LEU3_SCHPO
ID LEU3_SCHPO Reviewed; 371 AA.
AC P18869; Q76PD7;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=3-isopropylmalate dehydrogenase;
DE Short=3-IPM-DH;
DE Short=IMDH;
DE EC=1.1.1.85 {ECO:0000305|PubMed:3063400};
DE AltName: Full=Beta-IPM dehydrogenase;
GN Name=leu1; ORFNames=SPBC1A4.02c, SPBC1E8.07c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP PATHWAY.
RX PubMed=3063400; DOI=10.1007/bf00419995;
RA Kikuchi Y., Kitazawa Y., Shimatake G., Yamamoto M.;
RT "The primary structure of the leu1+ gene of Schizosaccharomyces pombe.";
RL Curr. Genet. 14:375-379(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-55, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
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 {ECO:0000305|PubMed:3063400}.
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 Evidence={ECO:0000305|PubMed:3063400};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32272;
CC Evidence={ECO:0000305|PubMed:3063400};
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. {ECO:0000305|PubMed:3063400}.
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; M36910; AAA35316.1; -; Genomic_DNA.
DR EMBL; CU329671; CAA16840.1; -; Genomic_DNA.
DR PIR; T43407; T43407.
DR RefSeq; NP_595804.2; NM_001021706.3.
DR AlphaFoldDB; P18869; -.
DR SMR; P18869; -.
DR BioGRID; 276814; 36.
DR STRING; 4896.SPBC1A4.02c.1; -.
DR iPTMnet; P18869; -.
DR MaxQB; P18869; -.
DR PaxDb; P18869; -.
DR PRIDE; P18869; -.
DR EnsemblFungi; SPBC1A4.02c.1; SPBC1A4.02c.1:pep; SPBC1A4.02c.
DR GeneID; 2540283; -.
DR KEGG; spo:SPBC1A4.02c; -.
DR PomBase; SPBC1A4.02c; leu1.
DR VEuPathDB; FungiDB:SPBC1A4.02c; -.
DR eggNOG; KOG0786; Eukaryota.
DR HOGENOM; CLU_031953_0_3_1; -.
DR InParanoid; P18869; -.
DR OMA; EYDLGAR; -.
DR PhylomeDB; P18869; -.
DR UniPathway; UPA00048; UER00072.
DR PRO; PR:P18869; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; IGI:PomBase.
DR GO; GO:0003862; F:3-isopropylmalate dehydrogenase activity; IGI:PomBase.
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; IGI:PomBase.
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 1: Evidence at protein level;
KW Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; Cytoplasm;
KW Leucine biosynthesis; Magnesium; Manganese; Metal-binding; NAD;
KW Oxidoreductase; Phosphoprotein; Reference proteome.
FT CHAIN 1..371
FT /note="3-isopropylmalate dehydrogenase"
FT /id="PRO_0000083618"
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 290..302
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"
FT MOD_RES 55
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 371 AA; 39733 MW; 65AA2E6AA94D45EE CRC64;
MCAKKIVVLP GDHIGPEIVA SALEVLKVVE KKRPELKLEF EEHKIGGASI DAYGTPLTDE
TVKACLEADG VLLGAVGGPE WTNPNCRPEQ GLLKLRKSMG VWANLRPCNF ASKSLVKYSP
LKPEIVEGVD FCVVRELTGG CYFGERTEDN GSGYAMDTWP YSLEEVSRIA RLAAWLAETS
NPPAPVTLLD KANVLATSRL WRKTVAKIFK EEYPHLTLKN QLIDSAAMLL VKSPRTLNGV
VLTDNLFGDI ISDEASVIPG SLGLLPSASL SGVVGKSEEK VHCLVEPIHG SAPDIAGKGI
VNPVGTILSA SLLLRYGLNA PKEAEAIEAA VRKVLDDTSI GGRGLYTRDL GGEASTADIT
KAVVEELEKI L
