ID MDH_KLEVA Reviewed; 232 AA. AC P61896; DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot. DT 07-JUN-2004, sequence version 1. DT 13-SEP-2023, entry version 73. DE RecName: Full=Malate dehydrogenase; DE EC=1.1.1.37; DE Flags: Fragment; GN Name=mdh; OS Klebsiella variicola. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella. OX NCBI_TaxID=244366; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=6A2, 801, and F2R9; RX PubMed=15053318; DOI=10.1078/0723-2020-00261; RA Rosenblueth M., Martinez L., Silva J., Martinez-Romero E.; RT "Klebsiella variicola, a novel species with clinical and plant-associated RT isolates."; RL Syst. Appl. Microbiol. 27:27-35(2004). CC -!- FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate. CC {ECO:0000250}. 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|PROSITE-ProRule:PRU10004}; CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 1 family. CC {ECO:0000305}. 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; AY367377; AAQ72403.1; -; Genomic_DNA. DR EMBL; AY367378; AAQ72404.1; -; Genomic_DNA. DR EMBL; AY367379; AAQ72405.1; -; Genomic_DNA. DR AlphaFoldDB; P61896; -. DR SMR; P61896; -. DR GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0006108; P:malate metabolic process; IEA:InterPro. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW. 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 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; 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 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..>232 FT /note="Malate dehydrogenase" FT /id="PRO_0000113312" FT ACT_SITE 147 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT BINDING 4 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 51 FT /ligand="substrate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004" FT BINDING 57 FT /ligand="substrate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004" FT BINDING 64 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 87..89 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 89 FT /ligand="substrate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004" FT BINDING 123 FT /ligand="substrate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004" FT BINDING 197 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT NON_TER 1 FT NON_TER 232 SQ SEQUENCE 232 AA; 23972 MW; 19C78AB8CCF568E6 CRC64; SLYDIAPVTP GVAVDLSHIP TDVKIKGFSG EDATPALEGA DVVLISAGVA RKPGMDRSDL FNVNAGIVKN LVQQIAKTCP QACIGVITNP VNTTVAIAAE VLKKAGVYDK NKLFGVTTLD IIRSNTFVAE LKGKSATEVE VPVIGGHSGV TILPLLSQIP GVSFSDQEVA DLTKRIQNAG TEVVEAKAGG GSATLSMGQA AARFGLSLVR AMQGEKGVVE CAYVEGDGHY AR //