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Database: UniProt
Entry: Q0T876_SHIF8
LinkDB: Q0T876_SHIF8
Original site: Q0T876_SHIF8 
ID   Q0T876_SHIF8            Unreviewed;       802 AA.
AC   Q0T876;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   27-MAR-2024, entry version 87.
DE   SubName: Full=Glucose dehydrogenase {ECO:0000313|EMBL:ABF02400.1};
GN   Name=gcd {ECO:0000313|EMBL:ABF02400.1};
GN   OrderedLocusNames=SFV_0115 {ECO:0000313|EMBL:ABF02400.1};
OS   Shigella flexneri serotype 5b (strain 8401).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=373384 {ECO:0000313|EMBL:ABF02400.1, ECO:0000313|Proteomes:UP000000659};
RN   [1] {ECO:0000313|EMBL:ABF02400.1, ECO:0000313|Proteomes:UP000000659}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=8401 {ECO:0000313|EMBL:ABF02400.1,
RC   ECO:0000313|Proteomes:UP000000659};
RX   PubMed=16822325; DOI=10.1186/1471-2164-7-173;
RA   Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z., Peng J.,
RA   Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y., Jin Q.;
RT   "Complete genome sequence of Shigella flexneri 5b and comparison with
RT   Shigella flexneri 2a.";
RL   BMC Genomics 7:173-173(2006).
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; CP000266; ABF02400.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q0T876; -.
DR   KEGG; sfv:SFV_0115; -.
DR   HOGENOM; CLU_018478_1_0_6; -.
DR   Proteomes; UP000000659; Chromosome.
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; 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   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; 6.
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   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        21..41
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..87
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        119..146
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          626..645
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   802 AA;  87608 MW;  B5492065DC3EBDCE CRC64;
     MKWCLFMAIN NTGSRRLLVT LTALFAALCG LYLLIGGGWL VAIGGSWYYP IAGLVMLGVA
     WMLWRSKRAA LWLYAALLLG TMIWGVWEVG FDFWALTPRS DILVFFGIWL ILPFVWRRLV
     IPASGAVAAL VVALLISGGI LTWAGFNDPQ EINGTLSADA TPAEAISPVA DQDWPAYGRN
     QEGQRFSPLK QIHADNVHKL KEAWVFRTGD VKQPNDPGEI TNEVTPIKVG DTLYLCTAHQ
     RLFALDAASG KEKWHYDPEL KTNESFQHVT CRGVSYHEAK AETASPEVMA DCPRRIILPV
     NDGRLIAINA ENGKLCETFA NKGVLNLQSN MPDTKPGLYE PTSPPIITDK TIVMAGSVTD
     NFSTRETSGV IRGFDVNTGE LLWAFDPGAK DPNAIPSDEH TFTFNSPNSW APAAYDAKLD
     LVYLPMGVTT PDIWGGNRTP EQERYASSIL ALNATTGKLA WSYQTVHHDL WDMDLPAQPT
     LADITVNGQK VPIIYAPAKT GNIFVLDRRN GELVVPAPEK PVPQGAAKGD YVTPTQPFSE
     LSFRPTKDLS GADMWGATMF DQLVCRVMFH QMRYEGIFTP PSEQGTLVFP GNLGMFEWGG
     ISVDPNREVA IANPMALPFV SKLLPRGPGN PMEQPKDAKG TGTESGIQPQ YGVPYGVTLN
     PFLSPFGLPC KQPAWGYISA LDLKTNEVVW KKRIGTPQDS MPFPMPVPVP FNMGMPMLGG
     PISTAGNVLF IAATADNYLR AYNMSNGEKL WQGRLPAGGQ ATPMTYEVNG KQYVVISAGG
     HGSFGTKMGD YIVAYALPDD VK
//
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