ID   A0A149QAB6_9PROT        Unreviewed;       813 AA.
AC   A0A149QAB6;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=Glucose dehydrogenase {ECO:0000313|EMBL:KXU94086.1};
GN   ORFNames=AD928_07530 {ECO:0000313|EMBL:KXU94086.1};
OS   Acetobacter cerevisiae.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Acetobacter.
OX   NCBI_TaxID=178900 {ECO:0000313|EMBL:KXU94086.1, ECO:0000313|Proteomes:UP000075473};
RN   [1] {ECO:0000313|EMBL:KXU94086.1, ECO:0000313|Proteomes:UP000075473}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 1625 {ECO:0000313|EMBL:KXU94086.1,
RC   ECO:0000313|Proteomes:UP000075473};
RA   Li L., Cleenwerck I., De Vuyst L., Vandamme P.;
RT   "Improved classification and identification of acetic acid bacteria using
RT   matrix-assisted laser desorption/ionization time-of-flight mass
RT   spectrometry; Gluconobacter nephelii and Gluconobacter uchimurae are later
RT   heterotypic synonyms of Gluconobacter japonicus and Gluconobacter oxydans,
RT   respectively.";
RL   Submitted (JUN-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:KXU94086.1}.
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DR   EMBL; LHZA01000143; KXU94086.1; -; Genomic_DNA.
DR   RefSeq; WP_062249529.1; NZ_LHZA01000143.1.
DR   AlphaFoldDB; A0A149QAB6; -.
DR   PATRIC; fig|178900.5.peg.2556; -.
DR   Proteomes; UP000075473; 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; 2.
DR   Pfam; PF13360; PQQ_2; 1.
DR   SMART; SM00564; PQQ; 6.
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   Reference proteome {ECO:0000313|Proteomes:UP000075473};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        15..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        46..64
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        70..86
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        93..115
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          527..548
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        527..547
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   813 AA;  87316 MW;  5AF0226AF1D46EC2 CRC64;
     MGDGQPADHH SPLGGIYRAV FSVISLAAGL ALAYGGIKLL MLGGSAYYLL AGLAYCALAV
     LVFLKHPYTL VVSAVVFAAT FVWALCDTPE IGYWALLPRL VVPAILFTLS LWAVATFPAT
     SSPIRRGSVF GGLGIVGCLL VTLAEAFFPH GQISNPDAAS ANPQVAQAGK TDAPEDWEFF
     GRNAQGTRYA PYTQITPDNV SKLKVAWVYH TGRRTHGPGA GVDENTPQQI GNVLYSCTPE
     NLITALEADT GKELWKFDPK AHSAEHVTCR GVGYYDATKD ASLTAEEKAA DDAAPMCHQR
     ILVSTVDARF IALDAHTGAE CSGFGENGVV DLKKQMGPTA AGKRYHPTST PVVMGHVAVI
     GGWVRDIVHG EPSGVVRAYD VRTGALAWAW DVGDPDNTGA PADDQTYTLE TPNVWTIPTY
     DKELNLVYLP TGNGPPDYWG GDRTVAKEKF GAAVVAVDAS TGKTKWVFQT VHHDVWDYDL
     PSQPVLYDVT NAQGEKVPAL IQTTKTGHIF VLDRRTGTPV TEVQERRVAT SPSAQGEHLS
     PTQPFSVGMP TIGADPLTES SMWGVSTFDQ LYCRIMFKDS VYEGPFTPPG EKPYIEWPSL
     LGGMNWGGIS IDEARGVMFV NDMRMPLRMS LVNLEEAKKY KASTDEVPGF MGTMRPQVAG
     SYAGVRIDIL QSPLQVPCNT PPFGTMSAID LHTKKLLWQV PMGTTQDLGP MGIKTHLPVP
     MGMPTLGGPT STASGLVFFA GTQDYYLRAL DSGTGKEVWR ERLPVGAVAA PLIFRSPKTG
     KEYVVISAGG MSHSPDVGDY IIAYTLPDDG AAK
//