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 ...
1-327
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: 619.38 E-value: 0e+00
ketol-acid reductoisomerase; This is the second enzyme in the parallel isoleucine-valine ...
14-326
5.57e-148
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: 419.09 E-value: 5.57e-148
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: 287.90 E-value: 1.63e-98
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
14-81
1.19e-03
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases 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. 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. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. 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. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.
Pssm-ID: 240642 [Multi-domain] Cd Length: 314 Bit Score: 40.30 E-value: 1.19e-03
Ketol-acid reductoisomerase [Amino acid transport and metabolism, Coenzyme transport and ...
1-327
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: 619.38 E-value: 0e+00
ketol-acid reductoisomerase; This is the second enzyme in the parallel isoleucine-valine ...
14-326
5.57e-148
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: 419.09 E-value: 5.57e-148
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: 287.90 E-value: 1.63e-98
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: 234.67 E-value: 6.75e-78
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
14-81
1.19e-03
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases 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. 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. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. 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. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.
Pssm-ID: 240642 [Multi-domain] Cd Length: 314 Bit Score: 40.30 E-value: 1.19e-03
D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; This domain is inserted ...
14-81
7.90e-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: 7.90e-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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Functional characterization of the conserved domain architecture found on the query.
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(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
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