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3-isopropylmalate dehydrogenase (3-IPM-DH) (IMDH) (EC 1.1.1.85) (Beta-IPM dehydrogenase)

 LEU3_YEAST              Reviewed;         364 AA.
P04173; D6VQZ6;
20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
15-MAR-2004, sequence version 4.
23-MAY-2018, entry version 166.
RecName: Full=3-isopropylmalate dehydrogenase;
Short=3-IPM-DH;
Short=IMDH;
EC=1.1.1.85;
AltName: Full=Beta-IPM dehydrogenase;
Name=LEU2; OrderedLocusNames=YCL018W; ORFNames=YCL18W;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3010239; DOI=10.1093/nar/14.8.3475;
Warmington J.R., Anwar R., Newlon C.S., Waring R.B., Davies R.W.,
Indge K.J., Oliver S.G.;
"A 'hot-spot' for Ty transposition on the left arm of yeast chromosome
III.";
Nucleic Acids Res. 14:3475-3485(1986).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 38626 / AH22 / NRRL Y-12843;
PubMed=6330094;
Andreadis A., Hsu Y.-P., Hermodson M., Kohlhaw G., Schimmel P.;
"Yeast LEU2. Repression of mRNA levels by leucine and primary
structure of the gene product.";
J. Biol. Chem. 259:8059-8062(1984).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Lu Q.;
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=1574125; DOI=10.1038/357038a0;
Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M.,
Fabre F., Fairhead C., Faye G., Feldmann H., Fiers W.,
Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H.,
Fuller L.J., Galland P., Gent M.E., Gigot D., Gilliquet V.,
Glansdorff N., Goffeau A., Grenson M., Grisanti P., Grivell L.A.,
de Haan M., Haasemann M., Hatat D., Hoenicka J., Hegemann J.H.,
Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., Huse K.,
Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B.,
Pohl F.M., Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A.,
Remacha M.A., Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y.,
Skala J., Slonimski P.P., Sor F., Soustelle C., Spiegelberg R.,
Stateva L.I., Steensma H.Y., Steiner S., Thierry A., Thireos G.,
Tzermia M., Urrestarazu L.A., Valle G., Vetter I.,
van Vliet-Reedijk J.C., Voet M., Volckaert G., Vreken P., Wang H.,
Warmington J.R., von Wettstein D., Wicksteed B.L., Wilson C.,
Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., Sgouros J.G.;
"The complete DNA sequence of yeast chromosome III.";
Nature 357:38-46(1992).
[5]
SEQUENCE REVISION TO 69.
Valles G., Volckaerts G.;
Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
[6]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 213-364.
PubMed=6396161; DOI=10.1016/0378-1119(84)90218-X;
Froman B.E., Tait R.C., Rodriguez R.L.;
"Nucleotide sequence of the 3' terminal region of the LEU2 gene from
Saccharomyces cerevisiae.";
Gene 31:257-261(1984).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
-!- FUNCTION: Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-
methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-
oxopentanoate. The product decarboxylates to 4-methyl-2
oxopentanoate.
-!- CATALYTIC ACTIVITY: (2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl-
2-oxopentanoate + CO(2) + NADH.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. {ECO:0000250};
-!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-
leucine from 3-methyl-2-oxobutanoate: step 3/4.
-!- SUBUNIT: Homodimer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
dehydrogenases family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X03840; CAA27459.1; -; Genomic_DNA.
EMBL; X59720; CAA42366.2; -; Genomic_DNA.
EMBL; M12909; AAA66917.1; -; Genomic_DNA.
EMBL; BK006937; DAA07465.1; -; Genomic_DNA.
PIR; S19344; DEBYI.
RefSeq; NP_009911.2; NM_001178665.1.
ProteinModelPortal; P04173; -.
SMR; P04173; -.
BioGrid; 30966; 17.
DIP; DIP-7880N; -.
IntAct; P04173; 157.
MINT; P04173; -.
STRING; 4932.YCL018W; -.
SWISS-2DPAGE; P04173; -.
PaxDb; P04173; -.
PRIDE; P04173; -.
EnsemblFungi; CAA42366; CAA42366; CAA42366.
EnsemblFungi; YCL018W; YCL018W; YCL018W.
GeneID; 850342; -.
KEGG; sce:YCL018W; -.
EuPathDB; FungiDB:YCL018W; -.
SGD; S000000523; LEU2.
GeneTree; ENSGT00550000076087; -.
HOGENOM; HOG000021112; -.
InParanoid; P04173; -.
KO; K00052; -.
OMA; EYDLGAR; -.
OrthoDB; EOG092C306Q; -.
BioCyc; MetaCyc:YCL018W-MONOMER; -.
BioCyc; YEAST:YCL018W-MONOMER; -.
UniPathway; UPA00048; UER00072.
PRO; PR:P04173; -.
Proteomes; UP000002311; Chromosome III.
GO; GO:0005829; C:cytosol; IDA:SGD.
GO; GO:0003862; F:3-isopropylmalate dehydrogenase activity; IDA:SGD.
GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
GO; GO:0051287; F:NAD binding; IEA:InterPro.
GO; GO:0006097; P:glyoxylate cycle; IMP:SGD.
GO; GO:0009098; P:leucine biosynthetic process; IMP:SGD.
InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
InterPro; IPR024084; IsoPropMal-DH-like_dom.
InterPro; IPR004429; Isopropylmalate_DH.
PANTHER; PTHR42979; PTHR42979; 1.
Pfam; PF00180; Iso_dh; 1.
SMART; SM01329; Iso_dh; 1.
TIGRFAMs; TIGR00169; leuB; 1.
PROSITE; PS00470; IDH_IMDH; 1.
1: Evidence at protein level;
Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
Complete proteome; Cytoplasm; Leucine biosynthesis; Magnesium;
Manganese; Metal-binding; NAD; Oxidoreductase; Reference proteome.
CHAIN 1 364 3-isopropylmalate dehydrogenase.
/FTId=PRO_0000083623.
NP_BIND 79 90 NAD. {ECO:0000250}.
NP_BIND 289 300 NAD. {ECO:0000250}.
METAL 225 225 Magnesium or manganese. {ECO:0000250}.
METAL 250 250 Magnesium or manganese. {ECO:0000250}.
METAL 254 254 Magnesium or manganese. {ECO:0000250}.
BINDING 97 97 Substrate. {ECO:0000250}.
BINDING 107 107 Substrate. {ECO:0000250}.
BINDING 136 136 Substrate. {ECO:0000250}.
BINDING 225 225 Substrate. {ECO:0000250}.
SITE 143 143 Important for catalysis. {ECO:0000250}.
SITE 192 192 Important for catalysis. {ECO:0000250}.
CONFLICT 69 69 A -> V (in Ref. 1, 2 and 3).
{ECO:0000305}.
CONFLICT 300 300 N -> D (in Ref. 2 and 3). {ECO:0000305}.
SEQUENCE 364 AA; 38953 MW; 4F312E81D829E2A3 CRC64;
MSAPKKIVVL PGDHVGQEIT AEAIKVLKAI SDVRSNVKFD FENHLIGGAA IDATGVPLPD
EALEASKKAD AVLLGAVGGP KWGTGSVRPE QGLLKIRKEL QLYANLRPCN FASDSLLDLS
PIKPQFAKGT DFVVVRELVG GIYFGKRKED DGDGVAWDSE QYTVPEVQRI TRMAAFMALQ
HEPPLPIWSL DKANVLASSR LWRKTVEETI KNEFPTLKVQ HQLIDSAAMI LVKNPTHLNG
IIITSNMFGD IISDEASVIP GSLGLLPSAS LASLPDKNTA FGLYEPCHGS APDLPKNKVN
PIATILSAAM MLKLSLNLPE EGKAIEDAVK KVLDAGIRTG DLGGSNSTTE VGDAVAEEVK
KILA


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