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Protein

Ketol-acid reductoisomerase (NADP(+))

Gene

ilvC

Organism
Psychrobacter cryohalolentis (strain K5)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate.UniRule annotation

Catalytic activityi

(2R)-2,3-dihydroxy-3-methylbutanoate + NADP+ = (2S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH.UniRule annotation
(2R,3R)-2,3-dihydroxy-3-methylpentanoate + NADP+ = (S)-2-hydroxy-2-ethyl-3-oxobutanoate + NADPH.UniRule annotation

Cofactori

Mg2+UniRule annotationNote: Binds 2 magnesium ions per subunit.UniRule annotation

Pathwayi: L-isoleucine biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes L-isoleucine from 2-oxobutanoate.UniRule annotation
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Acetolactate synthase (Pcryo_0522)
  2. Ketol-acid reductoisomerase (NADP(+)) (ilvC)
  3. Dihydroxy-acid dehydratase (ilvD)
  4. no protein annotated in this organism
This subpathway is part of the pathway L-isoleucine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-isoleucine from 2-oxobutanoate, the pathway L-isoleucine biosynthesis and in Amino-acid biosynthesis.

Pathwayi: L-valine biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes L-valine from pyruvate.UniRule annotation
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Acetolactate synthase (Pcryo_0522)
  2. Ketol-acid reductoisomerase (NADP(+)) (ilvC)
  3. Dihydroxy-acid dehydratase (ilvD)
  4. no protein annotated in this organism
This subpathway is part of the pathway L-valine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-valine from pyruvate, the pathway L-valine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei47 – 471NADPUniRule annotation
Binding sitei50 – 501NADPUniRule annotation
Binding sitei52 – 521NADPUniRule annotation
Active sitei107 – 1071UniRule annotation
Binding sitei133 – 1331NADP; via amide nitrogenUniRule annotation
Metal bindingi190 – 1901Magnesium 1UniRule annotation
Metal bindingi190 – 1901Magnesium 2UniRule annotation
Metal bindingi194 – 1941Magnesium 1UniRule annotation
Metal bindingi226 – 2261Magnesium 2UniRule annotation
Metal bindingi230 – 2301Magnesium 2UniRule annotation
Binding sitei251 – 2511SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi24 – 274NADPUniRule annotation
Nucleotide bindingi82 – 854NADPUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Amino-acid biosynthesis, Branched-chain amino acid biosynthesis

Keywords - Ligandi

Magnesium, Metal-binding, NADP, Nucleotide-binding

Enzyme and pathway databases

BioCyciPCRY335284:GHE9-541-MONOMER.
UniPathwayiUPA00047; UER00056.
UPA00049; UER00060.

Names & Taxonomyi

Protein namesi
Recommended name:
Ketol-acid reductoisomerase (NADP(+))UniRule annotation (EC:1.1.1.86UniRule annotation)
Short name:
KARIUniRule annotation
Alternative name(s):
Acetohydroxy-acid isomeroreductaseUniRule annotation
Short name:
AHIRUniRule annotation
Alpha-keto-beta-hydroxylacyl reductoisomeraseUniRule annotation
Ketol-acid reductoisomerase type 1UniRule annotation
Ketol-acid reductoisomerase type IUniRule annotation
Gene namesi
Name:ilvCUniRule annotation
Ordered Locus Names:Pcryo_0524
OrganismiPsychrobacter cryohalolentis (strain K5)
Taxonomic identifieri335284 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaePsychrobacter
Proteomesi
  • UP000002425 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 338338Ketol-acid reductoisomerase (NADP(+))PRO_0000252774Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi335284.Pcryo_0524.

Structurei

3D structure databases

ProteinModelPortaliQ1QDE6.
SMRiQ1QDE6. Positions 1-327.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini14 – 177164IlvNUniRule annotationAdd
BLAST
Domaini183 – 326144IlvCUniRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the ketol-acid reductoisomerase family.UniRule annotation
Contains 1 IlvC domain.UniRule annotation
Contains 1 IlvN domain.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105C6M. Bacteria.
COG0059. LUCA.
HOGENOMiHOG000016230.
KOiK00053.
OMAiWEGGIAK.
OrthoDBiPOG091H063Y.

Family and domain databases

Gene3Di1.10.1040.10. 1 hit.
3.50.50.60. 1 hit.
HAMAPiMF_00435. IlvC. 1 hit.
InterProiIPR008927. 6-PGluconate_DH_C-like.
IPR013328. 6PGD_dom_2.
IPR000506. AcH_isomrdctse_C.
IPR023753. FAD/NAD-binding_dom.
IPR013116. IlvN.
IPR013023. Ketol-acid_reductoisomrdctse.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR21371. PTHR21371. 1 hit.
PfamiPF01450. IlvC. 1 hit.
PF07991. IlvN. 1 hit.
[Graphical view]
SUPFAMiSSF48179. SSF48179. 1 hit.
SSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR00465. ilvC. 1 hit.

Sequencei

Sequence statusi: Complete.

Q1QDE6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNVYYDKDCD LSIVQGKKVA IIGYGSQGHA HALNLQDSNV DVTVGLRANS
60 70 80 90 100
GSWKKAENAG LKVAEVEEAV KAADIIMILT PDEFQKELYN DVIEPNIKQG
110 120 130 140 150
ATLAFAHGFA IHYNQVIPRS DLDVIMVAPK APGHTVRSEF AKGGGIPDLI
160 170 180 190 200
AIYQDASGQA KQLALSYAAG VGGGRSGIIE TTFKDETETD LFGEQAVLCG
210 220 230 240 250
GAVELVKMGF ETLTEAGYAP EMAYFECLHE LKLIVDLMYE GGIADMNYSI
260 270 280 290 300
SNNAEYGEYV TGPEVINEQS REAMRNALKR IQSGEYAKMF ISEGATNYPS
310 320 330
MTARRRNNAE HQIEITGAKL RGMMPWIGGN KIIDKDKN
Length:338
Mass (Da):36,799
Last modified:May 16, 2006 - v1
Checksum:i5EAA1C2215AD99C6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000323 Genomic DNA. Translation: ABE74307.1.
RefSeqiWP_011512878.1. NC_007969.1.

Genome annotation databases

EnsemblBacteriaiABE74307; ABE74307; Pcryo_0524.
KEGGipcr:Pcryo_0524.
PATRICi23060511. VBIPsyCry128170_0593.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000323 Genomic DNA. Translation: ABE74307.1.
RefSeqiWP_011512878.1. NC_007969.1.

3D structure databases

ProteinModelPortaliQ1QDE6.
SMRiQ1QDE6. Positions 1-327.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi335284.Pcryo_0524.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABE74307; ABE74307; Pcryo_0524.
KEGGipcr:Pcryo_0524.
PATRICi23060511. VBIPsyCry128170_0593.

Phylogenomic databases

eggNOGiENOG4105C6M. Bacteria.
COG0059. LUCA.
HOGENOMiHOG000016230.
KOiK00053.
OMAiWEGGIAK.
OrthoDBiPOG091H063Y.

Enzyme and pathway databases

UniPathwayiUPA00047; UER00056.
UPA00049; UER00060.
BioCyciPCRY335284:GHE9-541-MONOMER.

Family and domain databases

Gene3Di1.10.1040.10. 1 hit.
3.50.50.60. 1 hit.
HAMAPiMF_00435. IlvC. 1 hit.
InterProiIPR008927. 6-PGluconate_DH_C-like.
IPR013328. 6PGD_dom_2.
IPR000506. AcH_isomrdctse_C.
IPR023753. FAD/NAD-binding_dom.
IPR013116. IlvN.
IPR013023. Ketol-acid_reductoisomrdctse.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR21371. PTHR21371. 1 hit.
PfamiPF01450. IlvC. 1 hit.
PF07991. IlvN. 1 hit.
[Graphical view]
SUPFAMiSSF48179. SSF48179. 1 hit.
SSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR00465. ilvC. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiILVC_PSYCK
AccessioniPrimary (citable) accession number: Q1QDE6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: May 16, 2006
Last modified: September 7, 2016
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.