ID   MDH_CORJK               Reviewed;         330 AA.
AC   Q4JWV0;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Malate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01517};
DE            EC=1.1.1.37 {ECO:0000255|HAMAP-Rule:MF_01517};
GN   Name=mdh {ECO:0000255|HAMAP-Rule:MF_01517}; OrderedLocusNames=jk0548;
OS   Corynebacterium jeikeium (strain K411).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=306537;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K411;
RX   PubMed=15968079; DOI=10.1128/jb.187.13.4671-4682.2005;
RA   Tauch A., Kaiser O., Hain T., Goesmann A., Weisshaar B., Albersmeier A.,
RA   Bekel T., Bischoff N., Brune I., Chakraborty T., Kalinowski J., Meyer F.,
RA   Rupp O., Schneiker S., Viehoever P., Puehler A.;
RT   "Complete genome sequence and analysis of the multiresistant nosocomial
RT   pathogen Corynebacterium jeikeium K411, a lipid-requiring bacterium of the
RT   human skin flora.";
RL   J. Bacteriol. 187:4671-4682(2005).
CC   -!- FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate.
CC       {ECO:0000255|HAMAP-Rule:MF_01517}.
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_01517};
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01517}.
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DR   EMBL; CR931997; CAI36707.1; -; Genomic_DNA.
DR   RefSeq; WP_011273212.1; NC_007164.1.
DR   AlphaFoldDB; Q4JWV0; -.
DR   SMR; Q4JWV0; -.
DR   STRING; 306537.jk0548; -.
DR   EnsemblBacteria; CAI36707; CAI36707; jk0548.
DR   GeneID; 56650087; -.
DR   KEGG; cjk:jk0548; -.
DR   PATRIC; fig|306537.10.peg.560; -.
DR   eggNOG; COG0039; Bacteria.
DR   HOGENOM; CLU_040727_2_0_11; -.
DR   OMA; TKGMERG; -.
DR   OrthoDB; 870724at2; -.
DR   Proteomes; UP000000545; Chromosome.
DR   GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006108; P:malate metabolic process; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.90.110.10; -; 1.
DR   HAMAP; MF_01517; Malate_dehydrog_2; 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; IPR010945; Malate_DH_type2.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR23382; PTHR23382; 1.
DR   Pfam; PF02866; Ldh_1_C; 1.
DR   Pfam; PF00056; Ldh_1_N; 1.
DR   PIRSF; PIRSF000102; Lac_mal_DH; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF56327; SSF56327; 1.
DR   TIGRFAMs; TIGR01759; MalateDH-SF1; 1.
PE   3: Inferred from homology;
KW   NAD; Oxidoreductase; Reference proteome; Tricarboxylic acid cycle.
FT   CHAIN           1..330
FT                   /note="Malate dehydrogenase"
FT                   /id="PRO_0000113365"
FT   ACT_SITE        190
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
FT   BINDING         15..21
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
FT   BINDING         95
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
FT   BINDING         101
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
FT   BINDING         108
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
FT   BINDING         115
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
FT   BINDING         132..134
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
FT   BINDING         134
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
FT   BINDING         165
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
SQ   SEQUENCE   330 AA;  35064 MW;  F4DFB482B252F646 CRC64;
     MTTNNQNAVT VTVTGAGGQI GYSLLFRIAK GEVFGDRVVN LRLLETEQGV QAARGVALEL
     ADCAFPLLGE VSITTELSEG FKDANAVFLV GAKPRQKGEE RADLLAANGK IFGPQGKAIA
     EYAADDVRVI VVGNPANTNA AIVAAHAEGL DPRRVTALTR LDHNRGLAQV ADKLGVAVRD
     LKNMTVWGNH SASQFPDVAE LTLNGEKVAD KLDAAWVNDE FIPRVAKRGA EIIEVRGRSS
     AASAASAALD HMRDWVNGTA EGDWVSVALP SDGSYGIPEG LVFSFPCRSV DGEWEIVQGL
     EISPAQQERI DANIKELQEE KAAVEEAGLL