(data stored in ACNUC9543 zone)

SWISSPROT: ILVC_YERPA

ID   ILVC_YERPA              Reviewed;         492 AA.
AC   Q1CBS1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   08-MAY-2019, entry version 99.
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 2 {ECO:0000255|HAMAP-Rule:MF_00435};
DE   AltName: Full=Ketol-acid reductoisomerase type II {ECO:0000255|HAMAP-Rule:MF_00435};
GN   Name=ilvC {ECO:0000255|HAMAP-Rule:MF_00435};
GN   OrderedLocusNames=YPA_0132;
OS   Yersinia pestis bv. Antiqua (strain Antiqua).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=360102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Antiqua;
RX   PubMed=16740952; DOI=10.1128/JB.00124-06;
RA   Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F.,
RA   Vergez L.M., Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and
RT   Nepal516: evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(2006).
CC   -!- FUNCTION: Involved in the biosynthesis of branched-chain amino
CC       acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-
CC       acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-
CC       dihydroxy-isovalerate. In the isomerase reaction, S2AL is
CC       rearranged via a Mg-dependent methyl migration to produce 3-
CC       hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction,
CC       this 2-ketoacid undergoes a metal-dependent reduction by NADPH to
CC       yield (R)-2,3-dihydroxy-isovalerate. {ECO:0000255|HAMAP-
CC       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,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:49072, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:58476; EC=1.1.1.86;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00435};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R,3R)-2,3-dihydroxy-3-methylpentanoate + NADP(+) = (S)-
CC         2-ethyl-2-hydroxy-3-oxobutanoate + H(+) + NADPH;
CC         Xref=Rhea:RHEA:13493, ChEBI:CHEBI:15378, ChEBI:CHEBI:49256,
CC         ChEBI:CHEBI:49258, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         EC=1.1.1.86; 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
CC       from 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}.
DR   EMBL; CP000308; ABG12101.1; -; Genomic_DNA.
DR   RefSeq; WP_002212007.1; NZ_CP009906.1.
DR   SMR; Q1CBS1; -.
DR   PRIDE; Q1CBS1; -.
DR   EnsemblBacteria; ABG12101; ABG12101; YPA_0132.
DR   KEGG; ypa:YPA_0132; -.
DR   HOGENOM; HOG000286135; -.
DR   KO; K00053; -.
DR   OMA; KLFEMNR; -.
DR   UniPathway; UPA00047; UER00056.
DR   UniPathway; UPA00049; UER00060.
DR   Proteomes; UP000001971; 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:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.1040.10; -; 1.
DR   HAMAP; MF_00435; IlvC; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR013328; 6PGD_dom2.
DR   InterPro; IPR013023; KARI.
DR   InterPro; IPR000506; KARI_C.
DR   InterPro; IPR013116; KARI_N.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR21371; PTHR21371; 2.
DR   Pfam; PF01450; IlvC; 2.
DR   Pfam; PF07991; IlvN; 1.
DR   SUPFAM; SSF48179; SSF48179; 2.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR00465; ilvC; 1.
DR   PROSITE; PS51851; KARI_C; 2.
DR   PROSITE; PS51850; KARI_N; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q1CBS1.
DR   SWISS-2DPAGE; Q1CBS1.
KW   Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW   Complete proteome; Magnesium; Metal-binding; NADP; Oxidoreductase;
KW   Repeat.
FT   CHAIN         1    492       Ketol-acid reductoisomerase (NADP(+)).
FT                                /FTId=PRO_1000050592.
FT   DOMAIN       15    208       KARI N-terminal Rossmann.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01197}.
FT   DOMAIN      209    344       KARI C-terminal knotted 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01198}.
FT   DOMAIN      345    485       KARI C-terminal knotted 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01198}.
FT   NP_BIND      45     48       NADP. {ECO:0000255|HAMAP-Rule:MF_00435}.
FT   NP_BIND     108    110       NADP. {ECO:0000255|HAMAP-Rule:MF_00435}.
FT   ACT_SITE    132    132       {ECO:0000255|HAMAP-Rule:MF_00435}.
FT   METAL       217    217       Magnesium 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_00435}.
FT   METAL       217    217       Magnesium 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_00435}.
FT   METAL       221    221       Magnesium 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_00435}.
FT   METAL       389    389       Magnesium 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_00435}.
FT   METAL       393    393       Magnesium 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_00435}.
FT   BINDING      68     68       NADP. {ECO:0000255|HAMAP-Rule:MF_00435}.
FT   BINDING      76     76       NADP. {ECO:0000255|HAMAP-Rule:MF_00435}.
FT   BINDING      78     78       NADP. {ECO:0000255|HAMAP-Rule:MF_00435}.
FT   BINDING     158    158       NADP; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00435}.
FT   BINDING     414    414       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00435}.
SQ   SEQUENCE   492 AA;  53993 MW;  42367AEF8252A80D CRC64;
     MANYFNTLNL RQQLAQLGKC RFMARDEFAD EAGYLKGKKV VIVGCGAQGL NQGLNMRDSG
     LDVAYALRKE AIAEKRASWR KATENGFKVG TYEELIPQAD LVVNLTPDKQ HSAVVKAVQP
     LMKEGAALGY SHGFNIVEVG EQVRKDITVV MVAPKCPGTE VREEYKRGFG VPTLIAVHPE
     NDPKGEGMAI AKAWAAATGG HRAGVLEFSF VAEVKSDLMG EQTILCGMLQ AGSLLCFDKL
     VSEGTDAAYA EKLIQFGWET ITEALKQGGI TLMMDRLSNP AKLRAYALSE QLKEIMAPLF
     QKHMDDIISG AFSSGMMADW ANDDVKLLNW REETGRTAFE NAPQFEGKIS EQEYFDHGVL
     MIAMVKAGVE LAFETMVDSG IIEESAYYES LHELPLIANT IARKRLYEMN VVISDTAEYG
     NYLFANAAVP LLKEKFMDSL QAGDLGKSIP GSAVDNAQLR DVNEAIRNHP IEAVGHKLRG
     YMTDMKRIAV AG
//

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