ID ILVC_CORGL Reviewed; 338 AA.
AC Q57179;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 154.
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};
GN OrderedLocusNames=Cgl1273, cg1437;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=8366043; DOI=10.1128/jb.175.17.5595-5603.1993;
RA Keilhauer C., Eggeling L., Sahm H.;
RT "Isoleucine synthesis in Corynebacterium glutamicum: molecular analysis of
RT the ilvB-ilvN-ilvC operon.";
RL J. Bacteriol. 175:5595-5603(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=MJ233;
RX PubMed=8173081; DOI=10.3109/10425179309020148;
RA Inui M., Vertes A.A., Kobayashi M., Kurusu Y., Yukawa H.;
RT "Identification and sequence determination of the acetohydroxy acid
RT isomeroreductase gene from Brevibacterium flavum MJ233.";
RL DNA Seq. 4:95-103(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
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; L09232; AAA62431.1; -; Genomic_DNA.
DR EMBL; D14551; BAA03414.1; -; Genomic_DNA.
DR EMBL; BA000036; BAB98666.1; -; Genomic_DNA.
DR EMBL; BX927151; CAF19976.1; -; Genomic_DNA.
DR PIR; C48648; C48648.
DR RefSeq; NP_600495.1; NC_003450.3.
DR RefSeq; WP_003854117.1; NC_006958.1.
DR PDB; 6JX2; X-ray; 2.60 A; A/B/C/D=1-338.
DR PDBsum; 6JX2; -.
DR AlphaFoldDB; Q57179; -.
DR SMR; Q57179; -.
DR STRING; 196627.cg1437; -.
DR World-2DPAGE; 0001:Q57179; -.
DR GeneID; 69621795; -.
DR KEGG; cgb:cg1437; -.
DR KEGG; cgl:Cgl1273; -.
DR PATRIC; fig|196627.13.peg.1250; -.
DR eggNOG; COG0059; Bacteria.
DR HOGENOM; CLU_033821_0_1_11; -.
DR OrthoDB; 9804088at2; -.
DR BioCyc; CORYNE:G18NG-10846-MONOMER; -.
DR UniPathway; UPA00047; UER00056.
DR UniPathway; UPA00049; UER00060.
DR Proteomes; UP000000582; Chromosome.
DR Proteomes; UP000001009; Chromosome.
DR GO; GO:0008677; F:2-dehydropantoate 2-reductase activity; IMP:CACAO.
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 Gene3D; 6.10.240.10; -; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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 NCBIfam; TIGR00465; ilvC; 1.
DR PANTHER; PTHR21371; KETOL-ACID REDUCTOISOMERASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR21371:SF1; KETOL-ACID REDUCTOISOMERASE, MITOCHONDRIAL; 1.
DR Pfam; PF01450; IlvC; 1.
DR Pfam; PF07991; IlvN; 1.
DR PIRSF; PIRSF000116; IlvC_gammaproteo; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS51851; KARI_C; 1.
DR PROSITE; PS51850; KARI_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis;
KW Branched-chain amino acid biosynthesis; Magnesium; Metal-binding; NADP;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..338
FT /note="Ketol-acid reductoisomerase (NADP(+))"
FT /id="PRO_0000151306"
FT DOMAIN 3..183
FT /note="KARI N-terminal Rossmann"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01197"
FT DOMAIN 184..329
FT /note="KARI C-terminal knotted"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"
FT ACT_SITE 109
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 52
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT BINDING 54
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT BINDING 84..87
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT BINDING 135
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT BINDING 192
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT BINDING 192
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT BINDING 196
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT BINDING 228
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT BINDING 232
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT BINDING 253
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT HELIX 8..10
FT /evidence="ECO:0007829|PDB:6JX2"
FT HELIX 14..17
FT /evidence="ECO:0007829|PDB:6JX2"
FT STRAND 19..24
FT /evidence="ECO:0007829|PDB:6JX2"
FT HELIX 28..39
FT /evidence="ECO:0007829|PDB:6JX2"
FT STRAND 43..48
FT /evidence="ECO:0007829|PDB:6JX2"
FT HELIX 54..60
FT /evidence="ECO:0007829|PDB:6JX2"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:6JX2"
FT HELIX 68..74
FT /evidence="ECO:0007829|PDB:6JX2"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:6JX2"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:6JX2"
FT HELIX 87..94
FT /evidence="ECO:0007829|PDB:6JX2"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:6JX2"
FT STRAND 104..110
FT /evidence="ECO:0007829|PDB:6JX2"
FT HELIX 111..114
FT /evidence="ECO:0007829|PDB:6JX2"
FT STRAND 124..133
FT /evidence="ECO:0007829|PDB:6JX2"
FT HELIX 135..143
FT /evidence="ECO:0007829|PDB:6JX2"
FT STRAND 150..156
FT /evidence="ECO:0007829|PDB:6JX2"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:6JX2"
FT HELIX 162..173
FT /evidence="ECO:0007829|PDB:6JX2"
FT HELIX 175..178
FT /evidence="ECO:0007829|PDB:6JX2"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:6JX2"
FT HELIX 185..198
FT /evidence="ECO:0007829|PDB:6JX2"
FT TURN 199..201
FT /evidence="ECO:0007829|PDB:6JX2"
FT HELIX 202..217
FT /evidence="ECO:0007829|PDB:6JX2"
FT HELIX 222..229
FT /evidence="ECO:0007829|PDB:6JX2"
FT TURN 230..232
FT /evidence="ECO:0007829|PDB:6JX2"
FT HELIX 233..242
FT /evidence="ECO:0007829|PDB:6JX2"
FT HELIX 245..251
FT /evidence="ECO:0007829|PDB:6JX2"
FT HELIX 254..267
FT /evidence="ECO:0007829|PDB:6JX2"
FT HELIX 270..284
FT /evidence="ECO:0007829|PDB:6JX2"
FT HELIX 287..297
FT /evidence="ECO:0007829|PDB:6JX2"
FT TURN 298..300
FT /evidence="ECO:0007829|PDB:6JX2"
FT HELIX 301..311
FT /evidence="ECO:0007829|PDB:6JX2"
FT HELIX 314..323
FT /evidence="ECO:0007829|PDB:6JX2"
SQ SEQUENCE 338 AA; 36159 MW; 9BA1697FA7D2A082 CRC64;
MAIELLYDAD ADLSLIQGRK VAIVGYGSQG HAHSQNLRDS GVEVVIGLRE GSKSAEKAKE
AGFEVKTTAE AAAWADVIML LAPDTSQAEI FTNDIEPNLN AGDALLFGHG LNIHFDLIKP
ADDIIVGMVA PKGPGHLVRR QFVDGKGVPC LIAVDQDPTG TAQALTLSYA AAIGGARAGV
IPTTFEAETV TDLFGEQAVL CGGTEELVKV GFEVLTEAGY EPEMAYFEVL HELKLIVDLM
FEGGISNMNY SVSDTAEFGG YLSGPRVIDA DTKSRMKDIL TDIQDGTFTK RLIANVENGN
TELEGLRASY NNHPIEETGA KLRDLMSWVK VDARAETA
//
