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Database: UniProt
Entry: Q2CEL7_OCEGH
LinkDB: Q2CEL7_OCEGH
Original site: Q2CEL7_OCEGH 
ID   Q2CEL7_OCEGH            Unreviewed;       635 AA.
AC   Q2CEL7;
DT   04-APR-2006, integrated into UniProtKB/TrEMBL.
DT   04-APR-2006, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   SubName: Full=Glucose dehydrogenase {ECO:0000313|EMBL:EAR51115.1};
GN   ORFNames=OG2516_18135 {ECO:0000313|EMBL:EAR51115.1};
OS   Oceanicola granulosus (strain ATCC BAA-861 / DSM 15982 / KCTC 12143 /
OS   HTCC2516).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Oceanicola.
OX   NCBI_TaxID=314256 {ECO:0000313|EMBL:EAR51115.1, ECO:0000313|Proteomes:UP000003635};
RN   [1] {ECO:0000313|EMBL:EAR51115.1, ECO:0000313|Proteomes:UP000003635}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-861 / DSM 15982 / KCTC 12143 / HTCC2516
RC   {ECO:0000313|Proteomes:UP000003635};
RX   PubMed=20418400; DOI=10.1128/JB.00412-10;
RA   Thrash J.C., Cho J.C., Vergin K.L., Giovannoni S.J.;
RT   "Genome sequences of Oceanicola granulosus HTCC2516(T) and Oceanicola
RT   batsensis HTCC2597(TDelta).";
RL   J. Bacteriol. 192:3549-3550(2010).
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:EAR51115.1}.
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DR   EMBL; AAOT01000017; EAR51115.1; -; Genomic_DNA.
DR   RefSeq; WP_007257095.1; NZ_CH724110.1.
DR   AlphaFoldDB; Q2CEL7; -.
DR   STRING; 314256.OG2516_18135; -.
DR   eggNOG; COG4993; Bacteria.
DR   HOGENOM; CLU_018478_1_1_5; -.
DR   OrthoDB; 9794322at2; -.
DR   Proteomes; UP000003635; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
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   PANTHER; PTHR32303; QUINOPROTEIN ALCOHOL DEHYDROGENASE (CYTOCHROME C); 1.
DR   PANTHER; PTHR32303:SF4; QUINOPROTEIN GLUCOSE DEHYDROGENASE; 1.
DR   Pfam; PF13360; PQQ_2; 2.
DR   SMART; SM00564; PQQ; 6.
DR   SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003635};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..635
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004207494"
SQ   SEQUENCE   635 AA;  69365 MW;  BEF9887249A00936 CRC64;
     MRFRDIAALA APIALATPAT AQDWTSFHGN LAAQKFSPAD QITPDNVSAL ERAWEYHTGD
     VSDGSGDLPP TYFNSTPIYA NGTLYIGTPF YRIIALDPAT GTEIWTYDTG SSLEQLTQPG
     LKTRGVSYWE SASPSADEPC QKIVYMGTND AKMHAVDAET GAPCEAFGDG GVLDLNQWNT
     TNDKWPLSIL QPPTIHGDQV VTGWSGYDFR YAEAPPGSVF AFDAQTGEKN WEIQFIPEDI
     RPRTGTANVW THMTVDDERG ILYMPVSSPS PNFWGGNRTE EIPLATSVTA ADIETGEILW
     SQQLIHHDIW DYDTVAAPTL IDVEKDGETV PALVQTTKQG LFFVFDRVTG EPIWPIEEED
     VPPSTVEGEV AAPTQPIPRH PEPILDPDEW PGVWGLADTV SFGACSSFVE DLRNEGLYTP
     PTDEGNGTLL WPSFAGGLQW GGGSYDPTTG LYIANASIMV DYLQLIPREE YDALSEEEQN
     AKGSPFSYYA QEGAPYAVKT GKIMNGLGMP CWEPPFGVIA AYDMRTGEQV WKRPFGRTQR
     WGFYLPEAWG SPNIGGPAQT ATGLIFIGAS MDSRVRALSA ETGDELWSDL LEAPAVSNPA
     IFVHEGRQYV VFTGGGNYIL KPEVSDQVVA YALPE
//
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