MDH_HELHP
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 03-AUG-2022, entry version 114.
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; Proteobacteria; 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 EnsemblBacteria; AAP78168; AAP78168; HH_1571.
DR KEGG; hhe:HH_1571; -.
DR eggNOG; COG0039; Bacteria.
DR HOGENOM; CLU_045401_2_1_7; -.
DR OMA; ASCAEYI; -.
DR OrthoDB; 870724at2; -.
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; -; 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.
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