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ILVC_STRT1
ID   ILVC_STRT1              Reviewed;         340 AA.
AC   Q5LXV0;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 100.
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=str1871;
OS   Streptococcus thermophilus (strain CNRZ 1066).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=299768;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CNRZ 1066;
RX   PubMed=15543133; DOI=10.1038/nbt1034;
RA   Bolotin A., Quinquis B., Renault P., Sorokin A., Ehrlich S.D.,
RA   Kulakauskas S., Lapidus A., Goltsman E., Mazur M., Pusch G.D., Fonstein M.,
RA   Overbeek R., Kyprides N., Purnelle B., Prozzi D., Ngui K., Masuy D.,
RA   Hancy F., Burteau S., Boutry M., Delcour J., Goffeau A., Hols P.;
RT   "Complete sequence and comparative genome analysis of the dairy bacterium
RT   Streptococcus thermophilus.";
RL   Nat. Biotechnol. 22:1554-1558(2004).
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; CP000024; AAV63385.1; -; Genomic_DNA.
DR   RefSeq; WP_011226634.1; NC_006449.1.
DR   AlphaFoldDB; Q5LXV0; -.
DR   SMR; Q5LXV0; -.
DR   GeneID; 66899603; -.
DR   KEGG; stc:str1871; -.
DR   HOGENOM; CLU_033821_0_1_9; -.
DR   OMA; RAMFSWL; -.
DR   UniPathway; UPA00047; UER00056.
DR   UniPathway; UPA00049; UER00060.
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;
KW   Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; Magnesium;
KW   Metal-binding; NADP; Oxidoreductase.
FT   CHAIN           1..340
FT                   /note="Ketol-acid reductoisomerase (NADP(+))"
FT                   /id="PRO_0000226206"
FT   DOMAIN          3..182
FT                   /note="KARI N-terminal Rossmann"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01197"
FT   DOMAIN          183..328
FT                   /note="KARI C-terminal knotted"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"
FT   ACT_SITE        108
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT   BINDING         26..29
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT   BINDING         49
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT   BINDING         53
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT   BINDING         83..86
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT   BINDING         134
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT   BINDING         191
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT   BINDING         191
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT   BINDING         195
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT   BINDING         227
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT   BINDING         231
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT   BINDING         252
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
SQ   SEQUENCE   340 AA;  37401 MW;  A284F41C1C1C9C6B CRC64;
     MAVQMEYEKD VKVPALDGKK IAVIGYGSQG HAHSQNLRDT GHDVIIGVRP GKSFDKAKED
     GFDTYTVAEA TKLADVIMIL APDEIQQELY EAEIAPNLEA GNAVGFAHGF NIHFEFIKVP
     ADVDVFMCAP KGPGHLVRRT FEEGFGVPAL YAVYQDATGN AKDIAMDWCK GIGAARVGLL
     ETTYKEETEE DLFGEQAVLC GGLTALIETG FEVLTEAGYA PELAYFEVLH EMKLIVDLIY
     EGGFKKMRQS ISNTAEFGDY VSGPRVITEQ VKENMKAVLT DIQNGKFAND FVNDYKAGRP
     KLTAYREEAA NLEIEKVGAE LRKAMPFVGQ NDDDAFKIYN
 
 
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