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P05804

- BGLR_ECOLI

UniProt

P05804 - BGLR_ECOLI

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Protein
Beta-glucuronidase
Gene
uidA, gurA, gusA, b1617, JW1609
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

pH dependencei

Optimum pH is 5.0-7.5.

Temperature dependencei

Resistant to thermal inactivation at 50 degrees Celsius.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei413 – 4131Proton donor By similarity

GO - Molecular functioni

  1. beta-glucuronidase activity Source: EcoCyc

GO - Biological processi

  1. glucuronoside catabolic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Enzyme and pathway databases

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

Protein family/group databases

CAZyiGH2. Glycoside Hydrolase Family 2.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-glucuronidase (EC:3.2.1.31)
Short name:
GUS
Alternative name(s):
Beta-D-glucuronoside glucuronosohydrolase
Gene namesi
Name:uidA
Synonyms:gurA, gusA
Ordered Locus Names:b1617, JW1609
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG11055. uidA.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 603603Beta-glucuronidase
PRO_0000057680Add
BLAST

Proteomic databases

PRIDEiP05804.

Expressioni

Gene expression databases

GenevestigatoriP05804.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
nadEP188431EBI-1124641,EBI-548960

Protein-protein interaction databases

DIPiDIP-11086N.
IntActiP05804. 2 interactions.
STRINGi511145.b1617.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 83
Beta strandi10 – 123
Beta strandi18 – 269
Turni29 – 335
Helixi34 – 363
Beta strandi43 – 497
Turni52 – 554
Helixi58 – 614
Beta strandi65 – 7410
Helixi77 – 793
Beta strandi80 – 823
Beta strandi83 – 897
Beta strandi92 – 10110
Beta strandi103 – 1075
Beta strandi110 – 1123
Beta strandi114 – 1174
Helixi119 – 1213
Beta strandi126 – 13510
Beta strandi142 – 1443
Beta strandi146 – 1505
Beta strandi156 – 1649
Beta strandi174 – 1796
Beta strandi181 – 19111
Beta strandi194 – 1974
Beta strandi201 – 2099
Beta strandi211 – 2177
Beta strandi219 – 2213
Beta strandi223 – 2286
Beta strandi233 – 2353
Turni244 – 2463
Beta strandi250 – 2578
Beta strandi262 – 2698
Beta strandi274 – 2774
Beta strandi280 – 2834
Beta strandi290 – 2956
Turni300 – 3045
Helixi308 – 32114
Beta strandi325 – 3284
Helixi335 – 34410
Beta strandi347 – 3515
Beta strandi364 – 3663
Beta strandi374 – 3763
Turni377 – 3793
Helixi382 – 39918
Beta strandi405 – 4139
Helixi421 – 43515
Beta strandi437 – 4393
Beta strandi441 – 4466
Beta strandi447 – 4493
Turni451 – 4533
Helixi457 – 4593
Beta strandi460 – 4667
Turni469 – 4713
Beta strandi472 – 4743
Helixi478 – 49619
Beta strandi500 – 5045
Beta strandi520 – 5223
Helixi523 – 53715
Beta strandi543 – 55210
Beta strandi558 – 5614
Beta strandi562 – 5665
Beta strandi569 – 5713
Helixi580 – 59011
Beta strandi598 – 6003

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP05804.

Miscellaneous databases

EvolutionaryTraceiP05804.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG3250.
HOGENOMiHOG000120896.
KOiK01195.
OMAiFADFQTT.
OrthoDBiEOG6DRPFW.
PhylomeDBiP05804.

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
2.60.40.320. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR008979. 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]
PfamiPF00703. Glyco_hydro_2. 1 hit.
PF02836. Glyco_hydro_2_C. 1 hit.
PF02837. Glyco_hydro_2_N. 1 hit.
[Graphical view]
PRINTSiPR00132. GLHYDRLASE2.
SUPFAMiSSF49303. SSF49303. 1 hit.
SSF49785. SSF49785. 1 hit.
SSF51445. SSF51445. 1 hit.
PROSITEiPS00719. GLYCOSYL_HYDROL_F2_1. 1 hit.
PS00608. GLYCOSYL_HYDROL_F2_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P05804-1 [UniParc]FASTAAdd to Basket

« Hide

MLRPVETPTR EIKKLDGLWA FSLDRENCGI DQRWWESALQ ESRAIAVPGS    50
FNDQFADADI RNYAGNVWYQ REVFIPKGWA GQRIVLRFDA VTHYGKVWVN 100
NQEVMEHQGG YTPFEADVTP YVIAGKSVRI TVCVNNELNW QTIPPGMVIT 150
DENGKKKQSY FHDFFNYAGI HRSVMLYTTP NTWVDDITVV THVAQDCNHA 200
SVDWQVVANG DVSVELRDAD QQVVATGQGT SGTLQVVNPH LWQPGEGYLY 250
ELCVTAKSQT ECDIYPLRVG IRSVAVKGEQ FLINHKPFYF TGFGRHEDAD 300
LRGKGFDNVL MVHDHALMDW IGANSYRTSH YPYAEEMLDW ADEHGIVVID 350
ETAAVGFNLS LGIGFEAGNK PKELYSEEAV NGETQQAHLQ AIKELIARDK 400
NHPSVVMWSI ANEPDTRPQG AREYFAPLAE ATRKLDPTRP ITCVNVMFCD 450
AHTDTISDLF DVLCLNRYYG WYVQSGDLET AEKVLEKELL AWQEKLHQPI 500
IITEYGVDTL AGLHSMYTDM WSEEYQCAWL DMYHRVFDRV SAVVGEQVWN 550
FADFATSQGI LRVGGNKKGI FTRDRKPKSA AFLLQKRWTG MNFGEKPQQG 600
GKQ 603
Length:603
Mass (Da):68,447
Last modified:October 1, 1994 - v2
Checksum:iE769C8D61A3B9A76
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiC64918. GBECGC.
RefSeqiNP_416134.1. NC_000913.3.
YP_489880.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC74689; AAC74689; b1617.
BAA15368; BAA15368; BAA15368.
GeneIDi12934489.
946149.
KEGGiecj:Y75_p1593.
eco:b1617.
PATRICi32118536. VBIEscCol129921_1688.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
PIRi C64918. GBECGC.
RefSeqi NP_416134.1. NC_000913.3.
YP_489880.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3K46 X-ray 2.50 A/B 1-603 [» ]
3K4A X-ray 2.90 A/B 1-603 [» ]
3K4D X-ray 2.39 A/B 1-603 [» ]
3LPF X-ray 2.26 A/B 1-603 [» ]
3LPG X-ray 2.42 A/B 1-603 [» ]
4JHZ X-ray 2.83 A/B 1-601 [» ]
ProteinModelPortali P05804.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-11086N.
IntActi P05804. 2 interactions.
STRINGi 511145.b1617.

Protein family/group databases

CAZyi GH2. Glycoside Hydrolase Family 2.

Proteomic databases

PRIDEi P05804.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC74689 ; AAC74689 ; b1617 .
BAA15368 ; BAA15368 ; BAA15368 .
GeneIDi 12934489.
946149.
KEGGi ecj:Y75_p1593.
eco:b1617.
PATRICi 32118536. VBIEscCol129921_1688.

Organism-specific databases

EchoBASEi EB1048.
EcoGenei EG11055. uidA.

Phylogenomic databases

eggNOGi COG3250.
HOGENOMi HOG000120896.
KOi K01195.
OMAi FADFQTT.
OrthoDBi EOG6DRPFW.
PhylomeDBi P05804.

Enzyme and pathway databases

BioCyci EcoCyc:BETA-GLUCURONID-MONOMER.
ECOL316407:JW1609-MONOMER.
MetaCyc:BETA-GLUCURONID-MONOMER.
SABIO-RK P05804.

Miscellaneous databases

EvolutionaryTracei P05804.
PROi P05804.

Gene expression databases

Genevestigatori P05804.

Family and domain databases

Gene3Di 2.60.120.260. 1 hit.
2.60.40.320. 1 hit.
3.20.20.80. 1 hit.
InterProi IPR008979. 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 ]
Pfami PF00703. Glyco_hydro_2. 1 hit.
PF02836. Glyco_hydro_2_C. 1 hit.
PF02837. Glyco_hydro_2_N. 1 hit.
[Graphical view ]
PRINTSi PR00132. GLHYDRLASE2.
SUPFAMi SSF49303. SSF49303. 1 hit.
SSF49785. SSF49785. 1 hit.
SSF51445. SSF51445. 1 hit.
PROSITEi PS00719. GLYCOSYL_HYDROL_F2_1. 1 hit.
PS00608. GLYCOSYL_HYDROL_F2_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. 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.

Entry informationi

Entry nameiBGLR_ECOLI
AccessioniPrimary (citable) accession number: P05804
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Substrates for this enzyme are generally water-soluble.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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