NADP-dependent ketol-acid reductoisomerase catalyzes the conversion of 2-(S)-acetolactate (2SAL) into (R)-dihydroxyisovalerate (RDHIV), the second step in the biosynthesis of the branched-chain amino acids (BCAAs) valine, leucine and isoleucine
Ketol-acid reductoisomerase [Amino acid transport and metabolism, Coenzyme transport and ...
1-329
0e+00
Ketol-acid reductoisomerase [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Ketol-acid reductoisomerase is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
Pssm-ID: 439829 [Multi-domain] Cd Length: 328 Bit Score: 580.86 E-value: 0e+00
ketol-acid reductoisomerase; This is the second enzyme in the parallel isoleucine-valine ...
15-330
9.37e-144
ketol-acid reductoisomerase; This is the second enzyme in the parallel isoleucine-valine biosynthetic pathway [Amino acid biosynthesis, Pyruvate family]
Pssm-ID: 273093 [Multi-domain] Cd Length: 314 Bit Score: 408.30 E-value: 9.37e-144
Acetohydroxy acid isomeroreductase, NADPH-binding domain; Acetohydroxy acid isomeroreductase catalyzes the conversion of acetohydroxy acids into dihydroxy valerates. This reaction is the second in the synthetic pathway of the essential branched side chain amino acids valine and isoleucine. This N-terminal region of the enzyme carries the binding-site for NADPH. The active-site for enzymatic activity lies in the C-terminal part, IlvC, pfam01450.
Pssm-ID: 285265 Cd Length: 165 Bit Score: 272.50 E-value: 1.72e-92
Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxy acid dehydrogenase ...
15-82
6.79e-03
Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxy acid dehydrogenase family; Formate dehydrogenase, D-specific 2-hydroxy acid dehydrogenase, Phosphoglycerate Dehydrogenase, Lactate dehydrogenase, Thermostable Phosphite Dehydrogenase, and Hydroxy(phenyl)pyruvate reductase, among others, share a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. 2-hydroxyacid dehydrogenases are enzymes that catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. Formate dehydrogenase (FDH) catalyzes the NAD+-dependent oxidation of formate ion to carbon dioxide with the concomitant reduction of NAD+ to NADH. FDHs of this family contain no metal ions or prosthetic groups. Catalysis occurs though direct transfer of hydride ion to NAD+ without the stages of acid-base catalysis typically found in related dehydrogenases. FDHs are found in all methylotrophic microorganisms in energy production and in the stress responses of plants. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-Adenosylhomocysteine Hydrolase, among others. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.
Pssm-ID: 240622 [Multi-domain] Cd Length: 302 Bit Score: 37.61 E-value: 6.79e-03
Ketol-acid reductoisomerase [Amino acid transport and metabolism, Coenzyme transport and ...
1-329
0e+00
Ketol-acid reductoisomerase [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Ketol-acid reductoisomerase is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
Pssm-ID: 439829 [Multi-domain] Cd Length: 328 Bit Score: 580.86 E-value: 0e+00
ketol-acid reductoisomerase; This is the second enzyme in the parallel isoleucine-valine ...
15-330
9.37e-144
ketol-acid reductoisomerase; This is the second enzyme in the parallel isoleucine-valine biosynthetic pathway [Amino acid biosynthesis, Pyruvate family]
Pssm-ID: 273093 [Multi-domain] Cd Length: 314 Bit Score: 408.30 E-value: 9.37e-144
Acetohydroxy acid isomeroreductase, NADPH-binding domain; Acetohydroxy acid isomeroreductase catalyzes the conversion of acetohydroxy acids into dihydroxy valerates. This reaction is the second in the synthetic pathway of the essential branched side chain amino acids valine and isoleucine. This N-terminal region of the enzyme carries the binding-site for NADPH. The active-site for enzymatic activity lies in the C-terminal part, IlvC, pfam01450.
Pssm-ID: 285265 Cd Length: 165 Bit Score: 272.50 E-value: 1.72e-92
Acetohydroxy acid isomeroreductase, catalytic domain; Acetohydroxy acid isomeroreductase catalyzes the conversion of acetohydroxy acids into dihydroxy valerates. This reaction is the second in the synthetic pathway of the essential branched side chain amino acids valine and isoleucine.
Pssm-ID: 460215 [Multi-domain] Cd Length: 138 Bit Score: 240.06 E-value: 3.95e-80
Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxy acid dehydrogenase ...
15-82
6.79e-03
Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxy acid dehydrogenase family; Formate dehydrogenase, D-specific 2-hydroxy acid dehydrogenase, Phosphoglycerate Dehydrogenase, Lactate dehydrogenase, Thermostable Phosphite Dehydrogenase, and Hydroxy(phenyl)pyruvate reductase, among others, share a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. 2-hydroxyacid dehydrogenases are enzymes that catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. Formate dehydrogenase (FDH) catalyzes the NAD+-dependent oxidation of formate ion to carbon dioxide with the concomitant reduction of NAD+ to NADH. FDHs of this family contain no metal ions or prosthetic groups. Catalysis occurs though direct transfer of hydride ion to NAD+ without the stages of acid-base catalysis typically found in related dehydrogenases. FDHs are found in all methylotrophic microorganisms in energy production and in the stress responses of plants. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-Adenosylhomocysteine Hydrolase, among others. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.
Pssm-ID: 240622 [Multi-domain] Cd Length: 302 Bit Score: 37.61 E-value: 6.79e-03
D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; This domain is inserted ...
15-82
7.39e-03
D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; This domain is inserted into the catalytic domain, the large dehydrogenase and D-lactate dehydrogenase families in SCOP. N-terminal portion of which is represented by family pfam00389.
Pssm-ID: 427007 [Multi-domain] Cd Length: 178 Bit Score: 36.71 E-value: 7.39e-03
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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