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ILVC_BUCAI
ID   ILVC_BUCAI              Reviewed;         490 AA.
AC   P57655; Q9AQ95;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 1.
DT   03-AUG-2022, entry version 127.
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}; OrderedLocusNames=BU599;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS   pisum symbiotic bacterium).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=107806;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APS;
RX   PubMed=10993077; DOI=10.1038/35024074;
RA   Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT   "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT   sp. APS.";
RL   Nature 407:81-86(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 67-412.
RA   Wernegreen J.J., Moran N.A.;
RT   "Accelerated evolutionary rates at biosynthetic loci of Buchnera-
RT   Uroleucon.";
RL   Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; BA000003; BAB13284.1; -; Genomic_DNA.
DR   EMBL; AF217558; AAK01029.1; -; Genomic_DNA.
DR   RefSeq; NP_240398.1; NC_002528.1.
DR   RefSeq; WP_009874547.1; NC_002528.1.
DR   AlphaFoldDB; P57655; -.
DR   SMR; P57655; -.
DR   STRING; 107806.10039250; -.
DR   EnsemblBacteria; BAB13284; BAB13284; BAB13284.
DR   KEGG; buc:BU599; -.
DR   PATRIC; fig|107806.10.peg.602; -.
DR   eggNOG; COG0059; Bacteria.
DR   HOGENOM; CLU_551905_0_0_6; -.
DR   OMA; CGLLQTG; -.
DR   UniPathway; UPA00047; UER00056.
DR   UniPathway; UPA00049; UER00060.
DR   Proteomes; UP000001806; 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;
KW   Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; Magnesium;
KW   Metal-binding; NADP; Oxidoreductase; Reference proteome; Repeat.
FT   CHAIN           1..490
FT                   /note="Ketol-acid reductoisomerase (NADP(+))"
FT                   /id="PRO_0000151286"
FT   DOMAIN          16..207
FT                   /note="KARI N-terminal Rossmann"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01197"
FT   DOMAIN          208..343
FT                   /note="KARI C-terminal knotted 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"
FT   DOMAIN          344..483
FT                   /note="KARI C-terminal knotted 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"
FT   ACT_SITE        131
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT   BINDING         44..47
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT   BINDING         67
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT   BINDING         77
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT   BINDING         107..109
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT   BINDING         157
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT   BINDING         216
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT   BINDING         216
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT   BINDING         220
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT   BINDING         388
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT   BINDING         392
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT   BINDING         413
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
SQ   SEQUENCE   490 AA;  55828 MW;  0C108D0AF1476504 CRC64;
     MNYFNTLNFT QKINQINKCR FMKKEEFNKK NDILKNKNIV IVGCGAQGLN QGLNMRDAGL
     NISYALKKNS IANKNQSWIN AIENNFKVDD YDALIPDADL VINLTPDKQH HSVIKKLQKL
     MKKNAVLGYS HGFNIVEFGE KIRKDITVIM VAPKCPGTEV REEYKRGFGV PTLIAVHHEN
     DINKIGLEVA KAWAFSTGGH RAGVLESSFI AEVKSDLMGE QTILCGMLQT ASLLCYEKLI
     TEKCNPAYSA KLIQNGWETI TESLKHGGIT LMMDRLSNSS KIRAYKLSKE IKKILSPLFQ
     KHMDDIISGE FSNEMMKDWE NQDLKLLNWR YKTKNTSFET APVYNEKIPE QEYYDHGILM
     IAILKSGIEL SFEKMIETGI KEESAYYESL HELPLIANTI ARKKLYEMNK VISDTAEYGS
     YLFSESAYPI LKEFISTLNK SDLGCALSHQ SVNNIELYRI NQKIQNHPIE IIGCTLRNYM
     KKMKAITVAK
 
 
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