IDHP_YEAST
ID IDHP_YEAST Reviewed; 428 AA.
AC P21954; D6VRT1;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Isocitrate dehydrogenase [NADP], mitochondrial;
DE Short=IDH;
DE EC=1.1.1.42;
DE AltName: Full=IDP;
DE AltName: Full=NADP(+)-specific ICDH;
DE AltName: Full=Oxalosuccinate decarboxylase;
DE Flags: Precursor;
GN Name=IDP1; OrderedLocusNames=YDL066W;
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 17-36.
RX PubMed=1989987; DOI=10.1016/s0021-9258(18)52249-3;
RA Haselbeck R.J., McAlister-Henn L.;
RT "Isolation, nucleotide sequence, and disruption of the Saccharomyces
RT cerevisiae gene encoding mitochondrial NADP(H)-specific isocitrate
RT dehydrogenase.";
RL J. Biol. Chem. 266:2339-2345(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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).
CC -!- FUNCTION: Mitochondrial IDP1 may regulate flux through the
CC tricarboxylic acid cycle and respiration. Its probably critical
CC function is the production of NADPH.
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: The enzyme is subject to end product inhibition by
CC NADPH and 2-oxoglutarate.
CC -!- SUBUNIT: Homodimer.
CC -!- INTERACTION:
CC P21954; P16474: KAR2; NbExp=2; IntAct=EBI-8898, EBI-7876;
CC -!- SUBCELLULAR LOCATION: Mitochondrion.
CC -!- INDUCTION: By growth with glucose as a carbon source.
CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC dehydrogenases family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M57229; AAA34703.1; -; Genomic_DNA.
DR EMBL; Z74114; CAA98631.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11791.1; -; Genomic_DNA.
DR PIR; A38610; DCBYIS.
DR RefSeq; NP_010217.1; NM_001180125.1.
DR PDB; 2QFV; X-ray; 2.30 A; A/B/C/D=16-428.
DR PDB; 2QFW; X-ray; 2.60 A; A/B/C/D/E/F=16-428.
DR PDB; 2QFX; X-ray; 2.70 A; A/B/C/D/E/F=16-428.
DR PDB; 2QFY; X-ray; 2.10 A; A/B/C/D/E/F=16-428.
DR PDBsum; 2QFV; -.
DR PDBsum; 2QFW; -.
DR PDBsum; 2QFX; -.
DR PDBsum; 2QFY; -.
DR AlphaFoldDB; P21954; -.
DR SMR; P21954; -.
DR BioGRID; 31993; 79.
DR DIP; DIP-4494N; -.
DR IntAct; P21954; 19.
DR MINT; P21954; -.
DR STRING; 4932.YDL066W; -.
DR iPTMnet; P21954; -.
DR MaxQB; P21954; -.
DR PaxDb; P21954; -.
DR PRIDE; P21954; -.
DR EnsemblFungi; YDL066W_mRNA; YDL066W; YDL066W.
DR GeneID; 851493; -.
DR KEGG; sce:YDL066W; -.
DR SGD; S000002224; IDP1.
DR VEuPathDB; FungiDB:YDL066W; -.
DR eggNOG; KOG1526; Eukaryota.
DR GeneTree; ENSGT00390000012547; -.
DR HOGENOM; CLU_023296_1_1_1; -.
DR InParanoid; P21954; -.
DR OMA; HGTVQRH; -.
DR BioCyc; YEAST:YDL066W-MON; -.
DR BRENDA; 1.1.1.42; 984.
DR Reactome; R-SCE-389542; NADPH regeneration.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR Reactome; R-SCE-9033241; Peroxisomal protein import.
DR SABIO-RK; P21954; -.
DR EvolutionaryTrace; P21954; -.
DR PRO; PR:P21954; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P21954; protein.
DR GO; GO:0042645; C:mitochondrial nucleoid; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; 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:0006537; P:glutamate biosynthetic process; IGI:SGD.
DR GO; GO:0006097; P:glyoxylate cycle; IEA:UniProtKB-KW.
DR GO; GO:0006102; P:isocitrate metabolic process; IBA:GO_Central.
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 3D-structure; Direct protein sequencing; Glyoxylate bypass; Magnesium;
KW Manganese; Metal-binding; Mitochondrion; NADP; Oxidoreductase;
KW Reference proteome; Transit peptide; Tricarboxylic acid cycle.
FT TRANSIT 1..16
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:1989987"
FT CHAIN 17..428
FT /note="Isocitrate dehydrogenase [NADP], mitochondrial"
FT /id="PRO_0000014426"
FT BINDING 91..93
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 93
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 98
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 110..116
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 125
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 148
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 269
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 277
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 292
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 327..332
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 345
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT SITE 155
FT /note="Critical for catalysis"
FT /evidence="ECO:0000250"
FT SITE 229
FT /note="Critical for catalysis"
FT /evidence="ECO:0000250"
FT STRAND 26..30
FT /evidence="ECO:0007829|PDB:2QFY"
FT HELIX 33..46
FT /evidence="ECO:0007829|PDB:2QFY"
FT TURN 47..50
FT /evidence="ECO:0007829|PDB:2QFY"
FT STRAND 55..59
FT /evidence="ECO:0007829|PDB:2QFY"
FT HELIX 62..67
FT /evidence="ECO:0007829|PDB:2QFY"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:2QFY"
FT HELIX 71..83
FT /evidence="ECO:0007829|PDB:2QFY"
FT STRAND 84..88
FT /evidence="ECO:0007829|PDB:2QFY"
FT HELIX 96..101
FT /evidence="ECO:0007829|PDB:2QFY"
FT HELIX 111..119
FT /evidence="ECO:0007829|PDB:2QFY"
FT STRAND 121..127
FT /evidence="ECO:0007829|PDB:2QFY"
FT STRAND 142..149
FT /evidence="ECO:0007829|PDB:2QFY"
FT HELIX 153..156
FT /evidence="ECO:0007829|PDB:2QFY"
FT STRAND 158..162
FT /evidence="ECO:0007829|PDB:2QFY"
FT STRAND 164..175
FT /evidence="ECO:0007829|PDB:2QFY"
FT TURN 177..179
FT /evidence="ECO:0007829|PDB:2QFY"
FT STRAND 183..192
FT /evidence="ECO:0007829|PDB:2QFY"
FT STRAND 194..202
FT /evidence="ECO:0007829|PDB:2QFY"
FT HELIX 203..220
FT /evidence="ECO:0007829|PDB:2QFY"
FT STRAND 224..228
FT /evidence="ECO:0007829|PDB:2QFY"
FT TURN 230..232
FT /evidence="ECO:0007829|PDB:2QFY"
FT HELIX 236..251
FT /evidence="ECO:0007829|PDB:2QFY"
FT HELIX 253..259
FT /evidence="ECO:0007829|PDB:2QFY"
FT STRAND 263..267
FT /evidence="ECO:0007829|PDB:2QFY"
FT HELIX 268..277
FT /evidence="ECO:0007829|PDB:2QFY"
FT STRAND 280..286
FT /evidence="ECO:0007829|PDB:2QFY"
FT HELIX 288..302
FT /evidence="ECO:0007829|PDB:2QFY"
FT STRAND 307..313
FT /evidence="ECO:0007829|PDB:2QFY"
FT STRAND 315..318
FT /evidence="ECO:0007829|PDB:2QFX"
FT STRAND 320..323
FT /evidence="ECO:0007829|PDB:2QFY"
FT HELIX 330..337
FT /evidence="ECO:0007829|PDB:2QFY"
FT HELIX 347..364
FT /evidence="ECO:0007829|PDB:2QFY"
FT HELIX 367..385
FT /evidence="ECO:0007829|PDB:2QFY"
FT HELIX 392..397
FT /evidence="ECO:0007829|PDB:2QFY"
FT HELIX 403..405
FT /evidence="ECO:0007829|PDB:2QFY"
FT HELIX 409..426
FT /evidence="ECO:0007829|PDB:2QFY"
SQ SEQUENCE 428 AA; 48190 MW; 7F885785B8682416 CRC64;
MSMLSRRLFS TSRLAAFSKI KVKQPVVELD GDEMTRIIWD KIKKKLILPY LDVDLKYYDL
SVESRDATSD KITQDAAEAI KKYGVGIKCA TITPDEARVK EFNLHKMWKS PNGTIRNILG
GTVFREPIVI PRIPRLVPRW EKPIIIGRHA HGDQYKATDT LIPGPGSLEL VYKPSDPTTA
QPQTLKVYDY KGSGVAMAMY NTDESIEGFA HSSFKLAIDK KLNLFLSTKN TILKKYDGRF
KDIFQEVYEA QYKSKFEQLG IHYEHRLIDD MVAQMIKSKG GFIMALKNYD GDVQSDIVAQ
GFGSLGLMTS ILVTPDGKTF ESEAAHGTVT RHYRKYQKGE ETSTNSIASI FAWSRGLLKR
GELDNTPALC KFANILESAT LNTVQQDGIM TKDLALACGN NERSAYVTTE EFLDAVEKRL
QKEIKSIE
