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Protein

Ketol-acid reductoisomerase (NADP(+))

Gene

ilvC

Organism
Thermosynechococcus elongatus (strain BP-1)
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 (ilvG)
  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 (ilvG)
  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 sitei51 – 511NADPUniRule annotation
Binding sitei53 – 531NADPUniRule annotation
Active sitei108 – 1081UniRule annotation
Binding sitei134 – 1341NADP; via amide nitrogenUniRule annotation
Metal bindingi191 – 1911Magnesium 1UniRule annotation
Metal bindingi191 – 1911Magnesium 2UniRule annotation
Metal bindingi195 – 1951Magnesium 1UniRule annotation
Metal bindingi227 – 2271Magnesium 2UniRule annotation
Metal bindingi231 – 2311Magnesium 2UniRule annotation
Binding sitei252 – 2521SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi25 – 284NADPUniRule annotation
Nucleotide bindingi83 – 864NADPUniRule 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

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:tll2254
OrganismiThermosynechococcus elongatus (strain BP-1)
Taxonomic identifieri197221 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesThermosynechococcus
Proteomesi
  • UP000000440 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 331331Ketol-acid reductoisomerase (NADP(+))PRO_0000151370Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi197221.tll2254.

Structurei

3D structure databases

ProteinModelPortaliQ8DGR0.
SMRiQ8DGR0. Positions 3-328.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini15 – 178164IlvNUniRule annotationAdd
BLAST
Domaini184 – 327144IlvCUniRule 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.
OMAiFETCHEL.
OrthoDBiPOG091H063Y.

Family and domain databases

Gene3Di1.10.1040.10. 1 hit.
HAMAPiMF_00435. IlvC. 1 hit.
InterProiIPR008927. 6-PGluconate_DH_C-like.
IPR013328. 6PGD_dom_2.
IPR000506. AcH_isomrdctse_C.
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.

Q8DGR0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARMYYDADA QLELLKDKTI AIIGYGSQGH AHALNLRDSG LNVVVGLYAG
60 70 80 90 100
SRSAERARAE GLAVHPVAEA AKMADWIMIL LPDEVQRVVY EQEIAPHLQP
110 120 130 140 150
GNVLSFAHGF NIHFGQIVPP AHVDVVMVAP KGPGHLVRRT YAQGEGVPCL
160 170 180 190 200
FAVYQDASGQ ARDLAMAYAK GIGGTRAGIL ETTFREETET DLFGEQVVLC
210 220 230 240 250
GGLSALIKAG FETLVQAGYQ PELAYFECLH EVKLIVDLIV EGGLAKMRDS
260 270 280 290 300
ISNTAEYGDL TRGPRIITEE TRAEMRKILH EIQTGQFARE FVLENMAGKP
310 320 330
GFTAMRRREA EHPIEQVGQE LRSMFSWLKR A
Length:331
Mass (Da):36,404
Last modified:June 6, 2003 - v2
Checksum:iE1E1626D0B57D375
GO

Sequence cautioni

The sequence BAC09806 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000039 Genomic DNA. Translation: BAC09806.1. Different initiation.
RefSeqiNP_683044.1. NC_004113.1.
WP_011058087.1. NC_004113.1.

Genome annotation databases

EnsemblBacteriaiBAC09806; BAC09806; BAC09806.
GeneIDi1012299.
KEGGitel:tll2254.
PATRICi23929964. VBITheElo119873_2363.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000039 Genomic DNA. Translation: BAC09806.1. Different initiation.
RefSeqiNP_683044.1. NC_004113.1.
WP_011058087.1. NC_004113.1.

3D structure databases

ProteinModelPortaliQ8DGR0.
SMRiQ8DGR0. Positions 3-328.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi197221.tll2254.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAC09806; BAC09806; BAC09806.
GeneIDi1012299.
KEGGitel:tll2254.
PATRICi23929964. VBITheElo119873_2363.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayiUPA00047; UER00056.
UPA00049; UER00060.

Family and domain databases

Gene3Di1.10.1040.10. 1 hit.
HAMAPiMF_00435. IlvC. 1 hit.
InterProiIPR008927. 6-PGluconate_DH_C-like.
IPR013328. 6PGD_dom_2.
IPR000506. AcH_isomrdctse_C.
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_THEEB
AccessioniPrimary (citable) accession number: Q8DGR0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 6, 2003
Last sequence update: June 6, 2003
Last modified: September 7, 2016
This is version 85 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference 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.