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ILVC_STRTR
ID   ILVC_STRTR              Reviewed;         340 AA.
AC   Q9F0I7;
DT   29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 107.
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};
OS   Streptococcus thermophilus.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ST18;
RX   PubMed=11097879; DOI=10.1128/aem.66.12.5128-5133.2000;
RA   Garault P., Letort C., Juillard V., Monnet V.;
RT   "Branched-chain amino acid biosynthesis is essential for optimal growth of
RT   Streptococcus thermophilus in milk.";
RL   Appl. Environ. Microbiol. 66:5128-5133(2000).
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; AF220670; AAG39032.1; -; Genomic_DNA.
DR   RefSeq; WP_002952054.1; NZ_WMLD01000010.1.
DR   AlphaFoldDB; Q9F0I7; -.
DR   SMR; Q9F0I7; -.
DR   STRING; 322159.STER_1848; -.
DR   eggNOG; COG0059; Bacteria.
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_0000151369"
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;  37371 MW;  BEF4F41C09099C7E 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 VKENMKAVLA DIQNGKFAND FVNDYKAGRP
     KLTAYREEAA NLEIEKVGAE LRKAMPFVGQ NDDDAFKIYN
 
 
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