ID IDHP_SCHPO Reviewed; 418 AA. AC O14254; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 16-JUN-2009, entry version 65. DE RecName: Full=Probable isocitrate dehydrogenase [NADP], mitochondrial; DE Short=IDH; DE EC=1.1.1.42; DE AltName: Full=Oxalosuccinate decarboxylase; DE AltName: Full=NADP(+)-specific ICDH; DE AltName: Full=IDP; DE Flags: Precursor; GN Name=idp1; ORFNames=SPAC6G10.08; OS Schizosaccharomyces pombe (Fission yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; OC Schizosaccharomycetes; Schizosaccharomycetales; OC Schizosaccharomycetaceae; Schizosaccharomyces. OX NCBI_TaxID=4896; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 38366 / 972; RX MEDLINE=21848401; 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., RA Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A., RA Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., RA Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., RA James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., RA Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., RA Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., RA Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., RA Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., RA Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., RA Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., RA Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., RA Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., RA Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., RA Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., RA Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., RA Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., RA Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., RA Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., RA Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., RA Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., RA Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.; RT "The genome sequence of Schizosaccharomyces pombe."; RL Nature 415:871-880(2002). CC -!- CATALYTIC ACTIVITY: Isocitrate + NADP(+) = 2-oxoglutarate + CO(2) CC + NADPH. CC -!- CATALYTIC ACTIVITY: Oxalosuccinate + NADP(+) = 2-oxoglutarate + CC CO(2) + NADPH. CC -!- COFACTOR: Binds 1 magnesium or manganese ion per subunit (By CC similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion (By similarity). CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate CC dehydrogenases family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CU329670; CAB11294.1; -; Genomic_DNA. DR PIR; T39058; T39058. DR RefSeq; NP_594105.1; -. DR HSSP; P33198; 1LWD. DR GeneID; 2542598; -. DR KEGG; spo:SPAC6G10.08; -. DR NMPDR; fig|4896.1.peg.4075; -. DR GeneDB_Spombe; SPAC6G10.08; -. DR OMA; O14254; GGMLWAC. DR BioCyc; SPOM-XXX-01:SPOM-XXX-01-001728-MON; -. DR BRENDA; 1.1.1.42; 653. DR ArrayExpress; O14254; -. DR GO; GO:0005739; C:mitochondrion; IDA:GeneDB_SPombe. DR GO; GO:0004450; F:isocitrate dehydrogenase (NADP+) activity; IEA:EC. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW. DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-KW. DR GO; GO:0051287; F:NAD or NADH binding; IEA:InterPro. DR GO; GO:0006102; P:isocitrate metabolic process; IEA:InterPro. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR GO; GO:0006099; P:tricarboxylic acid cycle; IC:GeneDB_SPombe. DR InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS. DR InterPro; IPR001804; Isocitrate/isopropylmalate_DH. DR InterPro; IPR004790; Isocitrate_DH_NADP-dep_euk. DR Gene3D; G3DSA:3.40.718.10; IDH_IMDH; 1. DR PANTHER; PTHR11822; IDH_NADP_euk; 1. DR Pfam; PF00180; Iso_dh; 1. DR PIRSF; PIRSF000108; IDH_NADP; 1. DR TIGRFAMs; TIGR00127; nadp_idh_euk; 1. DR PROSITE; PS00470; IDH_IMDH; 1. PE 2: Evidence at transcript level; KW Complete proteome; Magnesium; Manganese; Metal-binding; Mitochondrion; KW NADP; Oxidoreductase; Transit peptide; Tricarboxylic acid cycle. FT TRANSIT 1 ? Mitochondrion. FT CHAIN ? 418 Probable isocitrate dehydrogenase [NADP], FT mitochondrial. FT /FTId=PRO_0000014425. FT NP_BIND 85 87 NADP (By similarity). FT NP_BIND 320 325 NADP (By similarity). FT REGION 104 110 Substrate binding (By similarity). FT METAL 262 262 Magnesium or manganese (By similarity). FT METAL 285 285 Magnesium or manganese (By similarity). FT BINDING 87 87 Substrate (By similarity). FT BINDING 92 92 NADP (By similarity). FT BINDING 119 119 Substrate (By similarity). FT BINDING 142 142 Substrate (By similarity). FT BINDING 270 270 NADP (By similarity). FT BINDING 338 338 NADP; via amide nitrogen and carbonyl FT oxygen (By similarity). FT SITE 149 149 Critical for catalysis (By similarity). FT SITE 222 222 Critical for catalysis (By similarity). SQ SEQUENCE 418 AA; 47293 MW; 6E114B379C8AD61E CRC64; MNMRMASSKS FQKITVKNPV VEMDGDEMTR VIWKIIREKL VLPYMDIKLD YYDLGIEARD KTNDQITVDA AKAILKNDVG IKCATITPDE ARVKEYNLKK MWKSPNGTIR NILNGTVFRE PILIKNIPKY IPGWTNPICI GRHAFGDQYK STDLVASGPG KLELSFTPKG NPSAKETYNV YEFNGSGVAM SMYNTDDSIR GFAHSSFQMA LQKKMPLYLS TKNTILKKYD GRFKDTFQEV YESDYKQKFE ELGLWYQHRL IDDMVAQAIK SNGGFVWACK NYDGDVMSDV VAQAYGSLGL MTSVLIHPNG RTFESEAAHG TVQRHYMQYL KGKKTSTNSI ASIFAWTRGL AHRGRLDGNE RLVKFANALE HACVRCVEKG IMTKDLYLLS KSPNGYVDTF EFLDAVKSEL DSELVNIA //