Quinoprotein glucose dehydrogenase B

Details

Name
Quinoprotein glucose dehydrogenase B
Synonyms
  • 1.1.5.2
  • Glucose dehydrogenase B [pyrroloquinoline-quinone]
  • s-GDH
  • Soluble glucose dehydrogenase
Gene Name
gdhB
Organism
Acinetobacter calcoaceticus
Amino acid sequence
>lcl|BSEQ0020557|Quinoprotein glucose dehydrogenase B
MNKHLLAKIALLSAVQLVTLSAFADVPLTPSQFAKAKSENFDKKVILSNLNKPHALLWGP
DNQIWLTERATGKILRVNPESGSVKTVFQVPEIVNDADGQNGLLGFAFHPDFKNNPYIYI
SGTFKNPKSTDKELPNQTIIRRYTYNKSTDTLEKPVDLLAGLPSSKDHQSGRLVIGPDQK
IYYTIGDQGRNQLAYLFLPNQAQHTPTQQELNGKDYHTYMGKVLRLNLDGSIPKDNPSFN
GVVSHIYTLGHRNPQGLAFTPNGKLLQSEQGPNSDDEINLIVKGGNYGWPNVAGYKDDSG
YAYANYSAAANKSIKDLAQNGVKVAAGVPVTKESEWTGKNFVPPLKTLYTVQDTYNYNDP
TCGEMTYICWPTVAPSSAYVYKGGKKAITGWENTLLVPSLKRGVIFRIKLDPTYSTTYDD
AVPMFKSNNRYRDVIASPDGNVLYVLTDTAGNVQKDDGSVTNTLENPGSLIKFTYKAK
Number of residues
478
Molecular Weight
52772.255
Theoretical pI
9.27
GO Classification
Functions
metal ion binding / quinone binding / quinoprotein glucose dehydrogenase activity
Processes
carbohydrate metabolic process
General Function
Quinoprotein glucose dehydrogenase activity
Specific Function
Oxidizes glucose to gluconolactone.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0003426|1437 bp
ATGAATAAACATTTATTGGCTAAAATTGCTTTATTAAGCGCTGTTCAGCTAGTTACACTC
TCAGCATTTGCTGATGTTCCTCTAACTCCATCTCAATTTGCTAAAGCGAAATCAGAGAAC
TTTGACAAGAAAGTTATTCTATCTAATCTAAATAAGCCGCATGCTTTGTTATGGGGACCA
GATAATCAAATTTGGTTAACTGAGCGAGCAACAGGTAAGATTCTAAGAGTTAATCCAGAG
TCGGGTAGTGTAAAAACAGTTTTTCAGGTACCAGAGATTGTCAATGATGCTGATGGGCAG
AATGGTTTATTAGGTTTTGCCTTCCATCCTGATTTTAAAAATAATCCTTATATCTATATT
TCAGGTACATTTAAAAATCCGAAATCTACAGATAAAGAATTACCGAACCAAACGATTATT
CGTCGTTATACCTATAATAAATCAACAGATACGCTCGAGAAGCCAGTCGATTTATTAGCA
GGATTACCTTCATCAAAAGACCATCAGTCAGGTCGTCTTGTCATTGGGCCAGATCAAAAG
ATTTATTATACGATTGGTGACCAAGGGCGTAACCAGCTTGCTTATTTGTTCTTGCCAAAT
CAAGCACAACATACGCCAACTCAACAAGAACTGAATGGTAAAGACTATCACACCTATATG
GGTAAAGTACTACGCTTAAATCTTGATGGAAGTATTCCAAAGGATAATCCAAGTTTTAAC
GGGGTGGTTAGCCATATTTATACACTTGGACATCGTAATCCGCAGGGCTTAGCATTCACT
CCAAATGGTAAATTATTGCAGTCTGAACAAGGCCCAAACTCTGACGATGAAATTAACCTC
ATTGTCAAAGGTGGCAATTATGGTTGGCCGAATGTAGCAGGTTATAAAGATGATAGTGGC
TATGCTTATGCAAATTATTCAGCAGCAGCCAATAAGTCAATTAAGGATTTAGCTCAAAAT
GGAGTAAAAGTAGCCGCAGGGGTCCCTGTGACGAAAGAATCTGAATGGACTGGTAAAAAC
TTTGTCCCACCATTAAAAACTTTATATACCGTTCAAGATACCTACAACTATAACGATCCA
ACTTGTGGAGAGATGACCTACATTTGCTGGCCAACAGTTGCACCGTCATCTGCCTATGTC
TATAAGGGCGGTAAAAAAGCAATTACTGGTTGGGAAAATACATTATTGGTTCCATCTTTA
AAACGTGGTGTCATTTTCCGTATTAAGTTAGATCCAACTTATAGCACTACTTATGATGAC
GCTGTACCGATGTTTAAGAGCAACAACCGTTATCGTGATGTGATTGCAAGTCCAGATGGG
AATGTCTTATATGTATTAACTGATACTGCCGGAAATGTCCAAAAAGATGATGGCTCAGTA
ACAAATACATTAGAAAACCCAGGATCTCTCATTAAGTTCACCTATAAGGCTAAGTAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP13650
UniProtKB Entry NameDHGB_ACICA
GenBank Protein ID38708
GenBank Gene IDX15871
General References
  1. Cleton-Jansen AM, Goosen N, Vink K, van de Putte P: Cloning, characterization and DNA sequencing of the gene encoding the Mr 50,000 quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus. Mol Gen Genet. 1989 Jun;217(2-3):430-6. [Article]
  2. Oubrie A, Rozeboom HJ, Kalk KH, Duine JA, Dijkstra BW: The 1.7 A crystal structure of the apo form of the soluble quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus reveals a novel internal conserved sequence repeat. J Mol Biol. 1999 Jun 4;289(2):319-33. [Article]
  3. Oubrie A, Rozeboom HJ, Kalk KH, Olsthoorn AJ, Duine JA, Dijkstra BW: Structure and mechanism of soluble quinoprotein glucose dehydrogenase. EMBO J. 1999 Oct 1;18(19):5187-94. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB03205Pyrroloquinoline QuinoneexperimentalunknownDetails
DB02379Beta-D-GlucoseexperimentalunknownDetails
DB04361MethyldiazeneexperimentalunknownDetails