ID   ILVC_ALCBS              Reviewed;         338 AA.
AC   Q0VSB5;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 2.
DT   16-JUN-2009, entry version 21.
DE   RecName: Full=Ketol-acid reductoisomerase;
DE            EC=1.1.1.86;
DE   AltName: Full=Acetohydroxy-acid isomeroreductase;
DE   AltName: Full=Alpha-keto-beta-hydroxylacil reductoisomerase;
GN   Name=ilvC; OrderedLocusNames=ABO_0485;
OS   Alcanivorax borkumensis (strain SK2 / ATCC 700651 / DSM 11573).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alcanivorax.
OX   NCBI_TaxID=393595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16878126; DOI=10.1038/nbt1232;
RA   Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T.,
RA   Brecht M., Buhrmester J., Chernikova T.N., Denaro R., Ferrer M.,
RA   Gertler C., Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N.,
RA   Lang S., Linke B., McHardy A.C., Meyer F., Nechitaylo T., Puehler A.,
RA   Regenhardt D., Rupp O., Sabirova J.S., Selbitschka W., Yakimov M.M.,
RA   Timmis K.N., Vorhoelter F.-J., Weidner S., Kaiser O., Golyshin P.N.;
RT   "Genome sequence of the ubiquitous hydrocarbon-degrading marine
RT   bacterium Alcanivorax borkumensis.";
RL   Nat. Biotechnol. 24:997-1004(2006).
CC   -!- CATALYTIC ACTIVITY: (R)-2,3-dihydroxy-3-methylbutanoate + NADP(+)
CC       = (S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH.
CC   -!- CATALYTIC ACTIVITY: (2R,3R)-2,3-dihydroxy-3-methylpentanoate +
CC       NADP(+) = (S)-2-hydroxy-2-ethyl-3-oxobutanoate + NADPH.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC       isoleucine from 2-oxobutanoate: step 2/4.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine
CC       from pyruvate: step 2/4.
CC   -!- SIMILARITY: Belongs to the ketol-acid reductoisomerase family.
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DR   EMBL; AM286690; CAL15933.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_692205.1; -.
DR   SMR; Q0VSB5; 1-327.
DR   GeneID; 4211352; -.
DR   GenomeReviews; AM286690_GR; ABO_0485.
DR   KEGG; abo:ABO_0485; -.
DR   NMPDR; fig|393595.12.peg.482; -.
DR   HOGENOM; Q0VSB5; -.
DR   BioCyc; ABOR393595:ABO_0485-MON; -.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0004455; F:ketol-acid reductoisomerase activity; IEA:HAMAP.
DR   GO; GO:0009097; P:isoleucine biosynthetic process; IEA:HAMAP.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0009099; P:valine biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_00435; -; 1.
DR   InterPro; IPR013023; AcH_isomrdctse.
DR   InterPro; IPR000506; AcH_isomrdctse_C.
DR   InterPro; IPR013116; IlvN.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   PANTHER; PTHR21371; AcH_isomrdctse; 1.
DR   Pfam; PF01450; IlvC; 1.
DR   Pfam; PF07991; IlvN; 1.
DR   TIGRFAMs; TIGR00465; ilvC; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW   Complete proteome; NADP; Oxidoreductase.
FT   CHAIN         1    338       Ketol-acid reductoisomerase.
FT                                /FTId=PRO_0000252748.
FT   ACT_SITE    107    107       Potential.
SQ   SEQUENCE   338 AA;  36297 MW;  3E503EF2FAFB470F CRC64;
     MQVYYDKDCD LSIIQGKKVA ILGYGSQGHA HACNLKDSGV DVVVGLRTGS TSIAKAEAHG
     LSVTDVPSAV AAADVVMVLT PDEFQAHLYK SDIEPNLKEG ATLAFAHGFA IHYNQIVPRA
     DLDVIMIAPK APGHTVRTEF TKGGGIPDLI AIFQDASGSA KELALSYACG VGGGRTGIIE
     TTFKDETETD LFGEQAVLCG GAVELVKAGF ETLTEAGYAP EMAYFECLHE LKLIVDLMYE
     GGIANMNYSI SNNAEYGEYV TGPEVINDES RAAMRNALKR IQSGEYAKMF IAEGAHNYPS
     MTAARRNNAA HPIEQVGEKL RGMMPWIQAN QIVDKTKN
//