ID MDH_SALRD Reviewed; 314 AA. AC Q2S289; DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 24-JAN-2006, sequence version 1. DT 27-MAR-2024, entry version 114. 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=SRU_1571; OS Salinibacter ruber (strain DSM 13855 / M31). OC Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Salinibacteraceae; OC Salinibacter. OX NCBI_TaxID=309807; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 13855 / CECT 5946 / M31; RX PubMed=16330755; DOI=10.1073/pnas.0509073102; RA Mongodin E.F., Nelson K.E., Daugherty S., DeBoy R.T., Wister J., Khouri H., RA Weidman J., Walsh D.A., Papke R.T., Sanchez Perez G., Sharma A.K., RA Nesbo C.L., MacLeod D., Bapteste E., Doolittle W.F., Charlebois R.L., RA Legault B., Rodriguez-Valera F.; RT "The genome of Salinibacter ruber: convergence and gene exchange among RT hyperhalophilic bacteria and archaea."; RL Proc. Natl. Acad. Sci. U.S.A. 102:18147-18152(2005). 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; CP000159; ABC45135.1; -; Genomic_DNA. DR RefSeq; WP_011404318.1; NC_007677.1. DR RefSeq; YP_445692.1; NC_007677.1. DR PDB; 3NEP; X-ray; 1.55 A; X=1-314. DR PDBsum; 3NEP; -. DR AlphaFoldDB; Q2S289; -. DR SMR; Q2S289; -. DR STRING; 309807.SRU_1571; -. DR EnsemblBacteria; ABC45135; ABC45135; SRU_1571. DR GeneID; 83728483; -. DR KEGG; sru:SRU_1571; -. DR PATRIC; fig|309807.25.peg.1625; -. DR eggNOG; COG0039; Bacteria. DR HOGENOM; CLU_045401_2_1_10; -. DR OrthoDB; 9802969at2; -. DR Proteomes; UP000008674; 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; NAD; Oxidoreductase; Reference proteome; KW Tricarboxylic acid cycle. FT CHAIN 1..314 FT /note="Malate dehydrogenase" FT /id="PRO_0000241967" 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:3NEP" FT HELIX 10..22 FT /evidence="ECO:0007829|PDB:3NEP" FT STRAND 25..31 FT /evidence="ECO:0007829|PDB:3NEP" FT HELIX 37..52 FT /evidence="ECO:0007829|PDB:3NEP" FT STRAND 57..64 FT /evidence="ECO:0007829|PDB:3NEP" FT HELIX 65..67 FT /evidence="ECO:0007829|PDB:3NEP" FT STRAND 71..75 FT /evidence="ECO:0007829|PDB:3NEP" FT HELIX 88..106 FT /evidence="ECO:0007829|PDB:3NEP" FT STRAND 113..116 FT /evidence="ECO:0007829|PDB:3NEP" FT HELIX 121..132 FT /evidence="ECO:0007829|PDB:3NEP" FT HELIX 136..138 FT /evidence="ECO:0007829|PDB:3NEP" FT STRAND 139..141 FT /evidence="ECO:0007829|PDB:3NEP" FT HELIX 144..159 FT /evidence="ECO:0007829|PDB:3NEP" FT HELIX 163..165 FT /evidence="ECO:0007829|PDB:3NEP" FT STRAND 166..174 FT /evidence="ECO:0007829|PDB:3NEP" FT HELIX 175..177 FT /evidence="ECO:0007829|PDB:3NEP" FT STRAND 178..187 FT /evidence="ECO:0007829|PDB:3NEP" FT HELIX 192..194 FT /evidence="ECO:0007829|PDB:3NEP" FT HELIX 198..209 FT /evidence="ECO:0007829|PDB:3NEP" FT HELIX 211..219 FT /evidence="ECO:0007829|PDB:3NEP" FT HELIX 225..240 FT /evidence="ECO:0007829|PDB:3NEP" FT STRAND 244..254 FT /evidence="ECO:0007829|PDB:3NEP" FT HELIX 255..257 FT /evidence="ECO:0007829|PDB:3NEP" FT STRAND 259..270 FT /evidence="ECO:0007829|PDB:3NEP" FT STRAND 273..277 FT /evidence="ECO:0007829|PDB:3NEP" FT HELIX 284..309 FT /evidence="ECO:0007829|PDB:3NEP" SQ SEQUENCE 314 AA; 33256 MW; FD2F7BDA3F8249E8 CRC64; MKVTVIGAGN VGATVAECVA RQDVAKEVVM VDIKDGMPQG KALDMRESSP IHGFDTRVTG TNDYGPTEDS DVCIITAGLP RSPGMSRDDL LAKNTEIVGG VTEQFVEGSP DSTIIVVANP LDVMTYVAYE ASGFPTNRVM GMAGVLDTGR FRSFIAEELD VSVRDVQALL MGGHGDTMVP LPRYTTVGGI PVPQLIDDAR IEEIVERTKG AGGEIVDLMG TSAWYAPGAA AAEMTEAILK DNKRILPCAA YCDGEYGLDD LFIGVPVKLG AGGVEEVIEV DLDADEKAQL KTSAGHVHSN LDDLQRLRDE GKIG //