ID   MQO_XYLFM               Reviewed;         562 AA.
AC   B0U4L2;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Probable malate:quinone oxidoreductase {ECO:0000255|HAMAP-Rule:MF_00212};
DE            EC=1.1.5.4 {ECO:0000255|HAMAP-Rule:MF_00212};
DE   AltName: Full=MQO {ECO:0000255|HAMAP-Rule:MF_00212};
DE   AltName: Full=Malate dehydrogenase [quinone] {ECO:0000255|HAMAP-Rule:MF_00212};
GN   Name=mqo {ECO:0000255|HAMAP-Rule:MF_00212}; OrderedLocusNames=Xfasm12_1915;
OS   Xylella fastidiosa (strain M12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xylella.
OX   NCBI_TaxID=405440;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M12;
RX   PubMed=20601474; DOI=10.1128/jb.00651-10;
RA   Chen J., Xie G., Han S., Chertkov O., Sims D., Civerolo E.L.;
RT   "Whole genome sequences of two Xylella fastidiosa strains (M12 and M23)
RT   causing almond leaf scorch disease in California.";
RL   J. Bacteriol. 192:4534-4534(2010).
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         Evidence={ECO:0000255|HAMAP-Rule:MF_00212};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00212};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle;
CC       oxaloacetate from (S)-malate (quinone route): step 1/1.
CC       {ECO:0000255|HAMAP-Rule:MF_00212}.
CC   -!- SIMILARITY: Belongs to the MQO family. {ECO:0000255|HAMAP-
CC       Rule:MF_00212}.
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DR   EMBL; CP000941; ACA12791.1; -; Genomic_DNA.
DR   RefSeq; WP_004086424.1; NC_010513.1.
DR   AlphaFoldDB; B0U4L2; -.
DR   KEGG; xfm:Xfasm12_1915; -.
DR   HOGENOM; CLU_028151_0_0_6; -.
DR   OMA; PHLDTRW; -.
DR   OrthoDB; 1371190at2; -.
DR   UniPathway; UPA00223; UER01008.
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.
DR   TIGRFAMs; TIGR01320; mal_quin_oxido; 1.
PE   3: Inferred from homology;
KW   FAD; Flavoprotein; Oxidoreductase; Tricarboxylic acid cycle.
FT   CHAIN           1..562
FT                   /note="Probable malate:quinone oxidoreductase"
FT                   /id="PRO_1000099884"
FT   REGION          530..562
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        541..562
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   562 AA;  62582 MW;  7AA79FD74534EF0D CRC64;
     MKKSLKGLTG LIVAFALATL LFLYWPLYQR SVPKANNDTP VDVVLIGGGI MSVTLGTYLQ
     ELQPDWKIEL FERLNGIAQE SSDGWNNAGT GHSAFAELNY TPELQDGTIE IKRAIKIAEQ
     FEISREFWSH QVRHGRLPAP TEFINATPHM SFVWGEDRIE YLRKRHNALI KNPLFYGMQF
     STDPAVIQQW APLLMEGRTQ DQKVAATYMP LGTDVNFGVI TRDLAKHLQD SQNFALHLDH
     EVTALRQNPD KTWNVTVKDL NNGQERSIKS RFVFIGAGGA ALKLLQLSGI PESKDYAGFP
     VGGQFLSFEN TAITKRHNVK AYGMAESGSP PMSVPHLDAR KLDGKSIVLF GPFALYSTKF
     LKNGSWFDLY SSVNHHNAAG MLSVGKNNID LVKYLMKQAT LTDADRHAEL LKYFPNAKPT
     DWTLVTAGQR VQIIKRDPEK GMILQFGTEI VMDKDHTLAT LLGASPGAST SPSIMLDLLA
     KAFPQQMKNG WETQLKKIIP SYGQHINDSP ALTNKIRRMT SETLSLPYLE VPDKSATPTD
     PTIAPKHQHS TTHNANSEMQ AL