ID G8PMX1_PSEUV Unreviewed; 320 AA. AC G8PMX1; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAR-2024, entry version 64. DE RecName: Full=Malate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00487}; DE EC=1.1.1.37 {ECO:0000256|HAMAP-Rule:MF_00487}; GN Name=mdh {ECO:0000256|HAMAP-Rule:MF_00487, GN ECO:0000313|EMBL:AEV35126.1}; GN OrderedLocusNames=PSE_0614 {ECO:0000313|EMBL:AEV35126.1}; OS Pseudovibrio sp. (strain FO-BEG1). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Stappiaceae; Pseudovibrio. OX NCBI_TaxID=911045 {ECO:0000313|EMBL:AEV35126.1, ECO:0000313|Proteomes:UP000005634}; RN [1] {ECO:0000313|Proteomes:UP000005634} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FO-BEG1 {ECO:0000313|Proteomes:UP000005634}; RA Bondarev V., Richter M., Piel J., Schwedt A., Schulz-Vogt H.N.; RT "The genus Pseudovibrio contains metabolically versatile and symbiotically RT interacting bacteria."; RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AEV35126.1, ECO:0000313|Proteomes:UP000005634} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FO-BEG1 {ECO:0000313|EMBL:AEV35126.1, RC ECO:0000313|Proteomes:UP000005634}; RX PubMed=23601235; DOI=10.1111/1462-2920.12123; RA Bondarev V., Richter M., Romano S., Piel J., Schwedt A., Schulz-Vogt H.N.; RT "The genus Pseudovibrio contains metabolically versatile bacteria adapted RT for symbiosis."; RL Environ. Microbiol. 15:2095-2113(2013). CC -!- FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate. CC {ECO:0000256|ARBA:ARBA00003966, ECO:0000256|HAMAP-Rule:MF_00487}. 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_00487}; CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 3 family. CC {ECO:0000256|HAMAP-Rule:MF_00487}. 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; CP003147; AEV35126.1; -; Genomic_DNA. DR RefSeq; WP_008548788.1; NC_016642.1. DR AlphaFoldDB; G8PMX1; -. DR STRING; 911045.PSE_0614; -. DR KEGG; psf:PSE_0614; -. DR eggNOG; COG0039; Bacteria. DR HOGENOM; CLU_045401_2_1_5; -. DR Proteomes; UP000005634; Chromosome. DR GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-UniRule. DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule. DR CDD; cd01339; LDH-like_MDH; 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_00487; Malate_dehydrog_3; 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; IPR011275; Malate_DH_type3. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR NCBIfam; TIGR01763; MalateDH_bact; 1. DR PANTHER; PTHR43128; L-2-HYDROXYCARBOXYLATE DEHYDROGENASE (NAD(P)(+)); 1. DR PANTHER; PTHR43128:SF34; L-LACTATE DEHYDROGENASE; 1. DR Pfam; PF02866; Ldh_1_C; 1. DR Pfam; PF00056; Ldh_1_N; 1. DR PIRSF; PIRSF000102; Lac_mal_DH; 1. DR PRINTS; PR00086; LLDHDRGNASE. 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 {ECO:0000256|HAMAP-Rule:MF_00487, ECO:0000256|PIRSR:PIRSR000102-3}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00487, KW ECO:0000256|RuleBase:RU003369}; KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532, ECO:0000256|HAMAP- KW Rule:MF_00487}. FT DOMAIN 5..143 FT /note="Lactate/malate dehydrogenase N-terminal" FT /evidence="ECO:0000259|Pfam:PF00056" FT DOMAIN 148..304 FT /note="Lactate/malate dehydrogenase C-terminal" FT /evidence="ECO:0000259|Pfam:PF02866" FT ACT_SITE 176 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00487, FT ECO:0000256|PIRSR:PIRSR000102-1" FT BINDING 10..15 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00487, FT ECO:0000256|PIRSR:PIRSR000102-3" FT BINDING 34 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00487, FT ECO:0000256|PIRSR:PIRSR000102-3" FT BINDING 83 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00487, FT ECO:0000256|PIRSR:PIRSR000102-2" FT BINDING 89 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00487, FT ECO:0000256|PIRSR:PIRSR000102-2" FT BINDING 96 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00487, FT ECO:0000256|PIRSR:PIRSR000102-3" FT BINDING 119..121 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00487, FT ECO:0000256|PIRSR:PIRSR000102-3" FT BINDING 121 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00487, FT ECO:0000256|PIRSR:PIRSR000102-2" FT BINDING 152 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00487, FT ECO:0000256|PIRSR:PIRSR000102-2" SQ SEQUENCE 320 AA; 33893 MW; CC3B2B5B88936B7A CRC64; MARNKIALIG SGQIGGTLAH LAGLKELGDI VLFDIAEGMP QGKALDLAES SPVDGFDSGL SGTNTYEGIE GADVVIVTAG VPRKPGMSRD DLLEINLKVM EQVGAGIKKY APDAFVICIT NPLDAMVWAL QKFSGLPANK VVGMAGVLDS ARFRYFLAEE FNVSVEDVTA FVLGGHGDTM VPLTRYSTVA GVPLTDLVKM GWLTAERLEE IVQRTRDGGA EIVGLLKTGS AFYAPAASAI QMAESYLKDK KRVLPCAAHL DGQYGQKDMY VGVPTVIGAN GIERIIEIDL NSDEKAMFDK SVASVNGLVD ACKKIQPALA //