ID   MDH_CAMJE               Reviewed;         300 AA.
AC   Q9PHY2; Q0PAY4;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Probable malate dehydrogenase {ECO:0000305};
DE            EC=1.1.1.37 {ECO:0000250|UniProtKB:P61889};
GN   Name=mdh; OrderedLocusNames=Cj0532;
OS   Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS   11168).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=192222;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700819 / NCTC 11168;
RX   PubMed=10688204; DOI=10.1038/35001088;
RA   Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA   Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA   Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA   Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA   Barrell B.G.;
RT   "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT   reveals hypervariable sequences.";
RL   Nature 403:665-668(2000).
CC   -!- FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate.
CC       {ECO:0000250|UniProtKB:P61889}.
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:0000250|UniProtKB:P61889};
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. {ECO:0000305}.
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DR   EMBL; AL111168; CAL34678.1; -; Genomic_DNA.
DR   PIR; D81399; D81399.
DR   RefSeq; WP_002858544.1; NC_002163.1.
DR   RefSeq; YP_002343963.1; NC_002163.1.
DR   AlphaFoldDB; Q9PHY2; -.
DR   SMR; Q9PHY2; -.
DR   IntAct; Q9PHY2; 1.
DR   STRING; 192222.Cj0532; -.
DR   PaxDb; Q9PHY2; -.
DR   PRIDE; Q9PHY2; -.
DR   EnsemblBacteria; CAL34678; CAL34678; Cj0532.
DR   GeneID; 904860; -.
DR   KEGG; cje:Cj0532; -.
DR   PATRIC; fig|192222.6.peg.524; -.
DR   eggNOG; COG0039; Bacteria.
DR   HOGENOM; CLU_045401_2_1_7; -.
DR   OMA; ASCAEYI; -.
DR   Proteomes; UP000000799; Chromosome.
DR   GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.110.10; -; 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; 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.
PE   3: Inferred from homology;
KW   NAD; Oxidoreductase; Reference proteome; Tricarboxylic acid cycle.
FT   CHAIN           1..300
FT                   /note="Probable malate dehydrogenase"
FT                   /id="PRO_0000113445"
FT   ACT_SITE        174
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P61889"
FT   BINDING         6..12
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P61889"
FT   BINDING         81
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P61889"
FT   BINDING         87
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P61889"
FT   BINDING         94
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P61889"
FT   BINDING         117..119
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P61889"
FT   BINDING         119
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P61889"
FT   BINDING         150
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P61889"
SQ   SEQUENCE   300 AA;  33513 MW;  45DABA8AAA648A9A CRC64;
     MKITVIGAGN VGSSVAYALI LREIANEIVL VDINEDLLYA KELELTQSIA ALNLNIDLLC
     TKDYTHTKNS DIVLFSAGFA RKDGQSREEL LQLNTSIMLD CAKKIKDFTE DPLFIILTNP
     VDFLLNTLYE SGIFSSKKII AMAGVLDNAR FKYELAKKLN VKMSRVDTRL IGFHNDDMVL
     VKSYASVKNK NISEFLNEEE FEDLENEVKT GGAKVIKHLK TSAYLAPASA CIRMLESIRS
     GEFLPMSVIL HGEFGVQNKA LGVMARLGLE GVIEIMKMDL SLQEKDKLEK SLIKYQYKGE