ID   BGLR_ECOLI              Reviewed;         603 AA.
AC   P05804;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 2.
DT   02-SEP-2008, entry version 75.
DE   RecName: Full=Beta-glucuronidase;
DE            Short=GUS;
DE            EC=3.2.1.31;
DE   AltName: Full=Beta-D-glucuronoside glucuronosohydrolase;
GN   Name=uidA; Synonyms=gurA, gusA; OrderedLocusNames=b1617, JW1609;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RX   MEDLINE=87041472; PubMed=3534890;
RA   Jefferson R.A., Burgess S.M., Hirsh D.;
RT   "Beta-glucuronidase from Escherichia coli as a gene-fusion marker.";
RL   Proc. Natl. Acad. Sci. U.S.A. 83:8447-8451(1986).
RN   [2]
RP   SEQUENCE REVISION TO 279.
RX   MEDLINE=94171050; PubMed=8125312; DOI=10.1016/0378-1119(94)90820-6;
RA   Schlaman H.R., Risseeuw E., Franke-Van Dijk M.E., Hooykaas P.J.;
RT   "Nucleotide sequence corrections of the uidA open reading frame
RT   encoding beta-glucuronidase.";
RL   Gene 138:259-260(1994).
RN   [3]
RP   SEQUENCE REVISION TO 420-425.
RX   MEDLINE=91355907; PubMed=2103475; DOI=10.1007/BF00039422;
RA   Farrell L.B., Beachy R.N.;
RT   "Manipulation of beta-glucuronidase for use as a reporter in vacuolar
RT   targeting studies.";
RL   Plant Mol. Biol. 15:821-825(1990).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   MEDLINE=97251357; PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA   Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA   Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M.,
RA   Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K.,
RA   Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N.,
RA   Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J.,
RA   Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T.;
RT   "A 570-kb DNA sequence of the Escherichia coli K-12 genome
RT   corresponding to the 28.0-40.1 min region on the linkage map.";
RL   DNA Res. 3:363-377(1996).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   MEDLINE=97426617; PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA   Mau B., Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1474(1997).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains
RT   MG1655 and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
CC   -!- CATALYTIC ACTIVITY: A beta-D-glucuronoside + H(2)O = D-glucuronate
CC       + an alcohol.
CC   -!- INTERACTION:
CC       P18843:nadE; NbExp=1; IntAct=EBI-1124641, EBI-548960;
CC   -!- MISCELLANEOUS: Substrates for this enzyme are generally water-
CC       soluble.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
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DR   EMBL; M14641; AAA68923.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; S69414; AAB30197.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC74689.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA15368.1; -; Genomic_DNA.
DR   PIR; C64918; GBECGC.
DR   RefSeq; AP_002238.1; -.
DR   RefSeq; NP_416134.1; -.
DR   HSSP; P08236; 1BHG.
DR   IntAct; P05804; -.
DR   GeneID; 946149; -.
DR   GenomeReviews; U00096_GR; b1617.
DR   GenomeReviews; AP009048_GR; JW1609.
DR   KEGG; ecj:JW1609; -.
DR   KEGG; eco:b1617; -.
DR   EchoBASE; EB1048; -.
DR   EcoGene; EG11055; uidA.
DR   HOGENOM; P05804; -.
DR   BioCyc; EcoCyc:BETA-GLUCURONID-MON; -.
DR   BioCyc; MetaCyc:BETA-GLUCURONID-MON; -.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   InterPro; IPR006101; Glyco_hydro_2.
DR   InterPro; IPR013812; Glyco_hydro_2/20_Ig-like.
DR   InterPro; IPR006104; Glyco_hydro_2_carb-bd.
DR   InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR   InterPro; IPR006103; Glyco_hydro_2_TIM.
DR   InterPro; IPR013781; Glyco_hydro_sub_cat.
DR   Gene3D; G3DSA:2.60.40.320; Glyco_hydro_2/20_Ig-like; 1.
DR   Gene3D; G3DSA:3.20.20.80; Glyco_hydro_cat; 1.
DR   Pfam; PF00703; Glyco_hydro_2; 1.
DR   Pfam; PF02836; Glyco_hydro_2_C; 1.
DR   Pfam; PF02837; Glyco_hydro_2_N; 1.
DR   PRINTS; PR00132; GLHYDRLASE2.
DR   PROSITE; PS00719; GLYCOSYL_HYDROL_F2_1; 1.
DR   PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Glycosidase; Hydrolase.
FT   CHAIN         1    603       Beta-glucuronidase.
FT                                /FTId=PRO_0000057680.
FT   ACT_SITE    413    413       Proton donor (By similarity).
SQ   SEQUENCE   603 AA;  68447 MW;  E769C8D61A3B9A76 CRC64;
     MLRPVETPTR EIKKLDGLWA FSLDRENCGI DQRWWESALQ ESRAIAVPGS FNDQFADADI
     RNYAGNVWYQ REVFIPKGWA GQRIVLRFDA VTHYGKVWVN NQEVMEHQGG YTPFEADVTP
     YVIAGKSVRI TVCVNNELNW QTIPPGMVIT DENGKKKQSY FHDFFNYAGI HRSVMLYTTP
     NTWVDDITVV THVAQDCNHA SVDWQVVANG DVSVELRDAD QQVVATGQGT SGTLQVVNPH
     LWQPGEGYLY ELCVTAKSQT ECDIYPLRVG IRSVAVKGEQ FLINHKPFYF TGFGRHEDAD
     LRGKGFDNVL MVHDHALMDW IGANSYRTSH YPYAEEMLDW ADEHGIVVID ETAAVGFNLS
     LGIGFEAGNK PKELYSEEAV NGETQQAHLQ AIKELIARDK NHPSVVMWSI ANEPDTRPQG
     AREYFAPLAE ATRKLDPTRP ITCVNVMFCD AHTDTISDLF DVLCLNRYYG WYVQSGDLET
     AEKVLEKELL AWQEKLHQPI IITEYGVDTL AGLHSMYTDM WSEEYQCAWL DMYHRVFDRV
     SAVVGEQVWN FADFATSQGI LRVGGNKKGI FTRDRKPKSA AFLLQKRWTG MNFGEKPQQG
     GKQ
//