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Database: UniProt
Entry: A0A0A3X4X0_9GAMM
LinkDB: A0A0A3X4X0_9GAMM
Original site: A0A0A3X4X0_9GAMM 
ID   A0A0A3X4X0_9GAMM        Unreviewed;       800 AA.
AC   A0A0A3X4X0;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=Quinoprotein glucose dehydrogenase A {ECO:0000313|EMBL:KGT47973.1};
DE            EC=1.1.5.2 {ECO:0000313|EMBL:KGT47973.1};
GN   ORFNames=GW12_09900 {ECO:0000313|EMBL:KGT47973.1};
OS   Acinetobacter sp. HR7.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=1509403 {ECO:0000313|EMBL:KGT47973.1, ECO:0000313|Proteomes:UP000032870};
RN   [1] {ECO:0000313|EMBL:KGT47973.1, ECO:0000313|Proteomes:UP000032870}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HR7 {ECO:0000313|EMBL:KGT47973.1,
RC   ECO:0000313|Proteomes:UP000032870};
RA   Ahn S., Kim B.-C.;
RT   "Genome sequencing of Acinetobacter sp. strain HR7.";
RL   Submitted (OCT-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}.
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:KGT47973.1}.
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DR   EMBL; JPQO01000088; KGT47973.1; -; Genomic_DNA.
DR   RefSeq; WP_034584397.1; NZ_JPQO01000088.1.
DR   AlphaFoldDB; A0A0A3X4X0; -.
DR   STRING; 1509403.GW12_09900; -.
DR   PATRIC; fig|1509403.3.peg.979; -.
DR   eggNOG; COG4993; Bacteria.
DR   OrthoDB; 9794322at2; -.
DR   Proteomes; UP000032870; Unassembled WGS sequence.
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; 5.
DR   SMART; SM00564; PQQ; 5.
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|SAM:Phobius};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:KGT47973.1}; 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..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        38..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        62..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        85..107
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        119..137
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   800 AA;  86649 MW;  F87DA9DF957AD704 CRC64;
     MNTSSSGSVL KTILAAIAAI FGLVLLFGGI YLATLGGSWY YIIAGLFFLA TAVLLQKRKS
     TALIVYAVLV LGTVVWGLWE VGSDFFALAP RLDILGLFGL ALLIPAVTRG FGETKGAKIV
     LTSSLAITIA VMIYSVFNDP QEIRGELKSQ QPEVHQSIPG IADEDWPAYG RTQSGLRYSP
     LKQINSENVK DLELAWEFHT GDTKTDKDSG ETTNQVTPIK IGNNLFMCST HQQLIALDPA
     TGKEKWRYDP KVKSDNTYQH LTCRGVSYYD ANNTVGFESS LAARSTTSAE CPQKVILPVN
     DGRLVAVNAT TGKVCSDFGN NGEVDLQKDM PFPYPGGYNP TSPPVITGTT IIIAGSTTDN
     YSTEEPSGVI RGYDVNTGEL LWVFDTGAED PNAIPAPGQK FVNNSPNAWA PLAYDAQLDI
     VYVPTGVGTP DIYGGHRTEL DERYANSMLA LNASTGKLIW NFQTTHHDLW DMDVPAQPTL
     TEIKDKNGNM VPAIYVLTKT GNAFVLDRRT GEAIVPITEK PVPQSVKRGP QTKGEWYSKT
     QPFSDFNLAP KDKLTDKDMW GATMFDQLMC RVSFKKLNYD GIYTPPSENG TLVFPGNLGV
     FEWGGMSVNP DRQIALTNPI GLPFVTRLIP ADPNREQTAK GAGTEAGVQP MYGVPYGVEI
     SAFLSPFGLP CKQPAWGYVA GVDLTNHEIA WKRRIGTIRD SMPGIPLPPF KMGVPMLGGP
     ISTAGNVMFV GATQDNYIRA INVTNGDELW KGRLPAGGQA TPMTYEANGK QYVVIMAGGH
     GSFGTKMGDS LVAYALPDNK
//
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