDFLKAEQ--AAQEVGMPKDSYSVLHCDLASLDSVRQFVDNFRRTG 77

                         90
                 ....*....|..
gi 751368104  82 QRLDCIYLNAGI 93
Cdd:cd09810   78 RPLDALVCNAAV 89

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 751368104   3 KVVLITGASSGIGLALCKRLLAEDDELHLClacrnmSKAEAVCAALLASHPTAEvtIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:cd05370    6 NTVLITGGTSGIGLALARKFLEAGNTVIIT------GRREERLAEAKKELPNIH--TIVLDVGDAESVEALAEALLSEYP 77

                         90
                 ....*....|..
gi 751368104  83 RLDCIYLNAGIM 94
Cdd:cd05370   78 NLDILINNAGIQ 89

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 751368104   5 VLITGASSGIGLALCKRLLAeDDELHLCLACRNMSKAEAVcAALLASHPtaEVTIVQVDVSNLQSvfRASKELKQRFQ-- 82
Cdd:cd05325    1 VLITGASRGIGLELVRQLLA-RGNNTVIATCRDPSAATEL-AALGASHS--RLHILELDVTDEIA--ESAEAVAERLGda 74

                         90
                 ....*....|....*..
gi 751368104  83 RLDCIYLNAGIMPNPQL 99
Cdd:cd05325   75 GLDVLINNAGILHSYGP 91

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 751368104   3 KVVLITGASSGIGLALCKRLLAEDDelHLCLACRNMSKAEAVCAALLASH--PTAEVTIVQVDVSNLQSVFRASKELKQR 80
Cdd:cd08939    2 KHVLITGGSSGIGKALAKELVKEGA--NVIIVARSESKLEEAVEEIEAEAnaSGQKVSYISADLSDYEEVEQAFAQAVEK 79

                         90
                 ....*....|...
gi 751368104  81 FQRLDCIYLNAGI 93
Cdd:cd08939   80 GGPPDLVVNCAGI 92

(S)-acetoin forming diacetyl reductase;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368104   1 MRKVVLITGASSGIGLALCKRLLAedDELHLCLACRNMSKAEAVCAALlaSHPTAEVTIVQVDVSNLQSVFRASKELKQR 80
Cdd:PRK08643   1 MSKVALVTGAGQGIGFAIAKRLVE--DGFKVAIVDYNEETAQAAADKL--SKDGGKAIAVKADVSDRDQVFAAVRQVVDT 76

                         90
                 ....*....|....*
gi 751368104  81 FQRLDCIYLNAGIMP 95
Cdd:PRK08643  77 FGDLNVVVNNAGVAP 91

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 751368104   3 KVVLITGASSGIGLALCKRLLAEDDelHLCLACRNMSKAEAVCAALLASHPTaEVTIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:cd05346    1 KTVLITGASSGIGEATARRFAKAGA--KLILTGRRAERLQELADELGAKFPV-KVLPLQLDVSDRESIEAALENLPEEFR 77

                         90
                 ....*....|
gi 751368104  83 RLDCIYLNAG 92
Cdd:cd05346   78 DIDILVNNAG 87

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 751368104   3 KVVLITGASSGIGLALCKRLLAEDDELHLClacrNMSKAEAVCAALLASHPTAEVTIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:cd05323    1 KVAIITGGASGIGLATAKLLLKKGAKVAIL----DRNENPGAAAELQAINPKVKATFVQCDVTSWEQLAAAFKKAIEKFG 76

                         90
                 ....*....|....*
gi 751368104  83 RLDCIYLNAGIMPNP 97
Cdd:cd05323   77 RVDILINNAGILDEK 91

protochlorophyllide reductase

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368104   6 LITGASSGIGLAlCKRLLAEDDELHLCLACRNMSKAEAvcAALLASHPTAEVTIVQVDVSNLQSVFRASKELKQRFQRLD 85
Cdd:PLN00015   1 IITGASSGLGLA-TAKALAETGKWHVVMACRDFLKAER--AAKSAGMPKDSYTVMHLDLASLDSVRQFVDNFRRSGRPLD 77

                 ....*...
gi 751368104  86 CIYLNAGI 93
Cdd:PLN00015  78 VLVCNAAV 85

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368104   3 KVVLITGASSGIGLALCKRLLAEDdelhLCLACrnMSKAEAVCAALLASHPTAeVTIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:PRK06200   7 QVALITGGGSGIGRALVERFLAEG----ARVAV--LERSAEKLASLRQRFGDH-VLVVEGDVTSYADNQRAVDQTVDAFG 79

                         90
                 ....*....|.
gi 751368104  83 RLDCIYLNAGI 93
Cdd:PRK06200  80 KLDCFVGNAGI 90

SDR family oxidoreductase;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368104   3 KVVLITGASSGIGLALCKRLLAEDDelHLCLACRNMSKAEAVcAALLASHPTAevTIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:PRK07231   6 KVAIVTGASSGIGEGIARRFAAEGA--RVVVTDRNEEAAERV-AAEILAGGRA--IAVAADVSDEADVEAAVAAALERFG 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 751368104  83 RLDCIYLNAGIMPNPQ---------------LNIKALFFG 107
Cdd:PRK07231  81 SVDILVNNAGTTHRNGplldvdeaefdrifaVNVKSPYLW 120

human WWOX (WW domain-containing oxidoreductase)-like, classical (c)-like SDRs; Classical-like SDR domain of human WWOX and related proteins. Proteins in this subfamily share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. 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 751368104   3 KVVLITGASSGIGLALCKRLLAEDdeLHLCLACRNMSKAEAVCAALLASHPTAEVTIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:cd09809    2 KVIIITGANSGIGFETARSFALHG--AHVILACRNMSRASAAVSRILEEWHKARVEAMTLDLASLRSVQRFAEAFKAKNS 79

                         90
                 ....*....|....*
gi 751368104  83 RLDCIYLNAGIMPNP 97
Cdd:cd09809   80 PLHVLVCNAAVFALP 94

cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol reductases,including (6R)-2,2,6-trimethyl-1,4-cyclohexanedione (levodione) reductase of Corynebacterium aquaticum, catalyze the reversible oxidoreduction of hydroxycyclohexanone derivatives. 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 751368104   3 KVVLITGASSGIGLALCKRLLAEDDELhlCLACRNMSKAEAVCAALLASHPTAEVTIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:cd05330    4 KVVLITGGGSGLGLATAVRLAKEGAKL--SLVDLNEEGLEAAKAALLEIAPDAEVLLIKADVSDEAQVEAYVDATVEQFG 81

                         90
                 ....*....|.
gi 751368104  83 RLDCIYLNAGI 93
Cdd:cd05330   82 RIDGFFNNAGI 92

SDR family oxidoreductase;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368104   3 KVVLITGASSGIGLALCKRLLAEDDELhlCLACRNMSKAEAVCAALLASHPTAEVTIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:PRK07063   8 KVALVTGAAQGIGAAIARAFAREGAAV--ALADLDAALAERAAAAIARDVAGARVLAVPADVTDAASVAAAVAAAEEAFG 85

                         90
                 ....*....|.
gi 751368104  83 RLDCIYLNAGI 93
Cdd:PRK07063  86 PLDVLVNNAGI 96

cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB) is a classical SDR, it is of particular importance for its role in the degradation of biphenyl/polychlorinated biphenyls(PCBs); PCBs are a significant source of environmental contamination. This subgroup also includes Pseudomonas putida F1 cis-biphenyl-1,2-dihydrodiol-1,2-dehydrogenase (aka cis-benzene glycol dehydrogenase, encoded by the bnzE gene), which participates in benzene metabolism. In addition it includes Pseudomonas sp. C18 putative 1,2-dihydroxy-1,2-dihydronaphthalene dehydrogenase (aka dibenzothiophene dihydrodiol dehydrogenase, encoded by the doxE gene) which participates in an upper naphthalene catabolic pathway. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368104   3 KVVLITGASSGIGLALCKRLLAEDDELHLclacrnMSKAEAVCAALLASHPTAeVTIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:cd05348    5 EVALITGGGSGLGRALVERFVAEGAKVAV------LDRSAEKVAELRADFGDA-VVGVEGDVRSLADNERAVARCVERFG 77

                         90
                 ....*....|.
gi 751368104  83 RLDCIYLNAGI 93
Cdd:cd05348   78 KLDCFIGNAGI 88

SDR family oxidoreductase;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368104   2 RKVVLITGASSGIGLALCKRLLAEDdeLHLCLACRNMSKAEAVcAALLASHPtAEVTIVQVDVSNLQSVFRASKELKQRF 81
Cdd:PRK06181   1 GKVVIITGASEGIGRALAVRLARAG--AQLVLAARNETRLASL-AQELADHG-GEALVVPTDVSDAEACERLIEAAVARF 76

                         90
                 ....*....|..
gi 751368104  82 QRLDCIYLNAGI 93
Cdd:PRK06181  77 GGIDILVNNAGI 88

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368104   5 VLITGASSGIGLALCKRLLAEDdeLHLCLACRNMSKAEAVCAALLAshPTAEVTIVQVDVSNLQSVFRASKELKQRFQRL 84
Cdd:cd05350    1 VLITGASSGIGRALAREFAKAG--YNVALAARRTDRLDELKAELLN--PNPSVEVEILDVTDEERNQLVIAELEAELGGL 76

                 ....*....
gi 751368104  85 DCIYLNAGI 93
Cdd:cd05350   77 DLVIINAGV 85

short chain dehydrogenase; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368104   3 KVVLITGASSGIGLAlCKRLLAEDDElHLCLACRNMSKAEaVCAALLASHPTAevtiVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:PRK06841  16 KVAVVTGGASGIGHA-IAELFAAKGA-RVALLDRSEDVAE-VAAQLLGGNAKG----LVCDVSDSQSVEAAVAAVISAFG 88

                         90
                 ....*....|...
gi 751368104  83 RLDCIYLNAGIMP 95
Cdd:PRK06841  89 RIDILVNSAGVAL 101

SDR family oxidoreductase;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368104   3 KVVLITGASSGIGLALCKRLLAEDDELHLClaCRNMSKAEAVCAALLASHPTAEVTIVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:PRK07062   9 RVAVVTGGSSGIGLATVELLLEAGASVAIC--GRDEERLASAEARLREKFPGARLLAARCDVLDEADVAAFAAAVEARFG 86

                         90
                 ....*....|
gi 751368104  83 RLDCIYLNAG 92
Cdd:PRK07062  87 GVDMLVNNAG 96

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 751368104   3 KVVLITGASSGIGLALCKRLLaeddEL--HLCLACRNMSKAEAVCAALLASHPtAEVTIVQVDVSNLQSVFRASKELKQR 80
Cdd:cd05369    4 KVAFITGGGTGIGKAIAKAFA----ELgaSVAIAGRKPEVLEAAAEEISSATG-GRAHPIQCDVRDPEAVEAAVDETLKE 78

                         90       100
                 ....*....|....*....|....*.
gi 751368104  81 FQRLDCIYLNAG---IMPNPQLNIKA 103
Cdd:cd05369   79 FGKIDILINNAAgnfLAPAESLSPNG 104

SDR family oxidoreductase;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368104   3 KVVLITGASSGIGLALCKRLLaeDDELHLCLACRNMSKAEAVcaallasHPTAEVTIVQVDVSNLQSVfrasKELKQRF- 81
Cdd:PRK08177   2 RTALIIGASRGLGLGLVDRLL--ERGWQVTATVRGPQQDTAL-------QALPGVHIEKLDMNDPASL----DQLLQRLq 68

                         90       100       110
                 ....*....|....*....|....*....|....
gi 751368104  82 -QRLDCIYLNAGIM-PNPQLNIKA-------LFF 106
Cdd:PRK08177  69 gQRFDLLFVNAGISgPAHQSAADAtaaeigqLFL 102

SDR family oxidoreductase;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751368104   3 KVVLITGASSGIGLALCKRlLAEDDELHLCLAcRNMSKAEAVCAALLASHPTAEVtiVQVDVSNLQSVFRASKELKQRFQ 82
Cdd:PRK07201 372 KVVLITGASSGIGRATAIK-VAEAGATVFLVA-RNGEALDELVAEIRAKGGTAHA--YTCDLTDSAAVDHTVKDILAEHG 447

                         90
                 ....*....|
gi 751368104  83 RLDCIYLNAG 92
Cdd:PRK07201 448 HVDYLVNNAG 457