ID MDHM_SCHPO Reviewed; 341 AA. AC Q9Y7R8; DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 25-NOV-2008, entry version 46. DE RecName: Full=Malate dehydrogenase, mitochondrial; DE EC=1.1.1.37; DE Flags: Precursor; GN Name=MDH1; ORFNames=SPCC306.08c; 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). CC -!- CATALYTIC ACTIVITY: (S)-malate + NAD(+) = oxaloacetate + NADH. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix. CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 1 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; CU329672; CAB41656.1; -; Genomic_DNA. DR PIR; T41286; T41286. DR RefSeq; NP_587816.1; -. DR HSSP; P00346; 1MLD. DR GeneID; 2538766; -. DR KEGG; spo:SPCC306.08c; -. DR NMPDR; fig|4896.1.peg.154; -. DR GeneDB_Spombe; SPCC306.08c; -. DR ArrayExpress; Q9Y7R8; -. DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell. DR GO; GO:0005488; F:binding; IEA:InterPro. DR GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:InterPro. DR GO; GO:0033554; P:cellular response to stress; IEP:GeneDB_SPombe. DR GO; GO:0006096; P:glycolysis; IEA:InterPro. DR GO; GO:0006108; P:malate metabolic process; IEA:InterPro. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW. DR InterPro; IPR001557; L-lactate/malate_DHase. DR InterPro; IPR001236; Lactate/malate_DHase. DR InterPro; IPR015955; Lactate_DHase/Glyco_Ohase_4_C. DR InterPro; IPR010097; Malate_DHase_NAD-dep_euk_g_bac. DR InterPro; IPR016040; NAD(P)-bd. DR Gene3D; G3DSA:3.90.110.10; lact_mal_DH; 1. DR Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1. DR PANTHER; PTHR11540:SF1; MDH_euk_g_bac; 1. DR Pfam; PF02866; Ldh_1_C; 1. DR Pfam; PF00056; Ldh_1_N; 1. DR PIRSF; PIRSF000102; Lac_mal_DH; 1. DR TIGRFAMs; TIGR01772; MDH_euk_gproteo; 1. PE 2: Evidence at transcript level; KW Complete proteome; Mitochondrion; NAD; Oxidoreductase; KW Transit peptide; Tricarboxylic acid cycle. FT TRANSIT 1 ? Mitochondrion (Potential). FT CHAIN ? 341 Malate dehydrogenase, mitochondrial. FT /FTId=PRO_0000310436. FT NP_BIND 35 41 NAD (By similarity). FT ACT_SITE 205 205 Proton acceptor (By similarity). FT BINDING 61 61 NAD (By similarity). FT BINDING 109 109 Substrate (By similarity). FT BINDING 115 115 Substrate (By similarity). FT BINDING 122 122 NAD (By similarity). FT BINDING 147 147 Substrate (By similarity). FT BINDING 181 181 Substrate (By similarity). FT BINDING 254 254 NAD (By similarity). SQ SEQUENCE 341 AA; 35787 MW; 4681EBFD2B1F7716 CRC64; MFAKVAFKNF TPLKSIAPRS FSTTSSRAFK VAVLGAGGGI GQPLSMLLKL NDKVSELALF DIRGAPGVAA DIGHINTTSN VVGYAPDDKG LEKALNGADV VIIPAGVPRK PGMTRDDLFA TNASIVRDLA FAAGETCPEA KYLVVTNPVN STVPIFKKAL ERVGVHQPKH LFGVTTLDSV RASRFTSQVT NGKAELLHIP VVGGHSGATI VPLLSQGGVE LTGEKRDALI HRIQFGGDEV VKAKAGAGSA TLSMAYAGAR MASSVLRALA GESGVEECTF VESPLYKDQG IDFFASRVTL GKDGVDTIHP VGKINDYEES LLKVALGELK KSITKGEQFV A //