(data stored in ACNUC7421 zone)

SWISSPROT: ILVC_EDWI9

ID   ILVC_EDWI9              Reviewed;         492 AA.
AC   C5BBA8;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 61.
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=NT01EI_0083;
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146;
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
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: (2R)-2,3-dihydroxy-3-methylbutanoate + NADP(+)
CC       = (2S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH.
CC       {ECO:0000255|HAMAP-Rule:MF_00435}.
CC   -!- CATALYTIC ACTIVITY: (2R,3R)-2,3-dihydroxy-3-methylpentanoate +
CC       NADP(+) = (S)-2-hydroxy-2-ethyl-3-oxobutanoate + NADPH.
CC       {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; CP001600; ACR67343.1; -; Genomic_DNA.
DR   RefSeq; WP_015869564.1; NC_012779.2.
DR   ProteinModelPortal; C5BBA8; -.
DR   SMR; C5BBA8; -.
DR   STRING; 634503.NT01EI_0083; -.
DR   PRIDE; C5BBA8; -.
DR   EnsemblBacteria; ACR67343; ACR67343; NT01EI_0083.
DR   GeneID; 7959802; -.
DR   KEGG; eic:NT01EI_0083; -.
DR   PATRIC; fig|634503.3.peg.76; -.
DR   eggNOG; ENOG4105C6M; Bacteria.
DR   eggNOG; COG0059; LUCA.
DR   HOGENOM; HOG000286135; -.
DR   KO; K00053; -.
DR   OMA; KLFEMNR; -.
DR   OrthoDB; POG091H063Y; -.
DR   UniPathway; UPA00047; UER00056.
DR   UniPathway; UPA00049; UER00060.
DR   Proteomes; UP000001485; Chromosome.
DR   GO; GO:0004455; F:ketol-acid reductoisomerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.10.1040.10; -; 1.
DR   HAMAP; MF_00435; IlvC; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH_C-like.
DR   InterPro; IPR013328; 6PGD_dom_2.
DR   InterPro; IPR000506; AcH_isomrdctse_C.
DR   InterPro; IPR013116; IlvN.
DR   InterPro; IPR013023; KARI.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   PANTHER; PTHR21371; PTHR21371; 1.
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.
PE   3: Inferred from homology;
DR   PRODOM; C5BBA8.
DR   SWISS-2DPAGE; C5BBA8.
KW   Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW   Complete proteome; Magnesium; Metal-binding; NADP; Nucleotide-binding;
KW   Oxidoreductase; Reference proteome; Repeat.
FT   CHAIN         1    492       Ketol-acid reductoisomerase (NADP(+)).
FT                                /FTId=PRO_1000206082.
FT   DOMAIN       35    204       IlvN. {ECO:0000255|HAMAP-Rule:MF_00435}.
FT   DOMAIN      210    342       IlvC 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_00435}.
FT   DOMAIN      359    483       IlvC 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_00435}.
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;  53434 MW;  F6E28196A59F2983 CRC64;
     MSNYFNTLNL RQQLAQLGKC RFMARTEFAD GVNALRGKKV VIVGCGAQGL NQGLNMRDSG
     LDVAYALRAE AIAERRDSYR RATEHGFCVG DYQALIPQAD LVINLTPDKQ HAAVVSAVQP
     LMKPGAALGY SHGFNIVEVG QQIRPDITVV MVAPKCPGTE VREEYKRGFG VPTLIAVHPE
     NDPRGAGMAI AKAWASATGG DRAGVLESSF VAEVKSDLMG EQTILCGMLQ TGSLLCYERL
     VAEGADPAWA GKLIQFGWET ITEALKQGGI TLMMDRLSNP AKLRAYTLAG QLKTLMAPLF
     AKHMDDILSG AFSQGMMADW AADDAHLLTW RAETGESAFE KAPPFEGKID EQTYFDRGVL
     LVAMVKAGVE LAFETMVASG IVAESAYYES LHELPLIANT IARRRLYEMN VVISDTAEYG
     NYLFANAAVP LLRQGFMETL QPGDLGQPLP AEAVDNAALR EVNQAIRQHP IETVGERLRG
     YMTDMKRVAV AG
//

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