ID MDH_BACAN Reviewed; 312 AA. AC Q6HSF4; Q6KLP9; Q81KZ7; DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2004, sequence version 1. DT 27-MAR-2024, entry version 142. 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=BA_4837, GBAA_4837, BAS4486; OS Bacillus anthracis. OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=1392; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ames / isolate Porton; RX PubMed=12721629; DOI=10.1038/nature01586; RA Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., RA Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., RA Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., RA Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L., RA DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C., RA Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y., RA Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M., RA Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E., RA White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M., RA Hanna P.C., Kolstoe A.-B., Fraser C.M.; RT "The genome sequence of Bacillus anthracis Ames and comparison to closely RT related bacteria."; RL Nature 423:81-86(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ames ancestor; RX PubMed=18952800; DOI=10.1128/jb.01347-08; RA Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D., RA Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.; RT "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'."; RL J. Bacteriol. 191:445-446(2009). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Sterne; RA Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., RA Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., RA Richardson P., Rubin E., Tice H.; RT "Complete genome sequence of Bacillus anthracis Sterne."; RL Submitted (JAN-2004) 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; AE016879; AAP28526.1; -; Genomic_DNA. DR EMBL; AE017334; AAT33956.1; -; Genomic_DNA. DR EMBL; AE017225; AAT56784.1; -; Genomic_DNA. DR RefSeq; NP_847040.1; NC_003997.3. DR RefSeq; WP_000153232.1; NZ_WXXJ01000026.1. DR RefSeq; YP_030734.1; NC_005945.1. DR PDB; 3TL2; X-ray; 1.70 A; A=1-312. DR PDBsum; 3TL2; -. DR AlphaFoldDB; Q6HSF4; -. DR SMR; Q6HSF4; -. DR STRING; 261594.GBAA_4837; -. DR DNASU; 1083988; -. DR GeneID; 75087749; -. DR KEGG; ban:BA_4837; -. DR KEGG; bar:GBAA_4837; -. DR KEGG; bat:BAS4486; -. DR PATRIC; fig|198094.11.peg.4798; -. DR eggNOG; COG0039; Bacteria. DR HOGENOM; CLU_045401_2_1_9; -. DR OMA; ASCAEYI; -. DR OrthoDB; 9802969at2; -. DR Proteomes; UP000000427; Chromosome. DR Proteomes; UP000000594; 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; Phosphoprotein; Reference proteome; KW Tricarboxylic acid cycle. FT CHAIN 1..312 FT /note="Malate dehydrogenase" FT /id="PRO_0000113424" FT ACT_SITE 180 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487" FT BINDING 12..17 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487" FT BINDING 36 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487" FT BINDING 87 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487" FT BINDING 93 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487" FT BINDING 100 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487" FT BINDING 123..125 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487" FT BINDING 125 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487" FT BINDING 156 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487" FT MOD_RES 149 FT /note="Phosphoserine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487" FT STRAND 7..11 FT /evidence="ECO:0007829|PDB:3TL2" FT HELIX 15..26 FT /evidence="ECO:0007829|PDB:3TL2" FT STRAND 31..35 FT /evidence="ECO:0007829|PDB:3TL2" FT HELIX 38..40 FT /evidence="ECO:0007829|PDB:3TL2" FT HELIX 41..58 FT /evidence="ECO:0007829|PDB:3TL2" FT STRAND 64..68 FT /evidence="ECO:0007829|PDB:3TL2" FT HELIX 70..73 FT /evidence="ECO:0007829|PDB:3TL2" FT STRAND 77..81 FT /evidence="ECO:0007829|PDB:3TL2" FT HELIX 93..114 FT /evidence="ECO:0007829|PDB:3TL2" FT STRAND 119..122 FT /evidence="ECO:0007829|PDB:3TL2" FT HELIX 127..138 FT /evidence="ECO:0007829|PDB:3TL2" FT HELIX 142..144 FT /evidence="ECO:0007829|PDB:3TL2" FT STRAND 145..147 FT /evidence="ECO:0007829|PDB:3TL2" FT HELIX 150..165 FT /evidence="ECO:0007829|PDB:3TL2" FT HELIX 169..171 FT /evidence="ECO:0007829|PDB:3TL2" FT STRAND 176..178 FT /evidence="ECO:0007829|PDB:3TL2" FT HELIX 181..183 FT /evidence="ECO:0007829|PDB:3TL2" FT HELIX 188..190 FT /evidence="ECO:0007829|PDB:3TL2" FT HELIX 198..200 FT /evidence="ECO:0007829|PDB:3TL2" FT HELIX 204..215 FT /evidence="ECO:0007829|PDB:3TL2" FT HELIX 217..225 FT /evidence="ECO:0007829|PDB:3TL2" FT STRAND 226..228 FT /evidence="ECO:0007829|PDB:3TL2" FT HELIX 232..246 FT /evidence="ECO:0007829|PDB:3TL2" FT STRAND 251..261 FT /evidence="ECO:0007829|PDB:3TL2" FT HELIX 262..264 FT /evidence="ECO:0007829|PDB:3TL2" FT STRAND 266..277 FT /evidence="ECO:0007829|PDB:3TL2" FT STRAND 280..284 FT /evidence="ECO:0007829|PDB:3TL2" FT HELIX 291..308 FT /evidence="ECO:0007829|PDB:3TL2" SQ SEQUENCE 312 AA; 33498 MW; 615A61C61CA217FD CRC64; MTIKRKKVSV IGAGFTGATT AFLLAQKELA DVVLVDIPQL ENPTKGKALD MLEASPVQGF DANIIGTSDY ADTADSDVVV ITAGIARKPG MSRDDLVATN SKIMKSITRD IAKHSPNAII VVLTNPVDAM TYSVFKEAGF PKERVIGQSG VLDTARFRTF IAQELNLSVK DITGFVLGGH GDDMVPLVRY SYAGGIPLET LIPKERLEAI VERTRKGGGE IVGLLGNGSA YYAPAASLVE MTEAILKDQR RVLPAIAYLE GEYGYSDLYL GVPVILGGNG IEKIIELELL ADEKEALDRS VESVRNVMKV LV //