ID   MQO_HELPY               Reviewed;         450 AA.
AC   O24913;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   16-JUN-2009, entry version 57.
DE   RecName: Full=Malate:quinone oxidoreductase;
DE            EC=1.1.99.16;
DE   AltName: Full=Malate dehydrogenase [acceptor];
DE   AltName: Full=MQO;
GN   Name=mqo; OrderedLocusNames=HP_0086;
OS   Helicobacter pylori (Campylobacter pylori).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=210;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700392 / 26695;
RX   MEDLINE=97394467; PubMed=9252185; DOI=10.1038/41483;
RA   Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA   Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R.,
RA   Dougherty B.A., Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F.,
RA   Peterson S.N., Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G.,
RA   Glodek A., McKenney K., FitzGerald L.M., Lee N., Adams M.D.,
RA   Hickey E.K., Berg D.E., Gocayne J.D., Utterback T.R., Peterson J.D.,
RA   Kelley J.M., Cotton M.D., Weidman J.F., Fujii C., Bowman C.,
RA   Watthey L., Wallin E., Hayes W.S., Borodovsky M., Karp P.D.,
RA   Smith H.O., Fraser C.M., Venter J.C.;
RT   "The complete genome sequence of the gastric pathogen Helicobacter
RT   pylori.";
RL   Nature 388:539-547(1997).
RN   [2]
RP   CHARACTERIZATION.
RC   STRAIN=ATCC 49503 / 60190;
RX   MEDLINE=20270151; PubMed=10809701;
RX   DOI=10.1128/JB.182.11.3204-3209.2000;
RA   Kather B., Stingl K., van der Rest M.E., Altendorf K., Molenaar D.;
RT   "Another unusual type of citric acid cycle enzyme in Helicobacter
RT   pylori: the malate:quinone oxidoreductase.";
RL   J. Bacteriol. 182:3204-3209(2000).
CC   -!- FUNCTION: Catalyzes oxidation of malate to oxaloacetate in the
CC       citric acid cycle. Donates electrons to quinones of the electron
CC       transfer chain.
CC   -!- CATALYTIC ACTIVITY: (S)-malate + acceptor = oxaloacetate + reduced
CC       acceptor.
CC   -!- COFACTOR: FAD. The FAD is tightly bound.
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
CC   -!- SIMILARITY: Belongs to the MQO family.
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DR   EMBL; AE000511; AAD07155.1; -; Genomic_DNA.
DR   PIR; F64530; F64530.
DR   RefSeq; NP_206886.1; -.
DR   GeneID; 899112; -.
DR   GenomeReviews; AE000511_GR; HP_0086.
DR   KEGG; hpy:HP0086; -.
DR   NMPDR; fig|85962.1.peg.84; -.
DR   TIGR; HP_0086; -.
DR   HOGENOM; O24913; -.
DR   OMA; O24913; FELERFY.
DR   BioCyc; MetaCyc:HP0086-MON; -.
DR   BRENDA; 1.1.99.16; 1131.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008924; F:malate dehydrogenase (acceptor) activity; IEA:HAMAP.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:HAMAP.
DR   HAMAP; MF_00212; -; 1.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   Pfam; PF01266; DAO; 2.
PE   1: Evidence at protein level;
KW   Cell membrane; Complete proteome; FAD; Flavoprotein; Membrane;
KW   Oxidoreductase; Tricarboxylic acid cycle.
FT   CHAIN         1    450       Malate:quinone oxidoreductase.
FT                                /FTId=PRO_0000128717.
SQ   SEQUENCE   450 AA;  50713 MW;  5435E75D22E6E40B 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 LKMDLNKDVF KIAFDLMSDK EIRNYVFKNM VFELPIIGKR KFLKDAQKII
     PSLSLEDLEY AHGFGEVRPQ VLDRTKRKLE LGEKKICTHK GITFNMTPSP GATSCLQNAL
     VDSQEIAAYL GESFELERFY KDLSPEELEN
//