ID MDH_YERPN Reviewed; 312 AA. AC Q1CEJ3; C4GXW8; DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot. DT 11-JUL-2006, sequence version 1. DT 27-MAR-2024, entry version 99. DE RecName: Full=Malate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01516}; DE EC=1.1.1.37 {ECO:0000255|HAMAP-Rule:MF_01516}; GN Name=mdh {ECO:0000255|HAMAP-Rule:MF_01516}; GN OrderedLocusNames=YPN_3260; ORFNames=YP516_3703; OS Yersinia pestis bv. Antiqua (strain Nepal516). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Yersiniaceae; Yersinia. OX NCBI_TaxID=377628; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Nepal516; RX PubMed=16740952; DOI=10.1128/jb.00124-06; RA Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F., Vergez L.M., RA Worsham P., Chu M.C., Andersen G.L.; RT "Complete genome sequence of Yersinia pestis strains Antiqua and Nepal516: RT evidence of gene reduction in an emerging pathogen."; RL J. Bacteriol. 188:4453-4463(2006). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Nepal516; RA Plunkett G. III, Anderson B.D., Baumler D.J., Burland V., Cabot E.L., RA Glasner J.D., Mau B., Neeno-Eckwall E., Perna N.T., Munk A.C., Tapia R., RA Green L.D., Rogers Y.C., Detter J.C., Bruce D.C., Brettin T.S.; RT "Yersinia pestis Nepal516A whole genome shotgun sequencing project."; RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate. CC {ECO:0000255|HAMAP-Rule:MF_01516}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(S)-malate + NAD(+) = H(+) + NADH + oxaloacetate; CC Xref=Rhea:RHEA:21432, ChEBI:CHEBI:15378, ChEBI:CHEBI:15589, CC ChEBI:CHEBI:16452, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.37; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01516}; CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01516}. CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 1 family. CC {ECO:0000255|HAMAP-Rule:MF_01516}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000305; ABG19587.1; -; Genomic_DNA. DR EMBL; ACNQ01000017; EEO75768.1; -; Genomic_DNA. DR RefSeq; WP_002210174.1; NZ_ACNQ01000017.1. DR AlphaFoldDB; Q1CEJ3; -. DR SMR; Q1CEJ3; -. DR GeneID; 66843123; -. DR KEGG; ypn:YPN_3260; -. DR HOGENOM; CLU_047181_1_0_6; -. DR Proteomes; UP000008936; Chromosome. DR GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006108; P:malate metabolic process; IEA:InterPro. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule. DR CDD; cd01337; MDH_glyoxysomal_mitochondrial; 1. DR Gene3D; 3.90.110.10; Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR HAMAP; MF_01516; Malate_dehydrog_1; 1. DR InterPro; IPR001557; L-lactate/malate_DH. DR InterPro; IPR022383; Lactate/malate_DH_C. DR InterPro; IPR001236; Lactate/malate_DH_N. DR InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C. DR InterPro; IPR001252; Malate_DH_AS. DR InterPro; IPR010097; Malate_DH_type1. DR InterPro; IPR023958; Malate_DH_type1_bac. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR NCBIfam; TIGR01772; MDH_euk_gproteo; 1. DR PANTHER; PTHR11540; MALATE AND LACTATE DEHYDROGENASE; 1. DR PANTHER; PTHR11540:SF16; MALATE DEHYDROGENASE, MITOCHONDRIAL; 1. DR Pfam; PF02866; Ldh_1_C; 1. DR Pfam; PF00056; Ldh_1_N; 1. DR PIRSF; PIRSF000102; Lac_mal_DH; 1. DR SUPFAM; SSF56327; LDH C-terminal domain-like; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR PROSITE; PS00068; MDH; 1. PE 3: Inferred from homology; KW NAD; Oxidoreductase; Tricarboxylic acid cycle. FT CHAIN 1..312 FT /note="Malate dehydrogenase" FT /id="PRO_0000294314" FT ACT_SITE 177 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01516" FT BINDING 7..13 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01516" FT BINDING 34 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01516" FT BINDING 81 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01516" FT BINDING 87 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01516" FT BINDING 94 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01516" FT BINDING 117..119 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01516" FT BINDING 119 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01516" FT BINDING 153 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01516" FT BINDING 227 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01516" SQ SEQUENCE 312 AA; 32625 MW; 9672E49F70B1849D CRC64; MKVAVLGAAG GIGQALALLL KTQLPSGSDL SLYDIAPVTP GVAVDLSHIP TAVNIKGFSG EDATPALQGA DIVLISAGVA RKPGMDRSDL FNVNAGIVRN LVEQIARTCP NALIGIITNP VNTTVAIAAE VLKKAGVYDK NKLFGITTLD TIRSNTFVAE LKGKQPQDIE VPVIGGHSGV TILPLLSQIP GVSFTEQEVA DLTKRIQNAG TEVVEAKAGG GSATLSMGQA AARFGLSLVR ALQGESNVVE CSYVEGDGKY ARFFAQPILL GKNGVAERKD IGKLSAFEQQ ALENMLDVLH KDIELGEKFV NQ //