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Database: UniProt
Entry: E6WBE1_PANSA
LinkDB: E6WBE1_PANSA
Original site: E6WBE1_PANSA 
ID   E6WBE1_PANSA            Unreviewed;       809 AA.
AC   E6WBE1;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   SubName: Full=Membrane-bound PQQ-dependent dehydrogenase, glucose/quinate/shikimate family {ECO:0000313|EMBL:ADU68910.1};
DE            EC=1.1.5.8 {ECO:0000313|EMBL:ADU68910.1};
GN   OrderedLocusNames=Pat9b_1593 {ECO:0000313|EMBL:ADU68910.1};
OS   Pantoea sp. (strain At-9b).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Pantoea.
OX   NCBI_TaxID=592316 {ECO:0000313|EMBL:ADU68910.1, ECO:0000313|Proteomes:UP000001624};
RN   [1] {ECO:0000313|EMBL:ADU68910.1, ECO:0000313|Proteomes:UP000001624}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=At-9b {ECO:0000313|EMBL:ADU68910.1,
RC   ECO:0000313|Proteomes:UP000001624};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Davenport K., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Ovchinnikova G., Pinto A., Currie C., Woyke T.;
RT   "Complete sequence chromosome of Pantoea sp. At-9b.";
RL   Submitted (DEC-2010) 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; CP002433; ADU68910.1; -; Genomic_DNA.
DR   RefSeq; WP_013508771.1; NC_014837.1.
DR   AlphaFoldDB; E6WBE1; -.
DR   STRING; 592316.Pat9b_1593; -.
DR   KEGG; pao:Pat9b_1593; -.
DR   eggNOG; COG4993; Bacteria.
DR   HOGENOM; CLU_018478_1_0_6; -.
DR   OrthoDB; 9794322at2; -.
DR   Proteomes; UP000001624; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0047519; F:quinate dehydrogenase (quinone) activity; IEA:UniProtKB-EC.
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   ECO:0000313|EMBL:ADU68910.1}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        47..64
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        71..95
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        101..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        129..149
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          525..544
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   809 AA;  88236 MW;  CD6E4F067E62C257 CRC64;
     MDIKEQRSGR RSGLSFVLSI IFALLTLATA IAIIIGGGKL ISLGGSAYYL IAGIAYIVLV
     VLYFKKPVTG FYFSCLIFAL TLIWSLAEVG GFIYWDLLPR LVVPALLFLL SLLVTATDKG
     ALSLQRRLSG GLSLVVFVAL IATFIGGFFP HNTVYNPEAV SAEPLQPTDS DASKAGQDWR
     YISRNASGTR FVPLDQINAD NVKDLQVAWT YHTGRRLTGN AAGVDENTPI QIGSVLYTCT
     PENLIAAVDA DTGKPIWKFD PHARTYEHVT CRSVGYYDYD SDETLSAEQK AAYTDTACRQ
     RIIVSTVDAR LIALDAHTGA LCPNFGQNGM VNLQQGMGDT ADSRRYHPTS VPVIMGHLTV
     FGSWVRDITE DEPSGVLRAY DVRDGSLAWA WDVGNVEGAK QGDDHYTLST PNVWAIPTYD
     KDLGLVYVST GNGPPDYWGG NRNAAKEKFG SSVIALDVNT GKTKWVFQTV HHDIWDYDLP
     SQPVMYNMKN EQGEVVPALI QTSKMGEIFV LDRRTGKPVS KVEEKAVPTS PAAQEEHLSP
     TQPFSVDMPT IGLEQLNEQK MWGVSMFDQL YCRILFKSAL YSGIFQPNSE KTYLEFPATM
     GGMNWGGVSI DETSGILYVN DIRLGMLMAL KSKEAAQGQK ISLNEVPQWA GTIRPQISGP
     YVGVRMDNFA SFLQVPCQHP PFGTMTAIDL HSKKIVWQVP MGTVEDTGPL GVKTHLPMPV
     GMPTLGGPTT TKSGLVFFAG SQDNYLRALD SKTGKEVWKV RLPVGATASP LIYQSAKTGK
     EYIVISAGGA AHSPDVGDYL IAYALPDKA
//
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