LEU3_PICST
ID LEU3_PICST Reviewed; 373 AA.
AC O94114; A3M0K5;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 3.
DT 03-AUG-2022, entry version 122.
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; ORFNames=PICST_68561;
OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS Y-11545) (Yeast) (Pichia stipitis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX NCBI_TaxID=322104;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX PubMed=9534253; DOI=10.1007/s002530051150;
RA Lu P., Davis B.P., Hendrick J., Jeffries T.W.;
RT "Cloning and disruption of the beta-isopropylmalate dehydrogenase gene
RT (LEU2) of Pichia stipitis with URA3 and recovery of the double auxotroph.";
RL Appl. Microbiol. Biotechnol. 49:141-146(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX PubMed=17334359; DOI=10.1038/nbt1290;
RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA Passoth V., Richardson P.M.;
RT "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT yeast Pichia stipitis.";
RL Nat. Biotechnol. 25:319-326(2007).
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; U83626; AAD00548.2; -; Genomic_DNA.
DR EMBL; CP000502; ABN68719.2; -; Genomic_DNA.
DR RefSeq; XP_001386748.2; XM_001386711.1.
DR AlphaFoldDB; O94114; -.
DR SMR; O94114; -.
DR STRING; 4924.XP_001386748.2; -.
DR EnsemblFungi; ABN68719; ABN68719; PICST_68561.
DR GeneID; 4841123; -.
DR KEGG; pic:PICST_68561; -.
DR eggNOG; KOG0786; Eukaryota.
DR HOGENOM; CLU_031953_0_3_1; -.
DR InParanoid; O94114; -.
DR OMA; EYDLGAR; -.
DR OrthoDB; 868374at2759; -.
DR BRENDA; 1.1.1.85; 4832.
DR UniPathway; UPA00048; UER00072.
DR Proteomes; UP000002258; Chromosome 8.
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; Reference proteome.
FT CHAIN 1..373
FT /note="3-isopropylmalate dehydrogenase"
FT /id="PRO_0000083617"
FT BINDING 82..93
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 100
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 110
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 139
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 231
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 231
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 260
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 295..306
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 146
FT /note="Important for catalysis"
FT /evidence="ECO:0000250"
FT SITE 198
FT /note="Important for catalysis"
FT /evidence="ECO:0000250"
FT CONFLICT 256
FT /note="D -> Y (in Ref. 1; AAD00548)"
FT /evidence="ECO:0000305"
FT CONFLICT 364
FT /note="A -> G (in Ref. 1; AAD00548)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 373 AA; 40019 MW; C1C44AF98FC69473 CRC64;
MSTVTKTITV LPGDHVGTEI CNEAIKVLEA IEQATPYQKI HFEFKHHLIG GAAIDSTGVP
LPDDSLAAAK SSDAVLLGAV GGPKWGTGAV RPEQGLLKIR KELNLYANLR PCNFASDALL
ELSPLKSEIV KGTNFTVVRE LVGGIYFGER QEQEESADGE SAWDTEKYSV AEVTRITRMA
AFMALQHNPP LPIWSLDKAN VLASSRLWRK TVDKVMKEEF PQLTIQHQLI DSAAMILVQS
PTKLNGIVIT SNMFGDIISD EASVIPGSLG LLPSASLASL PDTNSAFGLY EPCHGSAPDL
PENKVNPIAT ILSVAMMLRL SLDSLKEAEA LEEAVRQVLD SGVRTADLRG TNSTKEVGEA
VVAAVTKILK DAA
