ID MDH_AERHH Reviewed; 311 AA. AC A0KG16; DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot. DT 12-DEC-2006, sequence version 1. DT 16-JUN-2009, entry version 17. DE RecName: Full=Malate dehydrogenase; DE EC=1.1.1.37; GN Name=mdh; OrderedLocusNames=AHA_0659; OS Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / NCIB 9240). OC Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales; OC Aeromonadaceae; Aeromonas. OX NCBI_TaxID=380703; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16980456; DOI=10.1128/JB.00621-06; RA Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J., RA Haft D.H., Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M., RA Jin S., Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.; RT "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all RT trades."; RL J. Bacteriol. 188:8272-8282(2006). CC -!- FUNCTION: Catalyzes the reversible oxidation of malate to CC oxaloacetate (By similarity). CC -!- CATALYTIC ACTIVITY: (S)-malate + NAD(+) = oxaloacetate + NADH. CC -!- SUBUNIT: Homodimer (By similarity). 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; CP000462; ABK35951.1; -; Genomic_DNA. DR RefSeq; YP_855201.1; -. DR SMR; A0KG16; 1-310. DR GeneID; 4486843; -. DR GenomeReviews; CP000462_GR; AHA_0659. DR KEGG; aha:AHA_0659; -. DR TIGR; AHA_0659; -. DR OMA; A0KG16; MGWTTQE. DR GO; GO:0005488; F:binding; IEA:InterPro. DR GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:HAMAP. 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:HAMAP. DR HAMAP; MF_01516; -; 1. DR InterPro; IPR001557; L-lactate/malate_DH. DR InterPro; IPR001236; Lactate/malate_DH. DR InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C. DR InterPro; IPR001252; Malate_DH_AS. DR InterPro; IPR010097; Malate_DH_NAD-dep_euk_g_bac. DR InterPro; IPR016040; NAD(P)-bd_dom. 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 3: Inferred from homology; KW Complete proteome; NAD; Oxidoreductase; Tricarboxylic acid cycle. FT CHAIN 1 311 Malate dehydrogenase. FT /FTId=PRO_0000294292. FT NP_BIND 7 13 NAD (By similarity). FT NP_BIND 117 119 NAD (By similarity). FT ACT_SITE 177 177 Proton acceptor (By similarity). FT BINDING 34 34 NAD (By similarity). FT BINDING 81 81 Substrate (By similarity). FT BINDING 87 87 Substrate (By similarity). FT BINDING 94 94 NAD (By similarity). FT BINDING 119 119 Substrate (By similarity). FT BINDING 153 153 Substrate (By similarity). FT BINDING 227 227 NAD (By similarity). SQ SEQUENCE 311 AA; 32113 MW; B7976C035279DA6E CRC64; MKVAVLGAAG GIGQALALLL KNRLPAGSEL SLYDIAPVTP GVAVDLSHIP TDVKVKGFCG EDPSPALVGA DVVLISAGVA RKPGMDRSDL FNINAGIVKN LVEKCAASCP KALIGIITNP VNTTVAIAAE VLKKAGVYDK RRLFGVTTLD VIRAETFVAE AKGLNVDKVR VNVIGGHSGV TILPLLSQIE GASFTADEVA AMTKRIQNAG TEVVEAKAGG GSATLSMGQA ACRFGLSLIK GLQGEANVIE CAYVEGDGKH ATFFAQPILL GKNGVETVLD YGKLSAFEQE AMDGMLATLK ADIQLGVEFV K //