LEU3_YARLI
ID LEU3_YARLI Reviewed; 405 AA.
AC P18120; Q6CDH8;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 2.
DT 03-AUG-2022, entry version 129.
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; OrderedLocusNames=YALI0C00407g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2836077; DOI=10.1007/bf00378180;
RA Davidow L.S., Kaczmarek F.S., Dezeeuw J.R., Colon S.W., Lauth M.R.,
RA Pereira D.A., Franke A.E.;
RT "The Yarrowia lipolytica LEU2 gene.";
RL Curr. Genet. 11:377-383(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Rojas Quijano R., Lepingle A., Gaillardin C.;
RT "Yarrowia lipolytica LEU2 region.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-226.
RX PubMed=2453299; DOI=10.1007/bf00378179;
RA Gaillardin C., Ribet A.M.;
RT "LEU2 directed expression of beta-galactosidase activity and phleomycin
RT resistance in Yarrowia lipolytica.";
RL Curr. Genet. 11:369-375(1987).
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 -!- SEQUENCE CAUTION:
CC Sequence=CAG81579.1; Type=Frameshift; Note=Defective LEU2 (leu2-270) in genome strain CLIB 122 / E 150.; Evidence={ECO:0000305};
CC Sequence=CAG81579.1; Type=Miscellaneous discrepancy; Note=Defective LEU2 (leu2-270) in genome strain CLIB 122 / E 150 lacks the central section (positions 43 to 269).; Evidence={ECO:0000305};
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DR EMBL; M37309; AAA35244.1; -; Genomic_DNA.
DR EMBL; AF260230; AAF70314.1; -; Genomic_DNA.
DR EMBL; CR382129; CAG81579.1; ALT_SEQ; Genomic_DNA.
DR EMBL; M35579; AAA35243.1; -; Genomic_DNA.
DR RefSeq; XP_501284.1; XM_501284.1.
DR AlphaFoldDB; P18120; -.
DR SMR; P18120; -.
DR STRING; 4952.CAG81579; -.
DR PRIDE; P18120; -.
DR GeneID; 2909561; -.
DR KEGG; yli:YALI0C00407g; -.
DR InParanoid; P18120; -.
DR UniPathway; UPA00048; UER00072.
DR Proteomes; UP000001300; Chromosome C.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0003862; F:3-isopropylmalate dehydrogenase activity; IBA:GO_Central.
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; IBA:GO_Central.
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..405
FT /note="3-isopropylmalate dehydrogenase"
FT /id="PRO_0000083621"
FT REGION 352..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 86..104
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 111
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 121
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 148
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 237
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 237
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 262
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 266
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 301..312
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 155
FT /note="Important for catalysis"
FT /evidence="ECO:0000250"
FT SITE 204
FT /note="Important for catalysis"
FT /evidence="ECO:0000250"
SQ SEQUENCE 405 AA; 43359 MW; 06CA7B276504F79E CRC64;
MEPETKKTKT DSKKIVLLGG DFCGPEVIAE AVKVLKSVAE ASGTEFVFED RLIGGAAIEK
EGEPITDATL DICRKADSIM LGAVGGAANT VWTTPDGRTD VRPEQGLLKL RKDLNLYANL
RPCQLLSPKL ADLSPIRNVE GTDFIIVREL VGGIYFGERK EDDGSGVASD TETYSVPEVE
RIARMAAFLA LQHNPPLPVW SLDKANVLAS SRLWRKTVTR VLKDEFPQLE LNHQLIDSAA
MILIKQPSKM NGIIITTNMF GDIISDEASV IPGSLGLLPS ASLASLPDTN EAFGLYEPCH
GSAPDLGKQK VNPIATILSA AMMLKFSLNM KPAGDAVEAA VKESVEAGIT TADIGGSSST
SEVGDLLPTR SRSCSRRSKS FLRRIDGRSK LTRLRVGLPA GSASV
