ID   IDHP_SCHPO              Reviewed;         439 AA.
AC   O14254;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2012, sequence version 2.
DT   27-MAR-2024, entry version 161.
DE   RecName: Full=Probable 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; ORFNames=SPAC6G10.08;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   REVISION OF GENE MODEL.
RX   PubMed=21511999; DOI=10.1126/science.1203357;
RA   Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA   Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA   Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA   Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA   French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA   Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA   Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA   Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA   Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA   Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT   "Comparative functional genomics of the fission yeasts.";
RL   Science 332:930-936(2011).
RN   [3]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
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   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC       dehydrogenases family. {ECO:0000305}.
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DR   EMBL; CU329670; CAB11294.2; -; Genomic_DNA.
DR   PIR; T39058; T39058.
DR   RefSeq; NP_594105.2; NM_001019529.2.
DR   AlphaFoldDB; O14254; -.
DR   SMR; O14254; -.
DR   BioGRID; 279052; 74.
DR   STRING; 284812.O14254; -.
DR   MaxQB; O14254; -.
DR   PaxDb; 4896-SPAC6G10-08-1; -.
DR   EnsemblFungi; SPAC6G10.08.1; SPAC6G10.08.1:pep; SPAC6G10.08.
DR   GeneID; 2542598; -.
DR   KEGG; spo:SPAC6G10.08; -.
DR   PomBase; SPAC6G10.08; idp1.
DR   VEuPathDB; FungiDB:SPAC6G10.08; -.
DR   eggNOG; KOG1526; Eukaryota.
DR   HOGENOM; CLU_023296_1_1_1; -.
DR   InParanoid; O14254; -.
DR   OMA; HGTVQRH; -.
DR   Reactome; R-SPO-389542; NADPH regeneration.
DR   Reactome; R-SPO-6798695; Neutrophil degranulation.
DR   Reactome; R-SPO-9033241; Peroxisomal protein import.
DR   PRO; PR:O14254; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR   GO; GO:0004450; F:isocitrate dehydrogenase (NADP+) activity; IBA:GO_Central.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
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:0006740; P:NADPH regeneration; ISO:PomBase.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IC:PomBase.
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:SF21; ISOCITRATE DEHYDROGENASE [NADP], MITOCHONDRIAL; 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   3: Inferred from homology;
KW   Magnesium; Manganese; Metal-binding; Mitochondrion; NADP; Oxidoreductase;
KW   Reference proteome; Transit peptide; Tricarboxylic acid cycle.
FT   TRANSIT         1..26
FT                   /note="Mitochondrion"
FT   CHAIN           27..439
FT                   /note="Probable isocitrate dehydrogenase [NADP],
FT                   mitochondrial"
FT                   /id="PRO_0000014425"
FT   BINDING         106..108
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         108
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         113
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         125..131
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         140
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         163
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         283
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         291
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         306
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         341..346
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         359
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   SITE            170
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000250"
FT   SITE            243
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   439 AA;  49479 MW;  CF68839E7C423F5D CRC64;
     MLEVRAAVKA PFKLAAAGRG FMNMRMASSK SFQKITVKNP VVEMDGDEMT RVIWKIIREK
     LVLPYMDIKL DYYDLGIEAR DKTNDQITVD AAKAILKNDV GIKCATITPD EARVKEYNLK
     KMWKSPNGTI RNILNGTVFR EPILIKNIPK YIPGWTNPIC IGRHAFGDQY KSTDLVASGP
     GKLELSFTPK GNPSAKETYN VYEFNGSGVA MSMYNTDDSI RGFAHSSFQM ALQKKMPLYL
     STKNTILKKY DGRFKDTFQE VYESDYKQKF EELGLWYQHR LIDDMVAQAI KSNGGFVWAC
     KNYDGDVMSD VVAQAYGSLG LMTSVLIHPN GRTFESEAAH GTVQRHYMQY LKGKKTSTNS
     IASIFAWTRG LAHRGRLDGN ERLVKFANAL EHACVRCVEK GIMTKDLYLL SKSPNGYVDT
     FEFLDAVKSE LDSELVNIA
//