ID MDH_CHLTE Reviewed; 310 AA. AC P80039; P94677; DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot. DT 30-AUG-2002, sequence version 3. DT 27-MAR-2024, entry version 172. 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=CT1507; OS Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS) OS (Chlorobium tepidum). OC Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae; OC Chlorobaculum. OX NCBI_TaxID=194439; 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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49652 / DSM 12025 / NBRC 103806 / TLS; RX PubMed=12093901; DOI=10.1073/pnas.132181499; RA Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M., Dodson R.J., RA DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H., Hickey E.K., Peterson J.D., RA Durkin A.S., Kolonay J.F., Yang F., Holt I.E., Umayam L.A., Mason T.M., RA Brenner M., Shea T.P., Parksey D.S., Nierman W.C., Feldblyum T.V., RA Hansen C.L., Craven M.B., Radune D., Vamathevan J.J., Khouri H.M., RA White O., Gruber T.M., Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A., RA Fraser C.M.; RT "The complete genome sequence of Chlorobium tepidum TLS, a photosynthetic, RT anaerobic, green-sulfur bacterium."; RL Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002). RN [3] RP PROTEIN SEQUENCE OF 1-34. RX PubMed=1735722; DOI=10.1128/jb.174.4.1307-1313.1992; RA Charnock C.B., Refseth U.H., Strevaag R.; RT "Malate dehydrogenase from Chlorobium vibrioforme, Chlorobium tepidum, and RT Heliobacterium gestii: purification, characterization, and investigation of RT dinucleotide binding by dehydrogenases by use of empirical methods of RT protein sequence analysis."; RL J. Bacteriol. 174:1307-1313(1992). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH NAD, 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; X80838; CAA56810.1; -; Genomic_DNA. DR EMBL; AE006470; AAM72734.1; -; Genomic_DNA. DR RefSeq; NP_662392.1; NC_002932.3. DR RefSeq; WP_010933173.1; NC_002932.3. DR PDB; 1GUZ; X-ray; 2.00 A; A/B/C/D=1-71. DR PDB; 1GV0; X-ray; 2.50 A; A/B=1-310. DR PDBsum; 1GUZ; -. DR PDBsum; 1GV0; -. DR AlphaFoldDB; P80039; -. DR SMR; P80039; -. DR STRING; 194439.CT1507; -. DR EnsemblBacteria; AAM72734; AAM72734; CT1507. DR KEGG; cte:CT1507; -. DR PATRIC; fig|194439.7.peg.1367; -. DR eggNOG; COG0039; Bacteria. DR HOGENOM; CLU_045401_2_1_10; -. DR OrthoDB; 9802969at2; -. DR EvolutionaryTrace; P80039; -. DR Proteomes; UP000001007; 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 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; NAD; Oxidoreductase; KW Reference proteome; Tricarboxylic acid cycle. FT CHAIN 1..310 FT /note="Malate dehydrogenase" FT /id="PRO_0000113448" 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 ECO:0000269|PubMed:12054817" FT BINDING 32 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487, FT ECO:0000269|PubMed:12054817" 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 ECO:0000269|PubMed:12054817" FT BINDING 117..119 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487, FT ECO:0000269|PubMed:12054817" 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 CONFLICT 227 FT /note="A -> S (in Ref. 1; CAA56810)" FT /evidence="ECO:0000305" FT STRAND 2..6 FT /evidence="ECO:0007829|PDB:1GV0" FT HELIX 10..22 FT /evidence="ECO:0007829|PDB:1GV0" FT STRAND 26..31 FT /evidence="ECO:0007829|PDB:1GUZ" FT STRAND 33..36 FT /evidence="ECO:0007829|PDB:1GUZ" FT HELIX 37..46 FT /evidence="ECO:0007829|PDB:1GUZ" FT HELIX 49..52 FT /evidence="ECO:0007829|PDB:1GUZ" FT STRAND 57..62 FT /evidence="ECO:0007829|PDB:1GUZ" FT HELIX 64..67 FT /evidence="ECO:0007829|PDB:1GUZ" FT STRAND 71..73 FT /evidence="ECO:0007829|PDB:1GUZ" FT HELIX 92..105 FT /evidence="ECO:0007829|PDB:1GV0" FT TURN 106..108 FT /evidence="ECO:0007829|PDB:1GV0" FT STRAND 113..116 FT /evidence="ECO:0007829|PDB:1GV0" FT STRAND 118..120 FT /evidence="ECO:0007829|PDB:1GV0" FT HELIX 121..132 FT /evidence="ECO:0007829|PDB:1GV0" FT HELIX 136..138 FT /evidence="ECO:0007829|PDB:1GV0" FT STRAND 139..142 FT /evidence="ECO:0007829|PDB:1GV0" FT HELIX 144..159 FT /evidence="ECO:0007829|PDB:1GV0" FT HELIX 163..165 FT /evidence="ECO:0007829|PDB:1GV0" FT STRAND 166..172 FT /evidence="ECO:0007829|PDB:1GV0" FT HELIX 175..177 FT /evidence="ECO:0007829|PDB:1GV0" FT STRAND 178..187 FT /evidence="ECO:0007829|PDB:1GV0" FT HELIX 192..194 FT /evidence="ECO:0007829|PDB:1GV0" FT HELIX 198..209 FT /evidence="ECO:0007829|PDB:1GV0" FT HELIX 211..219 FT /evidence="ECO:0007829|PDB:1GV0" FT STRAND 220..222 FT /evidence="ECO:0007829|PDB:1GV0" FT HELIX 226..240 FT /evidence="ECO:0007829|PDB:1GV0" FT STRAND 245..255 FT /evidence="ECO:0007829|PDB:1GV0" FT HELIX 256..258 FT /evidence="ECO:0007829|PDB:1GV0" FT STRAND 260..271 FT /evidence="ECO:0007829|PDB:1GV0" FT STRAND 274..278 FT /evidence="ECO:0007829|PDB:1GV0" FT HELIX 285..304 FT /evidence="ECO:0007829|PDB:1GV0" SQ SEQUENCE 310 AA; 33092 MW; 30A92ACFE9442A93 CRC64; MKITVIGAGN VGATTAFRLA EKQLARELVL LDVVEGIPQG KALDMYESGP VGLFDTKVTG SNDYADTANS DIVVITAGLP RKPGMTREDL LSMNAGIVRE VTGRIMEHSK NPIIVVVSNP LDIMTHVAWQ KSGLPKERVI GMAGVLDSAR FRSFIAMELG VSMQDVTACV LGGHGDAMVP VVKYTTVAGI PVADLISAER IAELVERTRT GGAEIVNHLK QGSAFYAPAT SVVEMVESIV LDRKRVLTCA VSLDGQYGID GTFVGVPVKL GKNGVEHIYE IKLDQSDLDL LQKSAKIVDE NCKMLDASQG //