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Protein

Ketol-acid reductoisomerase (NADP(+))

Gene

ilvC

Organism
Staphylococcus aureus (strain MSSA476)
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.

Catalytic activityi

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

Cofactori

Mg2+Note: Binds 2 magnesium ions per subunit.

Pathwayi: L-isoleucine biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes L-isoleucine from 2-oxobutanoate.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Ketol-acid reductoisomerase (NADP(+)) (ilvC)
  3. Dihydroxy-acid dehydratase (ilvD)
  4. Probable 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.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Ketol-acid reductoisomerase (NADP(+)) (ilvC)
  3. Dihydroxy-acid dehydratase (ilvD)
  4. Probable 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 sitei48NADP1
Binding sitei52NADP1
Active sitei1071
Binding sitei133NADP; via amide nitrogen1
Metal bindingi190Magnesium 11
Metal bindingi190Magnesium 21
Metal bindingi194Magnesium 11
Metal bindingi226Magnesium 21
Metal bindingi230Magnesium 21
Binding sitei251Substrate1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi25 – 28NADP4
Nucleotide bindingi82 – 85NADP4

GO - Molecular functioni

GO - Biological processi

Keywordsi

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

Enzyme and pathway databases

UniPathwayiUPA00047; UER00056.
UPA00049; UER00060.

Names & Taxonomyi

Protein namesi
Recommended name:
Ketol-acid reductoisomerase (NADP(+)) (EC:1.1.1.86)
Short name:
KARI
Alternative name(s):
Acetohydroxy-acid isomeroreductase
Short name:
AHIR
Alpha-keto-beta-hydroxylacyl reductoisomerase
Ketol-acid reductoisomerase type 1
Ketol-acid reductoisomerase type I
Gene namesi
Name:ilvC
Ordered Locus Names:SAS1961
OrganismiStaphylococcus aureus (strain MSSA476)
Taxonomic identifieri282459 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001513591 – 334Ketol-acid reductoisomerase (NADP(+))Add BLAST334

Structurei

3D structure databases

ProteinModelPortaliQ6G7Q2.
SMRiQ6G7Q2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini15 – 177IlvNAdd BLAST163
Domaini183 – 325IlvCAdd BLAST143

Sequence similaritiesi

Belongs to the ketol-acid reductoisomerase family.

Phylogenomic databases

HOGENOMiHOG000016230.
KOiK00053.
OMAiRAMFSWL.

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.
IPR000506. AcH_isomrdctse_C.
IPR013116. IlvN.
IPR013023. KARI.
IPR014359. KARI_prok.
IPR036291. NAD(P)-bd_dom_sf.
PANTHERiPTHR21371. PTHR21371. 1 hit.
PfamiView protein in Pfam
PF01450. IlvC. 1 hit.
PF07991. IlvN. 1 hit.
PIRSFiPIRSF000116. IlvC_gammaproteo. 1 hit.
SUPFAMiSSF48179. SSF48179. 1 hit.
SSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR00465. ilvC. 1 hit.

Sequencei

Sequence statusi: Complete.

Q6G7Q2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTVYYDQDV KTDALQGKKI AVVGYGSQGH AHAQNLKDNG YDVVIGIRPG
60 70 80 90 100
RSFDKAKEDG FDVFPVAEAV KQADVIMVLL PDEIQGDVYK NEIEPNLEKH
110 120 130 140 150
NALAFAHGFN IHFGVIQPPA DVDVFLVAPK GPGHLVRRTF VEGSAVPSLF
160 170 180 190 200
GIQQDASGQA RNIALSYAKG IGATRAGVIE TTFKEETETD LFGEQAVLCG
210 220 230 240 250
GVSKLIQSGF ETLVEAGYQP ELAYFEVLHE MKLIVDLMYE GGTENVRYSI
260 270 280 290 300
SNTAEFGDYV SGPRVITPDV KENMKAVLTD IQNGNFSNRF IEDNKNGFKE
310 320 330
FYKLREEQHG HQIEKVGREL REMMPFIKSK SIEK
Length:334
Mass (Da):36,984
Last modified:July 19, 2004 - v1
Checksum:iD6B48BE5B5598859
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX571857 Genomic DNA. Translation: CAG43768.1.
RefSeqiWP_000214555.1. NC_002953.3.

Genome annotation databases

KEGGisas:SAS1961.

Similar proteinsi

Entry informationi

Entry nameiILVC_STAAS
AccessioniPrimary (citable) accession number: Q6G7Q2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 21, 2004
Last sequence update: July 19, 2004
Last modified: November 22, 2017
This is version 94 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

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