LEU3_LACLA
ID LEU3_LACLA Reviewed; 345 AA.
AC Q02143; Q9CG87;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 3.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=3-isopropylmalate dehydrogenase;
DE EC=1.1.1.85;
DE AltName: Full=3-IPM-DH;
DE AltName: Full=Beta-IPM dehydrogenase;
DE Short=IMDH;
GN Name=leuB; OrderedLocusNames=LL1218; ORFNames=L0074;
OS Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=272623;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NCDO 2118;
RX PubMed=1400210; DOI=10.1128/jb.174.20.6580-6589.1992;
RA Godon J.-J., Chopin M.-C., Ehrlich S.D.;
RT "Branched-chain amino acid biosynthesis genes in Lactococcus lactis subsp.
RT lactis.";
RL J. Bacteriol. 174:6580-6589(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=IL1403;
RX PubMed=8331070; DOI=10.1128/jb.175.14.4383-4390.1993;
RA Godon J.-J., Delorme C., Bardowski J., Chopin M.-C., Ehrlich S.D.,
RA Renault P.;
RT "Gene inactivation in Lactococcus lactis: branched-chain amino acid
RT biosynthesis.";
RL J. Bacteriol. 175:4383-4390(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IL1403;
RX PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "The complete genome sequence of the lactic acid bacterium Lactococcus
RT lactis ssp. lactis IL1403.";
RL Genome Res. 11:731-753(2001).
CC -!- FUNCTION: Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-
CC methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-
CC oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl-2-oxopentanoate
CC + CO2 + NADH; Xref=Rhea:RHEA:32271, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:17865, ChEBI:CHEBI:35121, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.1.1.85;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. {ECO:0000250};
CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC from 3-methyl-2-oxobutanoate: step 3/4.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC dehydrogenases family. LeuB type 1 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK05316.1; Type=Erroneous termination; Note=Truncated C-terminus. The resulting protein is truncated and inactive in the dairy strain IL1403, where the leucine biosynthesis pathway is not functional.; Evidence={ECO:0000305};
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DR EMBL; U92974; AAB81914.1; -; Genomic_DNA.
DR EMBL; AE005176; AAK05316.1; ALT_SEQ; Genomic_DNA.
DR PIR; B86777; B86777.
DR PIR; S35133; S35133.
DR RefSeq; NP_267374.1; NC_002662.1.
DR AlphaFoldDB; Q02143; -.
DR SMR; Q02143; -.
DR STRING; 272623.L0074; -.
DR PaxDb; Q02143; -.
DR EnsemblBacteria; AAK05316; AAK05316; L0074.
DR KEGG; lla:L0074; -.
DR PATRIC; fig|272623.7.peg.1317; -.
DR eggNOG; COG0473; Bacteria.
DR HOGENOM; CLU_031953_0_3_9; -.
DR UniPathway; UPA00048; UER00072.
DR Proteomes; UP000002196; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003862; F:3-isopropylmalate dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01033; LeuB_type1; 1.
DR InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR InterPro; IPR004429; Isopropylmalate_DH.
DR PANTHER; PTHR42979; PTHR42979; 1.
DR Pfam; PF00180; Iso_dh; 1.
DR SMART; SM01329; Iso_dh; 1.
DR TIGRFAMs; TIGR00169; leuB; 1.
DR PROSITE; PS00470; IDH_IMDH; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; Cytoplasm;
KW Leucine biosynthesis; Magnesium; Manganese; Metal-binding; NAD;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..345
FT /note="3-isopropylmalate dehydrogenase"
FT /id="PRO_0000083701"
FT BINDING 94
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 104
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 130
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 215
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 215
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 239
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 243
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 273..285
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 137
FT /note="Important for catalysis"
FT /evidence="ECO:0000250"
FT SITE 183
FT /note="Important for catalysis"
FT /evidence="ECO:0000250"
FT VARIANT 128
FT /note="V -> M (in strain: IL1403)"
FT VARIANT 308
FT /note="A -> T (in strain: IL1403)"
FT CONFLICT 16
FT /note="E -> G (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 66
FT /note="A -> R (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 345 AA; 37587 MW; FA84DABFDEF2119C CRC64;
MSKKIVTLAG DGIGPEIMSA GLSVLKAVSK KIDFEYELEA KDFGGIAIDK HGHPLPEETL
QAVKNADAIL LAAIGHPKYN NAKVRPEQGL LALRKELGLY ANVRPLKIYP ALKKLSPIRN
VENVDFLVIR ELTGGIYFGQ HELADDKARD VNDYSADEIR RILHFAFKSA QSRPRKLLTS
VDKQNVLATS KLWRKMADEI ADEYPDVRLE HQLVDSCAML LITNPQQFDV IVTENLFGDI
LSDEASSLAG SLGVMPSSSH GFNGLALYEP IHGSAPDIAG KGIANPVSMI LSIAMMLRES
FGQEDGAAMI EKAVTQTFTD GILTKDLGGT ATTKEMTEAI LKNCQ
