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IDH1_YEAST
ID   IDH1_YEAST              Reviewed;         360 AA.
AC   P28834; D6W1E2;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 2.
DT   03-AUG-2022, entry version 189.
DE   RecName: Full=Isocitrate dehydrogenase [NAD] subunit 1, mitochondrial;
DE            EC=1.1.1.41;
DE   AltName: Full=Isocitric dehydrogenase;
DE   AltName: Full=NAD(+)-specific ICDH;
DE   Flags: Precursor;
GN   Name=IDH1; OrderedLocusNames=YNL037C; ORFNames=N2690;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 49-61; 72-83;
RP   325-333 AND 339-356.
RX   PubMed=1644826; DOI=10.1016/s0021-9258(18)42019-4;
RA   Cupp J.R., McAlister-Henn L.;
RT   "Cloning and characterization of the gene encoding the IDH1 subunit of
RT   NAD(+)-dependent isocitrate dehydrogenase from Saccharomyces cerevisiae.";
RL   J. Biol. Chem. 267:16417-16423(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169873;
RA   Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA   Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA   Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA   Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA   Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA   Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA   Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA   Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA   Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA   Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA   Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA   Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA   Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA   Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA   Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA   Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA   Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT   evolutionary implications.";
RL   Nature 387:93-98(1997).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   PROTEIN SEQUENCE OF 12-27.
RC   STRAIN=SG7;
RX   PubMed=2198251; DOI=10.1128/jb.172.8.4280-4287.1990;
RA   Keys D.A., McAlister-Henn L.;
RT   "Subunit structure, expression, and function of NAD(H)-specific isocitrate
RT   dehydrogenase in Saccharomyces cerevisiae.";
RL   J. Bacteriol. 172:4280-4287(1990).
RN   [5]
RP   RNA-BINDING.
RX   PubMed=7505425; DOI=10.1093/nar/21.23.5328;
RA   Elzinga S.D.J., Bednarz A.L., van Oosterum K., Dekker P.J.T., Grivell L.A.;
RT   "Yeast mitochondrial NAD(+)-dependent isocitrate dehydrogenase is an RNA-
RT   binding protein.";
RL   Nucleic Acids Res. 21:5328-5331(1993).
RN   [6]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
CC   -!- FUNCTION: Performs an essential role in the oxidative function of the
CC       citric acid cycle. Also binds RNA; specifically to the 5'-untranslated
CC       leaders of mitochondrial mRNAs.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-threo-isocitrate + NAD(+) = 2-oxoglutarate + CO2 + NADH;
CC         Xref=Rhea:RHEA:23632, ChEBI:CHEBI:15562, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.41;
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   -!- ACTIVITY REGULATION: Allosterically regulated by several compounds
CC       including AMP, NAD(+), and citrate.
CC   -!- SUBUNIT: Octamer of two non-identical subunits IDH1 and IDH2.
CC   -!- INTERACTION:
CC       P28834; P28241: IDH2; NbExp=6; IntAct=EBI-8878, EBI-8883;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion.
CC   -!- MISCELLANEOUS: Present with 10500 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC       dehydrogenases family. {ECO:0000305}.
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DR   EMBL; M95203; AAA34711.1; -; Genomic_DNA.
DR   EMBL; Z71313; CAA95904.1; -; Genomic_DNA.
DR   EMBL; BK006947; DAA10508.1; -; Genomic_DNA.
DR   PIR; S31264; S31264.
DR   RefSeq; NP_014361.1; NM_001182876.1.
DR   PDB; 3BLV; X-ray; 3.20 A; A/C/E/G=12-360.
DR   PDB; 3BLW; X-ray; 4.30 A; A/C/E/G/I/K/M/O=12-360.
DR   PDB; 3BLX; X-ray; 2.70 A; A/C/E/G/I/K/M/O=12-360.
DR   PDBsum; 3BLV; -.
DR   PDBsum; 3BLW; -.
DR   PDBsum; 3BLX; -.
DR   AlphaFoldDB; P28834; -.
DR   SMR; P28834; -.
DR   BioGRID; 35787; 288.
DR   ComplexPortal; CPX-558; Mitochondrial isocitrate dehydrogenase complex (NAD+).
DR   DIP; DIP-4376N; -.
DR   IntAct; P28834; 26.
DR   MINT; P28834; -.
DR   STRING; 4932.YNL037C; -.
DR   MoonProt; P28834; -.
DR   MaxQB; P28834; -.
DR   PaxDb; P28834; -.
DR   PRIDE; P28834; -.
DR   EnsemblFungi; YNL037C_mRNA; YNL037C; YNL037C.
DR   GeneID; 855691; -.
DR   KEGG; sce:YNL037C; -.
DR   SGD; S000004982; IDH1.
DR   VEuPathDB; FungiDB:YNL037C; -.
DR   eggNOG; KOG0784; Eukaryota.
DR   GeneTree; ENSGT00950000182989; -.
DR   HOGENOM; CLU_031953_0_0_1; -.
DR   InParanoid; P28834; -.
DR   OMA; TCAHKAN; -.
DR   BioCyc; MetaCyc:YNL037C-MON; -.
DR   BioCyc; YEAST:YNL037C-MON; -.
DR   BRENDA; 1.1.1.41; 984.
DR   Reactome; R-SCE-71403; Citric acid cycle (TCA cycle).
DR   EvolutionaryTrace; P28834; -.
DR   PRO; PR:P28834; -.
DR   Proteomes; UP000002311; Chromosome XIV.
DR   RNAct; P28834; protein.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; TAS:Reactome.
DR   GO; GO:0005962; C:mitochondrial isocitrate dehydrogenase complex (NAD+); IDA:SGD.
DR   GO; GO:0005759; C:mitochondrial matrix; IDA:SGD.
DR   GO; GO:0042645; C:mitochondrial nucleoid; IDA:SGD.
DR   GO; GO:0005739; C:mitochondrion; IDA:ComplexPortal.
DR   GO; GO:0004449; F:isocitrate dehydrogenase (NAD+) 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:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006537; P:glutamate biosynthetic process; TAS:SGD.
DR   GO; GO:0006102; P:isocitrate metabolic process; IDA:SGD.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IDA:ComplexPortal.
DR   InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR   InterPro; IPR004434; Isocitrate_DH_NAD.
DR   InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR   Pfam; PF00180; Iso_dh; 1.
DR   SMART; SM01329; Iso_dh; 1.
DR   TIGRFAMs; TIGR00175; mito_nad_idh; 1.
DR   PROSITE; PS00470; IDH_IMDH; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Allosteric enzyme; Direct protein sequencing; Magnesium;
KW   Manganese; Metal-binding; Mitochondrion; NAD; Oxidoreductase;
KW   Reference proteome; RNA-binding; Transit peptide; Tricarboxylic acid cycle.
FT   TRANSIT         1..11
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000269|PubMed:2198251"
FT   CHAIN           12..360
FT                   /note="Isocitrate dehydrogenase [NAD] subunit 1,
FT                   mitochondrial"
FT                   /id="PRO_0000014431"
FT   BINDING         109
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         140
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         228
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P50213"
FT   BINDING         228
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            194
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000250"
FT   STRAND          29..37
FT                   /evidence="ECO:0007829|PDB:3BLX"
FT   HELIX           38..53
FT                   /evidence="ECO:0007829|PDB:3BLX"
FT   STRAND          57..62
FT                   /evidence="ECO:0007829|PDB:3BLX"
FT   HELIX           71..84
FT                   /evidence="ECO:0007829|PDB:3BLX"
FT   STRAND          85..91
FT                   /evidence="ECO:0007829|PDB:3BLX"
FT   HELIX           95..99
FT                   /evidence="ECO:0007829|PDB:3BLX"
FT   HELIX           102..110
FT                   /evidence="ECO:0007829|PDB:3BLX"
FT   STRAND          114..122
FT                   /evidence="ECO:0007829|PDB:3BLX"
FT   STRAND          135..141
FT                   /evidence="ECO:0007829|PDB:3BLX"
FT   HELIX           145..148
FT                   /evidence="ECO:0007829|PDB:3BLX"
FT   STRAND          150..153
FT                   /evidence="ECO:0007829|PDB:3BLX"
FT   STRAND          158..166
FT                   /evidence="ECO:0007829|PDB:3BLX"
FT   HELIX           167..183
FT                   /evidence="ECO:0007829|PDB:3BLX"
FT   STRAND          188..193
FT                   /evidence="ECO:0007829|PDB:3BLX"
FT   TURN            195..197
FT                   /evidence="ECO:0007829|PDB:3BLX"
FT   HELIX           201..216
FT                   /evidence="ECO:0007829|PDB:3BLX"
FT   STRAND          220..226
FT                   /evidence="ECO:0007829|PDB:3BLX"
FT   HELIX           227..236
FT                   /evidence="ECO:0007829|PDB:3BLX"
FT   HELIX           238..240
FT                   /evidence="ECO:0007829|PDB:3BLX"
FT   STRAND          242..246
FT                   /evidence="ECO:0007829|PDB:3BLX"
FT   HELIX           248..262
FT                   /evidence="ECO:0007829|PDB:3BLX"
FT   HELIX           265..267
FT                   /evidence="ECO:0007829|PDB:3BLX"
FT   STRAND          269..276
FT                   /evidence="ECO:0007829|PDB:3BLX"
FT   STRAND          278..280
FT                   /evidence="ECO:0007829|PDB:3BLX"
FT   TURN            283..286
FT                   /evidence="ECO:0007829|PDB:3BLX"
FT   HELIX           289..291
FT                   /evidence="ECO:0007829|PDB:3BLV"
FT   HELIX           300..313
FT                   /evidence="ECO:0007829|PDB:3BLX"
FT   HELIX           317..331
FT                   /evidence="ECO:0007829|PDB:3BLX"
FT   STRAND          332..335
FT                   /evidence="ECO:0007829|PDB:3BLX"
FT   HELIX           338..340
FT                   /evidence="ECO:0007829|PDB:3BLX"
FT   HELIX           346..358
FT                   /evidence="ECO:0007829|PDB:3BLX"
SQ   SEQUENCE   360 AA;  39324 MW;  0932E7B3CD685240 CRC64;
     MLNRTIAKRT LATAAQAERT LPKKYGGRFT VTLIPGDGVG KEITDSVRTI FEAENIPIDW
     ETINIKQTDH KEGVYEAVES LKRNKIGLKG LWHTPADQTG HGSLNVALRK QLDIYANVAL
     FKSLKGVKTR IPDIDLIVIR ENTEGEFSGL EHESVPGVVE SLKVMTRPKT ERIARFAFDF
     AKKYNRKSVT AVHKANIMKL GDGLFRNIIT EIGQKEYPDI DVSSIIVDNA SMQAVAKPHQ
     FDVLVTPSMY GTILGNIGAA LIGGPGLVAG ANFGRDYAVF EPGSRHVGLD IKGQNVANPT
     AMILSSTLML NHLGLNEYAT RISKAVHETI AEGKHTTRDI GGSSSTTDFT NEIINKLSTM
 
 
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