Identification
Name:Quinoprotein glucose dehydrogenase
Synonyms:
  • Glucose dehydrogenase [pyrroloquinoline-quinone]
Gene Name:gcd
Enzyme Class:
Biological Properties
General Function:Involved in oxidoreductase activity, acting on CH-OH group of donors
Specific Function:GDH is probably involved in energy conservation rather than in sugar metabolism
Cellular Location:Cell inner membrane; Multi-pass membrane protein; Periplasmic side
SMPDB Pathways:Not Available
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb
EcoCyc Reactions:
1.0Thumb+1.0a ubiquinone1.0Thumb+1.0a ubiquinol
1.0b-D-Glucose + 1.0a ubiquinone → 1.0Gluconolactone + 1.0a ubiquinol
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb+1.0Thumb
1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb
Metabolites:
ECMDB IDNameView
ECMDB00516b-D-GlucoseMetaboCard
ECMDB00122D-GlucoseMetaboCard
ECMDB00625Gluconic acidMetaboCard
ECMDB00150GluconolactoneMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB21461Pyrroloquinoline quinoneMetaboCard
ECMDB21574Ubiquinol-1MetaboCard
ECMDB01060Ubiquinol-8MetaboCard
ECMDB21438Ubiquinone-1MetaboCard
ECMDB01072Ubiquinone-10MetaboCard
ECMDB21296Ubiquinone-8MetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Component
cell part
integral to membrane
intrinsic to membrane
membrane part
outer membrane-bounded periplasmic space
periplasmic space
Function
binding
catalytic activity
cofactor binding
oxidoreductase activity
oxidoreductase activity, acting on CH-OH group of donors
quinone binding
Process
metabolic process
oxidation reduction
Gene Properties
Blattner:b0124
Gene OrientationCounterclockwise
Centisome Percentage:2.99
Left Sequence End138835
Right Sequence End141225
Gene Sequence:
>2391 bp
ATGGCAATTAACAATACAGGCTCGCGACGATTACTCGTCACGCTAACAGCCCTTTTTGCA
GCGCTTTGCGGGCTGTATCTACTCATTGGCGGAGGCTGGCTGGTCGCGATTGGCGGCTCC
TGGTACTACCCTATCGCTGGCCTTGTGATGCTCGGCGTCGCCTGGATGCTGTGGCGCAGT
AAACGCGCCGCGCTTTGGCTATACGCAGCCCTGCTGCTCGGCACCATGATTTGGGGCGTC
TGGGAAGTTGGTTTCGACTTCTGGGCGCTGACTCCGCGCAGCGACATTCTGGTCTTCTTC
GGCATCTGGCTGATCCTGCCGTTTGTCTGGCGTCGCCTGGTCATTCCTGCCAGCGGCGCA
GTTGCCGCACTGGTGGTCGCACTGCTGATTAGCGGTGGTATCCTGACCTGGGCCGGATTT
AACGATCCGCAGGAGATCAACGGCACCTTAAGCGCCGATGCCACACCTGCTGAAGCTATC
TCCCCCGTAGCCGATCAGGACTGGCCTGCCTATGGTCGTAATCAGGAAGGTCAACGCTTT
TCGCCGCTGAAACAAATTAACGCCGATAACGTCCATAATCTGAAAGAAGCCTGGGTGTTC
CGTACTGGCGATGTGAAGCAGCCGAACGATCCGGGTGAAATCACCAATGAAGTGACGCCG
ATTAAAGTGGGCGACACCCTTTACCTGTGTACCGCTCACCAGCGCCTGTTTGCGCTTGAT
GCCGCCAGCGGCAAAGAGAAATGGCATTACGATCCTGAGCTGAAAACCAACGAGTCTTTC
CAGCACGTAACCTGCCGTGGTGTCTCTTATCATGAAGCCAAAGCAGAAACCGCTTCGCCG
GAAGTGATGGCGGATTGCCCGCGTCGTATCATTCTTCCGGTCAATGATGGTCGACTGATT
GCGATTAACGCTGAAAACGGCAAACTGTGCGAAACCTTCGCCAATAAAGGCGTGCTCAAT
CTGCAAAGCAATATGCCAGACACCAAACCGGGTCTGTATGAACCGACTTCGCCACCGATT
ATCACCGATAAAACCATCGTGATGGCCGGTTCAGTTACCGATAACTTCTCAACCCGCGAA
ACGTCTGGCGTGATCCGTGGTTTTGATGTCAACACCGGGGAGCTGCTGTGGGCTTTTGAT
CCCGGCGCGAAAGATCCGAACGCAATCCCGTCTGACGAACACACCTTTACCTTTAACTCG
CCAAACTCCTGGGCACCAGCGGCCTATGACGCGAAGCTGGATCTGGTCTATCTGCCGATG
GGCGTGACCACGCCGGATATCTGGGGCGGTAACCGCACACCGGAACAGGAACGTTATGCC
AGCTCGATTCTGGCGCTGAATGCCACTACCGGGAAACTGGCGTGGAGCTACCAGACCGTT
CACCACGACCTGTGGGACATGGATCTTCCGGCACAGCCGACGCTGGCGGACATCACCGTT
AATGGTCAGAAAGTGCCAGTTATTTACGCTCCGGCGAAAACCGGCAACATTTTTGTGCTC
GATCGTCGTAATGGCGAACTGGTGGTTCCGGCACCGGAAAAACCGGTTCCCCAAGGTGCA
GCGAAAGGCGATTACGTAACCCCAACTCAACCGTTTTCTGAACTGAGCTTCCGTCCGACG
AAAGATTTGAGCGGTGCGGATATGTGGGGAGCCACCATGTTTGACCAACTGGTGTGCCGC
GTGATGTTCCACCAGATGCGCTATGAAGGCATTTTCACCCCGCCATCTGAACAGGGTACG
CTGGTCTTCCCGGGTAACCTGGGGATGTTCGAATGGGGCGGGATTTCCGTTGATCCAAAT
CGTGAAGTGGCGATTGCCAACCCAATGGCACTGCCGTTTGTTTCGAAACTGATCCCGCGT
GGTCCTGGCAACCCGATGGAGCAGCCGAAAGATGCCAAAGGCACGGGTACGGAATCCGGC
ATTCAGCCACAGTACGGTGTACCGTATGGTGTCACGCTCAACCCGTTCCTCTCACCATTT
GGTCTGCCATGTAAACAGCCAGCATGGGGTTATATCTCGGCGCTGGATCTGAAAACTAAT
GAAGTGGTGTGGAAGAAACGTATTGGTACGCCGCAGGACAGTATGCCGTTCCCGATGCCG
GTTCCGGTGCCGTTCAATATGGGTATGCCGATGCTGGGCGGGCCAATCTCCACGGCGGGT
AACGTGCTGTTTATCGCCGCTACGGCAGATAACTACCTGCGCGCTTACAACATGAGCAAC
GGTGAAAAACTGTGGCAGGGTCGTTTACCAGCGGGTGGTCAGGCTACGCCAATGACCTAT
GAAGTGAATGGTAAGCAGTATGTGGTGATCTCCGCAGGCGGTCACGGTTCATTTGGTACG
AAGATGGGCGACTATATTGTGGCTTATGCGCTGCCGGATGATGTGAAGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:796
Protein Molecular Weight:86747
Protein Theoretical pI:5
Signaling Regions:
  • None
Transmembrane Regions:
  • 11-37
  • 41-58
  • 63-81
  • 96-110
  • 119-141
Protein Sequence:
>Quinoprotein glucose dehydrogenase
MAINNTGSRRLLVTLTALFAALCGLYLLIGGGWLVAIGGSWYYPIAGLVMLGVAWMLWRS
KRAALWLYAALLLGTMIWGVWEVGFDFWALTPRSDILVFFGIWLILPFVWRRLVIPASGA
VAALVVALLISGGILTWAGFNDPQEINGTLSADATPAEAISPVADQDWPAYGRNQEGQRF
SPLKQINADNVHNLKEAWVFRTGDVKQPNDPGEITNEVTPIKVGDTLYLCTAHQRLFALD
AASGKEKWHYDPELKTNESFQHVTCRGVSYHEAKAETASPEVMADCPRRIILPVNDGRLI
AINAENGKLCETFANKGVLNLQSNMPDTKPGLYEPTSPPIITDKTIVMAGSVTDNFSTRE
TSGVIRGFDVNTGELLWAFDPGAKDPNAIPSDEHTFTFNSPNSWAPAAYDAKLDLVYLPM
GVTTPDIWGGNRTPEQERYASSILALNATTGKLAWSYQTVHHDLWDMDLPAQPTLADITV
NGQKVPVIYAPAKTGNIFVLDRRNGELVVPAPEKPVPQGAAKGDYVTPTQPFSELSFRPT
KDLSGADMWGATMFDQLVCRVMFHQMRYEGIFTPPSEQGTLVFPGNLGMFEWGGISVDPN
REVAIANPMALPFVSKLIPRGPGNPMEQPKDAKGTGTESGIQPQYGVPYGVTLNPFLSPF
GLPCKQPAWGYISALDLKTNEVVWKKRIGTPQDSMPFPMPVPVPFNMGMPMLGGPISTAG
NVLFIAATADNYLRAYNMSNGEKLWQGRLPAGGQATPMTYEVNGKQYVVISAGGHGSFGT
KMGDYIVAYALPDDVK
References
External Links:
ResourceLink
Uniprot ID:P15877
Uniprot Name:DHG_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:21238978
Ecogene ID:EG10369
Ecocyc:EG10369
ColiBase:b0124
Kegg Gene:b0124
EchoBASE ID:EB0364
CCDB:DHG_ECOLI
BacMap:16128117
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, 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. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Cleton-Jansen, A. M., Goosen, N., Fayet, O., van de Putte, P. (1990). "Cloning, mapping, and sequencing of the gene encoding Escherichia coli quinoprotein glucose dehydrogenase." J Bacteriol 172:6308-6315. Pubmed: 2228962
  • Cozier, G. E., Anthony, C. (1995). "Structure of the quinoprotein glucose dehydrogenase of Escherichia coli modelled on that of methanol dehydrogenase from Methylobacterium extorquens." Biochem J 312 ( Pt 3):679-685. Pubmed: 8554505
  • Daley, D. O., Rapp, M., Granseth, E., Melen, K., Drew, D., von Heijne, G. (2005). "Global topology analysis of the Escherichia coli inner membrane proteome." Science 308:1321-1323. Pubmed: 15919996
  • Fujita, N., Mori, H., Yura, T., Ishihama, A. (1994). "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. Pubmed: 8202364
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Stenberg, F., Chovanec, P., Maslen, S. L., Robinson, C. V., Ilag, L. L., von Heijne, G., Daley, D. O. (2005). "Protein complexes of the Escherichia coli cell envelope." J Biol Chem 280:34409-34419. Pubmed: 16079137
  • Yamada, M., Asaoka, S., Saier, M. H. Jr, Yamada, Y. (1993). "Characterization of the gcd gene from Escherichia coli K-12 W3110 and regulation of its expression." J Bacteriol 175:568-571. Pubmed: 8419307
  • Yamada, M., Sumi, K., Matsushita, K., Adachi, O., Yamada, Y. (1993). "Topological analysis of quinoprotein glucose dehydrogenase in Escherichia coli and its ubiquinone-binding site." J Biol Chem 268:12812-12817. Pubmed: 8509415