ID   MQO_CORGL               Reviewed;         500 AA.
AC   O69282;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 140.
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=Cgl2001, cg2192;
OS   Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS   JCM 1318 / LMG 3730 / NCIMB 10025).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=196627;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=R127;
RX   PubMed=9660197; DOI=10.1046/j.1432-1327.1998.2540395.x;
RA   Molenaar D., van der Rest M.E., Petrovic S.;
RT   "Biochemical and genetic characterization of the membrane-associated malate
RT   dehydrogenase (acceptor) from Corynebacterium glutamicum.";
RL   Eur. J. Biochem. 254:395-403(1998).
RN   [2]
RP   SEQUENCE REVISION TO N-TERMINUS.
RA   van der Rest M.E.;
RL   Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA   Ikeda M., Nakagawa S.;
RT   "The Corynebacterium glutamicum genome: features and impacts on
RT   biotechnological processes.";
RL   Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA   Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA   Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA   Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA   Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA   Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT   "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT   impact on the production of L-aspartate-derived amino acids and vitamins.";
RL   J. Biotechnol. 104:5-25(2003).
RN   [5]
RP   PROTEIN SEQUENCE OF 2-6.
RC   STRAIN=R127;
RA   Molenaar D., van der Rest M.E., Petrovic S.;
RL   Submitted (AUG-1998) to UniProtKB.
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;
CC       Note=The FAD is tightly bound.;
CC   -!- ACTIVITY REGULATION: Activated by lipids.
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle;
CC       oxaloacetate from (S)-malate (quinone route): step 1/1.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
CC   -!- SIMILARITY: Belongs to the MQO family. {ECO:0000305}.
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DR   EMBL; AJ224946; CAA12237.1; -; Genomic_DNA.
DR   EMBL; BA000036; BAB99394.1; -; Genomic_DNA.
DR   EMBL; BX927153; CAF20342.1; -; Genomic_DNA.
DR   RefSeq; NP_601207.1; NC_003450.3.
DR   RefSeq; WP_011014814.1; NC_006958.1.
DR   AlphaFoldDB; O69282; -.
DR   STRING; 196627.cg2192; -.
DR   World-2DPAGE; 0001:O69282; -.
DR   KEGG; cgb:cg2192; -.
DR   KEGG; cgl:Cgl2001; -.
DR   PATRIC; fig|196627.13.peg.1940; -.
DR   eggNOG; COG0579; Bacteria.
DR   HOGENOM; CLU_028151_0_0_11; -.
DR   OMA; PHLDTRW; -.
DR   BRENDA; 1.1.5.4; 960.
DR   UniPathway; UPA00223; UER01008.
DR   Proteomes; UP000000582; 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.
DR   TIGRFAMs; TIGR01320; mal_quin_oxido; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Direct protein sequencing; FAD; Flavoprotein; Membrane;
KW   Oxidoreductase; Reference proteome; Tricarboxylic acid cycle.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|Ref.5"
FT   CHAIN           2..500
FT                   /note="Malate:quinone oxidoreductase"
FT                   /id="PRO_0000128711"
SQ   SEQUENCE   500 AA;  54832 MW;  31E02BC151758319 CRC64;
     MSDSPKNAPR ITDEADVVLI GAGIMSSTLG AMLRQLEPSW TQIVFERLDG PAQESSSPWN
     NAGTGHSALC ELNYTPEVKG KVEIAKAVGI NEKFQVSRQF WSHLVEEGVL SDPKEFINPV
     PHVSFGQGAD QVAYIKARYE ALKDHPLFQG MTYADDEATF TEKLPLMAKG RDFSDPVAIS
     WIDEGTDINY GAQTKQYLDA AEVEGTEIRY GHEVKSIKAD GAKWIVTVKN VHTGDTKTIK
     ANFVFVGAGG YALDLLRSAG IPQVKGFAGF PVSGLWLRCT NEELIEQHAA KVYGKASVGA
     PPMSVPHLDT RVIEGEKGLL FGPYGGWTPK FLKEGSYLDL FKSIRPDNIP SYLGVAAQEF
     DLTKYLVTEV LKDQDKRMDA LREYMPEAQN GDWETIVAGQ RVQVIKPAGF PKFGSLEFGT
     TLINNSEGTI AGLLGASPGA SIAPSAMIEL LERCFGDRMI EWGDKLKDMI PSYGKKLASE
     PALFEQQWAR TQKTLKLEEA