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P05804 (BGLR_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length603 AA.
Sequence statusComplete.
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

Secondary structure

........................................................................................................................ 603
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P05804 [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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 277:1453-1462(1997) [PubMed] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-5, SUBUNIT.
[8]Jefferson R.A.
Thesis (1985), University of Colorado, United States
Cited for: CHARACTERIZATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_416134.1. NC_000913.3.
YP_489880.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3K46X-ray2.50A/B1-603[»]
3K4AX-ray2.90A/B1-603[»]
3K4DX-ray2.39A/B1-603[»]
3LPFX-ray2.26A/B1-603[»]
3LPGX-ray2.42A/B1-603[»]
4JHZX-ray2.83A/B1-601[»]
ProteinModelPortalP05804.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-11086N.
IntActP05804. 2 interactions.
STRING511145.b1617.

Protein family/group databases

CAZyGH2. Glycoside Hydrolase Family 2.

Proteomic databases

PRIDEP05804.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC74689; AAC74689; b1617.
BAA15368; BAA15368; BAA15368.
GeneID12934489.
946149.
KEGGecj:Y75_p1593.
eco:b1617.
PATRIC32118536. VBIEscCol129921_1688.

Organism-specific databases

EchoBASEEB1048.
EcoGeneEG11055. uidA.

Phylogenomic databases

eggNOGCOG3250.
HOGENOMHOG000120896.
KOK01195.
OMAFADFQTT.
OrthoDBEOG6DRPFW.
PhylomeDBP05804.

Enzyme and pathway databases

BioCycEcoCyc:BETA-GLUCURONID-MONOMER.
ECOL316407:JW1609-MONOMER.
MetaCyc:BETA-GLUCURONID-MONOMER.
SABIO-RKP05804.

Gene expression databases

GenevestigatorP05804.

Family and domain databases

Gene3D2.60.120.260. 1 hit.
2.60.40.320. 1 hit.
3.20.20.80. 1 hit.
InterProIPR008979. Galactose-bd-like.
IPR006101. Glyco_hydro_2.
IPR013812. Glyco_hydro_2/20_Ig-like.
IPR023232. Glyco_hydro_2_AS.
IPR023230. Glyco_hydro_2_CS.
IPR006102. Glyco_hydro_2_Ig-like.
IPR006104. Glyco_hydro_2_N.
IPR006103. Glyco_hydro_2_TIM.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF00703. Glyco_hydro_2. 1 hit.
PF02836. Glyco_hydro_2_C. 1 hit.
PF02837. Glyco_hydro_2_N. 1 hit.
[Graphical view]
PRINTSPR00132. GLHYDRLASE2.
SUPFAMSSF49303. SSF49303. 1 hit.
SSF49785. SSF49785. 1 hit.
SSF51445. SSF51445. 1 hit.
PROSITEPS00719. GLYCOSYL_HYDROL_F2_1. 1 hit.
PS00608. GLYCOSYL_HYDROL_F2_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP05804.
PROP05804.

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 11, 2014
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

Escherichia coli

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