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Database: UniProt/SWISS-PROT
Entry: IDHC_YEAST
LinkDB: IDHC_YEAST
Original site: IDHC_YEAST 
ID   IDHC_YEAST              Reviewed;         412 AA.
AC   P41939; D6VYH8;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   25-OCT-2017, entry version 150.
DE   RecName: Full=Isocitrate dehydrogenase [NADP] cytoplasmic;
DE            Short=IDH;
DE            EC=1.1.1.42;
DE   AltName: Full=IDP;
DE   AltName: Full=NADP(+)-specific ICDH;
DE   AltName: Full=Oxalosuccinate decarboxylase;
GN   Name=IDP2; OrderedLocusNames=YLR174W; ORFNames=L9470.12;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, AND
RP   CHARACTERIZATION.
RX   PubMed=8068643; DOI=10.1021/bi00198a035;
RA   Loftus T.M., Hall L.V., Anderson S.L., McAlister-Henn L.;
RT   "Isolation, characterization, and disruption of the yeast gene
RT   encoding cytosolic NADP-specific isocitrate dehydrogenase.";
RL   Biochemistry 33:9661-9667(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169871;
RA   Johnston M., Hillier L.W., Riles L., Albermann K., Andre B.,
RA   Ansorge W., Benes V., Brueckner M., Delius H., Dubois E.,
RA   Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U.,
RA   Heumann K., Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K.,
RA   Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T.,
RA   Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E.,
RA   Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M.,
RA   Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C.,
RA   Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M.,
RA   Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H.,
RA   Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A.,
RA   Hani J., Hoheisel J.D.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL   Nature 387:87-90(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.,
RA   Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and
RT   now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
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.,
RA   Dephoure N., O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA   Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA   Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-
RT   terminal acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC   -!- FUNCTION: May function in the production of NADPH for fatty acid
CC       and sterol synthesis.
CC   -!- CATALYTIC ACTIVITY: Isocitrate + NADP(+) = 2-oxoglutarate + CO(2)
CC       + NADPH.
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   -!- ENZYME REGULATION: By catabolite repression.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- MISCELLANEOUS: Present with 2620 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}.
DR   EMBL; L26312; AAA64516.1; -; Genomic_DNA.
DR   EMBL; U17246; AAB67464.1; -; Genomic_DNA.
DR   EMBL; BK006945; DAA09494.1; -; Genomic_DNA.
DR   PIR; S51419; S51419.
DR   RefSeq; NP_013275.1; NM_001182061.1.
DR   ProteinModelPortal; P41939; -.
DR   SMR; P41939; -.
DR   BioGrid; 31445; 80.
DR   DIP; DIP-4252N; -.
DR   IntAct; P41939; 2.
DR   MINT; MINT-545477; -.
DR   STRING; 4932.YLR174W; -.
DR   MaxQB; P41939; -.
DR   PRIDE; P41939; -.
DR   EnsemblFungi; YLR174W; YLR174W; YLR174W.
DR   GeneID; 850871; -.
DR   KEGG; sce:YLR174W; -.
DR   EuPathDB; FungiDB:YLR174W; -.
DR   SGD; S000004164; IDP2.
DR   GeneTree; ENSGT00900000141247; -.
DR   HOGENOM; HOG000019858; -.
DR   InParanoid; P41939; -.
DR   KO; K00031; -.
DR   OMA; MAYQKRW; -.
DR   OrthoDB; EOG092C2D51; -.
DR   BioCyc; MetaCyc:YLR174W-MONOMER; -.
DR   BioCyc; YEAST:YLR174W-MONOMER; -.
DR   BRENDA; 1.1.1.42; 984.
DR   SABIO-RK; P41939; -.
DR   PRO; PR:P41939; -.
DR   Proteomes; UP000002311; Chromosome XII.
DR   GO; GO:0005829; C:cytosol; IDA:SGD.
DR   GO; GO:0004450; F:isocitrate dehydrogenase (NADP+) activity; IDA:SGD.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0006097; P:glyoxylate cycle; IEA:UniProtKB-KW.
DR   GO; GO:0006102; P:isocitrate metabolic process; IMP:SGD.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR   InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR   InterPro; IPR004790; Isocitrate_DH_NADP.
DR   InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR   PANTHER; PTHR11822; PTHR11822; 1.
DR   Pfam; PF00180; Iso_dh; 1.
DR   PIRSF; PIRSF000108; IDH_NADP; 1.
DR   SMART; SM01329; Iso_dh; 1.
DR   TIGRFAMs; TIGR00127; nadp_idh_euk; 1.
DR   PROSITE; PS00470; IDH_IMDH; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Cytoplasm; Direct protein sequencing;
KW   Glyoxylate bypass; Magnesium; Manganese; Metal-binding; NADP;
KW   Oxidoreductase; Reference proteome; Tricarboxylic acid cycle.
FT   CHAIN         1    412       Isocitrate dehydrogenase [NADP]
FT                                cytoplasmic.
FT                                /FTId=PRO_0000083587.
FT   NP_BIND      75     77       NADP. {ECO:0000250}.
FT   NP_BIND     310    315       NADP. {ECO:0000250}.
FT   REGION       94    100       Substrate binding. {ECO:0000250}.
FT   METAL       252    252       Magnesium or manganese. {ECO:0000250}.
FT   METAL       275    275       Magnesium or manganese. {ECO:0000250}.
FT   BINDING      77     77       Substrate. {ECO:0000250}.
FT   BINDING      82     82       NADP. {ECO:0000250}.
FT   BINDING     109    109       Substrate. {ECO:0000250}.
FT   BINDING     132    132       Substrate. {ECO:0000250}.
FT   BINDING     260    260       NADP. {ECO:0000250}.
FT   BINDING     328    328       NADP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000250}.
FT   SITE        139    139       Critical for catalysis. {ECO:0000250}.
FT   SITE        212    212       Critical for catalysis. {ECO:0000250}.
FT   CONFLICT     24     27       HLIR -> SFNQ (in Ref. 1; AAA64516).
FT                                {ECO:0000305}.
FT   CONFLICT     68     68       G -> R (in Ref. 1; AAA64516).
FT                                {ECO:0000305}.
FT   CONFLICT    185    185       T -> N (in Ref. 1; AAA64516).
FT                                {ECO:0000305}.
FT   CONFLICT    232    239       ARSYKEKF -> LEVIKRSL (in Ref. 1;
FT                                AAA64516). {ECO:0000305}.
FT   CONFLICT    267    267       I -> M (in Ref. 1; AAA64516).
FT                                {ECO:0000305}.
FT   CONFLICT    306    307       EA -> DR (in Ref. 1; AAA64516).
FT                                {ECO:0000305}.
FT   CONFLICT    316    323       FRQHQQGK -> LTDYDKGR (in Ref. 1;
FT                                AAA64516). {ECO:0000305}.
SQ   SEQUENCE   412 AA;  46562 MW;  83EB54CC56A29857 CRC64;
     MTKIKVANPI VEMDGDEQTR IIWHLIRDKL VLPYLDVDLK YYDLSVEYRD QTNDQVTVDS
     ATATLKYGVA VKCATITPDE ARVEEFHLKK MWKSPNGTIR NILGGTVFRE PIIIPRIPRL
     VPQWEKPIII GRHAFGDQYK ATDVIVPEEG ELRLVYKSKS GTHDVDLKVF DYPEHGGVAM
     MMYNTTDSIE GFAKASFELA IERKLPLYST TKNTILKKYD GKFKDVFEAM YARSYKEKFE
     SLGIWYEHRL IDDMVAQMLK SKGGYIIAMK NYDGDVESDI VAQGFGSLGL MTSVLITPDG
     KTFESEAAHG TVTRHFRQHQ QGKETSTNSI ASIFAWTRGI IQRGKLDNTP DVVKFGQILE
     SATVNTVQED GIMTKDLALI LGKSERSAYV TTEEFIDAVE SRLKKEFEAA AL
//
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