ID MDH_DEIRA Reviewed; 330 AA. AC Q9RXI8; DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 27-MAR-2024, entry version 132. DE RecName: Full=Malate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01517}; DE EC=1.1.1.37 {ECO:0000255|HAMAP-Rule:MF_01517}; GN Name=mdh {ECO:0000255|HAMAP-Rule:MF_01517}; OrderedLocusNames=DR_0325; OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG OS 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1). OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae; OC Deinococcus. OX NCBI_TaxID=243230; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 / RC NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1; RX PubMed=10567266; DOI=10.1126/science.286.5444.1571; RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D., RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L., RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M., RA Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C., RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D., RA Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C., RA Fraser C.M.; RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans RT R1."; RL Science 286:1571-1577(1999). CC -!- FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate. CC {ECO:0000255|HAMAP-Rule:MF_01517}. 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_01517}; CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family. CC {ECO:0000255|HAMAP-Rule:MF_01517}. 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; AE000513; AAF09906.1; -; Genomic_DNA. DR PIR; E75535; E75535. DR RefSeq; NP_294048.1; NC_001263.1. DR RefSeq; WP_010886970.1; NZ_JMLF01000001.1. DR AlphaFoldDB; Q9RXI8; -. DR SMR; Q9RXI8; -. DR STRING; 243230.DR_0325; -. DR PaxDb; 243230-DR_0325; -. DR EnsemblBacteria; AAF09906; AAF09906; DR_0325. DR GeneID; 69516557; -. DR KEGG; dra:DR_0325; -. DR PATRIC; fig|243230.17.peg.491; -. DR eggNOG; COG0039; Bacteria. DR HOGENOM; CLU_040727_2_0_0; -. DR InParanoid; Q9RXI8; -. DR OrthoDB; 9802969at2; -. DR Proteomes; UP000002524; Chromosome I. DR GO; GO:0030060; F:L-malate dehydrogenase activity; IBA:GO_Central. DR GO; GO:0006108; P:malate metabolic process; IBA:GO_Central. DR GO; GO:0006734; P:NADH metabolic process; IBA:GO_Central. DR GO; GO:0006107; P:oxaloacetate metabolic process; IBA:GO_Central. DR GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central. DR CDD; cd01338; MDH_choloroplast_like; 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_01517; Malate_dehydrog_2; 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; IPR010945; Malate_DH_type2. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR NCBIfam; TIGR01759; MalateDH-SF1; 1. DR PANTHER; PTHR23382; MALATE DEHYDROGENASE; 1. DR PANTHER; PTHR23382:SF0; MALATE DEHYDROGENASE 2, MITOCHONDRIAL-RELATED; 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. PE 3: Inferred from homology; KW NAD; Oxidoreductase; Reference proteome; Tricarboxylic acid cycle. FT CHAIN 1..330 FT /note="Malate dehydrogenase" FT /id="PRO_0000113368" FT ACT_SITE 189 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01517" FT BINDING 13..19 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01517" FT BINDING 94 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01517" FT BINDING 100 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01517" FT BINDING 107 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01517" FT BINDING 114 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01517" FT BINDING 131..133 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01517" FT BINDING 133 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01517" FT BINDING 164 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01517" SQ SEQUENCE 330 AA; 35148 MW; 2F9710386D3A2110 CRC64; MTMKQPVRVA VTGAAGQIGY SLLFRIAAGD MLGQDQPVIL QLLEITPALK ALNGVVMELR DGAFPLLADV ITSDDPMVAF KDADYALLVG AMPRKAGMER GDLLGANGGI FKPQGEALGA VASRNVKVLV VGNPANTNAL IAQQNAPDLD PKCFTAMVRL DHNRALSQLA EKTGAAVSDI KNVTIWGNHS STQYPDLSQA TVNGKPALEQ VDRTWYENDY IPTVAKRGAA IIEARGASSA ASAASAAIDH MHDWALGTKD GEWVSMGIPS DGSYGIPEGL IYGFPVRVKD GKYEIVQGLD VSDFSRGKMD ATAQELEEER DEVRKLGLVK //