MQO_BAUCH
ID MQO_BAUCH Reviewed; 507 AA.
AC Q1LU84;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=BCI_0001;
OS Baumannia cicadellinicola subsp. Homalodisca coagulata.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Candidatus Baumannia.
OX NCBI_TaxID=374463;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16729848; DOI=10.1371/journal.pbio.0040188;
RA Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L., Khouri H.,
RA Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L., Moran N.A., Eisen J.A.;
RT "Metabolic complementarity and genomics of the dual bacterial symbiosis of
RT sharpshooters.";
RL PLoS Biol. 4:1079-1092(2006).
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; CP000238; ABF14239.1; -; Genomic_DNA.
DR RefSeq; WP_011520213.1; NC_007984.1.
DR AlphaFoldDB; Q1LU84; -.
DR STRING; 374463.BCI_0001; -.
DR EnsemblBacteria; ABF14239; ABF14239; BCI_0001.
DR KEGG; bci:BCI_0001; -.
DR HOGENOM; CLU_028151_0_0_6; -.
DR OMA; PHLDTRW; -.
DR OrthoDB; 1371190at2; -.
DR UniPathway; UPA00223; UER01008.
DR Proteomes; UP000002427; 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; Reference proteome;
KW Tricarboxylic acid cycle.
FT CHAIN 1..507
FT /note="Probable malate:quinone oxidoreductase"
FT /id="PRO_0000325486"
SQ SEQUENCE 507 AA; 57524 MW; BFC7F5928DE82374 CRC64;
MKSSCTINTK IVDIVLIGGG LMSATLGTYL QLLEPNWTIH MYERLENTAE ESSNGWNNAG
TGHAAFCELN YTPIQQNGSI DISKAILINE SFEISRQFWS YLVKNNLLTN PQSFINNMPH
INFVWGDENT RFLYQRFKAL QCCTIFNGME YSENHQQISE WAPLIMAGRN TYQKVAATRM
LMGTDVNFGE LTQQLLNSLQ RNPQFHLYMK TDVVDIKRNN DNTWTIYTLN SKDSYSNTEV
RSRYVFIGCG GRSLQLLQQS GLNEANNYAG FPVGGKFLVT NNPTIIKDHN AKVYGKAKIG
APPISVPHLD ARILNGQKML FFGPFATFSS KFLKYGSYLD FFQSITFKNM LPMLYVGKNN
FNLVKYLISQ LIMSETDRLD ALCEYYPKAS LKDWKIIQAG QRVQVIQKDK KTGGILQFGT
KVIYSQDRTL STLLGASPGA STAAYIMLEL LDVMFKQYIT SESWQRKLKE IIPSYGQILN
GNLSLTNQIR SYTCEVLNLN YIKAMPS