(data stored in ACNUC7421 zone)

SWISSPROT: ILVC_ALCBS

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   11-DEC-2019, entry version 86.
DE   RecName: Full=Ketol-acid reductoisomerase (NADP(+)) {ECO:0000255|HAMAP-Rule:MF_00435};
DE            Short=KARI {ECO:0000255|HAMAP-Rule:MF_00435};
DE            EC=1.1.1.86 {ECO:0000255|HAMAP-Rule:MF_00435};
DE   AltName: Full=Acetohydroxy-acid isomeroreductase {ECO:0000255|HAMAP-Rule:MF_00435};
DE            Short=AHIR {ECO:0000255|HAMAP-Rule:MF_00435};
DE   AltName: Full=Alpha-keto-beta-hydroxylacyl reductoisomerase {ECO:0000255|HAMAP-Rule:MF_00435};
DE   AltName: Full=Ketol-acid reductoisomerase type 1 {ECO:0000255|HAMAP-Rule:MF_00435};
DE   AltName: Full=Ketol-acid reductoisomerase type I {ECO:0000255|HAMAP-Rule:MF_00435};
GN   Name=ilvC {ECO:0000255|HAMAP-Rule:MF_00435}; OrderedLocusNames=ABO_0485;
OS   Alcanivorax borkumensis (strain ATCC 700651 / DSM 11573 / NCIMB 13689 /
OS   SK2).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alcanivorax.
OX   NCBI_TaxID=393595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700651 / DSM 11573 / NCIMB 13689 / SK2;
RX   PubMed=16878126; DOI=10.1038/nbt1232;
RA   Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T., Brecht M.,
RA   Buhrmester J., Chernikova T.N., Denaro R., Ferrer M., Gertler C.,
RA   Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N., Lang S., Linke B.,
RA   McHardy A.C., Meyer F., Nechitaylo T., Puehler A., Regenhardt D., Rupp O.,
RA   Sabirova J.S., Selbitschka W., Yakimov M.M., Timmis K.N., Vorhoelter F.-J.,
RA   Weidner S., Kaiser O., Golyshin P.N.;
RT   "Genome sequence of the ubiquitous hydrocarbon-degrading marine bacterium
RT   Alcanivorax borkumensis.";
RL   Nat. Biotechnol. 24:997-1004(2006).
CC   -!- FUNCTION: Involved in the biosynthesis of branched-chain amino acids
CC       (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction
CC       of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In
CC       the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl
CC       migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the
CC       reductase reaction, this 2-ketoacid undergoes a metal-dependent
CC       reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate.
CC       {ECO:0000255|HAMAP-Rule:MF_00435}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R)-2,3-dihydroxy-3-methylbutanoate + NADP(+) = (2S)-2-
CC         acetolactate + H(+) + NADPH; Xref=Rhea:RHEA:22068, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:49072, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:58476; EC=1.1.1.86; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00435};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R,3R)-2,3-dihydroxy-3-methylpentanoate + NADP(+) = (S)-2-
CC         ethyl-2-hydroxy-3-oxobutanoate + H(+) + NADPH; Xref=Rhea:RHEA:13493,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:49256, ChEBI:CHEBI:49258,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.86;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00435};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00435};
CC       Note=Binds 2 magnesium ions per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00435};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC       isoleucine from 2-oxobutanoate: step 2/4. {ECO:0000255|HAMAP-
CC       Rule:MF_00435}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC       pyruvate: step 2/4. {ECO:0000255|HAMAP-Rule:MF_00435}.
CC   -!- SIMILARITY: Belongs to the ketol-acid reductoisomerase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00435}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAL15933.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; AM286690; CAL15933.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_035459332.1; NC_008260.1.
DR   SMR; Q0VSB5; -.
DR   STRING; 393595.ABO_0485; -.
DR   EnsemblBacteria; CAL15933; CAL15933; ABO_0485.
DR   KEGG; abo:ABO_0485; -.
DR   eggNOG; ENOG4105C6M; Bacteria.
DR   eggNOG; COG0059; LUCA.
DR   HOGENOM; HOG000016230; -.
DR   KO; K00053; -.
DR   OrthoDB; 188901at2; -.
DR   BioCyc; ABOR393595:ABO_RS02510-MONOMER; -.
DR   UniPathway; UPA00047; UER00056.
DR   UniPathway; UPA00049; UER00060.
DR   Proteomes; UP000008871; Chromosome.
DR   GO; GO:0004455; F:ketol-acid reductoisomerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00435; IlvC; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR013023; KARI.
DR   InterPro; IPR000506; KARI_C.
DR   InterPro; IPR013116; KARI_N.
DR   InterPro; IPR014359; KARI_prok.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR21371; PTHR21371; 1.
DR   Pfam; PF01450; IlvC; 1.
DR   Pfam; PF07991; IlvN; 1.
DR   PIRSF; PIRSF000116; IlvC_gammaproteo; 1.
DR   SUPFAM; SSF48179; SSF48179; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR00465; ilvC; 1.
DR   PROSITE; PS51851; KARI_C; 1.
DR   PROSITE; PS51850; KARI_N; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q0VSB5.
DR   SWISS-2DPAGE; Q0VSB5.
KW   Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; Magnesium;
KW   Metal-binding; NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..338
FT                   /note="Ketol-acid reductoisomerase (NADP(+))"
FT                   /id="PRO_0000252748"
FT   DOMAIN          1..181
FT                   /note="KARI N-terminal Rossmann"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01197"
FT   DOMAIN          182..327
FT                   /note="KARI C-terminal knotted"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"
FT   NP_BIND         24..27
FT                   /note="NADP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT   NP_BIND         82..85
FT                   /note="NADP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT   ACT_SITE        107
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT   METAL           190
FT                   /note="Magnesium 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT   METAL           190
FT                   /note="Magnesium 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT   METAL           194
FT                   /note="Magnesium 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT   METAL           226
FT                   /note="Magnesium 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT   METAL           230
FT                   /note="Magnesium 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT   BINDING         47
FT                   /note="NADP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT   BINDING         50
FT                   /note="NADP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT   BINDING         52
FT                   /note="NADP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT   BINDING         133
FT                   /note="NADP; via amide nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT   BINDING         251
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
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
//

If you have problems or comments...

PBIL Back to PBIL home page