ID   MDH_HELHP               Reviewed;         315 AA.
AC   Q7VFV4;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   27-MAR-2024, entry version 121.
DE   RecName: Full=Malate dehydrogenase {ECO:0000250|UniProtKB:P61889};
DE            EC=1.1.1.37 {ECO:0000250|UniProtKB:P61889};
GN   Name=mdh {ECO:0000250|UniProtKB:P61889}; OrderedLocusNames=HH_1571;
OS   Helicobacter hepaticus (strain ATCC 51449 / 3B1).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=235279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51449 / 3B1;
RX   PubMed=12810954; DOI=10.1073/pnas.1332093100;
RA   Suerbaum S., Josenhans C., Sterzenbach T., Drescher B., Brandt P., Bell M.,
RA   Droege M., Fartmann B., Fischer H.-P., Ge Z., Hoerster A., Holland R.,
RA   Klein K., Koenig J., Macko L., Mendz G.L., Nyakatura G., Schauer D.B.,
RA   Shen Z., Weber J., Frosch M., Fox J.G.;
RT   "The complete genome sequence of the carcinogenic bacterium Helicobacter
RT   hepaticus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7901-7906(2003).
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; AE017125; AAP78168.1; -; Genomic_DNA.
DR   RefSeq; WP_011116411.1; NC_004917.1.
DR   AlphaFoldDB; Q7VFV4; -.
DR   SMR; Q7VFV4; -.
DR   STRING; 235279.HH_1571; -.
DR   GeneID; 82136094; -.
DR   KEGG; hhe:HH_1571; -.
DR   eggNOG; COG0039; Bacteria.
DR   HOGENOM; CLU_045401_2_1_7; -.
DR   OrthoDB; 9802969at2; -.
DR   Proteomes; UP000002495; 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   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   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   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   3: Inferred from homology;
KW   NAD; Oxidoreductase; Reference proteome; Tricarboxylic acid cycle.
FT   CHAIN           1..315
FT                   /note="Malate dehydrogenase"
FT                   /id="PRO_0000113456"
FT   ACT_SITE        177
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P61889"
FT   BINDING         9..15
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P61889"
FT   BINDING         84
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P61889"
FT   BINDING         90
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P61889"
FT   BINDING         97
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P61889"
FT   BINDING         120..122
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P61889"
FT   BINDING         122
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P61889"
FT   BINDING         153
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P61889"
SQ   SEQUENCE   315 AA;  34703 MW;  F652AE4ECD1D80BD CRC64;
     MFEKIAIIGG SGNVGSHIAF LGAMRHIAKE ILLFSNDIPR CKGVGLDISQ AAAIFDIPIL
     IKGCNSYEEI AESEVVIITA GFPRTPNMTR NDLLLKNASI IQEISSNVAR IAPQSLLIVV
     SNPLDAMCLV AKQWSKFEKE RVIGMAGILD SARLTYESKV MLGDFNKHIQ SYVIGSHSDD
     MLPLLRHCLC EGKVFTDIFT PKMQEELIKE TKGGGAKIVN YYQKGSAYFA PASGVIKILE
     AISTLNEEIL VCSVFTEGEY GIKDIYLGLP IKLGKKGVEH IVELPLNQQE QEMLNISTQG
     IKEQVEILKD NKLLY
//