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Reviewed, UniProtKB/Swiss-Prot P05804 (BGLR_ECOLI)

Last modified June 16, 2009. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Beta-glucuronidase
      Short name=GUS
    EC=3.2.1.31
Alternative name(s):
    Beta-D-glucuronoside glucuronosohydrolase
Gene names
Name: uidA
Synonyms: gurA, gusA
Ordered Locus Names: b1617, JW1609
OrganismEscherichia coli (strain K12) [Complete proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length603 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

A beta-D-glucuronoside + H2O = D-glucuronate + an alcohol.

Subunit structure

Homotetramer. Ref.7

Miscellaneous

Substrates for this enzyme are generally water-soluble.

Sequence similarities

Belongs to the glycosyl hydrolase 2 family.

biophysicochemical properties

pH dependence:

Optimum pH is 5.0-7.5.

Temperature dependence:

Resistant to thermal inactivation at 50 degrees Celsius.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

nadEP188431EBI-1124641,EBI-548960

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 603603Beta-glucuronidase
PRO_0000057680

Sites

Active site4131Proton donor By similarity

Sequences

Sequence LengthMass (Da)Tools
P05804-1 [UniParc].

Last modified October 1, 1994. Version 2.
Checksum: E769C8D61A3B9A76

FASTA60368,447
        10         20         30         40         50         60 
MLRPVETPTR EIKKLDGLWA FSLDRENCGI DQRWWESALQ ESRAIAVPGS FNDQFADADI 

        70         80         90        100        110        120 
RNYAGNVWYQ REVFIPKGWA GQRIVLRFDA VTHYGKVWVN NQEVMEHQGG YTPFEADVTP 

       130        140        150        160        170        180 
YVIAGKSVRI TVCVNNELNW QTIPPGMVIT DENGKKKQSY FHDFFNYAGI HRSVMLYTTP 

       190        200        210        220        230        240 
NTWVDDITVV THVAQDCNHA SVDWQVVANG DVSVELRDAD QQVVATGQGT SGTLQVVNPH 

       250        260        270        280        290        300 
LWQPGEGYLY ELCVTAKSQT ECDIYPLRVG IRSVAVKGEQ FLINHKPFYF TGFGRHEDAD 

       310        320        330        340        350        360 
LRGKGFDNVL MVHDHALMDW IGANSYRTSH YPYAEEMLDW ADEHGIVVID ETAAVGFNLS 

       370        380        390        400        410        420 
LGIGFEAGNK PKELYSEEAV NGETQQAHLQ AIKELIARDK NHPSVVMWSI ANEPDTRPQG 

       430        440        450        460        470        480 
AREYFAPLAE ATRKLDPTRP ITCVNVMFCD AHTDTISDLF DVLCLNRYYG WYVQSGDLET 

       490        500        510        520        530        540 
AEKVLEKELL AWQEKLHQPI IITEYGVDTL AGLHSMYTDM WSEEYQCAWL DMYHRVFDRV 

       550        560        570        580        590        600 
SAVVGEQVWN FADFATSQGI LRVGGNKKGI FTRDRKPKSA AFLLQKRWTG MNFGEKPQQG 


GKQ 

« Hide

References

« Hide 'large scale' references
[1]"Beta-glucuronidase from Escherichia coli as a gene-fusion marker."
Jefferson R.A., Burgess S.M., Hirsh D.
Proc. Natl. Acad. Sci. U.S.A. 83:8447-8451(1986) [PubMed: 3534890] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-11.
[2]"Nucleotide sequence corrections of the uidA open reading frame encoding beta-glucuronidase."
Schlaman H.R., Risseeuw E., Franke-Van Dijk M.E., Hooykaas P.J.
Gene 138:259-260(1994) [PubMed: 8125312] [Abstract]
Cited for: SEQUENCE REVISION TO 279.
[3]"Manipulation of beta-glucuronidase for use as a reporter in vacuolar targeting studies."
Farrell L.B., Beachy R.N.
Plant Mol. Biol. 15:821-825(1990) [PubMed: 2103475] [Abstract]
Cited for: SEQUENCE REVISION TO 420-425.
[4]"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."
Aiba H., Baba T., Fujita K., 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. expand/collapse author list , Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T.
DNA Res. 3:363-377(1996) [PubMed: 9097039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"The complete genome sequence of Escherichia coli K-12."
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.
Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[6]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[7]"One step purification of Escherichia coli beta-glucuronidase."
Blanco C., Nemoz G.
Biochimie 69:157-161(1987) [PubMed: 3105604] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-5, SUBUNIT.
[8]Jefferson R.A.
Thesis (1985), University of Colorado, United States
Cited for: CHARACTERIZATION.

Cross-references

Sequence databases

M14641 Genomic DNA. Translation: AAA68923.1. Sequence problems.
S69414 Genomic DNA. Translation: AAB30197.1.
U00096 Genomic DNA. Translation: AAC74689.1.
AP009048 Genomic DNA. Translation: BAA15368.1.
PIRGBECGC. C64918.
RefSeqAP_002238.1.
NP_416134.1.

3D structure databases

HSSPHSSP built from PDB template 1BHG based on UniProtKB P08236.
ModBaseSearch...

Protein-protein interaction databases

IntActP05804. 2 interactions.

Protein family/group databases

CAZyGH2. Glycoside Hydrolase Family 2.

Genome annotation databases

GeneID946149.
GenomeReviewsGene locus JW1609 in contig AP009048_GR.
Gene locus b1617 in contig U00096_GR.
KEGGecj:JW1609.
eco:b1617.

Organism-specific databases

EchoBASEEB1048.
EcoGeneEG11055. uidA.
CMRSearch...

Phylogenomic databases

HOGENOMP05804.
OMAP05804. GHMEVIQ.

Enzyme and pathway databases

BioCycEcoCyc:BETA-GLUCURONID-MON.
MetaCyc:BETA-GLUCURONID-MON.

Family and domain databases

InterProIPR006101. Glyco_hydro_2.
IPR013812. Glyco_hydro_2/20_Ig-like.
IPR006104. Glyco_hydro_2_carb-bd.
IPR006102. Glyco_hydro_2_Ig-like.
IPR006103. Glyco_hydro_2_TIM.
IPR013781. Glyco_hydro_sg_catalytic.
[Graphical view]
Gene3DG3DSA:2.60.40.320. Glyco_hydro_2/20_Ig-like. 1 hit.
G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
PfamPF00703. Glyco_hydro_2. 1 hit.
PF02836. Glyco_hydro_2_C. 1 hit.
PF02837. Glyco_hydro_2_N. 1 hit.
[Graphical view]
PRINTSPR00132. GLHYDRLASE2.
PROSITEPS00719. GLYCOSYL_HYDROL_F2_1. 1 hit.
PS00608. GLYCOSYL_HYDROL_F2_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameBGLR_ECOLI
AccessionPrimary (citable) accession number: P05804
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: October 1, 1994
Last modified: June 16, 2009
This is version 81 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents