ID MDH_PROVB Reviewed; 310 AA. AC P0C890; P80038; P94687; DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot. DT 14-OCT-2008, sequence version 1. DT 27-MAR-2024, entry version 66. 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}; OS Prosthecochloris vibrioformis (Chlorobium vibrioforme). OC Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae; OC Prosthecochloris. OX NCBI_TaxID=1098; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8955383; DOI=10.1128/jb.178.24.7047-7052.1996; RA Naterstad K., Lauvrak V., Sirevag R.; RT "Malate dehydrogenase from the mesophile Chlorobium vibrioforme and from RT the mild thermophile Chlorobium tepidum: molecular cloning, construction of RT a hybrid, and expression in Escherichia coli."; RL J. Bacteriol. 178:7047-7052(1996). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), AND SUBUNIT. RX PubMed=12054817; DOI=10.1016/s0022-2836(02)00050-5; RA Dalhus B., Saarinen M., Sauer U.H., Eklund P., Johansson K., Karlsson A., RA Ramaswamy S., Bjoerk A., Synstad B., Naterstad K., Sirevaag R., Eklund H.; RT "Structural basis for thermophilic protein stability: structures of RT thermophilic and mesophilic malate dehydrogenases."; RL J. Mol. Biol. 318:707-721(2002). 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 -!- SUBUNIT: Homotetramer; arranged as a dimer of dimers. CC {ECO:0000269|PubMed:12054817}. 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; X80837; CAA56809.1; -; Genomic_DNA. DR PDB; 1GUZ; X-ray; 2.00 A; A/B/C/D=72-310. DR PDB; 1GV1; X-ray; 2.50 A; A/B/C/D=1-310. DR PDBsum; 1GUZ; -. DR PDBsum; 1GV1; -. DR AlphaFoldDB; P0C890; -. DR SMR; P0C890; -. DR EvolutionaryTrace; P0C890; -. 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..310 FT /note="Malate dehydrogenase" FT /id="PRO_0000113449" FT ACT_SITE 174 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487" FT BINDING 7..12 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487" FT BINDING 32 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487" FT BINDING 81 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487" FT BINDING 87 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487" FT BINDING 94 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487" FT BINDING 117..119 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487" FT BINDING 119 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487" FT BINDING 150 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487" FT STRAND 2..6 FT /evidence="ECO:0007829|PDB:1GUZ" FT HELIX 10..18 FT /evidence="ECO:0007829|PDB:1GUZ" FT STRAND 26..31 FT /evidence="ECO:0007829|PDB:1GV1" FT STRAND 33..36 FT /evidence="ECO:0007829|PDB:1GV1" FT HELIX 37..46 FT /evidence="ECO:0007829|PDB:1GV1" FT HELIX 49..52 FT /evidence="ECO:0007829|PDB:1GV1" FT STRAND 57..62 FT /evidence="ECO:0007829|PDB:1GV1" FT HELIX 64..67 FT /evidence="ECO:0007829|PDB:1GV1" FT STRAND 71..75 FT /evidence="ECO:0007829|PDB:1GV1" FT HELIX 87..108 FT /evidence="ECO:0007829|PDB:1GUZ" FT STRAND 113..116 FT /evidence="ECO:0007829|PDB:1GUZ" FT HELIX 121..132 FT /evidence="ECO:0007829|PDB:1GUZ" FT HELIX 136..138 FT /evidence="ECO:0007829|PDB:1GUZ" FT STRAND 139..142 FT /evidence="ECO:0007829|PDB:1GUZ" FT HELIX 144..159 FT /evidence="ECO:0007829|PDB:1GUZ" FT HELIX 163..165 FT /evidence="ECO:0007829|PDB:1GUZ" FT STRAND 170..172 FT /evidence="ECO:0007829|PDB:1GUZ" FT HELIX 175..177 FT /evidence="ECO:0007829|PDB:1GUZ" FT STRAND 178..180 FT /evidence="ECO:0007829|PDB:1GUZ" FT HELIX 182..184 FT /evidence="ECO:0007829|PDB:1GUZ" FT HELIX 192..195 FT /evidence="ECO:0007829|PDB:1GUZ" FT HELIX 198..209 FT /evidence="ECO:0007829|PDB:1GUZ" FT HELIX 211..219 FT /evidence="ECO:0007829|PDB:1GUZ" FT STRAND 220..222 FT /evidence="ECO:0007829|PDB:1GUZ" FT HELIX 230..240 FT /evidence="ECO:0007829|PDB:1GUZ" FT STRAND 245..255 FT /evidence="ECO:0007829|PDB:1GUZ" FT HELIX 256..258 FT /evidence="ECO:0007829|PDB:1GUZ" FT STRAND 260..271 FT /evidence="ECO:0007829|PDB:1GUZ" FT STRAND 274..278 FT /evidence="ECO:0007829|PDB:1GUZ" FT HELIX 285..303 FT /evidence="ECO:0007829|PDB:1GUZ" SQ SEQUENCE 310 AA; 33273 MW; DFF3033B27FEC714 CRC64; MKITVIGAGN VGATTAFRIA DKKLARELVL LDVVEGIPQG KGLDMYETGP VGLFDTKITG SNDYADTADS DIVIITAGLP RKPGMTREDL LMKNAGIVKE VTDNIMKHSK NPIIIVVSNP LDIMTHVAWV RSGLPKERVI GMAGVLDAAR FRSFIAMELG VSMQDINACV LGGHGDAMVP VVKYTTVAGI PISDLLPAET IDKLVERTRN GGAEIVEHLK QGSAFYSPGS SVVEMVESIV LDRKRVLPCA VGLEGQYGID KTFVGVPVKL GRNGVEQIYE INLDQADLDL LQKSAKIVDE NCKMLESTIG //