ID D3FF93_CONWI Unreviewed; 331 AA. AC D3FF93; DT 23-MAR-2010, integrated into UniProtKB/TrEMBL. DT 23-MAR-2010, sequence version 1. DT 27-MAR-2024, entry version 93. DE RecName: Full=Malate dehydrogenase {ECO:0000256|ARBA:ARBA00020382, ECO:0000256|HAMAP-Rule:MF_01517}; DE EC=1.1.1.37 {ECO:0000256|ARBA:ARBA00012995, ECO:0000256|HAMAP-Rule:MF_01517}; GN Name=mdh {ECO:0000256|HAMAP-Rule:MF_01517}; GN OrderedLocusNames=Cwoe_5280 {ECO:0000313|EMBL:ADB53686.1}; OS Conexibacter woesei (strain DSM 14684 / CIP 108061 / JCM 11494 / NBRC OS 100937 / ID131577). OC Bacteria; Actinomycetota; Thermoleophilia; Solirubrobacterales; OC Conexibacteraceae; Conexibacter. OX NCBI_TaxID=469383 {ECO:0000313|EMBL:ADB53686.1, ECO:0000313|Proteomes:UP000008229}; RN [1] {ECO:0000313|EMBL:ADB53686.1, ECO:0000313|Proteomes:UP000008229} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14684 / CIP 108061 / JCM 11494 / NBRC 100937 / ID131577 RC {ECO:0000313|Proteomes:UP000008229}; RX PubMed=21304704; RA Pukall R., Lapidus A., Glavina Del Rio T., Copeland A., Tice H., RA Cheng J.-F., Lucas S., Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S., RA Mavromatis K., Ivanova N., Ovchinnikova G., Pati A., Chen A., RA Palaniappan K., Land M., Hauser L., Chang Y.-J., Jeffries C.D., Chain P., RA Meincke L., Sims D., Brettin T., Detter J.C., Rohde M., Goeker M., RA Bristow J., Eisen J.A., Markowitz V., Kyrpides N.C., Klenk H.-P., RA Hugenholtz P.; RT "Complete genome sequence of Conexibacter woesei type strain (ID131577)."; RL Stand. Genomic Sci. 2:212-219(2010). RN [2] {ECO:0000313|Proteomes:UP000008229} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14684 / CIP 108061 / JCM 11494 / NBRC 100937 / ID131577 RC {ECO:0000313|Proteomes:UP000008229}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N., RA Mikhailova N., Chertkov O., Brettin T., Detter J.C., Han C., Larimer F., RA Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., RA Wu D., Pukall R., Steenblock K., Schneider S., Klenk H.-P., Eisen J.A.; RT "The complete genome of Conexibacter woesei DSM 14684."; RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate. CC {ECO:0000256|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:0000256|HAMAP-Rule:MF_01517, CC ECO:0000256|RuleBase:RU000422}; CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family. CC {ECO:0000256|ARBA:ARBA00009613, ECO:0000256|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; CP001854; ADB53686.1; -; Genomic_DNA. DR RefSeq; WP_012936737.1; NC_013739.1. DR AlphaFoldDB; D3FF93; -. DR STRING; 469383.Cwoe_5280; -. DR KEGG; cwo:Cwoe_5280; -. DR eggNOG; COG0039; Bacteria. DR HOGENOM; CLU_040727_2_0_11; -. DR OrthoDB; 9802969at2; -. DR Proteomes; UP000008229; 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; 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; IPR001252; Malate_DH_AS. 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. DR PROSITE; PS00068; MDH; 1. PE 3: Inferred from homology; KW NAD {ECO:0000256|HAMAP-Rule:MF_01517, ECO:0000256|PIRSR:PIRSR000102-3}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01517, KW ECO:0000256|RuleBase:RU003369}; KW Reference proteome {ECO:0000313|Proteomes:UP000008229}; KW Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_01517, KW ECO:0000256|RuleBase:RU000422}. FT DOMAIN 7..149 FT /note="Lactate/malate dehydrogenase N-terminal" FT /evidence="ECO:0000259|Pfam:PF00056" FT DOMAIN 158..321 FT /note="Lactate/malate dehydrogenase C-terminal" FT /evidence="ECO:0000259|Pfam:PF02866" FT ACT_SITE 189 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01517, FT ECO:0000256|PIRSR:PIRSR000102-1" FT BINDING 13..19 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01517, FT ECO:0000256|PIRSR:PIRSR000102-3" FT BINDING 94 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01517, FT ECO:0000256|PIRSR:PIRSR000102-2" FT BINDING 100 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01517, FT ECO:0000256|PIRSR:PIRSR000102-2" FT BINDING 107 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01517, FT ECO:0000256|PIRSR:PIRSR000102-3" FT BINDING 114 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01517" FT BINDING 131..133 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01517, FT ECO:0000256|PIRSR:PIRSR000102-3" FT BINDING 133 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01517, FT ECO:0000256|PIRSR:PIRSR000102-2" FT BINDING 164 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01517, FT ECO:0000256|PIRSR:PIRSR000102-2" SQ SEQUENCE 331 AA; 34807 MW; D5942AFCCDCCE33A CRC64; MTDKQPVRVA VTGAAGQIGY ALLFRIASGA LLGPDQPVSL RLLEITPALK AVEGVIMELD DCAFPLLHSV EATDDANVAF DGASVGLLVG ARPRSRGMER ADLLEANGGI FKPQGQAINA HAADDIKVLV VGNPANTNAL IAASNAPDVP KDRFHAMTRL DHNRAIAQLS KKTGAAVKDI TNVTIWGNHS ATQYPDIFHA KVNGQNAAEL VNDQAWLEND FIPTVQKRGA AIIDARGASS AASAANAAID HVHDWVLGTP AGDWVSMSVP SDGSYGVPEG IISSFPCTTK PGGEYEIVQG LEIDAFSRAR IDASANELVE ERAAIRQLGL I //