ID LYS12_SCHPO Reviewed; 362 AA. AC O14104; DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 16-JUN-2009, entry version 47. DE RecName: Full=Probable homoisocitrate dehydrogenase; DE EC=1.1.1.87; GN Name=lys12; ORFNames=SPAC31G5.04; 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). RN [2] 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 RT fission yeast Schizosaccharomyces pombe."; RL Nat. Biotechnol. 24:841-847(2006). RN [3] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81 AND SER-91, AND MASS RP SPECTROMETRY. RX PubMed=18257517; DOI=10.1021/pr7006335; RA Wilson-Grady J.T., Villen J., Gygi S.P.; RT "Phosphoproteome analysis of fission yeast."; RL J. Proteome Res. 7:1088-1097(2008). CC -!- CATALYTIC ACTIVITY: (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + CC NAD(+) = 2-oxoadipate + CO(2) + NADH. CC -!- COFACTOR: Binds 1 magnesium or manganese ion per subunit (By CC similarity). CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via AAA CC pathway; L-alpha-aminoadipate from 2-oxoglutarate: step 3/4. CC -!- SUBCELLULAR LOCATION: Cytoplasm. 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; CAB11688.1; -; Genomic_DNA. DR PIR; T38621; T38621. DR RefSeq; NP_594004.1; -. DR HSSP; P12010; 2AYQ. DR GeneID; 2542609; -. DR KEGG; spo:SPAC31G5.04; -. DR NMPDR; fig|4896.1.peg.3974; -. DR GeneDB_Spombe; SPAC31G5.04; -. DR OMA; O14104; VEGYSSP. DR BRENDA; 1.1.1.87; 653. DR ArrayExpress; O14104; -. DR GO; GO:0005737; C:cytoplasm; IDA:GeneDB_SPombe. DR GO; GO:0047046; F:homoisocitrate dehydrogenase 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:0009085; P:lysine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS. DR InterPro; IPR001804; Isocitrate/isopropylmalate_DH. DR Gene3D; G3DSA:3.40.718.10; IDH_IMDH; 1. DR PANTHER; PTHR11835; IDH_IMDH_dimeric; 1. DR Pfam; PF00180; Iso_dh; 1. DR PROSITE; PS00470; IDH_IMDH; 1. PE 1: Evidence at protein level; KW Amino-acid biosynthesis; Complete proteome; Cytoplasm; KW Lysine biosynthesis; Magnesium; Manganese; Metal-binding; NAD; KW Oxidoreductase; Phosphoprotein. FT CHAIN 1 362 Probable homoisocitrate dehydrogenase. FT /FTId=PRO_0000310374. FT METAL 232 232 Magnesium or manganese (By similarity). FT METAL 256 256 Magnesium or manganese (By similarity). FT METAL 260 260 Magnesium or manganese (By similarity). FT BINDING 97 97 Substrate (By similarity). FT BINDING 107 107 Substrate (By similarity). FT BINDING 126 126 Substrate (By similarity). FT BINDING 232 232 Substrate (By similarity). FT SITE 133 133 Critical for catalysis (By similarity). FT SITE 196 196 Critical for catalysis (By similarity). FT MOD_RES 81 81 Phosphoserine. FT MOD_RES 91 91 Phosphoserine. SQ SEQUENCE 362 AA; 39256 MW; 85865AFD69BCE773 CRC64; MSATRRIVLG LIPADGIGKE VVPAARRLME NLPAKHKLKF DFIDLDAGWG TFERTGKALP ERTVERLKTE CNAALFGAVQ SPTHKVAGYS SPIVALRKKM GLYANVRPVK SLDGAKGKPV DLVIVRENTE CLYVKEERMV QNTPGKRVAE AIRRISEEAS TKIGKMAFEI AKSRQKIRES GTYSIHKKPL VTIIHKSNVM SVTDGLFRES CRHAQSLDPS YASINVDEQI VDSMVYRLFR EPECFDVVVA PNLYGDILSD GAASLIGSLG LVPSANVGDN FVMSEPVHGS APDIAGRGIA NPVATFRSVA LMLEFMGHQD AAADIYTAVD KVLTEGKVLT PDLGGKSGTN EITDAVLANI HN //