ID   MDH_STACT               Reviewed;         311 AA.
AC   B9DK67;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 79.
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=Sca_0338;
OS   Staphylococcus carnosus (strain TM300).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=396513;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TM300;
RX   PubMed=19060169; DOI=10.1128/aem.01982-08;
RA   Rosenstein R., Nerz C., Biswas L., Resch A., Raddatz G., Schuster S.C.,
RA   Goetz F.;
RT   "Genome analysis of the meat starter culture bacterium Staphylococcus
RT   carnosus TM300.";
RL   Appl. Environ. Microbiol. 75:811-822(2009).
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}.
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DR   EMBL; AM295250; CAL27251.1; -; Genomic_DNA.
DR   RefSeq; WP_015899596.1; NC_012121.1.
DR   AlphaFoldDB; B9DK67; -.
DR   SMR; B9DK67; -.
DR   STRING; 396513.SCA_0338; -.
DR   GeneID; 60545966; -.
DR   KEGG; sca:SCA_0338; -.
DR   eggNOG; COG0039; Bacteria.
DR   HOGENOM; CLU_045401_2_1_9; -.
DR   OMA; CYIIVLT; -.
DR   OrthoDB; 870724at2; -.
DR   BioCyc; SCAR396513:SCA_RS01725-MON; -.
DR   Proteomes; UP000000444; 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; -; 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   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; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF56327; SSF56327; 1.
DR   TIGRFAMs; TIGR01763; MalateDH_bact; 1.
PE   3: Inferred from homology;
KW   NAD; Oxidoreductase; Tricarboxylic acid cycle.
FT   CHAIN           1..311
FT                   /note="Malate dehydrogenase"
FT                   /id="PRO_1000191658"
FT   ACT_SITE        178
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT   BINDING         10..15
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT   BINDING         85
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT   BINDING         91
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT   BINDING         98
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT   BINDING         121..123
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT   BINDING         123
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT   BINDING         154
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
SQ   SEQUENCE   311 AA;  32969 MW;  68A032C142AC6569 CRC64;
     MAKNKIAIIG AGHTGSTLAF IIAERALADV VLLEIPKNEK PARGKALDIK ESGPILGFNG
     NVLGTSDYQD IAGADIVVIT AGAARKPGMS RDDLIQINEN VMAQVTEGIK KYAPESKIIV
     LTNPVDAMTY AVYKLSGFPK ERVLGQSGIL DTARYRTFVS EALNVAQTDV TGLVLGGHGD
     TMVPLLSTTM VGGVPLRELL AQDKIDAIVE RTRKGGAEIV GLLGNGSAYY APAAAIYEMA
     AAILNDERRL VPAITYLDGE YGFKDICLGV PTILGANGVE KVVEIELSDD EQQLRDSADA
     VEDVKSALKN K