ID MDH_RHOPA Reviewed; 322 AA. AC P80458; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 16-FEB-2004, sequence version 2. DT 28-JAN-2026, entry version 144. DE RecName: Full=Malate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00487}; DE EC=1.1.1.37 {ECO:0000255|HAMAP-Rule:MF_00487}; GN Name=mdh {ECO:0000255|HAMAP-Rule:MF_00487}; OrderedLocusNames=RPA0192; OS Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009). OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria; OC Hyphomicrobiales; Nitrobacteraceae; Rhodopseudomonas. OX NCBI_TaxID=258594; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-98 / CGA009; RX PubMed=14704707; DOI=10.1038/nbt923; RA Larimer F.W., Chain P., Hauser L., Lamerdin J.E., Malfatti S., Do L., RA Land M.L., Pelletier D.A., Beatty J.T., Lang A.S., Tabita F.R., RA Gibson J.L., Hanson T.E., Bobst C., Torres y Torres J.L., Peres C., RA Harrison F.H., Gibson J., Harwood C.S.; RT "Complete genome sequence of the metabolically versatile photosynthetic RT bacterium Rhodopseudomonas palustris."; RL Nat. Biotechnol. 22:55-61(2004). RN [2] RP PROTEIN SEQUENCE OF 5-25. RA Naterstad K., Synstad B., Sirevag R.; RL Submitted (SEP-1996) to UniProtKB. CC -!- FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate. CC {ECO:0000255|HAMAP-Rule:MF_00487}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(S)-malate + NAD(+) = oxaloacetate + NADH + H(+); 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_00487}; CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 3 family. CC {ECO:0000255|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; BX572593; CAE25636.1; -; Genomic_DNA. DR RefSeq; WP_011155760.1; NZ_CP116810.1. DR AlphaFoldDB; P80458; -. DR SMR; P80458; -. DR STRING; 258594.RPA0192; -. DR GeneID; 66891197; -. DR eggNOG; COG0039; Bacteria. DR HOGENOM; CLU_045401_2_1_5; -. DR PhylomeDB; P80458; -. DR GO; GO:0004459; F:L-lactate dehydrogenase (NAD+) activity; IEA:TreeGrafter. DR GO; GO:0030060; F:L-malate dehydrogenase (NAD+) activity; IEA:UniProtKB-UniRule. DR GO; GO:0006089; P:lactate metabolic process; IEA:TreeGrafter. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule. DR CDD; cd01339; LDH-like_MDH; 1. DR FunFam; 3.40.50.720:FF:000018; Malate dehydrogenase; 1. DR FunFam; 3.90.110.10:FF:000004; Malate dehydrogenase; 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 NCBIfam; NF004863; PRK06223.1; 1. DR PANTHER; PTHR43128; L-2-HYDROXYCARBOXYLATE DEHYDROGENASE (NAD(P)(+)); 1. DR PANTHER; PTHR43128:SF16; 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 1: Evidence at protein level; KW Direct protein sequencing; NAD; Oxidoreductase; Tricarboxylic acid cycle. FT CHAIN 1..322 FT /note="Malate dehydrogenase" FT /id="PRO_0000113465" FT ACT_SITE 176 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487" FT BINDING 10..15 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487" FT BINDING 34 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487" FT BINDING 83 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487" FT BINDING 89 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487" FT BINDING 96 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487" FT BINDING 119..121 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487" FT BINDING 121 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487" FT BINDING 152 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487" FT CONFLICT 13 FT /note="Q -> E (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 21..22 FT /note="LV -> MI (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" SQ SEQUENCE 322 AA; 33996 MW; 8F41556B89B2D187 CRC64; MARDKIALIG SGQIGGTLAH LVGLKELGDV VLFDIAEGVP QGKALDIAES SPVDGFDSKL TGANSYEAIE GARVVIVTAG VPRKPGMSRD DLLSINLKVM EQVGAGIKKY APDAFVICIT NPLDAMVWAL QKASGLPAKK VVGMAGVLDS ARFRYFLADE FNVSVEDVTA FVLGGHGDTM VPLVKYSTVA GIPLPDLVKM GWTSQARLDE IVDRTRNGGA EIVNLLKTGS AFYAPASSAI AMAESYLKDK KRVVPVAAHL NGEYGVKDMY VGVPVVIGDK GVERIVEIEL AGKDKEAFDR SVAAVQGLVE ACKKIAPDLL GR //