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P05804

- BGLR_ECOLI

UniProt

P05804 - BGLR_ECOLI

Protein

Beta-glucuronidase

Gene

uidA

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 123 (01 Oct 2014)
      Sequence version 2 (01 Oct 1994)
      Previous versions | rss
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    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 donorBy similarity

    GO - Molecular functioni

    1. beta-glucuronidase activity Source: EcoCyc

    GO - Biological processi

    1. glucuronoside catabolic process Source: EcoCyc

    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-glucuronidasePRO_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

    1
    603
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP05804.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 2 family.Curated

    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

    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: October 1, 2014
    This is version 123 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