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 03-AUG-2022, entry version 176.
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; 94.
DR DIP; DIP-4252N; -.
DR IntAct; P41939; 2.
DR STRING; 4932.YLR174W; -.
DR MaxQB; P41939; -.
DR PaxDb; P41939; -.
DR PRIDE; P41939; -.
DR EnsemblFungi; YLR174W_mRNA; YLR174W; YLR174W.
DR GeneID; 850871; -.
DR KEGG; sce:YLR174W; -.
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; IQKRWPL; -.
DR BioCyc; MetaCyc:YLR174W-MON; -.
DR BioCyc; YEAST:YLR174W-MON; -.
DR BRENDA; 1.1.1.42; 984.
DR SABIO-RK; P41939; -.
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 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 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
