MQO_XYLF2
ID MQO_XYLF2 Reviewed; 562 AA.
AC B2I8R2;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 25-MAY-2022, entry version 69.
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=XfasM23_1853;
OS Xylella fastidiosa (strain M23).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xylella.
OX NCBI_TaxID=405441;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M23;
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; CP001011; ACB93253.1; -; Genomic_DNA.
DR RefSeq; WP_004089665.1; NC_010577.1.
DR AlphaFoldDB; B2I8R2; -.
DR EnsemblBacteria; ACB93253; ACB93253; XfasM23_1853.
DR GeneID; 58017277; -.
DR KEGG; xfn:XfasM23_1853; -.
DR HOGENOM; CLU_028151_0_0_6; -.
DR OMA; PHLDTRW; -.
DR UniPathway; UPA00223; UER01008.
DR Proteomes; UP000001698; 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 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_1000099883"
FT REGION 535..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; 62597 MW; CF6F15499229A23E CRC64;
MKKSLKELTG LIVAFALATL LFLYWPLYQR SVPKANNDAP VDVVLIGGGI MSVTLGTYLQ
ELQPDWKIEL FERLNGIAQE SSDGWNNAGT GHSAFAELNY TPELQDGTIE IKRAIKIAEQ
FEISREFWSH QVRHGRLPAP TEFINATPHM SFVWGEDRIE YLRKRHNALI KNPLFYGMQF
STDPAIIQKW APLLMEGRTQ DQKVAATYMP LGTDVNFGVI TRDLAKHLQD SQNFALHLDH
EVTALRQNPD KTWNVTVKDL NNGQERSIKS RFVFIGAGGA ALKLLQLSGI PESKDYAGFP
VGGQFLSFEN TAITKRHNVK AYGMAESGSP PMSVPHLDAR KLDGKSIVLF GPFALYSTKF
LKNGSWFDLY SSVNHHNAAG MLSVGKNNID LVKYLMKQAT LTDADRHAEL LKYFPNAKPT
DWTLVTAGQR VQIIKRDPDK GMILQFGTEI VMDKDHTLAT LLGASPGAST SPSIMLDLLA
KAFPQQMKNG WETQLKKIIP SYGQHINDSP ALTNKIRRMT SETLSLPYLE VPDKSATPAD
PTIAPKNQHS TTYNANSEMQ AL