ID A0A0F3KQA0_9GAMM Unreviewed; 819 AA.
AC A0A0F3KQA0;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=Glucose dehydrogenase {ECO:0000313|EMBL:KJV33351.1};
GN ORFNames=VI08_11275 {ECO:0000313|EMBL:KJV33351.1};
OS Luteibacter yeojuensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Luteibacter.
OX NCBI_TaxID=345309 {ECO:0000313|EMBL:KJV33351.1, ECO:0000313|Proteomes:UP000033651};
RN [1] {ECO:0000313|EMBL:KJV33351.1, ECO:0000313|Proteomes:UP000033651}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SU11 {ECO:0000313|EMBL:KJV33351.1,
RC ECO:0000313|Proteomes:UP000033651};
RA Sulaiman J., Priya K., Chan K.-G.;
RT "Draft genome sequence of Luteibacter yeojuensis strain SU11.";
RL Submitted (MAR-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KJV33351.1}.
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DR EMBL; JZRB01000022; KJV33351.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F3KQA0; -.
DR PATRIC; fig|345309.4.peg.1600; -.
DR Proteomes; UP000033651; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR GO; GO:0048038; F:quinone binding; IEA:InterPro.
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 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.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {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..104
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 125..147
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 549..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 819 AA; 88640 MW; 7960E136520916C8 CRC64;
MIRARRFHPA TLFTAFVFVL AGAAMLYGGA RLVEAGGSPY FTIAGAWLLL VALLLAVRVR
FAVPLYTLFL LGSTGWAVWE VGFDWWQLLP RLDVWFALGL WLWLPWPRRG LSRDPYLETA
RGTGGGFLFV GLLIVAIVGV VAVAMPVPDL KGELPMADVS GPQGDRASLA DGDWVDYGGS
AWGQRYSPLK QITPENVAQL QVAWKIQTGD MPGPGDPTET TAENTPLKVG DTVFLCTPHS
RVIAVDATTG QKRWEFDPKI QSPVGFKHWE HMTCRGVSYH DDARYAAALI PAPATTAAGV
PAPASTAPLP TNVLAAGTCP RRLFLPTADA RLIALNADNG QVCDDFGNKG TVDLRANIGP
FTPGGYYSTS PPAVTKDLVI IGGHVTDDES TNEPSGVIRA FDVHDGHLVW NWDPGKPDDT
TPIAADGTYT RNAPNMWSLF SVDENLGMVY LPMGNQTPDQ FAGGRTPTSE KYGAGLVALD
IASGKVKWNY QFTHHDLWDM DVGGQPSLVD LTTDKGVKPA IIASTKQGSL YVLDRRDGTP
IVPIREVPRP QGAVEGDHAA PTQPMSDMNM APPDLREPDM WGTTPFDMLW CRVRFRSLRY
DGMYTPPSLQ GSLVYPGNFG VFDWGGVSVD PTRQLLLANP SYMAFQSKLI PKDQLAHMEV
VEAKSETQGI KKAEGIPYAI ELNPFLSPLG IPCQAPPWGY VAGVDLRSGK TMWKHRNGTI
VDSAPLPIPM PLGVPSMGGM VTTAGGVTFL SGTLDYYLRA YDVHTGRKLW ESRLPAGGQA
TPMTYADKDG RQYVLVVAGG HGSLGTKQGD WVIAYALPK
//