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Database: UniProt
Entry: A0A5J5G1L5_9GAMM
LinkDB: A0A5J5G1L5_9GAMM
Original site: A0A5J5G1L5_9GAMM 
ID   A0A5J5G1L5_9GAMM        Unreviewed;       811 AA.
AC   A0A5J5G1L5;
DT   11-DEC-2019, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2019, sequence version 1.
DT   13-SEP-2023, entry version 11.
DE   SubName: Full=Glucose/quinate/shikimate family membrane-bound PQQ-dependent dehydrogenase {ECO:0000313|EMBL:KAA9000538.1};
GN   ORFNames=FJU30_09885 {ECO:0000313|EMBL:KAA9000538.1};
OS   Affinibrenneria salicis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Affinibrenneria.
OX   NCBI_TaxID=2590031 {ECO:0000313|EMBL:KAA9000538.1, ECO:0000313|Proteomes:UP000335415};
RN   [1] {ECO:0000313|EMBL:KAA9000538.1, ECO:0000313|Proteomes:UP000335415}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L3-3HA {ECO:0000313|EMBL:KAA9000538.1,
RC   ECO:0000313|Proteomes:UP000335415};
RA   Li Y.;
RL   Submitted (SEP-2019) 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:KAA9000538.1}.
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DR   EMBL; VYKJ01000004; KAA9000538.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5J5G1L5; -.
DR   OrthoDB; 9794322at2; -.
DR   Proteomes; UP000335415; 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: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   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; 3.
DR   SMART; SM00564; PQQ; 6.
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   PQQ {ECO:0000256|ARBA:ARBA00022891};
KW   Reference proteome {ECO:0000313|Proteomes:UP000335415};
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..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        45..62
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        69..85
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        97..115
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        127..147
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   811 AA;  86972 MW;  31D025C9B66F30C1 CRC64;
     MVDAGVVPAK KWVRWWCYIL GLLLFLTGAF FVVAGGRLLS LGGSAYFLPA GLFIALSGVQ
     IFRRRASGVL IYSAVFIATV IWALADVGLE FWPLVSRLFY LAVLLLLAML CWPTLRRLSG
     KPTRCVFFYG ASGVIVVCLA ATGALMFQPH PTVAFSGQPL PLTPVDALHE QKDWDHYGNN
     AGGSRFVALD QITRDNVQNL KVAWTYHTGD TPLSPDGNGA EDQQTPLQVG NRVFLCTPHN
     NVIAIDADSG KELWKTEINA KSSVWMRCRG LAYFDATKPL TQPVAQDASP VPVAQVAPGA
     LCQRRILMNT IDARLIALDA GSGRFCPDFG QNGSVDLKAN MGAAADPSYV LTSAPTLAGS
     TVVVGGRVAD NVSTDMPGGV IRGFDVITGA QRWAFDPRAS DPNRELAAGE SYSRSSPNAW
     APMSYDASMN TLFIPMGSSS VDLWGADRTP LDHKYGASVL AVDATTGREK WVFQTVHNDL
     WDFDLPMQPS LIDFPAKDGG SKPALVIGTK AGQIYVLDRA TGQPLTEVKE IPVKAGAIPG
     EQYSPTQPLS VGMPQIGAQK LSEADMWGAT PFDQLMCRIA FKSMRYDGLY TVPDSDISLS
     FPGSLGGMNW GGMSTDPVNH YIFVNDMRLG LWIQMVKADP ASTATNSGGE SVNTGMGLVP
     MKGTPYAVNK NRFMSALGVP CQKPPFGTLS AIEMKTQQIV WQVPVGTVRD TGPLGVKMRL
     PIPVGLPTLG GTLATQGGLV FIAGTQDYYL RAFDSSTGKE VWKARLPVGS QGGPMSYKSP
     ATGKQYVLIS AGGGRQSPDR GDYVIAYALE K
//
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