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 13-NOV-2013, entry version 117. DE RecName: Full=Malate dehydrogenase; DE EC=1.1.1.37; GN Name=mdh; OrderedLocusNames=CT1507; OS Chlorobium tepidum (strain ATCC 49652 / DSM 12025 / TLS). OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; OC Chlorobaculum. OX NCBI_TaxID=194439; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8955383; RA Naterstad K., Lauvrak V., Sirevag R.; RT "Malate dehydrogenase from the mesophile Chlorobium vibrioforme and RT from the mild thermophile Chlorobium tepidum: molecular cloning, RT construction of 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 / TLS; RX PubMed=12093901; DOI=10.1073/pnas.132181499; RA Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M., RA Dodson R.J., DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H., RA Hickey E.K., Peterson J.D., Durkin A.S., Kolonay J.F., Yang F., RA Holt I.E., Umayam L.A., Mason T.M., Brenner M., Shea T.P., RA Parksey D.S., Nierman W.C., Feldblyum T.V., Hansen C.L., Craven M.B., RA Radune D., Vamathevan J.J., Khouri H.M., White O., Gruber T.M., RA Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A., Fraser C.M.; RT "The complete genome sequence of Chlorobium tepidum TLS, a RT photosynthetic, 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; RA Charnock C.B., Refseth U.H., Strevaag R.; RT "Malate dehydrogenase from Chlorobium vibrioforme, Chlorobium tepidum, RT and Heliobacterium gestii: purification, characterization, and RT investigation of dinucleotide binding by dehydrogenases by use of RT empirical methods of protein sequence analysis."; RL J. Bacteriol. 174:1307-1313(1992). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH NAD, AND RP SUBUNIT. RX PubMed=12054817; DOI=10.1016/S0022-2836(02)00050-5; RA Dalhus B., Saarinen M., Sauer U.H., Eklund P., Johansson K., RA Karlsson A., Ramaswamy S., Bjoerk A., Synstad B., Naterstad K., RA 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 CC oxaloacetate. CC -!- CATALYTIC ACTIVITY: (S)-malate + NAD(+) = oxaloacetate + NADH. CC -!- SUBUNIT: Homotetramer; arranged as a dimer of dimers. CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 3 family. 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 PDB; 1GUZ; X-ray; 2.00 A; A/B/C/D=1-305. DR PDB; 1GV0; X-ray; 2.50 A; A/B=1-310. DR PDBsum; 1GUZ; -. DR PDBsum; 1GV0; -. DR ProteinModelPortal; P80039; -. DR SMR; P80039; 1-305. DR STRING; 194439.CT1507; -. DR EnsemblBacteria; AAM72734; AAM72734; CT1507. DR GeneID; 1007223; -. DR KEGG; cte:CT1507; -. DR PATRIC; 21400925; VBIChlTep116050_1367. DR eggNOG; COG0039; -. DR HOGENOM; HOG000213794; -. DR KO; K00024; -. DR OMA; GANSYEA; -. DR OrthoDB; EOG6091FG; -. DR ProtClustDB; PRK06223; -. DR BioCyc; CTEP194439:GHN0-1546-MONOMER; -. DR EvolutionaryTrace; P80039; -. DR GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0044262; P:cellular carbohydrate metabolic process; IEA:InterPro. DR GO; GO:0006108; P:malate metabolic process; IEA:InterPro. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.720; -; 1. DR Gene3D; 3.90.110.10; -; 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; IPR016040; NAD(P)-bd_dom. DR PANTHER; PTHR11540; PTHR11540; 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; SSF56327; 1. DR TIGRFAMs; TIGR01763; MalateDH_bact; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Direct protein sequencing; NAD; KW Oxidoreductase; Reference proteome; Tricarboxylic acid cycle. FT CHAIN 1 310 Malate dehydrogenase. FT /FTId=PRO_0000113448. FT NP_BIND 7 12 NAD. FT NP_BIND 117 119 NAD. FT ACT_SITE 174 174 Proton acceptor (By similarity). FT BINDING 32 32 NAD. FT BINDING 81 81 Substrate (By similarity). FT BINDING 87 87 Substrate (By similarity). FT BINDING 94 94 NAD. FT BINDING 119 119 Substrate (By similarity). FT BINDING 150 150 Substrate (By similarity). FT CONFLICT 227 227 A -> S (in Ref. 1; CAA56810). FT STRAND 2 6 FT HELIX 10 21 FT STRAND 26 31 FT STRAND 33 36 FT HELIX 37 46 FT HELIX 49 52 FT STRAND 57 62 FT HELIX 64 67 FT STRAND 71 75 FT HELIX 92 105 FT TURN 106 108 FT STRAND 113 116 FT STRAND 118 120 FT HELIX 121 132 FT HELIX 136 138 FT STRAND 139 142 FT HELIX 144 159 FT HELIX 163 165 FT STRAND 166 172 FT HELIX 175 177 FT STRAND 178 187 FT HELIX 192 194 FT HELIX 198 209 FT HELIX 211 219 FT STRAND 220 222 FT HELIX 226 240 FT STRAND 245 255 FT HELIX 256 258 FT STRAND 260 271 FT STRAND 274 278 FT HELIX 285 304 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 //