ILVC_ALTMD
ID ILVC_ALTMD Reviewed; 492 AA.
AC B4S1X4; F2GCG5;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=MADE_1020145;
OS Alteromonas mediterranea (strain DSM 17117 / CIP 110805 / LMG 28347 / Deep
OS ecotype).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Alteromonas/Salinimonas group; Alteromonas.
OX NCBI_TaxID=1774373;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17117 / CIP 110805 / LMG 28347 / Deep ecotype;
RX PubMed=18670397; DOI=10.1038/ismej.2008.74;
RA Ivars-Martinez E., Martin-Cuadrado A.-B., D'Auria G., Mira A., Ferriera S.,
RA Johnson J., Friedman R., Rodriguez-Valera F.;
RT "Comparative genomics of two ecotypes of the marine planktonic copiotroph
RT Alteromonas macleodii suggests alternative lifestyles associated with
RT different kinds of particulate organic matter.";
RL ISME J. 2:1194-1212(2008).
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; CP001103; AEB00152.1; -; Genomic_DNA.
DR RefSeq; WP_012520183.1; NC_011138.3.
DR AlphaFoldDB; B4S1X4; -.
DR SMR; B4S1X4; -.
DR EnsemblBacteria; AEB00152; AEB00152; MADE_1020145.
DR KEGG; amc:MADE_1020145; -.
DR HOGENOM; CLU_551905_0_0_6; -.
DR OMA; CGLLQTG; -.
DR UniPathway; UPA00047; UER00056.
DR UniPathway; UPA00049; UER00060.
DR Proteomes; UP000001870; 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; Repeat.
FT CHAIN 1..492
FT /note="Ketol-acid reductoisomerase (NADP(+))"
FT /id="PRO_1000190903"
FT DOMAIN 14..208
FT /note="KARI N-terminal Rossmann"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01197"
FT DOMAIN 209..344
FT /note="KARI C-terminal knotted 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"
FT DOMAIN 345..487
FT /note="KARI C-terminal knotted 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"
FT ACT_SITE 132
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT BINDING 45..48
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT BINDING 68
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT BINDING 76
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT BINDING 78
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT BINDING 108..110
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT BINDING 158
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT BINDING 217
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT BINDING 217
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT BINDING 221
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT BINDING 389
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT BINDING 393
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT BINDING 414
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
SQ SEQUENCE 492 AA; 54009 MW; 56CF5E0475A22504 CRC64;
MANYFNTLSL RQQLDQLGRC RFMARDEFAD GCQFLKGKKV VIVGCGAQGL NQGLNMRDSG
LDVSYALRQA AIDEQRDSYK RASSNGFTVG TYQQLIPEAD VVYNLTPDKQ HASVVEAVMP
LMKKGATLGY SHGFNIVEEG QQIRSDITVI MCAPKSPGSE VREEYKRGFG VPTLIAVHPE
NDPEGKGWDQ AKALASATGG DRAGVLESSF VAEVKSDLMG EQTILCGMQQ VAAVLAFEKM
VDDGIDPGYA GALIQYGLEA ITEALKIGGV TNMMDRLSNP AKVKAFELSE QLTDLLRPLF
EKHQDDIISG EFSRTMMEDW ANGDANLLKW REETGETAFE NAPAYEGEIS EQEFFDHGIL
LVAMIKCGVE VAFDVMVEAG ILPESAYYES LHETPLISNT IARKRLYEMN VVISDTAEYG
NYLFANAAIP ILREKFMPTI DTTVIGKGLT AASNQVENKR LVEINEAIRS HGVESVGKTL
RGYMTDMKAI VV
