(data stored in SCRATCH zone)

SWISSPROT: C8U1J4_ECO10

ID   C8U1J4_ECO10            Unreviewed;       796 AA.
AC   C8U1J4;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   05-DEC-2018, entry version 53.
DE   SubName: Full=Glucose dehydrogenase {ECO:0000313|EMBL:BAI29002.1};
GN   Name=gcd {ECO:0000313|EMBL:BAI29002.1};
GN   OrderedLocusNames=ECO103_0124 {ECO:0000313|EMBL:BAI29002.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29002.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29002.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
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DR   EMBL; AP010958; BAI29002.1; -; Genomic_DNA.
DR   RefSeq; WP_000996827.1; NC_013353.1.
DR   EnsemblBacteria; BAI29002; BAI29002; ECO103_0124.
DR   KEGG; eoh:ECO103_0124; -.
DR   HOGENOM; HOG000116843; -.
DR   KO; K00117; -.
DR   OMA; LVWNWDS; -.
DR   BioCyc; ECOL585395:ECO103_RS00635-MONOMER; -.
DR   Proteomes; UP000000959; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; 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   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   PANTHER; PTHR32303:SF4; PTHR32303:SF4; 1.
DR   Pfam; PF01011; PQQ; 6.
DR   SMART; SM00564; PQQ; 6.
DR   SUPFAM; SSF50998; SSF50998; 1.
DR   TIGRFAMs; TIGR03074; PQQ_membr_DH; 1.
DR   PROSITE; PS00363; BACTERIAL_PQQ_1; 1.
DR   PROSITE; PS00364; BACTERIAL_PQQ_2; 1.
PE   4: Predicted;
DR   PRODOM; C8U1J4.
DR   SWISS-2DPAGE; C8U1J4.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     12     35       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     41     58       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     65     81       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    113    140       Helical. {ECO:0000256|SAM:Phobius}.
SQ   SEQUENCE   796 AA;  86773 MW;  5F12FE26CC71FAA3 CRC64;
     MAINNTGSRR LLVTLTALFA ALCGLYLLIG GGWLVAIGGS WYYPIAGLVM LGVAWMLWRS
     KRAALWLYAA LLLGTMIWGV WEVGFDFWAL TPRSDILVFF GIWLILPFVW RRLVIPASGA
     VAALVVALLI SGGILTWAGF NDPQEINGTL SANATPAEAI SPVADQDWPA YGRNQEGQRF
     SPLKQINADN VHNLKEAWVF RTGDVKQPND PGEITNEVTP IKVGDTLYLC TAHQRLFALD
     AASGKEKWHY DPELKTNESF QHVTCRGVSY HEAKAETASP EVMADCPRRI ILPVNDGRLI
     AINAENGKLC ETFANKGVLN LQSNMPDTKP GLYEPTSPPI ITDKTIVMAG SVTDNFSTRE
     TSGVIRGFDV NTGELLWAFD PGAKDPNAIP SDEHTFTFNS PNSWAPAAYD AKLDLVYLPM
     GVTTPDIWGG NRTPEQERYA SSILALNATT GKLAWSYQTV HHDLWDMDLP AQPTLADITV
     NGQKVPVIYA PAKTGNIFVL DRRNGELVVP APEKPVPQGA AKGDYVTPTQ PFSELSFRPK
     KDLSGADMWG ATMFDQLVCR VMFHQMRYEG IFTPPSEQGT LVFPGNLGMF EWGGISVDPN
     REVAIANPMA LPFVSKLIPR GPGNPMEQPK DAKGTGTESG IQPQYGVPYG VTLNPFLSPF
     GLPCKQPAWG YISALDLKTN EVVWKKRIGT PQDSMPFPMP VPVPFNMGMP MLGGPISTAG
     NVLFIAATAD NYLRAYNMSN GEKLWQGRLP AGGQATPMTY EVNGKQYVVI SAGGHGSFGT
     KMGDYIVAYA LPDDVK
//

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