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Database: UniProt/SWISS-PROT
Entry: IDHP_YEAST
LinkDB: IDHP_YEAST
Original site: 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   12-SEP-2018, entry version 172.
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;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 17-36.
RX   PubMed=1989987;
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.,
RA   Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M.,
RA   Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L.,
RA   Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M.,
RA   Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S.,
RA   Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M.,
RA   Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S.,
RA   Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K.,
RA   Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D.,
RA   Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C.,
RA   Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T.,
RA   Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E.,
RA   Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W.,
RA   Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K.,
RA   Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S.,
RA   Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A.,
RA   Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA   Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S.,
RA   Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M.,
RA   Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y.,
RA   Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M.,
RA   Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E.,
RA   Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R.,
RA   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.,
RA   Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and
RT   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: 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   -!- ACTIVITY REGULATION: The enzyme is subject to end product
CC       inhibition by NADPH and 2-oxoglutarate.
CC   -!- SUBUNIT: Homodimer.
CC   -!- INTERACTION:
CC       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}.
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   ProteinModelPortal; P21954; -.
DR   SMR; P21954; -.
DR   BioGrid; 31993; 71.
DR   DIP; DIP-4494N; -.
DR   IntAct; P21954; 19.
DR   MINT; P21954; -.
DR   STRING; 4932.YDL066W; -.
DR   MaxQB; P21954; -.
DR   PaxDb; P21954; -.
DR   PRIDE; P21954; -.
DR   EnsemblFungi; YDL066W; YDL066W; YDL066W.
DR   GeneID; 851493; -.
DR   KEGG; sce:YDL066W; -.
DR   EuPathDB; FungiDB:YDL066W; -.
DR   SGD; S000002224; IDP1.
DR   GeneTree; ENSGT00390000012547; -.
DR   HOGENOM; HOG000019858; -.
DR   InParanoid; P21954; -.
DR   KO; K00031; -.
DR   OMA; AMGMYNQ; -.
DR   OrthoDB; EOG092C2D51; -.
DR   BioCyc; YEAST:YDL066W-MONOMER; -.
DR   BRENDA; 1.1.1.42; 984.
DR   Reactome; R-SCE-2151201; Transcriptional activation of mitochondrial biogenesis.
DR   Reactome; R-SCE-389542; NADPH regeneration.
DR   Reactome; R-SCE-6798695; Neutrophil degranulation.
DR   Reactome; R-SCE-71403; Citric acid cycle (TCA cycle).
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   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; IEA:InterPro.
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; Complete proteome; Direct protein sequencing;
KW   Glyoxylate bypass; Magnesium; Manganese; Metal-binding; Mitochondrion;
KW   NADP; Oxidoreductase; Reference proteome; Transit peptide;
KW   Tricarboxylic acid cycle.
FT   TRANSIT       1     16       Mitochondrion.
FT                                {ECO:0000269|PubMed:1989987}.
FT   CHAIN        17    428       Isocitrate dehydrogenase [NADP],
FT                                mitochondrial.
FT                                /FTId=PRO_0000014426.
FT   NP_BIND      91     93       NADP. {ECO:0000250}.
FT   NP_BIND     327    332       NADP. {ECO:0000250}.
FT   REGION      110    116       Substrate binding. {ECO:0000250}.
FT   METAL       269    269       Magnesium or manganese. {ECO:0000250}.
FT   METAL       292    292       Magnesium or manganese. {ECO:0000250}.
FT   BINDING      93     93       Substrate. {ECO:0000250}.
FT   BINDING      98     98       NADP. {ECO:0000250}.
FT   BINDING     125    125       Substrate. {ECO:0000250}.
FT   BINDING     148    148       Substrate. {ECO:0000250}.
FT   BINDING     277    277       NADP. {ECO:0000250}.
FT   BINDING     345    345       NADP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000250}.
FT   SITE        155    155       Critical for catalysis. {ECO:0000250}.
FT   SITE        229    229       Critical for catalysis. {ECO:0000250}.
FT   STRAND       26     30       {ECO:0000244|PDB:2QFY}.
FT   HELIX        33     46       {ECO:0000244|PDB:2QFY}.
FT   TURN         47     50       {ECO:0000244|PDB:2QFY}.
FT   STRAND       55     59       {ECO:0000244|PDB:2QFY}.
FT   HELIX        62     67       {ECO:0000244|PDB:2QFY}.
FT   TURN         68     70       {ECO:0000244|PDB:2QFY}.
FT   HELIX        71     83       {ECO:0000244|PDB:2QFY}.
FT   STRAND       84     88       {ECO:0000244|PDB:2QFY}.
FT   HELIX        96    101       {ECO:0000244|PDB:2QFY}.
FT   HELIX       111    119       {ECO:0000244|PDB:2QFY}.
FT   STRAND      121    127       {ECO:0000244|PDB:2QFY}.
FT   STRAND      142    149       {ECO:0000244|PDB:2QFY}.
FT   HELIX       153    156       {ECO:0000244|PDB:2QFY}.
FT   STRAND      158    162       {ECO:0000244|PDB:2QFY}.
FT   STRAND      164    175       {ECO:0000244|PDB:2QFY}.
FT   TURN        177    179       {ECO:0000244|PDB:2QFY}.
FT   STRAND      183    192       {ECO:0000244|PDB:2QFY}.
FT   STRAND      194    202       {ECO:0000244|PDB:2QFY}.
FT   HELIX       203    220       {ECO:0000244|PDB:2QFY}.
FT   STRAND      224    228       {ECO:0000244|PDB:2QFY}.
FT   TURN        230    232       {ECO:0000244|PDB:2QFY}.
FT   HELIX       236    251       {ECO:0000244|PDB:2QFY}.
FT   HELIX       253    259       {ECO:0000244|PDB:2QFY}.
FT   STRAND      263    267       {ECO:0000244|PDB:2QFY}.
FT   HELIX       268    277       {ECO:0000244|PDB:2QFY}.
FT   STRAND      280    286       {ECO:0000244|PDB:2QFY}.
FT   HELIX       288    302       {ECO:0000244|PDB:2QFY}.
FT   STRAND      307    313       {ECO:0000244|PDB:2QFY}.
FT   STRAND      315    318       {ECO:0000244|PDB:2QFX}.
FT   STRAND      320    323       {ECO:0000244|PDB:2QFY}.
FT   HELIX       330    337       {ECO:0000244|PDB:2QFY}.
FT   HELIX       347    364       {ECO:0000244|PDB:2QFY}.
FT   HELIX       367    385       {ECO:0000244|PDB:2QFY}.
FT   HELIX       392    397       {ECO:0000244|PDB:2QFY}.
FT   HELIX       403    405       {ECO:0000244|PDB:2QFY}.
FT   HELIX       409    426       {ECO:0000244|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
//
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