ID   MQO_HELPJ               Reviewed;         450 AA.
AC   Q9ZMY5;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 118.
DE   RecName: Full=Malate:quinone oxidoreductase;
DE            EC=1.1.5.4;
DE   AltName: Full=MQO;
DE   AltName: Full=Malate dehydrogenase [quinone];
GN   Name=mqo; OrderedLocusNames=jhp_0079;
OS   Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J99 / ATCC 700824;
RX   PubMed=9923682; DOI=10.1038/16495;
RA   Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA   Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA   Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA   Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT   "Genomic sequence comparison of two unrelated isolates of the human gastric
RT   pathogen Helicobacter pylori.";
RL   Nature 397:176-180(1999).
CC   -!- FUNCTION: Catalyzes oxidation of malate to oxaloacetate in the citric
CC       acid cycle. Donates electrons to quinones of the electron transfer
CC       chain (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-malate + a quinone = a quinol + oxaloacetate;
CC         Xref=Rhea:RHEA:46012, ChEBI:CHEBI:15589, ChEBI:CHEBI:16452,
CC         ChEBI:CHEBI:24646, ChEBI:CHEBI:132124; EC=1.1.5.4;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC       Note=The FAD is tightly bound. {ECO:0000250};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle;
CC       oxaloacetate from (S)-malate (quinone route): step 1/1.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the MQO family. {ECO:0000305}.
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DR   EMBL; AE001439; AAD05663.1; -; Genomic_DNA.
DR   PIR; B71976; B71976.
DR   RefSeq; WP_000061443.1; NC_000921.1.
DR   AlphaFoldDB; Q9ZMY5; -.
DR   STRING; 85963.jhp_0079; -.
DR   EnsemblBacteria; AAD05663; AAD05663; jhp_0079.
DR   KEGG; hpj:jhp_0079; -.
DR   eggNOG; COG0579; Bacteria.
DR   OMA; DMGEAKI; -.
DR   UniPathway; UPA00223; UER01008.
DR   Proteomes; UP000000804; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0052589; F:malate dehydrogenase (menaquinone) activity; IEA:UniProtKB-EC.
DR   GO; GO:0008924; F:malate dehydrogenase (quinone) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.50.50.60; -; 1.
DR   HAMAP; MF_00212; MQO; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR006231; MQO.
DR   Pfam; PF06039; Mqo; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   3: Inferred from homology;
KW   Cell membrane; FAD; Flavoprotein; Membrane; Oxidoreductase;
KW   Tricarboxylic acid cycle.
FT   CHAIN           1..450
FT                   /note="Malate:quinone oxidoreductase"
FT                   /id="PRO_0000128718"
SQ   SEQUENCE   450 AA;  50755 MW;  7E42E03268E99E1C CRC64;
     MSMEFDAVII GGGVSGCATF YTLSEYSSLK RVAIVEKCSK LAQISSSAKA NSQTIHDGSI
     ETNYTPEKAK KVRLSAYKTR QYALNKGLQN EVIFETQKMA IGVGDEECEF MKKRYESFKE
     IFVGLEEFDK QKIKELEPNV ILGANGIDRH ENIIGHGYRK DWSTMNFAKL SENFVEEALK
     LKPNNQVFLN FKVKKIEKRN DTYAVISEDA EEVYAKFVLV NAGSYALPLA QSMGYGLDLG
     CLPVAGSFYF VPDLLRGKVY TVQNPKLPFA AVHGDPDAVI KGKTRIGPTA LTMPKLERNK
     CWLKGISLEL LKMDLNRDVF KIAFDLMSDK EIRNYVFKNM VFELPIIGKR KFLKDAQKII
     PTLSLEDLEY AHGFGEVRPQ VLDRTKRKLE LGEKKICTHK GITFNMTPSP GATSCLQNAL
     VDSQEIAAYL GESFELERFY KDLSPEELEN