MQO1_STAAS
ID MQO1_STAAS Reviewed; 492 AA.
AC Q6G6V5;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 2.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=Probable malate:quinone oxidoreductase 1 {ECO:0000255|HAMAP-Rule:MF_00212};
DE EC=1.1.5.4 {ECO:0000255|HAMAP-Rule:MF_00212};
DE AltName: Full=MQO 1 {ECO:0000255|HAMAP-Rule:MF_00212};
DE AltName: Full=Malate dehydrogenase [quinone] 1 {ECO:0000255|HAMAP-Rule:MF_00212};
GN Name=mqo1 {ECO:0000255|HAMAP-Rule:MF_00212}; OrderedLocusNames=SAS2256;
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAG44069.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BX571857; CAG44069.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_000211366.1; NC_002953.3.
DR AlphaFoldDB; Q6G6V5; -.
DR KEGG; sas:SAS2256; -.
DR HOGENOM; CLU_028151_0_0_9; -.
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..492
FT /note="Probable malate:quinone oxidoreductase 1"
FT /id="PRO_0000128745"
SQ SEQUENCE 492 AA; 54786 MW; 8D31D1A84F26D441 CRC64;
MTTQHSKTDV ILIGGGIMSA TLGTLLKELS PEKNIKVFEK LAQPGEESSN VWNNAGTGHS
ALCELNYTKE GKDGTVDCSK AIKINEQYQI SKQFWAYLVK TGQLDNPDRF IQAVPHMSFV
IGEDNVAFIK SRVATLKKSV LFEKMKLSQD EEEMKSWVPL MIEGRKSDEP IALTYDETGT
DVNFGALTAK LFENLEQRGV GIQYKQNVLD IKKQKSGAWL VKVKDLETNE TTTYESDFVF
IGAGGASLPL LQKTGIKQSK HIGGFPVSGL FLRCTNQEVI DRHHAKVYGK AAVGAPPMSV
PHLDTRFVDG KRSLLFGPFA GFSPKFLKTG SHMDLIKSVK PNNIVTMLSA GIKEMSLTKY
LVSQLMLSND ERMDDLRVFF PNAKNEDWEV ITAGQRVQVI KDTEDSKGNL QFGTEVITSD
DGTLAALLGA SPGASTAVDI MFDVLQRCYR DEFKGWEPKI KEMVPSFGYR LTDHEDLYHK
INEEVTKYLQ VK