ID MDH_METEP Reviewed; 320 AA. AC A9W386; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 05-FEB-2008, sequence version 1. DT 27-MAR-2024, entry version 96. 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}; GN OrderedLocusNames=Mext_1643; OS Methylorubrum extorquens (strain PA1) (Methylobacterium extorquens). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Methylobacteriaceae; Methylorubrum. OX NCBI_TaxID=419610; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PA1; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., RA Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Detter J.C., RA Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., RA Marx C., Richardson P.; RT "Complete sequence of Methylobacterium extorquens PA1."; RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases. 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(+) = 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_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; CP000908; ABY30042.1; -; Genomic_DNA. DR RefSeq; WP_003599890.1; NC_010172.1. DR PDB; 4ROS; X-ray; 1.95 A; A=1-320. DR PDB; 5ULV; X-ray; 1.66 A; A=1-320. DR PDBsum; 4ROS; -. DR PDBsum; 5ULV; -. DR AlphaFoldDB; A9W386; -. DR SMR; A9W386; -. DR KEGG; mex:Mext_1643; -. DR eggNOG; COG0039; Bacteria. DR HOGENOM; CLU_045401_2_1_5; -. DR BioCyc; MEXT419610:MEXT_RS08340-MONOMER; -. 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 1: Evidence at protein level; KW 3D-structure; NAD; Oxidoreductase; Tricarboxylic acid cycle. FT CHAIN 1..320 FT /note="Malate dehydrogenase" FT /id="PRO_1000126138" 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 STRAND 5..9 FT /evidence="ECO:0007829|PDB:4ROS" FT HELIX 13..24 FT /evidence="ECO:0007829|PDB:4ROS" FT STRAND 29..33 FT /evidence="ECO:0007829|PDB:4ROS" FT STRAND 35..38 FT /evidence="ECO:0007829|PDB:4ROS" FT HELIX 39..54 FT /evidence="ECO:0007829|PDB:4ROS" FT STRAND 60..65 FT /evidence="ECO:0007829|PDB:4ROS" FT HELIX 66..69 FT /evidence="ECO:0007829|PDB:4ROS" FT STRAND 73..77 FT /evidence="ECO:0007829|PDB:4ROS" FT HELIX 89..92 FT /evidence="ECO:0007829|PDB:4ROS" FT HELIX 93..110 FT /evidence="ECO:0007829|PDB:4ROS" FT STRAND 115..118 FT /evidence="ECO:0007829|PDB:4ROS" FT HELIX 123..134 FT /evidence="ECO:0007829|PDB:4ROS" FT HELIX 138..140 FT /evidence="ECO:0007829|PDB:4ROS" FT STRAND 141..143 FT /evidence="ECO:0007829|PDB:4ROS" FT HELIX 146..161 FT /evidence="ECO:0007829|PDB:4ROS" FT HELIX 165..167 FT /evidence="ECO:0007829|PDB:4ROS" FT STRAND 172..174 FT /evidence="ECO:0007829|PDB:4ROS" FT HELIX 184..186 FT /evidence="ECO:0007829|PDB:4ROS" FT HELIX 194..199 FT /evidence="ECO:0007829|PDB:4ROS" FT HELIX 205..216 FT /evidence="ECO:0007829|PDB:4ROS" FT HELIX 218..226 FT /evidence="ECO:0007829|PDB:4ROS" FT STRAND 227..229 FT /evidence="ECO:0007829|PDB:4ROS" FT HELIX 233..247 FT /evidence="ECO:0007829|PDB:4ROS" FT STRAND 252..262 FT /evidence="ECO:0007829|PDB:4ROS" FT HELIX 263..265 FT /evidence="ECO:0007829|PDB:4ROS" FT STRAND 267..278 FT /evidence="ECO:0007829|PDB:4ROS" FT STRAND 281..285 FT /evidence="ECO:0007829|PDB:4ROS" FT HELIX 292..314 FT /evidence="ECO:0007829|PDB:4ROS" SQ SEQUENCE 320 AA; 33647 MW; B2CF23AAA0F032EC CRC64; MARSKIALIG AGQIGGTLAH LAGLKELGDV VLFDIVDGVP QGKALDIAES APVDGFDAKY SGASDYSAIA GADVVIVTAG VPRKPGMSRD DLIGINLKVM EAVGAGIKEH APDAFVICIT NPLDAMVWAL QKFSGLPTNK VVGMAGVLDS ARFRHFLAEE FGVSVEDVTA FVLGGHGDDM VPLTRYSTVA GVPLTDLVKL GWTTQEKLDA MVERTRKGGG EIVNLLKTGS AFYAPAASAI AMAESYLRDK KRVLPCAAYL DGQYGIDGLY VGVPVVIGEN GVERVLEVTF NDDEKAMFEK SVNSVKGLIE ACKSVNDKLA //