ID A0A1H7WAK4_9GAMM Unreviewed; 815 AA.
AC A0A1H7WAK4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=Quinoprotein glucose dehydrogenase {ECO:0000313|EMBL:SEM18612.1};
GN ORFNames=SAMN05428989_3306 {ECO:0000313|EMBL:SEM18612.1};
OS Pseudoxanthomonas sp. GM95.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Pseudoxanthomonas.
OX NCBI_TaxID=1881043 {ECO:0000313|EMBL:SEM18612.1, ECO:0000313|Proteomes:UP000199164};
RN [1] {ECO:0000313|Proteomes:UP000199164}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GM95 {ECO:0000313|Proteomes:UP000199164};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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; FOAX01000003; SEM18612.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H7WAK4; -.
DR STRING; 1881043.SAMN05428989_3306; -.
DR OrthoDB; 9794322at2; -.
DR Proteomes; UP000199164; 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; 1.
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 Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 59..77
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 89..108
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 120..140
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 815 AA; 86774 MW; 8ECB360F6A212099 CRC64;
MRKLLTGLTI VVGIALVLAG LGLAGGGAYL LSLGGSWFYL PAGLAMAAVG GLLVARRALA
LWIALGLLVV AAVWAFSEVG TDFWQLVPRL IAFIVIALLA SAAAPLLRRK DGSPALGCKV
AGVLAAVFAI GLAGFFTGMF RPHPTVVADA GADAPVIQPD AGKADGNDWT AYGRNTSGDR
FAQFDQINKA NVKDLKVAWT YRTGDMAVDG AEYQVTPLKV DDTVYLCTPL SKVMAVDATT
GKEKWRFDPK AVVSASTKGW KRCRGVGYAD LDKLASATPV AADPAAPATD ATTAIAPATC
RKRIIETTID ARLLALDAET GTLCEDFGDH GYVDLSKGIA PAPAASDQGT YNVTSAPLVA
DGVVMVGGRL NDNLSVGEPG GVVRGYDVVT GKILWAWDAK RGTTDGQLAE GELFPLETPN
FWGTAAYDPK LGLAYFPLGN QTPDFWTGNR HPYSDEYNDA IVAVDLKTGK EAWHFRTANR
DQFDYDVSSQ PILYDIPQKD GSSTPVIIQA TKRGQIFVLD RRDGKPVFPV EQRAVATDAM
PGMNVAPTQP YSALSVGTTP FKESDMWGAS IFDQLVCRIE FKQMRWEGEW TPLSDKQRTL
IFPGYYGGMN WGGGAVDAAT GTLIINDIRM AQWGRFIKQD VAKATGLKPS TEGEYSTQTG
TPWGVERSMF VSPLGVPCFK PPFGTMTAID LTTGKTKWQV PMGSIQDAPV HGIVPGVRIP
LGMPTMGGPL VTKGGLTFFH GTLDYYVRAL DNDTGAELWR GRLPVGGQGA PMSYIGKDGK
QYIVVVAGGA TRTGTNANRG DYVIAYALPD KSSAP
//
