ID   MDH_BACP2               Reviewed;         312 AA.
AC   A8FG47;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   02-SEP-2026, entry version 97.
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=BPUM_2554;
OS   Bacillus pumilus (strain SAFR-032).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae;
OC   Bacillus.
OX   NCBI_TaxID=315750;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SAFR-032;
RX   PubMed=17895969; DOI=10.1371/journal.pone.0000928;
RA   Gioia J., Yerrapragada S., Qin X., Jiang H., Igboeli O.C., Muzny D.,
RA   Dugan-Rocha S., Ding Y., Hawes A., Liu W., Perez L., Kovar C., Dinh H.,
RA   Lee S., Nazareth L., Blyth P., Holder M., Buhay C., Tirumalai M.R., Liu Y.,
RA   Dasgupta I., Bokhetache L., Fujita M., Karouia F., Eswara Moorthy P.,
RA   Siefert J., Uzman A., Buzumbo P., Verma A., Zwiya H., McWilliams B.D.,
RA   Olowu A., Clinkenbeard K.D., Newcombe D., Golebiewski L., Petrosino J.F.,
RA   Nicholson W.L., Fox G.E., Venkateswaran K., Highlander S.K.,
RA   Weinstock G.M.;
RT   "Paradoxical DNA repair and peroxide resistance gene conservation in
RT   Bacillus pumilus SAFR-032.";
RL   PLoS ONE 2:E928-E928(2007).
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(+) = oxaloacetate + NADH + H(+);
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}.
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DR   EMBL; CP000813; ABV63214.1; -; Genomic_DNA.
DR   RefSeq; WP_007501693.1; NC_009848.4.
DR   AlphaFoldDB; A8FG47; -.
DR   SMR; A8FG47; -.
DR   STRING; 315750.BPUM_2554; -.
DR   PaxDb; 315750-BPUM_2554; -.
DR   GeneID; 5621819; -.
DR   GeneID; 66364122; -.
DR   KEGG; bpu:BPUM_2554; -.
DR   eggNOG; COG0039; Bacteria.
DR   HOGENOM; CLU_045401_2_1_9; -.
DR   OrthoDB; 9802969at2; -.
DR   Proteomes; UP000001355; Chromosome.
DR   GO; GO:0004459; F:L-lactate dehydrogenase (NAD+) activity; IEA:TreeGrafter.
DR   GO; GO:0030060; F:L-malate dehydrogenase (NAD+) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006089; P:lactate metabolic process; IEA:TreeGrafter.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule.
DR   CDD; cd01339; LDH-like_MDH; 1.
DR   FunFam; 3.40.50.720:FF:000018; Malate dehydrogenase; 1.
DR   FunFam; 3.90.110.10:FF:000004; Malate dehydrogenase; 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   NCBIfam; NF004863; PRK06223.1; 1.
DR   PANTHER; PTHR43128; L-2-HYDROXYCARBOXYLATE DEHYDROGENASE (NAD(P)(+)); 1.
DR   PANTHER; PTHR43128:SF16; 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   3: Inferred from homology;
KW   NAD; Oxidoreductase; Phosphoprotein; Reference proteome;
KW   Tricarboxylic acid cycle.
FT   CHAIN           1..312
FT                   /note="Malate dehydrogenase"
FT                   /id="PRO_1000060437"
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"
SQ   SEQUENCE   312 AA;  33663 MW;  BCCA82AFF3DA474A CRC64;
     MANKRKKVSV IGAGFTGATT AFLTAQKELA DVVLVDIPQL ENPTKGKALD MLEASPVQGF
     DANITGTSNY EDTAGSDVVV ITAGIARKPG MSRDDLVSTN EKIMRSVTRE IVKYSPEAII
     VVLTNPVDAM TYAVYKESGL PKEKVIGQSG ILDTARFRTF VAQELNLSVK DVTGFVLGGH
     GDDMVPLVRY SYAGGIPLET LIPKERIDAI VERTRKGGGE IVNLLGNGSA YYAPAASLVE
     MVEAILKDQR RVMPTIAYLE GEYGYEGIYL GVPTIVGGNG LEQIIELELT EEERSQLDRS
     VESVKNVMKV LS
//