NADP oxidoreductase coenzyme F420-dependent;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1568946656  43 SALARLWVEAG-HEVMI-SSRHPERLQALADELGERARVGTPREAAAFGEVILLAVPYAATPQVGRDYAAELAGKVLLDA 120
Cdd:pfam03807  10 EALARGLVAAGpHEVVVaNSRNPEKAEELAEEYGVGATAVDNEEAAEEADVVFLAVKPEDAPDVLSELSDLLKGKIVISI 89

                  ...
gi 1568946656 121 GNP 123
Cdd:pfam03807  90 AAG 92

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
                  ....*....|....*....|....*....|..
gi 1568946656  44 ALARLWVEAGHEVMISSRHPERLQALADELGE 75
Cdd:cd05346    15 ATARRFAKAGAKLILTGRRAERLQELADELGA 46

NADP oxidoreductase coenzyme F420-dependent;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1568946656  43 SALARLWVEAG-HEVMI-SSRHPERLQALADELGERARVGTPREAAAFGEVILLAVPYAATPQVGRDYAAELAGKVLLDA 120
Cdd:pfam03807  10 EALARGLVAAGpHEVVVaNSRNPEKAEELAEEYGVGATAVDNEEAAEEADVVFLAVKPEDAPDVLSELSDLLKGKIVISI 89

                  ...
gi 1568946656 121 GNP 123
Cdd:pfam03807  90 AAG 92

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
                  ....*....|....*....|....*....|....*.
gi 1568946656  44 ALARLWVEAGHEVMISSRHPERLQALADELGERARV 79
Cdd:COG4221    20 ATARALAAAGARVVLAARRAERLEALAAELGGRALA 55

bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase YdfG;

                          10        20        30
                  ....*....|....*....|....*....|..
gi 1568946656  44 ALARLWVEAGHEVMISSRHPERLQALADELGE 75
Cdd:PRK10538   15 CITRRFIQQGHKVIATGRRQERLQELKDELGD 46

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
                  ....*....|....*....|....*....|..
gi 1568946656  44 ALARLWVEAGHEVMISSRHPERLQALADELGE 75
Cdd:cd05346    15 ATARRFAKAGAKLILTGRRAERLQELADELGA 46

pyrroline-5-carboxylate reductase; Reviewed

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1568946656  38 TGNIGSALARLWVEAG---HEVMISSRHPERLQALADELGERArVGTPREAAAFGEVILLAVpyaaTPQVGRDYAAELAG 114
Cdd:PRK11880   10 GGNMASAIIGGLLASGvpaKDIIVSDPSPEKRAALAEEYGVRA-ATDNQEAAQEADVVVLAV----KPQVMEEVLSELKG 84

                  ..
gi 1568946656 115 KV 116
Cdd:PRK11880   85 QL 86