LEU3_WICAN
ID LEU3_WICAN Reviewed; 364 AA.
AC Q9HDQ1;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 83.
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 Wickerhamomyces anomalus (strain ATCC 8168 / CBS 5759 / DSM 6766 / JCM 3585
OS / IAM 12210 / NCYC 432 / NBRC 10213 / NRRL Y-366 / AJ 5027) (Yeast) (Pichia
OS anomala).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Wickerhamomyces.
OX NCBI_TaxID=885923;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 8168 / CBS 5759 / DSM 6766 / JCM 3585 / IAM 12210 / NCYC 432 /
RC NBRC 10213 / NRRL Y-366 / AJ 5027;
RX PubMed=11746605; DOI=10.1002/yea.794;
RA de la Rosa J.M., Perez J.A., Gutierrez F., Gonzalez J.M., Ruiz T.,
RA Rodriguez L.;
RT "Cloning and sequence analysis of the LEU2 homologue gene from Pichia
RT anomala.";
RL Yeast 18:1441-1448(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. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ294714; CAC08508.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9HDQ1; -.
DR SMR; Q9HDQ1; -.
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..364
FT /note="3-isopropylmalate dehydrogenase"
FT /id="PRO_0000083609"
FT BINDING 78..89
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 96
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 106
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 135
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 249
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 253
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 288..299
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 142
FT /note="Important for catalysis"
FT /evidence="ECO:0000250"
FT SITE 191
FT /note="Important for catalysis"
FT /evidence="ECO:0000250"
SQ SEQUENCE 364 AA; 38909 MW; 2105B1D2AABD7EFB CRC64;
MSEKTIVVLP GDHVGTEITN EAIKVLKAIE EVRPNVKFNF QHHLIGGAAI DATGVPLPDE
ALEAAKKADA VLLGAVGGPK WGTGAVRPEQ GLLKIRKELN LYANLRPCNF ASESLLELSP
IKAEFAKGTD FTVVRELVGG IYFGERKEDD GSGVASDTET YSVPEVQRIT RMAAFMALQH
NPPLPIWSLD KANVLASSRL WRKTVTETIE KEFPQLTVQH QLIDSAAMIL IKSPTTLNGI
VITSNMFGDI ISDEASVIPG SLGLLPSASL ASLPDTNKAF GLYEPCHGSA PDLPANKVNP
IATILSAAMM LKLSLDLFEE GVALEKAVKE VLDAGVRTGD LRGSNSTKEV GDAAVEAAKR
ILKN
