Beta-glucuronidase (P05804)

Identification
Name:Beta-glucuronidase
Synonyms:
  • GUS
  • Beta-D-glucuronoside glucuronosohydrolase
Gene Name:uidA
Enzyme Class:
Biological Properties
General Function:Involved in hydrolase activity, hydrolyzing O-glycosyl compounds
Specific Function:A beta-D-glucuronoside + H(2)O = D-glucuronate + an alcohol
Cellular Location:Cytoplasmic
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0beta-D-Glucuronoside+1.0Thumb ↔ 1.0Thumb+1.0Alcohol+1.0Alcohol
1.0Water + 1.0beta-D-Glucuronoside + 1.0beta-D-Glucuronoside ↔ 1.0D-Glucuronic acid + 1.0Alcohol + 1.0Alcohol
ReactionCard
1.0Thumb+2.0Thumb+3.0Reduced acceptor ↔ 1.0Thumb+2.0Thumb+3.0Acceptor
1.0Bilirubin diglucuronide + 2.0Water + 3.0Reduced acceptor ↔ 1.0D-Urobilinogen + 2.0D-Glucuronic acid + 3.0Acceptor
ReactionCard
1.0G13040+1.0Thumb ↔ 1.0G09660+1.0Thumb
1.0G13040 + 1.0Water ↔ 1.0G09660 + 1.0D-Glucuronic acid
ReactionCard
1.0Luteolin 7-O-[beta-D-glucuronosyl-(1->2)-beta-D-glucuronide]-4'-O-beta-D-glucuronide+1.0Thumb ↔ 1.0Luteolin 7-O-[beta-D-glucuronosyl-(1->2)-beta-D-glucuronide]+1.0Thumb
1.0Luteolin 7-O-[beta-D-glucuronosyl-(1->2)-beta-D-glucuronide]-4'-O-beta-D-glucuronide + 1.0Water ↔ 1.0Luteolin 7-O-[beta-D-glucuronosyl-(1->2)-beta-D-glucuronide] + 1.0D-Glucuronic acid
ReactionCard
1.0SN38 glucuronide+1.0Thumb ↔ 1.0SN-38+1.0Thumb
1.0SN38 glucuronide + 1.0Water ↔ 1.0SN-38 + 1.0D-Glucuronic acid
ReactionCard
SMPDB Reactions:
1.0Bilirubin diglucuronide+1.0Thumb → 1.0Thumb+1.0D-glucuronate
1.0Bilirubin diglucuronide + 1.0Water → 1.0Benzyl alcohol + 1.0D-glucuronate
ReactionCard
1.0Bilirubin diglucuronide+1.0Thumb → 1.0Thumb+1.0Ribitol+1.0Thumb
1.0Bilirubin diglucuronide + 1.0Water → 1.0D-Glucuronic acid + 1.0Ribitol + 1.0Ribitol
ReactionCard
Complex Reactions:
1.0A beta-D-glucuronoside+1.0Thumb → 1.0Thumb+1.0an alcohol
1.0A beta-D-glucuronoside + 1.0Water → 1.0D-Glucuronic acid + 1.0an alcohol
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB24002Benzyl alcoholMetaboCard
ECMDB23833beta-D-GlucuronosideMetaboCard
ECMDB03325Bilirubin diglucuronideMetaboCard
ECMDB04073D-Glucuronic acidMetaboCard
ECMDB21000D-UrobilinogenMetaboCard
ECMDB21421RibitolMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
binding
catalytic activity
cation binding
hydrolase activity
hydrolase activity, acting on glycosyl bonds
hydrolase activity, hydrolyzing O-glycosyl compounds
ion binding
Process
carbohydrate metabolic process
metabolic process
primary metabolic process
Gene Properties
Blattner:b1617
Gene OrientationCounterclockwise
Centisome Percentage:36.47
Left Sequence End1692284
Right Sequence End1694095
Gene Sequence:
>1812 bp
ATGTTACGTCCTGTAGAAACCCCAACCCGTGAAATCAAAAAACTCGACGGCCTGTGGGCA
TTCAGTCTGGATCGCGAAAACTGTGGAATTGATCAGCGTTGGTGGGAAAGCGCGTTACAA
GAAAGCCGGGCAATTGCTGTGCCAGGCAGTTTTAACGATCAGTTCGCCGATGCAGATATT
CGTAATTATGCGGGCAACGTCTGGTATCAGCGCGAAGTCTTTATACCGAAAGGTTGGGCA
GGCCAGCGTATCGTGCTGCGTTTCGATGCGGTCACTCATTACGGCAAAGTGTGGGTCAAT
AATCAGGAAGTGATGGAGCATCAGGGCGGCTATACGCCATTTGAAGCCGATGTCACGCCG
TATGTTATTGCCGGGAAAAGTGTACGTATCACCGTTTGTGTGAACAACGAACTGAACTGG
CAGACTATCCCGCCGGGAATGGTGATTACCGACGAAAACGGCAAGAAAAAGCAGTCTTAC
TTCCATGATTTCTTTAACTATGCCGGGATCCATCGCAGCGTAATGCTCTACACCACGCCG
AACACCTGGGTGGACGATATCACCGTGGTGACGCATGTCGCGCAAGACTGTAACCACGCG
TCTGTTGACTGGCAGGTGGTGGCCAATGGTGATGTCAGCGTTGAACTGCGTGATGCGGAT
CAACAGGTGGTTGCAACTGGACAAGGCACTAGCGGGACTTTGCAAGTGGTGAATCCGCAC
CTCTGGCAACCGGGTGAAGGTTATCTCTATGAACTGTGCGTCACAGCCAAAAGCCAGACA
GAGTGTGATATCTACCCGCTTCGCGTCGGCATCCGGTCAGTGGCAGTGAAGGGCGAACAG
TTCCTGATTAACCACAAACCGTTCTACTTTACTGGCTTTGGTCGTCATGAAGATGCGGAC
TTGCGTGGCAAAGGATTCGATAACGTGCTGATGGTGCACGACCACGCATTAATGGACTGG
ATTGGGGCCAACTCCTACCGTACCTCGCATTACCCTTACGCTGAAGAGATGCTCGACTGG
GCAGATGAACATGGCATCGTGGTGATTGATGAAACTGCTGCTGTCGGCTTTAACCTCTCT
TTAGGCATTGGTTTCGAAGCGGGCAACAAGCCGAAAGAACTGTACAGCGAAGAGGCAGTC
AACGGGGAAACTCAGCAAGCGCACTTACAGGCGATTAAAGAGCTGATAGCGCGTGACAAA
AACCACCCAAGCGTGGTGATGTGGAGTATTGCCAACGAACCGGATACCCGTCCGCAAGGT
GCACGGGAATATTTCGCGCCACTGGCGGAAGCAACGCGTAAACTCGACCCGACGCGTCCG
ATCACCTGCGTCAATGTAATGTTCTGCGACGCTCACACCGATACCATCAGCGATCTCTTT
GATGTGCTGTGCCTGAACCGTTATTACGGATGGTATGTCCAAAGCGGCGATTTGGAAACG
GCAGAGAAGGTACTGGAAAAAGAACTTCTGGCCTGGCAGGAGAAACTGCATCAGCCGATT
ATCATCACCGAATACGGCGTGGATACGTTAGCCGGGCTGCACTCAATGTACACCGACATG
TGGAGTGAAGAGTATCAGTGTGCATGGCTGGATATGTATCACCGCGTCTTTGATCGCGTC
AGCGCCGTCGTCGGTGAACAGGTATGGAATTTCGCCGATTTTGCGACCTCGCAAGGCATA
TTGCGCGTTGGCGGTAACAAGAAAGGGATCTTCACTCGCGACCGCAAACCGAAGTCGGCG
GCTTTTCTGCTGCAAAAACGCTGGACTGGCATGAACTTCGGTGAAAAACCGCAGCAGGGA
GGCAAACAATGA
Protein Properties
Pfam Domain Function:
Protein Residues:603
Protein Molecular Weight:68447
Protein Theoretical pI:5
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Beta-glucuronidase
MLRPVETPTREIKKLDGLWAFSLDRENCGIDQRWWESALQESRAIAVPGSFNDQFADADI
RNYAGNVWYQREVFIPKGWAGQRIVLRFDAVTHYGKVWVNNQEVMEHQGGYTPFEADVTP
YVIAGKSVRITVCVNNELNWQTIPPGMVITDENGKKKQSYFHDFFNYAGIHRSVMLYTTP
NTWVDDITVVTHVAQDCNHASVDWQVVANGDVSVELRDADQQVVATGQGTSGTLQVVNPH
LWQPGEGYLYELCVTAKSQTECDIYPLRVGIRSVAVKGEQFLINHKPFYFTGFGRHEDAD
LRGKGFDNVLMVHDHALMDWIGANSYRTSHYPYAEEMLDWADEHGIVVIDETAAVGFNLS
LGIGFEAGNKPKELYSEEAVNGETQQAHLQAIKELIARDKNHPSVVMWSIANEPDTRPQG
AREYFAPLAEATRKLDPTRPITCVNVMFCDAHTDTISDLFDVLCLNRYYGWYVQSGDLET
AEKVLEKELLAWQEKLHQPIIITEYGVDTLAGLHSMYTDMWSEEYQCAWLDMYHRVFDRV
SAVVGEQVWNFADFATSQGILRVGGNKKGIFTRDRKPKSAAFLLQKRWTGMNFGEKPQQG
GKQ
References
External Links:
ResourceLink
Uniprot ID:P05804
Uniprot Name:BGLR_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:1742671
Ecogene ID:EG11055
Ecocyc:EG11055
ColiBase:b1617
Kegg Gene:b1617
EchoBASE ID:EB1048
CCDB:BGLR_ECOLI
BacMap:16129575
General Reference:
  • Aiba, H., Baba, T., Hayashi, K., Inada, T., Isono, K., Itoh, T., Kasai, H., Kashimoto, K., Kimura, S., Kitakawa, M., Kitagawa, M., Makino, K., Miki, T., Mizobuchi, K., Mori, H., Mori, T., Motomura, K., Nakade, S., Nakamura, Y., Nashimoto, H., Nishio, Y., Oshima, T., Saito, N., Sampei, G., Horiuchi, T., et, a. l. .. (1996). "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map." DNA Res 3:363-377. Pubmed: 9097039
  • Blanco, C., Nemoz, G. (1987). "One step purification of Escherichia coli beta-glucuronidase." Biochimie 69:157-161. Pubmed: 3105604
  • 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
  • Farrell, L. B., Beachy, R. N. (1990). "Manipulation of beta-glucuronidase for use as a reporter in vacuolar targeting studies." Plant Mol Biol 15:821-825. Pubmed: 2103475
  • 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
  • Jefferson, R. A., Burgess, S. M., Hirsh, D. (1986). "beta-Glucuronidase from Escherichia coli as a gene-fusion marker." Proc Natl Acad Sci U S A 83:8447-8451. Pubmed: 3534890
  • Schlaman, H. R., Risseeuw, E., Franke-van Dijk, M. E., Hooykaas, P. J. (1994). "Nucleotide sequence corrections of the uidA open reading frame encoding beta-glucuronidase." Gene 138:259-260. Pubmed: 8125312