Entry Information
Protein Name Gcd
Accession No P15877
Protein description Quinoprotein glucose dehydrogenase
pI/Mw (Da)
Theoretical Experimental
5.4/86747.35 -
Protein function and expression Probably involved in energy conservation rather than in sugar metabolism.
Reference(s) Lopez-Campistrous, A., P. Semchuk, L. Burke, T. Palmer-Stone, S. J. Brokx, G. Broderick, D. Bottorff, S. Bolch, J. H. Weiner, and M. J. Ellison. 2005. Localization, annotation & comparison of the Escherichia coli K-12 proteome under two states of growth. Mol. Cell. Proteomics 4:1205-1209. (NCBI)

Swiss-Prot Database Reference

Entry information
Entry Name DHG_ECOLI
Primary accession number P15877
Secondary accession numbers
Integrated into Swiss-Prot on 1990-04-01
Sequence was last modified on 1997-11-01 (Sequence version 3)
Annotations were last modified on 2006-09-05 (Entry version 75)
Name and origin of the protein
Protein name Quinoprotein glucose dehydrogenase
Synonyms EC 1.1.5.2 Quinoprotein glucose dehydrogenase
Glucose dehydrogenase [pyrroloquinoline-quinone]
Gene name Name : gcd
OrderedLocusName : b0124
From Escherichia coli [TaxID:562] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia;
References
[1] NUCLEOTIDE SEQUENCE [GENOMIC DNA].
strain = K12
PubMed=2228962[NCBI, ExPASy, EBI, Israel, Japan]
Cleton-Jansen A.-M. , Goosen N. , Fayet O. , van de Putte P. ,
"Cloning, mapping, and sequencing of the gene encoding Escherichia coli quinoprotein glucose dehydrogenase."
J. Bacteriol.172:6308-6315(1990) 
[2] NUCLEOTIDE SEQUENCE [GENOMIC DNA].
strain = K12 / W3110 / ATCC 27325 / DSM 5911
PubMed=8419307[NCBI, ExPASy, EBI, Israel, Japan]
Yamada M. , Asaoka S. , Saier M.H. Jr. , Yamada Y. ,
"Characterization of the gcd gene from Escherichia coli K-12 W3110 and regulation of its expression."
J. Bacteriol.175:568-571(1993) 
[3] NUCLEOTIDE SEQUENCE [GENOMIC DNA].
strain = K12 / W3110 / ATCC 27325 / DSM 5911
PubMed=8202364[NCBI, ExPASy, EBI, Israel, Japan]
Fujita N. , Mori H. , Yura T. , Ishihama A. ,
"Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region."
Nucleic Acids Res.22:1637-1639(1994) 
[4] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
strain = K12 / MG1655 / ATCC 47076
DOI=10.1126/science.277.5331.1453;PubMed=9278503[NCBI, ExPASy, EBI, Israel, Japan]
Blattner F.R. , Plunkett G. III , Bloch C.A. , Perna N.T. , Burland V. , Riley M. , Collado-Vides J. , Glasner J.D. , Rode C.K. , Mayhew G.F. , Gregor J. , Davis N.W. , Kirkpatrick H.A. , Goeden M.A. , Rose D.J. , Mau B. , Shao Y. ,
"The complete genome sequence of Escherichia coli K-12."
Science277:1453-1474(1997) 
[5] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
strain = K12 / W3110 / ATCC 27325 / DSM 5911
DOI=10.1038/msb4100049;
Hayashi K. , Morooka N. , Yamamoto Y. , Fujita K. , Isono K. , Choi S. , Ohtsubo E. , Baba T. , Wanner B.L. , Mori H. , Horiuchi T. ,
"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Mol. Syst. Biol.2:E1-E5(2006) 
[6] TOPOLOGY.PubMed=8509415[NCBI, ExPASy, EBI, Israel, Japan]
Yamada M. , Sumi K. , Matsushita K. , Adachi O. , Yamada Y. ,
"Topological analysis of quinoprotein glucose dehydrogenase in Escherichia coli and its ubiquinone-binding site."
J. Biol. Chem.268:12812-12817(1993) 
[7] SUBCELLULAR LOCATION.
strain = BL21-DE3
DOI=10.1074/jbc.M506479200;PubMed=16079137[NCBI, ExPASy, EBI, Israel, Japan]
Stenberg F. , Chovanec P. , Maslen S.L. , Robinson C.V. , Ilag L. , von Heijne G. , Daley D.O. ,
"Protein complexes of the Escherichia coli cell envelope."
J. Biol. Chem.280:34409-34419(2005) 
[8] SUBCELLULAR LOCATION.
strain = K12 / MG1655 / ATCC 47076
DOI=10.1126/science.1109730;PubMed=15919996[NCBI, ExPASy, EBI, Israel, Japan]
Daley D.O. , Rapp M. , Granseth E. , Melen K. , Drew D. , von Heijne G. ,
"Global topology analysis of the Escherichia coli inner membrane proteome."
Science308:1321-1323(2005) 
[9] 3D-STRUCTURE MODELING.PubMed=8554505[NCBI, ExPASy, EBI, Israel, Japan]
Cozier G.E. , Anthony C. ,
"Structure of the quinoprotein glucose dehydrogenase of Escherichia coli modelled on that of methanol dehydrogenase from Methylobacterium extorquens."
Biochem. J.312:679-685(1995) 
Comments
  • FUNCTION : GDH is probably involved in energy conservation rather than in sugar metabolism
  • CATALYTIC ACTIVITY : D-glucose + ubiquinone = D-glucono-1,5-lactone + ubiquinol
  • COFACTOR : PQQ
  • SUBUNIT : Monomer
  • INTERACTION:
        Q46925:csdA; NbExp=1; InAct=EBI-545666, EBI-545660
        P37346:ycfH; NbExp=1; InAct=EBI-545666, EBI-560527
  • SUBCELLULAR LOCATION : Bacterial cell inner membrane; multi-pass membrane protein
  • SIMILARITY : Belongs to the bacterial PQQ dehydrogenase family
  • Copyright
    Copyrighted by the UniProt Consortium, see http://www.uniprot.org/. Distributed under the Creative Commons Attribution-NoDerivs License.
    Cross-reference
    Sequence databases
    EMBL X51323;CAA35706.1;-;Genomic_DNA [EMBL/GenBank/DDBJ][CoDingSequence].
    D12651;BAA02174.1;-;Genomic_DNA [EMBL/GenBank/DDBJ][CoDingSequence].
    U00096;AAC73235.1;-;Genomic_DNA [EMBL/GenBank/DDBJ][CoDingSequence].
    AP009048;BAB96699.1;-;Genomic_DNA [EMBL/GenBank/DDBJ][CoDingSequence].
    PIR D64735;JV0107.
    3D structure databases
    HSSP P38539;1G72[HSSP ENTRY / PDB].
    ModBase P15877
    Protein-protein interaction databases
    IntAct P15877;-.
    DIP P15877
    Enzyme and pathway databases
    BioCyc EcoCyc:GLUCDEHYDROG-MONOMER;-.
    2D gel databases
    SWISS-2DPAGE Get region on 2D PAGE
    Organism-specific gene databases
    EchoBASE EB0364;-.
    EcoGene EG10369;gcd.
    HOGENOM [Family / Alignment / Tree]
    Family and domain databases
    InterPro IPR001479;PQQ_bac.
    IPR002372;PQQ_repeat.
    IPR011047;Quino_alc_DH.
    Graphical view of domain structure
    Pfam PF01011;PQQ;3.
    Pfam graphical view of domain structure
    SMART SM00564;PQQ;2.
    SMART graphical view of domain structure
    BLOCKS P15877
    PROSITE PS00363;BACTERIAL_PQQ_1;1.
    PS00364;BACTERIAL_PQQ_2;1.
    Genome annotation databases
    GenomeReviews U00096_GR;b0124.
    Ontology
    GO GO:0005515;Molecular Function:protein binding(inferred from physical interaction)
    QuickGo View.
    Other
    ProtoNet P15877
    UniRef View cluster of proteins with at least 50% / 90% / 100% identity
    Keyword
    Complete proteome; Inner membrane; Membrane; Oxidoreductase; Periplasmic; PQQ; Transmembrane;
    Features
    Feature table viewer Feature aligner
    Key  From   To Length  Description  FTId
    CHAIN    1   796    796  Quinoprotein glucose dehydrogenase  PRO_0000205339
    TOPO_DOM    1    10     10  Cytoplasmic(probable)  
    TRANSMEM   11    37     27  (probable)  
    TOPO_DOM   38    40      3  Periplasmic(probable)  
    TRANSMEM   41    58     18  (probable)  
    TOPO_DOM   59    62      4  Cytoplasmic(probable)  
    TRANSMEM   63    81     19  (probable)  
    TOPO_DOM   82    95     14  Periplasmic(probable)  
    TRANSMEM   96   110     15  (probable)  
    TOPO_DOM  111   118      8  Cytoplasmic(probable)  
    TRANSMEM  119   141     23  (probable)  
    TOPO_DOM  142   796    655  Periplasmic(probable)  
    ACT_SITE  466   466    Proton acceptor(probable)  
    CONFLICT   59    59    R -> L: (in Ref. 1)  
    CONFLICT  149   156    TLSADATP -> HLKRRCHT: (in Ref. 1 and 2)  
    CONFLICT  193   193    N -> K: (in Ref. 1 and 2)  
    CONFLICT  666   666    Q -> H: (in Ref. 2)  
    Sequence information
    Length: 796AA [This is the length of the unprocessed precursor] Molecular weight: 86747Da [This is the MW of the unprocessed precursor] CRC64: D9EDC705A12894E9[This is a checksum on the sequence]
            10         20         30         40         50         60
    MAINNTGSRR LLVTLTALFA ALCGLYLLIG GGWLVAIGGS WYYPIAGLVM LGVAWMLWRS
            70         80         90        100        110        120
    KRAALWLYAA LLLGTMIWGV WEVGFDFWAL TPRSDILVFF GIWLILPFVW RRLVIPASGA
           130        140        150        160        170        180
    VAALVVALLI SGGILTWAGF NDPQEINGTL SADATPAEAI SPVADQDWPA YGRNQEGQRF
           190        200        210        220        230        240
    SPLKQINADN VHNLKEAWVF RTGDVKQPND PGEITNEVTP IKVGDTLYLC TAHQRLFALD
           250        260        270        280        290        300
    AASGKEKWHY DPELKTNESF QHVTCRGVSY HEAKAETASP EVMADCPRRI ILPVNDGRLI
           310        320        330        340        350        360
    AINAENGKLC ETFANKGVLN LQSNMPDTKP GLYEPTSPPI ITDKTIVMAG SVTDNFSTRE
           370        380        390        400        410        420
    TSGVIRGFDV NTGELLWAFD PGAKDPNAIP SDEHTFTFNS PNSWAPAAYD AKLDLVYLPM
           430        440        450        460        470        480
    GVTTPDIWGG NRTPEQERYA SSILALNATT GKLAWSYQTV HHDLWDMDLP AQPTLADITV
           490        500        510        520        530        540
    NGQKVPVIYA PAKTGNIFVL DRRNGELVVP APEKPVPQGA AKGDYVTPTQ PFSELSFRPT
           550        560        570        580        590        600
    KDLSGADMWG ATMFDQLVCR VMFHQMRYEG IFTPPSEQGT LVFPGNLGMF EWGGISVDPN
           610        620        630        640        650        660
    REVAIANPMA LPFVSKLIPR GPGNPMEQPK DAKGTGTESG IQPQYGVPYG VTLNPFLSPF
           670        680        690        700        710        720
    GLPCKQPAWG YISALDLKTN EVVWKKRIGT PQDSMPFPMP VPVPFNMGMP MLGGPISTAG
           730        740        750        760        770        780
    NVLFIAATAD NYLRAYNMSN GEKLWQGRLP AGGQATPMTY EVNGKQYVVI SAGGHGSFGT
           790 
    KMGDYIVAYA LPDDVK
    P15877 in FASTA format