ID Q13IJ1_PARXL Unreviewed; 799 AA.
AC Q13IJ1;
DT 22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT 22-AUG-2006, sequence version 1.
DT 27-MAR-2024, entry version 101.
DE SubName: Full=Quinoprotein glucose dehydrogenase {ECO:0000313|EMBL:ABE36098.1};
DE EC=1.1.5.2 {ECO:0000313|EMBL:ABE36098.1};
GN ORFNames=Bxe_C0173 {ECO:0000313|EMBL:ABE36098.1};
OS Paraburkholderia xenovorans (strain LB400).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE36098.1, ECO:0000313|Proteomes:UP000001817};
RN [1] {ECO:0000313|EMBL:ABE36098.1, ECO:0000313|Proteomes:UP000001817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LB400 {ECO:0000313|EMBL:ABE36098.1,
RC ECO:0000313|Proteomes:UP000001817};
RX PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA Chain P.S., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M., Lao V.,
RA Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A., Marx C.J.,
RA Parnell J.J., Ramette A., Richardson P., Seeger M., Smith D., Spilker T.,
RA Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B., Tiedje J.M.;
RT "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp genome
RT shaped for versatility.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
CC -!- COFACTOR:
CC Name=pyrroloquinoline quinone; Xref=ChEBI:CHEBI:58442;
CC Evidence={ECO:0000256|ARBA:ARBA00001931};
CC -!- SIMILARITY: Belongs to the bacterial PQQ dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00008156}.
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DR EMBL; CP000272; ABE36098.1; -; Genomic_DNA.
DR RefSeq; WP_011493358.1; NC_007953.1.
DR AlphaFoldDB; Q13IJ1; -.
DR STRING; 266265.Bxe_C0173; -.
DR KEGG; bxb:DR64_8255; -.
DR KEGG; bxe:Bxe_C0173; -.
DR PATRIC; fig|266265.5.peg.7956; -.
DR eggNOG; COG4993; Bacteria.
DR OrthoDB; 9794322at2; -.
DR Proteomes; UP000001817; Chromosome 3.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0048038; F:quinone binding; IEA:InterPro.
DR GO; GO:0008876; F:quinoprotein glucose dehydrogenase activity; IEA:UniProtKB-EC.
DR CDD; cd10280; PQQ_mGDH; 1.
DR Gene3D; 2.140.10.10; Quinoprotein alcohol dehydrogenase-like superfamily; 2.
DR InterPro; IPR018391; PQQ_beta_propeller_repeat.
DR InterPro; IPR017511; PQQ_mDH.
DR InterPro; IPR002372; PQQ_repeat.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR001479; Quinoprotein_DH_CS.
DR NCBIfam; TIGR03074; PQQ_membr_DH; 1.
DR PANTHER; PTHR32303; QUINOPROTEIN ALCOHOL DEHYDROGENASE (CYTOCHROME C); 1.
DR PANTHER; PTHR32303:SF4; QUINOPROTEIN GLUCOSE DEHYDROGENASE; 1.
DR Pfam; PF01011; PQQ; 3.
DR Pfam; PF13360; PQQ_2; 1.
DR SMART; SM00564; PQQ; 5.
DR SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1.
DR PROSITE; PS00363; BACTERIAL_PQQ_1; 1.
DR PROSITE; PS00364; BACTERIAL_PQQ_2; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:ABE36098.1}; PQQ {ECO:0000256|ARBA:ARBA00022891};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 39..56
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 63..79
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 85..108
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 120..138
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 799 AA; 85789 MW; 33572412495115AC CRC64;
MHSSASIRVA HLLSVLFASL SGVYLLVGGI WLAATGGSLY YVFAGIVMLV TAVLIYRRSP
LALGLYALLL LCTIVWSLWE VGTDFWALAP RLDVLVVFGI WLLLPYVYRA FEPSAKTHGL
ALGATLIVSV AVLVFAVFND PQEINGTLAS APAQAAATPA GERVAEGDWP AYGRTQHGTR
YSPLKQINAD NVKDLKVAWI FRTGDMKRST DPGEITNEVT PIKVGDMLYL CSPHQILFAL
DAATGQEKWR FDPKLKTDPS FQHVTCRGVS YHDSTASGSN NDSPDQAPAT APAICARRVY
LPVNNGHLYA LDAQTGQLCP DFANHGDLDL QVGQPVTTAG QYEPTSPPVI TGKVIVIAGS
VEDNYSTREP SGVIRGFDVN TGKLLWAFDP GAKNPEAVLG AGQHYSVNSP NSWAPAVYDA
KLDLVYLPMG VSTPDIWGGY RTPEQERFAS GLLALNATTG KLAWFYQTVH HDLWDMDLPA
QPTLADITDR SGNLVPAVYA PAKTGNIFVL DRRTGTPIVP APEKPVPQGA AQGDHVSPTQ
PFSALTFRPD RKLTGADMWG ATMFDQLVCR VMFQRLNYDG TFTPPSVKGT LVFPGNLGMF
EWGGIAVDTD RQIAIANPIA LPFVSRLMPR GPGNPIEPAA GGTGGSGTES GIQPQYGVPF
GVTLNAFMSP LGLPCKQPAW GYISAVDLKT NQIVWKKRIG TVRDSSPLPL PFKMGMPMLG
GPMTTAGDVF FIGATADNYI RAFDTNTGKQ LWQARLPAGG QATPMTYEAK GKQYVVIAAG
GHGSFGTRLG DYVMAYALP
//