ID MDH_SALTY Reviewed; 312 AA. AC P25077; DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2002, sequence version 2. DT 27-MAR-2024, entry version 154. 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}; OrderedLocusNames=STM3359; OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=99287; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=LT2; RX PubMed=8422999; DOI=10.1016/0378-1119(93)90554-g; RA Lu C.-D., Abdelal A.T.; RT "Complete sequence of the Salmonella typhimurium gene encoding malate RT dehydrogenase."; RL Gene 123:143-144(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LT2 / SGSC1412 / ATCC 700720; RX PubMed=11677609; DOI=10.1038/35101614; RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E., RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., RA Wilson R.K.; RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2."; RL Nature 413:852-856(2001). 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. 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; M95049; AAA27158.1; -; Genomic_DNA. DR EMBL; X61029; CAA43363.1; -; Genomic_DNA. DR EMBL; AE006468; AAL22228.1; -; Genomic_DNA. DR PIR; S16143; DEEBM. DR RefSeq; NP_462269.1; NC_003197.2. DR RefSeq; WP_000861586.1; NC_003197.2. DR AlphaFoldDB; P25077; -. DR SMR; P25077; -. DR STRING; 99287.STM3359; -. DR PaxDb; 99287-STM3359; -. DR GeneID; 1254882; -. DR KEGG; stm:STM3359; -. DR PATRIC; fig|99287.12.peg.3560; -. DR HOGENOM; CLU_047181_1_0_6; -. DR OMA; ASCAEYI; -. DR PhylomeDB; P25077; -. DR BioCyc; SENT99287:STM3359-MONOMER; -. DR Proteomes; UP000001014; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0030060; F:L-malate dehydrogenase activity; IBA:GO_Central. 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; Reference proteome; Tricarboxylic acid cycle. FT CHAIN 1..312 FT /note="Malate dehydrogenase" FT /id="PRO_0000113325" 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" FT CONFLICT 7 FT /note="G -> A (in Ref. 1; AAA27158/CAA43363)" FT /evidence="ECO:0000305" FT CONFLICT 156 FT /note="T -> P (in Ref. 1; AAA27158/CAA43363)" FT /evidence="ECO:0000305" FT CONFLICT 236 FT /note="L -> V (in Ref. 1; AAA27158/CAA43363)" FT /evidence="ECO:0000305" FT CONFLICT 308..309 FT /note="DF -> EI (in Ref. 1; AAA27158/CAA43363)" FT /evidence="ECO:0000305" SQ SEQUENCE 312 AA; 32476 MW; 123BA51986AA838B CRC64; MKVAVLGAAG GIGQALALLL KNQLPSGSEL SLYDIAPVTP GVAVDLSHIP TAVKIKGFSG EDATPALEGA DVVLISAGVA RKPGMDRSDL FNVNAGIVKN LVQQIAKTCP KACVGIITNP VNTTVAIAAE VLKKAGVYDK NKLFGVTTLD IIRSNTFVAE LKGKLPTEVE VPVIGGHSGV TILPLLSQIP GVSFTEQEAA ELTKRIQNAG TEVVEAKAGG GSATLSMGQA AARFGLSLVR ALQGEKGVVE CAYVEGDGQY ARFFSQPLLL GKNGVEERKS IGTLSAFEQH SLDAMLDTLK KDIQLGEDFI NK //