LEU3_CLOPA
ID LEU3_CLOPA Reviewed; 357 AA.
AC P31958;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 100.
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;
OS Clostridium pasteurianum.
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1501;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8173074; DOI=10.3109/10425179309020149;
RA Oultram J.D., Loughlin M., Walmsley R.W., Gunnery S.M., Minton N.P.;
RT "The nucleotide sequence of genes involved in the leucine biosynthetic
RT pathway of Clostridium pasteurianum.";
RL DNA Seq. 4:105-111(1993).
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 (By similarity). {ECO:0000250}.
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 {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC dehydrogenases family. LeuB type 1 subfamily. {ECO:0000305}.
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DR EMBL; L06666; AAC41394.1; -; Genomic_DNA.
DR RefSeq; WP_003441655.1; NZ_LFYL01000001.1.
DR AlphaFoldDB; P31958; -.
DR SMR; P31958; -.
DR BRENDA; 1.1.1.85; 1502.
DR UniPathway; UPA00048; UER00072.
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.
FT CHAIN 1..357
FT /note="3-isopropylmalate dehydrogenase"
FT /id="PRO_0000083681"
FT BINDING 77..90
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 97
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 107
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 136
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 224
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 224
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 248
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 252
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 282..294
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 143
FT /note="Important for catalysis"
FT /evidence="ECO:0000250"
FT SITE 192
FT /note="Important for catalysis"
FT /evidence="ECO:0000250"
SQ SEQUENCE 357 AA; 38925 MW; 39F343516E4D1C39 CRC64;
MKEFKIAVIP GDGIGPDIVR EAVKIMTKVG EKYDTKFNFV EVKAGGDAID AYGEPLPKET
IDVCKSSAAV LLGAVGGPKW DNLEGSKRPE RALLGLRGAL GLYANLRPAK VYNVLKSASP
LKNEIIDEGV DLLVVRELIG GIYFGDRGTK EVNGVETAFD TEKYNVDEVK RIAHSAFKAA
MKRRKKVTSV DKANVLDASR LWRKTVNEVS KEYPEVELSH LYVDNTAMQL VRKPSQFDVI
LTNNIFGDIL SDEASMITGS IGMLASSSIR EDSFGMYEPI HGSAPDIAGL DIANPLAQIL
SAAMLMEYSL DMSEAARDVE AAVEKVLNEG YRTADIYIEG TKKVGTSEMG NLVLERL