ID A0A0U5FQL2_9PROT Unreviewed; 803 AA.
AC A0A0U5FQL2;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Quinoprotein glucose dehydrogenase {ECO:0000313|EMBL:CEF42093.1};
DE EC=1.1.5.2 {ECO:0000313|EMBL:CEF42093.1};
GN Name=gcd {ECO:0000313|EMBL:CEF42093.1};
GN ORFNames=ASN_2834 {ECO:0000313|EMBL:CEF42093.1};
OS Acetobacter senegalensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acetobacter.
OX NCBI_TaxID=446692 {ECO:0000313|EMBL:CEF42093.1, ECO:0000313|Proteomes:UP000056109};
RN [1] {ECO:0000313|Proteomes:UP000056109}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=108B {ECO:0000313|Proteomes:UP000056109};
RA Illeghems K.G.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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; LN606600; CEF42093.1; -; Genomic_DNA.
DR RefSeq; WP_058988426.1; NZ_LN606600.1.
DR AlphaFoldDB; A0A0U5FQL2; -.
DR GeneID; 34783801; -.
DR KEGG; asz:ASN_2834; -.
DR PATRIC; fig|446692.3.peg.2979; -.
DR Proteomes; UP000056109; Chromosome I.
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; 4.
DR SMART; SM00564; PQQ; 4.
DR SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1.
DR PROSITE; PS00364; BACTERIAL_PQQ_2; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:CEF42093.1}; 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..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 40..57
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 64..80
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 86..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 803 AA; 86457 MW; E9D058FD46664D0A CRC64;
MPSSSSRSGL LLNLTITIFV LLGLYLAGGG AWLAALGGSW FYLLSGIVLL ITAIMLLKRW
REALWVYAAL VFATLIWSVA EAGFDFWALA PRGDVILPLG LLLLLPFVSR ELLPASPANC
VPLAVGIVAG LAVYGYALTQ DPQDLAGTLP TVAQQGPAVT PGDVAEAPAA DWPAYGRTQF
GNRYSPLTQI TPANVKDLKV AWVFRTHDLK TPNDPGEITD EVTPIKIRDT LYLCSPHQIL
FALDAATGKE KWKYDPKLKY NPSFQHMTCR GVSYAEAHEG DVTADGSPVP TECSRRVFLP
TNDGRLIALD AETGEACRGF GTEGTVDLTD GMPMRELGFY EPTSPPVVTS KVVIVSGAVT
DNYSTHEPSG VTRAYDLYSG RLVWAFDAGN PNPNELPSDT HHYVPNSPNS WITSAYDAKL
NLIYIPTGVA TPDIWGGHRS ADQERYASGI LALNGDTGEK VWFYQTVHHD LWDMDIPSQP
SLVDIRQKDG TVVPALYAPA KTGNIFVLDR RNGHLIVPAP ETPVPQGAAP GDHLAATQPF
SELTFRPKKN LTDADMWGGT MLDQMVCRIM FKRMRYEGPF TPPSLQGTLV FPGNLGMFEW
GGLAVDPVRQ VAFANPIAIP FVSTLIPRGP GNPAQPGLVS GGPSGSETGV QPQYGTPYGV
DLHAFLSPLG IPCKQPGWGY VAGIDLKTNK IMWMHRNGTV RDSSPLPLPF KVGIPSLGGP
LTTGGGVAFL TSTADYYIRA YDVTTGKQLW QDRLPAGGQS TPMTYEANGR QFVVTADGGH
GSFGTKLGDY IVAYALPDAS AKQ
//