LEU3_ACRCH
ID LEU3_ACRCH Reviewed; 380 AA.
AC Q12545;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=3-isopropylmalate dehydrogenase;
DE Short=3-IPM-DH;
DE Short=IMDH;
DE EC=1.1.1.85;
DE AltName: Full=Beta-IPM dehydrogenase;
GN Name=LEU2;
OS Acremonium chrysogenum (Cephalosporium acremonium).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreales incertae sedis; Acremonium.
OX NCBI_TaxID=5044;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=M8650;
RA Kimura H., Matumura S., Suzuki M., Sumino Y.;
RL Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000305}.
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DR EMBL; D50665; BAA09319.1; -; Genomic_DNA.
DR AlphaFoldDB; Q12545; -.
DR SMR; Q12545; -.
DR UniPathway; UPA00048; UER00072.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003862; F:3-isopropylmalate dehydrogenase activity; IEA:UniProtKB-EC.
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-UniPathway.
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..380
FT /note="3-isopropylmalate dehydrogenase"
FT /id="PRO_0000083607"
FT BINDING 79..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 229
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 229
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 254
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 258
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 294..306
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 196
FT /note="Important for catalysis"
FT /evidence="ECO:0000250"
SQ SEQUENCE 380 AA; 40637 MW; 0F99ACD5251CCB43 CRC64;
MTTTYKILVL PGDHIGPEIM AEAIKVLTTI ETHRPNLHFN LTTDLVGGTS IDTHGVPITQ
SVLDAAKASD AVLFGSIGGP EWAGVHPTPE SGLLQLRQHL DAFANLRPCE FLVPSLVGAS
PIREHVVKGT RFIVVRENCG GAYFGEKKEE EDVASDLWVY TRPEIERLAR VSAAVARIMG
RSEDDNQAAT VWSADKANVL ASGRLWRRIT SDIFAKEFPD ITLQHQLADS MAMLMVRDPR
RFNGVIHTDN TFGDILSDIS GAITGTLGLM PSASLCGVPG EGHRSNGIYE PVHGSAPDIS
GKGLANPVAQ ILSVAMMLRY SMGLEKEATA VERAVVKVLD AKSEGGLEIR TGDLGGRATC
SQVGDAVCEV LGPLLQGKKA
