MULTISPECIES: saccharopine dehydrogenase family protein [Burkholderia]
Protein Classification
saccharopine dehydrogenase family protein( domain architecture ID 11448323)
saccharopine dehydrogenase family protein such as saccharopine dehydrogenase, an enzyme of the alpha-aminoadipate pathway of lysine biosynthesis that catalyzes the reversible conversion of glutamate and alpha-aminoadipic-delta-semialdehyde to saccharopine
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||||
| Lys9 | COG1748 | Saccharopine dehydrogenase, NADP-dependent [Amino acid transport and metabolism]; Saccharopine ... |
25-355 | 1.27e-105 | ||||||
Saccharopine dehydrogenase, NADP-dependent [Amino acid transport and metabolism]; Saccharopine dehydrogenase, NADP-dependent is part of the Pathway/BioSystem: Lysine biosynthesis : Pssm-ID: 441354 [Multi-domain] Cd Length: 352 Bit Score: 314.08 E-value: 1.27e-105
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| trkA super family | cl35844 | Trk system potassium transporter TrkA; |
1-43 | 8.37e-05 | ||||||
Trk system potassium transporter TrkA; The actual alignment was detected with superfamily member PRK09496: Pssm-ID: 236541 [Multi-domain] Cd Length: 453 Bit Score: 44.34 E-value: 8.37e-05
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| Name | Accession | Description | Interval | E-value | ||||||
| Lys9 | COG1748 | Saccharopine dehydrogenase, NADP-dependent [Amino acid transport and metabolism]; Saccharopine ... |
25-355 | 1.27e-105 | ||||||
Saccharopine dehydrogenase, NADP-dependent [Amino acid transport and metabolism]; Saccharopine dehydrogenase, NADP-dependent is part of the Pathway/BioSystem: Lysine biosynthesis Pssm-ID: 441354 [Multi-domain] Cd Length: 352 Bit Score: 314.08 E-value: 1.27e-105
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| Sacchrp_dh_C | pfam16653 | Saccharopine dehydrogenase C-terminal domain; This family comprises the C-terminal domain of ... |
120-283 | 1.47e-20 | ||||||
Saccharopine dehydrogenase C-terminal domain; This family comprises the C-terminal domain of saccharopine dehydrogenase. In some organizms this enzyme is found as a bifunctional polypeptide with lysine ketoglutarate reductase. The saccharopine dehydrogenase can also function as a saccharopine reductase. Pssm-ID: 465219 Cd Length: 255 Bit Score: 89.66 E-value: 1.47e-20
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| SDR_e_a | cd05226 | Extended (e) and atypical (a) SDRs; Extended or atypical short-chain dehydrogenases/reductases ... |
3-72 | 3.86e-08 | ||||||
Extended (e) and atypical (a) SDRs; Extended or atypical short-chain dehydrogenases/reductases (SDRs, aka tyrosine-dependent oxidoreductases) are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they 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 numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, 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. 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. Pssm-ID: 187537 [Multi-domain] Cd Length: 176 Bit Score: 52.40 E-value: 3.86e-08
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| PRK07502 | PRK07502 | prephenate/arogenate dehydrogenase family protein; |
2-73 | 8.12e-07 | ||||||
prephenate/arogenate dehydrogenase family protein; Pssm-ID: 236034 [Multi-domain] Cd Length: 307 Bit Score: 49.97 E-value: 8.12e-07
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| trkA | PRK09496 | Trk system potassium transporter TrkA; |
1-43 | 8.37e-05 | ||||||
Trk system potassium transporter TrkA; Pssm-ID: 236541 [Multi-domain] Cd Length: 453 Bit Score: 44.34 E-value: 8.37e-05
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| Mdh | COG0039 | Malate/lactate dehydrogenase [Energy production and conversion]; Malate/lactate dehydrogenase ... |
1-46 | 2.46e-04 | ||||||
Malate/lactate dehydrogenase [Energy production and conversion]; Malate/lactate dehydrogenase is part of the Pathway/BioSystem: TCA cycle Pssm-ID: 439809 [Multi-domain] Cd Length: 302 Bit Score: 42.31 E-value: 2.46e-04
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| 2-desacetyl-2-hydroxyethyl_bacteriochlorophyllide_ | cd08255 | 2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup ... |
2-46 | 3.79e-03 | ||||||
2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family has members identified as 2-desacetyl-2-hydroxyethyl bacteriochlorophyllide A dehydrogenase and alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. Pssm-ID: 176217 [Multi-domain] Cd Length: 277 Bit Score: 38.79 E-value: 3.79e-03
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| NDP-sugDHase | TIGR03026 | nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ... |
1-40 | 5.61e-03 | ||||||
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent alcohol-to-acid oxidation of nucleotide-linked sugars. Examples include UDP-glucose 6-dehydrogenase (1.1.1.22), GDP-mannose 6-dehydrogenase (1.1.1.132), UDP-N-acetylglucosamine 6-dehydrogenase (1.1.1.136), UDP-N-acetyl-D-galactosaminuronic acid dehydrogenase, and UDP-N-acetyl-D-mannosaminuronic acid dehydrogenase. These enzymes are most often involved in the biosynthesis of polysaccharides and are often found in operons devoted to that purpose. All of these enzymes contain three Pfam domains, pfam03721, pfam00984, and pfam03720 for the N-terminal, central, and C-terminal regions respectively. Pssm-ID: 274399 [Multi-domain] Cd Length: 409 Bit Score: 38.36 E-value: 5.61e-03
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| Name | Accession | Description | Interval | E-value | ||||||
| Lys9 | COG1748 | Saccharopine dehydrogenase, NADP-dependent [Amino acid transport and metabolism]; Saccharopine ... |
25-355 | 1.27e-105 | ||||||
Saccharopine dehydrogenase, NADP-dependent [Amino acid transport and metabolism]; Saccharopine dehydrogenase, NADP-dependent is part of the Pathway/BioSystem: Lysine biosynthesis Pssm-ID: 441354 [Multi-domain] Cd Length: 352 Bit Score: 314.08 E-value: 1.27e-105
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| Sacchrp_dh_C | pfam16653 | Saccharopine dehydrogenase C-terminal domain; This family comprises the C-terminal domain of ... |
120-283 | 1.47e-20 | ||||||
Saccharopine dehydrogenase C-terminal domain; This family comprises the C-terminal domain of saccharopine dehydrogenase. In some organizms this enzyme is found as a bifunctional polypeptide with lysine ketoglutarate reductase. The saccharopine dehydrogenase can also function as a saccharopine reductase. Pssm-ID: 465219 Cd Length: 255 Bit Score: 89.66 E-value: 1.47e-20
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| YwnB | COG2910 | Putative NADH-flavin reductase [General function prediction only]; |
2-72 | 6.32e-11 | ||||||
Putative NADH-flavin reductase [General function prediction only]; Pssm-ID: 442154 [Multi-domain] Cd Length: 205 Bit Score: 61.03 E-value: 6.32e-11
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| TrkA | COG0569 | Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ... |
1-69 | 2.09e-09 | ||||||
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and metabolism, Signal transduction mechanisms]; Pssm-ID: 440335 [Multi-domain] Cd Length: 296 Bit Score: 57.77 E-value: 2.09e-09
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| TyrA | COG0287 | Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is ... |
1-73 | 2.16e-09 | ||||||
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis Pssm-ID: 440056 [Multi-domain] Cd Length: 278 Bit Score: 57.83 E-value: 2.16e-09
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| YbjT | COG0702 | Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General ... |
2-73 | 5.93e-09 | ||||||
Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General function prediction only]; Pssm-ID: 440466 [Multi-domain] Cd Length: 215 Bit Score: 55.62 E-value: 5.93e-09
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| SDR_e_a | cd05226 | Extended (e) and atypical (a) SDRs; Extended or atypical short-chain dehydrogenases/reductases ... |
3-72 | 3.86e-08 | ||||||
Extended (e) and atypical (a) SDRs; Extended or atypical short-chain dehydrogenases/reductases (SDRs, aka tyrosine-dependent oxidoreductases) are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they 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 numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, 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. 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. Pssm-ID: 187537 [Multi-domain] Cd Length: 176 Bit Score: 52.40 E-value: 3.86e-08
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| Sacchrp_dh_NADP | pfam03435 | Saccharopine dehydrogenase NADP binding domain; This family contains the NADP binding domain ... |
3-108 | 4.93e-08 | ||||||
Saccharopine dehydrogenase NADP binding domain; This family contains the NADP binding domain of saccharopine dehydrogenase. In some organizms this enzyme is found as a bifunctional polypeptide with lysine ketoglutarate reductase. The saccharopine dehydrogenase can also function as a saccharopine reductase. Pssm-ID: 397480 [Multi-domain] Cd Length: 120 Bit Score: 51.05 E-value: 4.93e-08
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| WcaG | COG0451 | Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis]; |
2-71 | 6.35e-08 | ||||||
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 440220 [Multi-domain] Cd Length: 295 Bit Score: 53.44 E-value: 6.35e-08
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| PCBER_SDR_a | cd05259 | phenylcoumaran benzylic ether reductase (PCBER) like, atypical (a) SDRs; PCBER and ... |
2-73 | 2.31e-07 | ||||||
phenylcoumaran benzylic ether reductase (PCBER) like, atypical (a) SDRs; PCBER and pinoresinol-lariciresinol reductases are NADPH-dependent aromatic alcohol reductases, and are atypical members of the SDR family. Other proteins in this subgroup are identified as eugenol synthase. These proteins contain an N-terminus characteristic of NAD(P)-binding proteins and a small C-terminal domain presumed to be involved in substrate binding, but they do not have the conserved active site Tyr residue typically found in SDRs. Numerous other members have unknown functions. The glycine rich NADP-binding motif in this subgroup is of 2 forms: GXGXXG and G[GA]XGXXG; it tends to be atypical compared with the forms generally seen in classical or extended SDRs. The usual SDR active site tetrad is not present, but a critical active site Lys at the usual SDR position has been identified in various members, though other charged and polar residues are found at this position in this subgroup. Atypical SDR-related proteins retain the Rossmann fold of the SDRs, but have limited sequence identity and generally lack the catalytic properties of the archetypical members. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they 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 numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, 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. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, 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. Pssm-ID: 187569 [Multi-domain] Cd Length: 282 Bit Score: 51.53 E-value: 2.31e-07
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| TrkA_N | pfam02254 | TrkA-N domain; This domain is found in a wide variety of proteins. These proteins include ... |
3-73 | 3.49e-07 | ||||||
TrkA-N domain; This domain is found in a wide variety of proteins. These proteins include potassium channels, phosphoesterases, and various other transporters. This domain binds to NAD. Pssm-ID: 426679 [Multi-domain] Cd Length: 115 Bit Score: 48.29 E-value: 3.49e-07
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| PRK07502 | PRK07502 | prephenate/arogenate dehydrogenase family protein; |
2-73 | 8.12e-07 | ||||||
prephenate/arogenate dehydrogenase family protein; Pssm-ID: 236034 [Multi-domain] Cd Length: 307 Bit Score: 49.97 E-value: 8.12e-07
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| FadB | COG1250 | 3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA ... |
1-68 | 1.80e-06 | ||||||
3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA dehydrogenase is part of the Pathway/BioSystem: Fatty acid biosynthesis Pssm-ID: 440862 [Multi-domain] Cd Length: 281 Bit Score: 48.95 E-value: 1.80e-06
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| AdhP | COG1064 | D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport ... |
2-73 | 2.71e-06 | ||||||
D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport and metabolism]; Pssm-ID: 440684 [Multi-domain] Cd Length: 332 Bit Score: 48.57 E-value: 2.71e-06
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| PRK14806 | PRK14806 | bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; ... |
2-73 | 6.31e-06 | ||||||
bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; Provisional Pssm-ID: 237820 [Multi-domain] Cd Length: 735 Bit Score: 48.07 E-value: 6.31e-06
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| 3HCDH_N | pfam02737 | 3-hydroxyacyl-CoA dehydrogenase, NAD binding domain; This family also includes lambda ... |
2-71 | 7.51e-06 | ||||||
3-hydroxyacyl-CoA dehydrogenase, NAD binding domain; This family also includes lambda crystallin. Pssm-ID: 397037 [Multi-domain] Cd Length: 180 Bit Score: 45.99 E-value: 7.51e-06
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| PRK07060 | PRK07060 | short chain dehydrogenase; Provisional |
3-70 | 7.99e-06 | ||||||
short chain dehydrogenase; Provisional Pssm-ID: 180817 [Multi-domain] Cd Length: 245 Bit Score: 46.63 E-value: 7.99e-06
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| MviM | COG0673 | Predicted dehydrogenase [General function prediction only]; |
1-73 | 8.09e-06 | ||||||
Predicted dehydrogenase [General function prediction only]; Pssm-ID: 440437 [Multi-domain] Cd Length: 295 Bit Score: 46.84 E-value: 8.09e-06
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| PRK08324 | PRK08324 | bifunctional aldolase/short-chain dehydrogenase; |
2-70 | 1.89e-05 | ||||||
bifunctional aldolase/short-chain dehydrogenase; Pssm-ID: 236241 [Multi-domain] Cd Length: 681 Bit Score: 46.38 E-value: 1.89e-05
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| MmsB | COG2084 | 3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ... |
1-75 | 2.52e-05 | ||||||
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport and metabolism]; Pssm-ID: 441687 [Multi-domain] Cd Length: 285 Bit Score: 45.49 E-value: 2.52e-05
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| PRK09599 | PRK09599 | NADP-dependent phosphogluconate dehydrogenase; |
1-73 | 2.88e-05 | ||||||
NADP-dependent phosphogluconate dehydrogenase; Pssm-ID: 236582 [Multi-domain] Cd Length: 301 Bit Score: 45.12 E-value: 2.88e-05
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| COG2085 | COG2085 | Predicted dinucleotide-binding enzyme [General function prediction only]; |
3-75 | 4.46e-05 | ||||||
Predicted dinucleotide-binding enzyme [General function prediction only]; Pssm-ID: 441688 [Multi-domain] Cd Length: 205 Bit Score: 44.01 E-value: 4.46e-05
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| BVR-B_like_SDR_a | cd05244 | biliverdin IX beta reductase (BVR-B, aka flavin reductase)-like proteins; atypical (a) SDRs; ... |
2-72 | 4.75e-05 | ||||||
biliverdin IX beta reductase (BVR-B, aka flavin reductase)-like proteins; atypical (a) SDRs; Human BVR-B catalyzes pyridine nucleotide-dependent production of bilirubin-IX beta during fetal development; in the adult BVR-B has flavin and ferric reductase activities. Human BVR-B catalyzes the reduction of FMN, FAD, and riboflavin. Recognition of flavin occurs mostly by hydrophobic interactions, accounting for the broad substrate specificity. Atypical SDRs are distinct from classical SDRs. BVR-B does not share the key catalytic triad, or conserved tyrosine typical of SDRs. The glycine-rich NADP-binding motif of BVR-B is GXXGXXG, which is similar but not identical to the pattern seen in extended SDRs. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they 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 numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, 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. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, 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. Pssm-ID: 187555 [Multi-domain] Cd Length: 207 Bit Score: 43.77 E-value: 4.75e-05
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| trkA | PRK09496 | Trk system potassium transporter TrkA; |
1-43 | 8.37e-05 | ||||||
Trk system potassium transporter TrkA; Pssm-ID: 236541 [Multi-domain] Cd Length: 453 Bit Score: 44.34 E-value: 8.37e-05
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| PRK06223 | PRK06223 | malate dehydrogenase; Reviewed |
1-67 | 8.88e-05 | ||||||
malate dehydrogenase; Reviewed Pssm-ID: 180477 [Multi-domain] Cd Length: 307 Bit Score: 43.96 E-value: 8.88e-05
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| NAD_binding_10 | pfam13460 | NAD(P)H-binding; |
7-72 | 1.13e-04 | ||||||
NAD(P)H-binding; Pssm-ID: 463885 [Multi-domain] Cd Length: 183 Bit Score: 42.59 E-value: 1.13e-04
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| CAD | cd08245 | Cinnamyl alcohol dehydrogenases (CAD) and related proteins; Cinnamyl alcohol dehydrogenases ... |
2-70 | 1.17e-04 | ||||||
Cinnamyl alcohol dehydrogenases (CAD) and related proteins; Cinnamyl alcohol dehydrogenases (CAD), members of the medium chain dehydrogenase/reductase family, reduce cinnamaldehydes to cinnamyl alcohols in the last step of monolignal metabolism in plant cells walls. CAD binds 2 zinc ions and is NADPH- dependent. CAD family members are also found in non-plant species, e.g. in yeast where they have an aldehyde reductase activity. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes, or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines. Pssm-ID: 176207 [Multi-domain] Cd Length: 330 Bit Score: 43.46 E-value: 1.17e-04
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| Zn_ADH10 | cd08263 | Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ... |
3-74 | 1.19e-04 | ||||||
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction. Pssm-ID: 176224 [Multi-domain] Cd Length: 367 Bit Score: 43.51 E-value: 1.19e-04
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| YdfG | COG4221 | NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ... |
2-70 | 1.70e-04 | ||||||
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 Pssm-ID: 443365 [Multi-domain] Cd Length: 240 Bit Score: 42.48 E-value: 1.70e-04
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| F420_oxidored | pfam03807 | NADP oxidoreductase coenzyme F420-dependent; |
4-75 | 1.79e-04 | ||||||
NADP oxidoreductase coenzyme F420-dependent; Pssm-ID: 397743 [Multi-domain] Cd Length: 92 Bit Score: 39.91 E-value: 1.79e-04
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| SDR_a5 | cd05243 | atypical (a) SDRs, subgroup 5; This subgroup contains atypical SDRs, some of which are ... |
2-72 | 2.05e-04 | ||||||
atypical (a) SDRs, subgroup 5; This subgroup contains atypical SDRs, some of which are identified as putative NAD(P)-dependent epimerases, one as a putative NAD-dependent epimerase/dehydratase. Atypical SDRs are distinct from classical SDRs. Members of this subgroup have a glycine-rich NAD(P)-binding motif that is very similar to the extended SDRs, GXXGXXG, and binds NADP. Generally, this subgroup has poor conservation of the active site tetrad; however, individual sequences do contain matches to the YXXXK active site motif, the upstream Ser, and there is a highly conserved Asp in place of the usual active site Asn throughout the subgroup. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they 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 numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, 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. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, 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. Pssm-ID: 187554 [Multi-domain] Cd Length: 203 Bit Score: 41.84 E-value: 2.05e-04
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| Mdh | COG0039 | Malate/lactate dehydrogenase [Energy production and conversion]; Malate/lactate dehydrogenase ... |
1-46 | 2.46e-04 | ||||||
Malate/lactate dehydrogenase [Energy production and conversion]; Malate/lactate dehydrogenase is part of the Pathway/BioSystem: TCA cycle Pssm-ID: 439809 [Multi-domain] Cd Length: 302 Bit Score: 42.31 E-value: 2.46e-04
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| ProC | COG0345 | Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ... |
1-69 | 3.72e-04 | ||||||
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; Pyrroline-5-carboxylate reductase is part of the Pathway/BioSystem: Proline biosynthesis Pssm-ID: 440114 [Multi-domain] Cd Length: 267 Bit Score: 41.59 E-value: 3.72e-04
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| PanE | COG1893 | Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of ... |
1-75 | 3.98e-04 | ||||||
Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis Pssm-ID: 441497 [Multi-domain] Cd Length: 305 Bit Score: 41.77 E-value: 3.98e-04
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| Epimerase | pfam01370 | NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. ... |
7-71 | 4.89e-04 | ||||||
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. The proteins in this family use nucleotide-sugar substrates for a variety of chemical reactions. Pssm-ID: 396097 [Multi-domain] Cd Length: 238 Bit Score: 41.13 E-value: 4.89e-04
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| DapB_N | pfam01113 | Dihydrodipicolinate reductase, N-terminus; Dihydrodipicolinate reductase (DapB) reduces the ... |
1-69 | 4.96e-04 | ||||||
Dihydrodipicolinate reductase, N-terminus; Dihydrodipicolinate reductase (DapB) reduces the alpha,beta-unsaturated cyclic imine, dihydro-dipicolinate. This reaction is the second committed step in the biosynthesis of L-lysine and its precursor meso-diaminopimelate, which are critical for both protein and cell wall biosynthesis. The N-terminal domain of DapB binds the dinucleotide NADPH. Pssm-ID: 460069 [Multi-domain] Cd Length: 121 Bit Score: 39.52 E-value: 4.96e-04
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| PRK09260 | PRK09260 | 3-hydroxyacyl-CoA dehydrogenase; |
2-73 | 5.45e-04 | ||||||
3-hydroxyacyl-CoA dehydrogenase; Pssm-ID: 236434 [Multi-domain] Cd Length: 288 Bit Score: 41.31 E-value: 5.45e-04
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| ApbA | pfam02558 | Ketopantoate reductase PanE/ApbA; This is a family of 2-dehydropantoate 2-reductases also ... |
3-74 | 8.39e-04 | ||||||
Ketopantoate reductase PanE/ApbA; This is a family of 2-dehydropantoate 2-reductases also known as ketopantoate reductases, EC:1.1.1.169. The reaction catalyzed by this enzyme is: (R)-pantoate + NADP(+) <=> 2-dehydropantoate + NADPH. AbpA catalyzes the NADPH reduction of ketopantoic acid to pantoic acid in the alternative pyrimidine biosynthetic (APB) pathway. ApbA and PanE are allelic. ApbA, the ketopantoate reductase enzyme is required for the synthesis of thiamine via the APB biosynthetic pathway. Pssm-ID: 426831 [Multi-domain] Cd Length: 147 Bit Score: 39.52 E-value: 8.39e-04
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| SDR_a3 | cd05229 | atypical (a) SDRs, subgroup 3; These atypical SDR family members of unknown function have a ... |
1-71 | 1.04e-03 | ||||||
atypical (a) SDRs, subgroup 3; These atypical SDR family members of unknown function have a glycine-rich NAD(P)-binding motif consensus that is very similar to the extended SDRs, GXXGXXG. Generally, this group has poor conservation of the active site tetrad, However, individual sequences do contain matches to the YXXXK active site motif, and generally Tyr or Asn in place of the upstream Ser found in most SDRs. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they 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 numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, 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. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, 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. Pssm-ID: 187540 [Multi-domain] Cd Length: 302 Bit Score: 40.39 E-value: 1.04e-03
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| NDUFA9_like_SDR_a | cd05271 | NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, subunit 9, 39 kDa, (NDUFA9) -like, ... |
1-71 | 1.19e-03 | ||||||
NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, subunit 9, 39 kDa, (NDUFA9) -like, atypical (a) SDRs; This subgroup of extended SDR-like proteins are atypical SDRs. They have a glycine-rich NAD(P)-binding motif similar to the typical SDRs, GXXGXXG, and have the YXXXK active site motif (though not the other residues of the SDR tetrad). Members identified include NDUFA9 (mitochondrial) and putative nucleoside-diphosphate-sugar epimerase. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they 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 numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, 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. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, 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. Pssm-ID: 187579 [Multi-domain] Cd Length: 273 Bit Score: 40.31 E-value: 1.19e-03
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| PRK06522 | PRK06522 | 2-dehydropantoate 2-reductase; Reviewed |
1-45 | 1.28e-03 | ||||||
2-dehydropantoate 2-reductase; Reviewed Pssm-ID: 235821 [Multi-domain] Cd Length: 304 Bit Score: 40.22 E-value: 1.28e-03
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| DH-DHB-DH_SDR_c | cd05331 | 2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ... |
5-71 | 1.69e-03 | ||||||
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 dihydrozybenzoate dehydrogenase shares the characteristics of the classical SDRs. This subgroup includes Escherichai coli EntA which catalyzes the NAD+-dependent oxidation of 2,3-dihydro-2,3-dihydroxybenzoate to 2,3-dihydroxybenzoate during biosynthesis of the siderophore Enterobactin. 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. Pssm-ID: 187592 [Multi-domain] Cd Length: 244 Bit Score: 39.76 E-value: 1.69e-03
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| MDR | cd05188 | Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ... |
2-71 | 2.29e-03 | ||||||
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; The medium chain reductase/dehydrogenases (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH) , quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc. Pssm-ID: 176178 [Multi-domain] Cd Length: 271 Bit Score: 39.23 E-value: 2.29e-03
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| PRK14027 | PRK14027 | quinate/shikimate dehydrogenase (NAD+); |
6-73 | 2.30e-03 | ||||||
quinate/shikimate dehydrogenase (NAD+); Pssm-ID: 172521 [Multi-domain] Cd Length: 283 Bit Score: 39.25 E-value: 2.30e-03
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| YqjQ | COG0300 | Short-chain dehydrogenase [General function prediction only]; |
3-71 | 3.13e-03 | ||||||
Short-chain dehydrogenase [General function prediction only]; Pssm-ID: 440069 [Multi-domain] Cd Length: 252 Bit Score: 38.70 E-value: 3.13e-03
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| Kch | COG1226 | Voltage-gated potassium channel Kch [Inorganic ion transport and metabolism]; |
5-45 | 3.25e-03 | ||||||
Voltage-gated potassium channel Kch [Inorganic ion transport and metabolism]; Pssm-ID: 440839 [Multi-domain] Cd Length: 279 Bit Score: 38.94 E-value: 3.25e-03
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| 2-desacetyl-2-hydroxyethyl_bacteriochlorophyllide_ | cd08255 | 2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup ... |
2-46 | 3.79e-03 | ||||||
2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family has members identified as 2-desacetyl-2-hydroxyethyl bacteriochlorophyllide A dehydrogenase and alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. Pssm-ID: 176217 [Multi-domain] Cd Length: 277 Bit Score: 38.79 E-value: 3.79e-03
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| LDH-like_MDH | cd01339 | L-lactate dehydrogenase-like malate dehydrogenase proteins; Members of this subfamily have an ... |
3-35 | 3.95e-03 | ||||||
L-lactate dehydrogenase-like malate dehydrogenase proteins; Members of this subfamily have an LDH-like structure and an MDH enzymatic activity. Some members, like MJ0490 from Methanococcus jannaschii, exhibit both MDH and LDH activities. Tetrameric MDHs, including those from phototrophic bacteria, are more similar to LDHs than to other MDHs. LDH catalyzes the last step of glycolysis in which pyruvate is converted to L-lactate. MDH is one of the key enzymes in the citric acid cycle, facilitating both the conversion of malate to oxaloacetate and replenishing levels of oxalacetate by reductive carboxylation of pyruvate. The LDH-like MDHs are part of the NAD(P)-binding Rossmann fold superfamily, which includes a wide variety of protein families including the NAD(P)-binding domains of alcohol dehydrogenases, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate dehydrogenases, formate/glycerate dehydrogenases, siroheme synthases, 6-phosphogluconate dehydrogenases, aminoacid dehydrogenases, repressor rex, and NAD-binding potassium channel domains, among others. Pssm-ID: 133424 [Multi-domain] Cd Length: 300 Bit Score: 38.61 E-value: 3.95e-03
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| PRK11749 | PRK11749 | dihydropyrimidine dehydrogenase subunit A; Provisional |
1-46 | 4.56e-03 | ||||||
dihydropyrimidine dehydrogenase subunit A; Provisional Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 38.62 E-value: 4.56e-03
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| DHDPR_N | cd02274 | N-terminal NAD(P)-binding domain of dihydrodipicolinate reductase (DHDPR) and similar proteins; ... |
1-69 | 4.76e-03 | ||||||
N-terminal NAD(P)-binding domain of dihydrodipicolinate reductase (DHDPR) and similar proteins; DHDPR (EC 1.17.1.8), also called 4-hydroxy-tetrahydrodipicolinate reductase, or HTPA reductase, is a product of an essential gene referred to as dapB. It catalyzes the NAD(P)H-dependent reduction of 2,3-dihydrodipicolinate (DHDP) to 2,3,4,5-tetrahydrodipicolinate (THDP). DHDPR could also function as a dehydratase in addition to the role of a nucleotide dependent reductase. DHDPR is a component of the biosynthetic pathway that generates meso-diaminopimelate, a component of bacterial cell walls, and the amino acid L-lysine in various bacteria, archaea, cyanobacteria and higher plants. The enzyme is a homotetramer where each monomer is composed of two domains, an N-terminal NAD(P)-binding domain which forms a Rossmann fold, and a C-terminal substrate-binding domain that forms an open, mixed alpha-beta sandwich. Pssm-ID: 467611 [Multi-domain] Cd Length: 139 Bit Score: 37.15 E-value: 4.76e-03
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| NDP-sugDHase | TIGR03026 | nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ... |
1-40 | 5.61e-03 | ||||||
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent alcohol-to-acid oxidation of nucleotide-linked sugars. Examples include UDP-glucose 6-dehydrogenase (1.1.1.22), GDP-mannose 6-dehydrogenase (1.1.1.132), UDP-N-acetylglucosamine 6-dehydrogenase (1.1.1.136), UDP-N-acetyl-D-galactosaminuronic acid dehydrogenase, and UDP-N-acetyl-D-mannosaminuronic acid dehydrogenase. These enzymes are most often involved in the biosynthesis of polysaccharides and are often found in operons devoted to that purpose. All of these enzymes contain three Pfam domains, pfam03721, pfam00984, and pfam03720 for the N-terminal, central, and C-terminal regions respectively. Pssm-ID: 274399 [Multi-domain] Cd Length: 409 Bit Score: 38.36 E-value: 5.61e-03
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| Tdh | COG1063 | Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ... |
2-67 | 6.74e-03 | ||||||
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and metabolism, General function prediction only]; Threonine dehydrogenase or related Zn-dependent dehydrogenase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway Pssm-ID: 440683 [Multi-domain] Cd Length: 341 Bit Score: 38.20 E-value: 6.74e-03
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| PRK07588 | PRK07588 | FAD-binding domain; |
1-32 | 7.09e-03 | ||||||
FAD-binding domain; Pssm-ID: 169028 [Multi-domain] Cd Length: 391 Bit Score: 38.18 E-value: 7.09e-03
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