ID MDHM_RAT Reviewed; 338 AA. AC P04636; Q6GSM4; DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot. DT 09-JAN-2007, sequence version 2. DT 04-NOV-2008, entry version 85. DE RecName: Full=Malate dehydrogenase, mitochondrial; DE EC=1.1.1.37; DE Flags: Precursor; GN Name=Mdh2; Synonyms=Mor1; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=86312879; PubMed=3755817; DOI=10.1093/nar/14.15.6053; RA Grant P.M., Tellam J., May V.L., Strauss A.W.; RT "Isolation and nucleotide sequence of a cDNA clone encoding rat RT mitochondrial malate dehydrogenase."; RL Nucleic Acids Res. 14:6053-6066(1986). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Pituitary anterior lobe; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP PROTEIN SEQUENCE OF 25-338. RX MEDLINE=87157605; PubMed=3828294; DOI=10.1021/bi00375a019; RA Grant P.M., Roderick S.L., Grant G.A., Banaszak L.J., Strauss A.W.; RT "Comparison of the precursor and mature forms of rat heart RT mitochondrial malate dehydrogenase."; RL Biochemistry 26:128-134(1987). RN [4] RP PROTEIN SEQUENCE OF 27-52; 53-74; 166-185; 192-203; 216-239; 242-296 RP AND 308-324, AND MASS SPECTROMETRY. RC STRAIN=Sprague-Dawley; TISSUE=Brain, Hippocampus, and Spinal cord; RA Lubec G., Afjehi-Sadat L., Chen W.-Q., Kang S.U.; RL Submitted (JUL-2007) to UniProtKB. CC -!- CATALYTIC ACTIVITY: (S)-malate + NAD(+) = oxaloacetate + NADH. CC -!- SUBUNIT: Homodimer. 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; X04240; CAA27812.1; -; mRNA. DR EMBL; BC063165; AAH63165.1; -; mRNA. DR PIR; A25509; DERTMM. DR RefSeq; NP_112413.2; -. DR UniGene; Rn.1011; -. DR HSSP; P00346; 1MLD. DR SMR; P04636; 25-337. DR Rat-heart-2DPAGE; P04636; -. DR Ensembl; ENSRNOG00000001440; Rattus norvegicus. DR GeneID; 81829; -. DR KEGG; rno:81829; -. DR NMPDR; fig|10116.3.peg.8382; -. DR RGD; 619719; Mor1. DR HOVERGEN; P04636; -. DR NextBio; 615775; -. DR ArrayExpress; P04636; -. DR GermOnline; ENSRNOG00000001440; Rattus norvegicus. DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell. 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; IPR001252; Malate_DHase_AS. 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. DR PROSITE; PS00068; MDH; 1. PE 1: Evidence at protein level; KW Acetylation; Direct protein sequencing; Mitochondrion; NAD; KW Oxidoreductase; Phosphoprotein; Transit peptide; KW Tricarboxylic acid cycle. FT TRANSIT 1 24 Mitochondrion. FT CHAIN 25 338 Malate dehydrogenase, mitochondrial. FT /FTId=PRO_0000018631. FT NP_BIND 31 37 NAD (By similarity). FT NP_BIND 140 142 NAD (By similarity). FT ACT_SITE 200 200 Proton acceptor (By similarity). FT BINDING 57 57 NAD (By similarity). FT BINDING 104 104 Substrate (By similarity). FT BINDING 110 110 Substrate (By similarity). FT BINDING 117 117 NAD (By similarity). FT BINDING 142 142 Substrate (By similarity). FT BINDING 176 176 Substrate (By similarity). FT BINDING 251 251 NAD (By similarity). FT MOD_RES 56 56 Phosphotyrosine (By similarity). FT MOD_RES 157 157 N6-acetyllysine (By similarity). FT MOD_RES 239 239 N6-acetyllysine (By similarity). FT MOD_RES 314 314 N6-acetyllysine (By similarity). FT CONFLICT 229 229 R -> K (in Ref. 1; CAA27812). SQ SEQUENCE 338 AA; 35684 MW; 13849CCFB78C87E7 CRC64; MLSALARPVG AALRRSFSTS AQNNAKVAVL GASGGIGQPL SLLLKNSPLV SRLTLYDIAH TPGVAADLSH IETRANVKGY LGPEQLPDCL KGCDVVVIPA GVPRKPGMTR DDLFNTNATI VATLTAACAQ HCPEAMICII SNPVNSTIPI TAEVFKKHGV YNPNKIFGVT TLDIVRANTF VAELKGLDPA RVNVPVIGGH AGKTIIPLIS QCTPKVDFPQ DQLATLTGRI QEAGTEVVKA KAGAGSATLS MAYAGARFVF SLVDAMNGKE GVIECSFVQS KETECTYFST PLLLGKKGLE KNLGIGKITP FEEKMIAEAI PELKASIKKG EDFVKNMK //