ID   MQO_BACC1               Reviewed;         500 AA.
AC   Q735Z0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 92.
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=BCE_3011;
OS   Bacillus cereus (strain ATCC 10987 / NRS 248).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=222523;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10987 / NRS 248;
RX   PubMed=14960714; DOI=10.1093/nar/gkh258;
RA   Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L.,
RA   Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F.,
RA   Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.;
RT   "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic
RT   adaptations and a large plasmid related to Bacillus anthracis pXO1.";
RL   Nucleic Acids Res. 32:977-988(2004).
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; AE017194; AAS41922.1; -; Genomic_DNA.
DR   RefSeq; WP_000069165.1; NC_003909.8.
DR   AlphaFoldDB; Q735Z0; -.
DR   EnsemblBacteria; AAS41922; AAS41922; BCE_3011.
DR   GeneID; 59156143; -.
DR   KEGG; bca:BCE_3011; -.
DR   HOGENOM; CLU_028151_0_0_9; -.
DR   OMA; PHLDTRW; -.
DR   UniPathway; UPA00223; UER01008.
DR   Proteomes; UP000002527; Chromosome.
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   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..500
FT                   /note="Probable malate:quinone oxidoreductase"
FT                   /id="PRO_1000023791"
SQ   SEQUENCE   500 AA;  55180 MW;  41C97084BAD3B75F CRC64;
     MSNMQQKTDV ILIGAGIMSA TLGSLLKELA PEWEIKVFEK LASAGEESSN EWNNAGTGHS
     ALCELNYTSE KSDGSIDISK AVKVNEQFQL SRQFWAYLVK SKLIRNPQDF IMPLPHMSLV
     QGEKNVQFLK NRFEALSKNP LFQGMEFSDA PETLKKWLPL IMEGRTSNEP MAATKIDSGT
     DVNFGALTRM LFDYLKTKDV ELNYKHSVEN IKRTKNGLWE VKVHDMNSGK IEHHTAKFVF
     IGGGGGSLPL LQKTGIPESK HIGGFPVSGL FMVCKNQKVV EQHHAKVYGK AKVGAPPMSV
     PHLDTRYIDN KKALLFGPFA GFSPKFLKTG SNLDLIGSVK PNNVLTMLAA GVKEMGLTKY
     LIQQVMLSHE KRMEELREFI PNAKSEDWDI VVAGQRVQVI KDTDAGGKGT LQFGTEVVSA
     ADGSIAALLG ASPGASTAVH VMLEVLEKCF PSRMVEWEGK IKEMIPSYGI SLTENPRLFQ
     DLHTSTGRTL GLNEKETVHN