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Database: UniProt
Entry: A0A0S9NH78_9BURK
LinkDB: A0A0S9NH78_9BURK
Original site: A0A0S9NH78_9BURK 
ID   A0A0S9NH78_9BURK        Unreviewed;       889 AA.
AC   A0A0S9NH78;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=Glucose dehydrogenase {ECO:0000313|EMBL:KQP44612.1};
GN   ORFNames=ASF44_27425 {ECO:0000313|EMBL:KQP44612.1};
OS   Pseudorhodoferax sp. Leaf274.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae.
OX   NCBI_TaxID=1736318 {ECO:0000313|EMBL:KQP44612.1, ECO:0000313|Proteomes:UP000051759};
RN   [1] {ECO:0000313|EMBL:KQP44612.1, ECO:0000313|Proteomes:UP000051759}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf274 {ECO:0000313|EMBL:KQP44612.1,
RC   ECO:0000313|Proteomes:UP000051759};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQP44612.1, ECO:0000313|Proteomes:UP000051759}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf274 {ECO:0000313|EMBL:KQP44612.1,
RC   ECO:0000313|Proteomes:UP000051759};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-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:KQP44612.1}.
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DR   EMBL; LMNA01000007; KQP44612.1; -; Genomic_DNA.
DR   RefSeq; WP_056899373.1; NZ_LMNA01000007.1.
DR   AlphaFoldDB; A0A0S9NH78; -.
DR   STRING; 1736318.ASF44_27425; -.
DR   OrthoDB; 9794322at2; -.
DR   Proteomes; UP000051759; 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; 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   Reference proteome {ECO:0000313|Proteomes:UP000051759};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        37..54
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        61..78
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        84..107
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        164..185
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          607..629
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   889 AA;  94017 MW;  78199E70B8A4FB57 CRC64;
     MQNNPRSLYT TILGFLMWLP GALLFAGGAW LMVLGGSIYY AVAGLLLALT GSLVHRRAPS
     AVWAFAVLFA GSLAWAVWES GLDWWPLAAR MGVLFMLGVL MLLPWTLRRL DGGRVQPPIE
     APITPPGTPP TGGQPEPVRP SRFELFTRNH RAHRAPRAAS WRRGGGMALS LAMACFALLS
     AVTWIRDVHA LEGALPPSQG ALVDQGSAVR GVPPGEWHAY GRTGFGQRYS PLADITPSNV
     ADLQVVWHAH TGDLRGQPGD PEETTFQATP LKIGNRLYLC TPHQTVMALD ATTGQEIWRH
     DAKVSRNLAL QHLTCRGLSY QPPAAAPAPA GTAETAETDA AAAAAGVADA PASASADAPA
     AAAAPASPAT PASPAPDATA AACPNGKLFM PTADGRLLAL DPERGGPCTA FGGGKGEIDL
     WQHMPNHRPG AYYSTSPVVV TARLVIVGGT VLDNVSTAEQ SGVIRAFDIE TGALVWNWDS
     GNPDTTTPIA EGARYTVNSP NSWSISSVDE ALGMVYVPMG NQPPDQWGGN RSAAVEKYSS
     SVVALDLATG QVRWVFQTVH HDLWDYDVPA QPSLVDLNID GATVPALVQP TKQGELFVLD
     RRTGVPIRPQ ADTPAPQGAA QGDRTAATQP RAAISFDPPM LRERSMWGVT MFDQLACRIA
     FKRLRYEGRF TPPSTQGSLI HPGNFGVFNW GGVAVDPRRQ IAFTTPTYLP FVSTLVPRPD
     DTALMVQKDG PPAGALPALN ENFGAPFAVK LGPFLSPLGV PCVAPPWGYV AGADLTSGKI
     VWQHRNGTVR DLSPIPVPIR MGVPNLGGPI VTAGGVAFLS GSLDNYVRAY DVTSGKQLWE
     SRLPAGGQAT PMTYTADDGR QFVLVVAGGH GSLGTTPGDS VIAYALPKR
//
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