MQO_BURL3
ID MQO_BURL3 Reviewed; 553 AA.
AC Q390Q5;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 87.
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};
GN OrderedLocusNames=Bcep18194_B2950;
OS Burkholderia lata (strain ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 /
OS R18194 / 383).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=482957;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 / R18194 / 383;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A.,
RA Richardson P.;
RT "Complete sequence of chromosome 2 of Burkholderia sp. 383.";
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000152; ABB13061.1; -; Genomic_DNA.
DR AlphaFoldDB; Q390Q5; -.
DR PRIDE; Q390Q5; -.
DR EnsemblBacteria; ABB13061; ABB13061; Bcep18194_B2950.
DR KEGG; bur:Bcep18194_B2950; -.
DR PATRIC; fig|482957.22.peg.6772; -.
DR HOGENOM; CLU_028151_0_0_4; -.
DR OMA; PHLDTRW; -.
DR UniPathway; UPA00223; UER01008.
DR Proteomes; UP000002705; Chromosome 2.
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 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..553
FT /note="Probable malate:quinone oxidoreductase"
FT /id="PRO_0000325491"
FT REGION 524..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..541
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 553 AA; 60590 MW; D38609F6EDF69809 CRC64;
MKKGSAVIKT LRVILSALAL CVATSSAHAA DTKKVDVLLV GGGIMSSTLG VWLHELQPDW
SMTMVERLDG VALESSNGWN NAGTGHSALA ELNYTPEKAD GKIDISKAIE INESFQISRQ
FWAWQVKQGV LKNPHSFINS TPHMSFVWGD DNVRFLKKRY EALQASPLFR GMQYSEDYDQ
IKQWVPLMME GRDPKQKVAA TWTPIGTDVN FGEITRQFVG YLKTQPNFTL SLSSEVREIS
RNADGTWHVS WVKLHSDEPA QSVDAKFVFI GAGGGALHLL QASGVPEAKD YGAFPVGGSF
LVTENPEVVK QHLAKAYGKA SVGSPPMSVP HLDTRIIDGK KIILFGPFAT FSTKFLKNGS
YFDLLKSTNT HNVAPMMRVG VDEFPLVQYL AGQLMLSDDD RFNALKEYFP NAKKEDWRLW
QAGQRVQIIK RDPVKGGVLK LGTEIVASQD GSIAGLLGAS PGASTAAPIM LNLMKKVFKD
KVATPEWQQK IRQIVPSYGT KLNDSPAKVV EEWTYTSDVL QLSPPPKIDV NTPSQATGTA
PARPAKASAD MAL
