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   27-MAR-2024, entry version 182.
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; Saccharomycetes;
OC   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 encoding
RT   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., Ansorge W.,
RA   Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA   Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA   Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA   Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA   Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA   Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA   Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA   Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA   Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA   Zollner A., 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., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and 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., Dephoure N.,
RA   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., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   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 and
CC       sterol synthesis.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-threo-isocitrate + NADP(+) = 2-oxoglutarate + CO2 + NADPH;
CC         Xref=Rhea:RHEA:19629, ChEBI:CHEBI:15562, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.42;
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: 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 medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC       dehydrogenases family. {ECO:0000305}.
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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   AlphaFoldDB; P41939; -.
DR   SMR; P41939; -.
DR   BioGRID; 31445; 96.
DR   DIP; DIP-4252N; -.
DR   IntAct; P41939; 2.
DR   STRING; 4932.YLR174W; -.
DR   MaxQB; P41939; -.
DR   PaxDb; 4932-YLR174W; -.
DR   PeptideAtlas; P41939; -.
DR   EnsemblFungi; YLR174W_mRNA; YLR174W; YLR174W.
DR   GeneID; 850871; -.
DR   KEGG; sce:YLR174W; -.
DR   AGR; SGD:S000004164; -.
DR   SGD; S000004164; IDP2.
DR   VEuPathDB; FungiDB:YLR174W; -.
DR   eggNOG; KOG1526; Eukaryota.
DR   GeneTree; ENSGT00390000012547; -.
DR   HOGENOM; CLU_023296_1_1_1; -.
DR   InParanoid; P41939; -.
DR   OMA; EYPVYNF; -.
DR   OrthoDB; 423at2759; -.
DR   BioCyc; MetaCyc:YLR174W-MONOMER; -.
DR   BioCyc; YEAST:YLR174W-MONOMER; -.
DR   BRENDA; 1.1.1.42; 984.
DR   SABIO-RK; P41939; -.
DR   BioGRID-ORCS; 850871; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P41939; -.
DR   Proteomes; UP000002311; Chromosome XII.
DR   RNAct; P41939; Protein.
DR   GO; GO:0005829; C:cytosol; IDA:SGD.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
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:0006739; P:NADP metabolic process; IBA:GO_Central.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1.
DR   InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR   InterPro; IPR004790; Isocitrate_DH_NADP.
DR   InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR   NCBIfam; TIGR00127; nadp_idh_euk; 1.
DR   PANTHER; PTHR11822:SF41; ISOCITRATE DEHYDROGENASE [NADP]-RELATED; 1.
DR   PANTHER; PTHR11822; NADP-SPECIFIC ISOCITRATE DEHYDROGENASE; 1.
DR   Pfam; PF00180; Iso_dh; 1.
DR   PIRSF; PIRSF000108; IDH_NADP; 1.
DR   SMART; SM01329; Iso_dh; 1.
DR   SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
DR   PROSITE; PS00470; IDH_IMDH; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Glyoxylate bypass; Magnesium;
KW   Manganese; Metal-binding; NADP; Oxidoreductase; Reference proteome;
KW   Tricarboxylic acid cycle.
FT   CHAIN           1..412
FT                   /note="Isocitrate dehydrogenase [NADP] cytoplasmic"
FT                   /id="PRO_0000083587"
FT   BINDING         75..77
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         77
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         82
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         94..100
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         109
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         132
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         252
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         260
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         275
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         310..315
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         328
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   SITE            139
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000250"
FT   SITE            212
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        24..27
FT                   /note="HLIR -> SFNQ (in Ref. 1; AAA64516)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        68
FT                   /note="G -> R (in Ref. 1; AAA64516)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        185
FT                   /note="T -> N (in Ref. 1; AAA64516)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        232..239
FT                   /note="ARSYKEKF -> LEVIKRSL (in Ref. 1; AAA64516)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        267
FT                   /note="I -> M (in Ref. 1; AAA64516)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        306..307
FT                   /note="EA -> DR (in Ref. 1; AAA64516)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        316..323
FT                   /note="FRQHQQGK -> LTDYDKGR (in Ref. 1; AAA64516)"
FT                   /evidence="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
//