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Protein

Ketol-acid reductoisomerase (NADP(+))

Gene

ilvC

Organism
Escherichia coli O81 (strain ED1a)
Status
Reviewed-Annotation score: -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 (ilvI), Acetolactate synthase (ilvB), Acetolactate synthase (ilvG)
  2. Ketol-acid reductoisomerase (NADP(+)) (ilvC)
  3. Dihydroxy-acid dehydratase (ilvD)
  4. Branched-chain-amino-acid aminotransferase (ilvE)
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 (ilvI), Acetolactate synthase (ilvB), Acetolactate synthase (ilvG)
  2. Ketol-acid reductoisomerase (NADP(+)) (ilvC)
  3. Dihydroxy-acid dehydratase (ilvD)
  4. Branched-chain-amino-acid aminotransferase (ilvE)
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)DescriptionActionsGraphical viewLength
Binding sitei68NADPUniRule annotation1
Binding sitei76NADPUniRule annotation1
Binding sitei78NADPUniRule annotation1
Active sitei132UniRule annotation1
Binding sitei158NADP; via amide nitrogenUniRule annotation1
Metal bindingi217Magnesium 1UniRule annotation1
Metal bindingi217Magnesium 2UniRule annotation1
Metal bindingi221Magnesium 1UniRule annotation1
Metal bindingi389Magnesium 2UniRule annotation1
Metal bindingi393Magnesium 2UniRule annotation1
Binding sitei414SubstrateUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi45 – 48NADPUniRule annotation4
Nucleotide bindingi108 – 110NADPUniRule annotation3

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processAmino-acid biosynthesis, Branched-chain amino acid biosynthesis
LigandMagnesium, Metal-binding, NADP

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 2UniRule annotation
Ketol-acid reductoisomerase type IIUniRule annotation
Gene namesi
Name:ilvCUniRule annotation
Ordered Locus Names:ECED1_4460
OrganismiEscherichia coli O81 (strain ED1a)
Taxonomic identifieri585397 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000748 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10001909631 – 491Ketol-acid reductoisomerase (NADP(+))Add BLAST491

Structurei

3D structure databases

ProteinModelPortaliB7N269
SMRiB7N269
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini15 – 208KARI N-terminal RossmannPROSITE-ProRule annotationAdd BLAST194
Domaini209 – 344KARI C-terminal knotted 1PROSITE-ProRule annotationAdd BLAST136
Domaini345 – 484KARI C-terminal knotted 2PROSITE-ProRule annotationAdd BLAST140

Sequence similaritiesi

Belongs to the ketol-acid reductoisomerase family.UniRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

HOGENOMiHOG000286135
KOiK00053
OMAiKLFEMNR

Family and domain databases

Gene3Di1.10.1040.10, 1 hit
HAMAPiMF_00435 IlvC, 1 hit
InterProiView protein in InterPro
IPR008927 6-PGluconate_DH-like_C_sf
IPR013328 6PGD_dom2
IPR013023 KARI
IPR000506 KARI_C
IPR013116 KARI_N
IPR036291 NAD(P)-bd_dom_sf
PANTHERiPTHR21371 PTHR21371, 2 hits
PfamiView protein in Pfam
PF01450 IlvC, 2 hits
PF07991 IlvN, 1 hit
SUPFAMiSSF48179 SSF48179, 2 hits
SSF51735 SSF51735, 1 hit
TIGRFAMsiTIGR00465 ilvC, 1 hit
PROSITEiView protein in PROSITE
PS51851 KARI_C, 2 hits
PS51850 KARI_N, 1 hit

Sequencei

Sequence statusi: Complete.

B7N269-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MANYFNTLNL RQQLAQLGKC RFMGRDEFAD GASYLQGKKV VIVGCGAQGL
60 70 80 90 100
NQGLNMRDSG LDISYALRKE AIAEKRASWR KATENGFKVG TYEELIPQAD
110 120 130 140 150
LVVNLTPDKQ HSDVVRTVQP LMKDGAALGY SHGFNIVEVG EQIRKDITVV
160 170 180 190 200
MVAPKCPGTE VREEYKRGFG VPTLIAVHPE NDPKGEGMAI AKAWAAATGG
210 220 230 240 250
HRAGVLESSF VAEVKSDLMG EQTILCGMLQ AGSLLCFDKL VEEGTDPAYA
260 270 280 290 300
EKLIQFGWET ITEALKQGGI TLMMDRLSNP AKLRAYALSE QLKEIMAPLF
310 320 330 340 350
QKHMDDIISG EFSSGMMADW ANDDKKLLTW REETGKTAFE TAPQYEGKIG
360 370 380 390 400
EQEYFDKGVL MIAMVKAGVE LAFETMVDSG IIEESAYYES LHELPLIANT
410 420 430 440 450
IARKRLYEMN VVISDTAEYG NYLFSYACVP LLKPFMAELQ PGDLGKAIPE
460 470 480 490
GAVDNAQLRD VNEAIRSHAI EQVGKKLRGY MTDMKRIAVA G
Length:491
Mass (Da):54,069
Last modified:February 10, 2009 - v1
Checksum:i9AF1AC3EDB6B7E89
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU928162 Genomic DNA Translation: CAR10440.1
RefSeqiWP_000024951.1, NC_011745.1

Genome annotation databases

EnsemblBacteriaiCAR10440; CAR10440; ECED1_4460
KEGGiecq:ECED1_4460

Entry informationi

Entry nameiILVC_ECO81
AccessioniPrimary (citable) accession number: B7N269
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: February 10, 2009
Last modified: May 23, 2018
This is version 69 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome
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Main funding by: National Institutes of Health