MQO2_STAAS
ID MQO2_STAAS Reviewed; 498 AA.
AC Q6G669;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=Probable malate:quinone oxidoreductase 2 {ECO:0000255|HAMAP-Rule:MF_00212};
DE EC=1.1.5.4 {ECO:0000255|HAMAP-Rule:MF_00212};
DE AltName: Full=MQO 2 {ECO:0000255|HAMAP-Rule:MF_00212};
DE AltName: Full=Malate dehydrogenase [quinone] 2 {ECO:0000255|HAMAP-Rule:MF_00212};
GN Name=mqo {ECO:0000255|HAMAP-Rule:MF_00212}; OrderedLocusNames=SAS2492;
OS Staphylococcus aureus (strain MSSA476).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282459;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSSA476;
RX PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT for the rapid evolution of virulence and drug resistance.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(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; BX571857; CAG44308.1; -; Genomic_DNA.
DR RefSeq; WP_001130051.1; NC_002953.3.
DR AlphaFoldDB; Q6G669; -.
DR KEGG; sas:SAS2492; -.
DR HOGENOM; CLU_028151_0_0_9; -.
DR OMA; RCDNPEV; -.
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..498
FT /note="Probable malate:quinone oxidoreductase 2"
FT /id="PRO_0000128746"
SQ SEQUENCE 498 AA; 55999 MW; 7D8D5ED706A4D183 CRC64;
MAKSNSKDIV LIGAGVLSTT FGSMLKEIEP DWNIHVYERL DRPAIESSNE RNNAGTGHAA
LCELNYTVLQ PDGSIDIEKA KVINEEFEIS KQFWGHLVKS GSIENPREFI NPLPHISYVR
GKNNVKFLKD RYEAMKAFPM FDNIEYTEDI EVMKKWIPLM MKGREDNPGI MAASKIDEGT
DVNFGELTRK MAKSIEAHPN ATVQFNHEVV DFEQLSNGQW EVTVKNRLTG EKFKQVTDYV
FIGAGGGAIP LLQKTGIPES KHLGGFPISG QFLACTNPQV IEQHDAKVYG KEPPGTPPMT
VPHLDTRYID GQRTLLFGPF ANVGPKFLKN GSNLDLFKSV KTYNITTLLA AAVKNLPLIK
YSFDQVIMTK EGCMNHLRTF YPEARNEDWQ LYTAGKRVQV IKDTPEHGKG FIQFGTEVVN
SQDHTVIALL GESPGASTSV SVALEVLERN FPEYKTEWAP KIKKMIPSYG ESLIEDEKLM
RKIRKQTSKD LELGYYEN