(data stored in ACNUC7421 zone)

SWISSPROT: ILVC_AERHH

ID   ILVC_AERHH              Reviewed;         493 AA.
AC   A0KEM1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   08-MAY-2019, entry version 96.
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=AHA_0153;
OS   Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 /
OS   JCM 1027 / KCTC 2358 / NCIMB 9240).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=380703;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 7966 / DSM 30187 / JCM 1027 / KCTC 2358 / NCIMB 9240;
RX   PubMed=16980456; DOI=10.1128/JB.00621-06;
RA   Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J.,
RA   Haft D.H., Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M.,
RA   Jin S., Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT   "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all
RT   trades.";
RL   J. Bacteriol. 188:8272-8282(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; CP000462; ABK38758.1; -; Genomic_DNA.
DR   RefSeq; WP_011704175.1; NC_008570.1.
DR   RefSeq; YP_854686.1; NC_008570.1.
DR   SMR; A0KEM1; -.
DR   STRING; 380703.AHA_0153; -.
DR   PRIDE; A0KEM1; -.
DR   EnsemblBacteria; ABK38758; ABK38758; AHA_0153.
DR   GeneID; 4490334; -.
DR   KEGG; aha:AHA_0153; -.
DR   PATRIC; fig|380703.7.peg.143; -.
DR   eggNOG; ENOG4105C6M; Bacteria.
DR   eggNOG; COG0059; LUCA.
DR   HOGENOM; HOG000286135; -.
DR   KO; K00053; -.
DR   OMA; KLFEMNR; -.
DR   BioCyc; AHYD380703:G1G7B-153-MONOMER; -.
DR   UniPathway; UPA00047; UER00056.
DR   UniPathway; UPA00049; UER00060.
DR   Proteomes; UP000000756; 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; A0KEM1.
DR   SWISS-2DPAGE; A0KEM1.
KW   Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW   Complete proteome; Magnesium; Metal-binding; NADP; Oxidoreductase;
KW   Reference proteome; Repeat.
FT   CHAIN         1    493       Ketol-acid reductoisomerase (NADP(+)).
FT                                /FTId=PRO_1000050474.
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    486       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   493 AA;  53827 MW;  116A6F2DC97F78C6 CRC64;
     MANYFNTLNL RQQLAQLGKC RFMQREEFAD GCNVLKGKKV VIVGCGAQGL NQGLNMRDSG
     LDISYALRKA AITEKRASWQ KATDNGFAVG TYEELIPTAD LVLNLTPDKQ HSDVVKTVMP
     LMKQGAALGY SHGFNVVEEG QQIRADITVV MVAPKCPGTE VREEYKRGFG VPTLIAVHPE
     NDPKGEGMAI AKAWASATGG DRAGVLESSF VAEVKSDLMG EQTILCGMLQ AGSLLCYDKL
     VAEGTDPAYA GKLIQFGWET ITEALKQGGI SLMMDRLSNP AKLRAFELSE QLKTLMRPLF
     EKHMDDIIAG EFSRGMMADW AEDDAKLFGW REETGKSAFE NAPAFAGKIA EQEYFDNGVV
     MVAMVKAGVE LAFETMVASG IYEESAYYES LHELPLIANT VARKRLYEMN VVISDTAEYG
     NYLFANAAVP LLREHFMPTL KAGDLGASKA EGQSVDNLAL LAANEATRNH PIEKIGQVLR
     GYMKDMKRIA VGG
//

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