ketol-acid reductoisomerase (KARI) catalyzes the conversion of acetohydroxy acids into dihydroxy valerates, which is the second reaction in the synthetic pathway of the essential branched side chain amino acids valine and isoleucine
ketol-acid reductoisomerase; This is the second enzyme in the parallel isoleucine-valine ...
116-449
1.90e-59
ketol-acid reductoisomerase; This is the second enzyme in the parallel isoleucine-valine biosynthetic pathway [Amino acid biosynthesis, Pyruvate family]
The actual alignment was detected with superfamily member TIGR00465:
Pssm-ID: 273093 [Multi-domain] Cd Length: 314 Bit Score: 200.68 E-value: 1.90e-59
ketol-acid reductoisomerase; This is the second enzyme in the parallel isoleucine-valine ...
116-449
1.90e-59
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: 200.68 E-value: 1.90e-59
Ketol-acid reductoisomerase [Amino acid transport and metabolism, Coenzyme transport and ...
113-444
4.15e-52
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: 181.41 E-value: 4.15e-52
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: 152.70 E-value: 2.17e-43
ketol-acid reductoisomerase; This is the second enzyme in the parallel isoleucine-valine ...
116-449
1.90e-59
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: 200.68 E-value: 1.90e-59
Ketol-acid reductoisomerase [Amino acid transport and metabolism, Coenzyme transport and ...
113-444
4.15e-52
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: 181.41 E-value: 4.15e-52
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: 152.70 E-value: 2.17e-43
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: 142.61 E-value: 3.90e-40
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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This image shows a graphical summary of conserved domains identified on the query sequence.
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if a domain or superfamily has been annotated with functional sites (conserved features),
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click on the bars or triangles to view your query sequence embedded in a multiple sequence alignment of the proteins used to develop the corresponding domain model.
The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
Click on the domain model's accession number to view the multiple sequence alignment of the proteins used to develop the corresponding domain model.
To view your query sequence embedded in that multiple sequence alignment, click on the colored bars in the Graphical Summary portion of the search results page,
or click on the triangles, if present, that represent functional sites (conserved features)
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Concise Display shows only the best scoring domain model, in each hit category listed below except non-specific hits, for each region on the query sequence.
(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.
(labeled illustration) Full Display shows all domain models, in each hit category below, that meet or exceed the RPS-BLAST threshold for statistical significance.
(labeled illustration) Four types of hits can be shown, as available,
for each region on the query sequence:
specific hits meet or exceed a domain-specific e-value threshold
(illustrated example)
and represent a very high confidence that the query sequence belongs to the same protein family as the sequences use to create the domain model
non-specific hits
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advanced search options)
the domain superfamily to which the specific and non-specific hits belong
multi-domain models that were computationally detected and are likely to contain multiple single domains
Retrieve proteins that contain one or more of the domains present in the query sequence, using the Conserved Domain Architecture Retrieval Tool
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