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Database: UniProt
Entry: E0IWU2_ECOLW
LinkDB: E0IWU2_ECOLW
Original site: E0IWU2_ECOLW 
ID   E0IWU2_ECOLW            Unreviewed;       603 AA.
AC   E0IWU2;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 76.
DE   RecName: Full=Beta-glucuronidase {ECO:0000256|ARBA:ARBA00016205};
DE            EC=3.2.1.31 {ECO:0000256|ARBA:ARBA00012761};
GN   Name=uidA {ECO:0000313|EMBL:ADT75250.1};
GN   OrderedLocusNames=ECW_m1783 {ECO:0000313|EMBL:ADT75250.1};
OS   Escherichia coli (strain ATCC 9637 / CCM 2024 / DSM 1116 / LMG 11080 / NBRC
OS   13500 / NCIMB 8666 / NRRL B-766 / W).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=566546 {ECO:0000313|EMBL:ADT75250.1, ECO:0000313|Proteomes:UP000008525};
RN   [1] {ECO:0000313|EMBL:ADT75250.1, ECO:0000313|Proteomes:UP000008525}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9637 / CCM 2024 / DSM 1116 / LMG 11080 / NBRC 13500 /
RC   NCIMB 8666 / NRRL B-766 / W {ECO:0000313|Proteomes:UP000008525};
RX   PubMed=21208457; DOI=10.1186/1471-2164-12-9;
RA   Archer C.T., Kim J.F., Jeong H., Park J.H., Vickers C.E., Lee S.Y.,
RA   Nielsen L.K.;
RT   "The genome sequence of E. coli W (ATCC 9637): comparative genome analysis
RT   and an improved genome-scale reconstruction of E. coli.";
RL   BMC Genomics 12:9-9(2011).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC       {ECO:0000256|ARBA:ARBA00007401, ECO:0000256|RuleBase:RU361154}.
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DR   EMBL; CP002185; ADT75250.1; -; Genomic_DNA.
DR   RefSeq; WP_000945924.1; NZ_WBMH01000021.1.
DR   AlphaFoldDB; E0IWU2; -.
DR   KEGG; elw:ECW_m1783; -.
DR   PATRIC; fig|566546.30.peg.1818; -.
DR   Proteomes; UP000008525; Chromosome.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR006101; Glyco_hydro_2.
DR   InterPro; IPR023232; Glyco_hydro_2_AS.
DR   InterPro; IPR006103; Glyco_hydro_2_cat.
DR   InterPro; IPR023230; Glyco_hydro_2_CS.
DR   InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR   InterPro; IPR006104; Glyco_hydro_2_N.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   PANTHER; PTHR10066; BETA-GLUCURONIDASE; 1.
DR   PANTHER; PTHR10066:SF67; BETA-GLUCURONIDASE; 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   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   PROSITE; PS00719; GLYCOSYL_HYDROL_F2_1; 1.
DR   PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361154};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361154}.
FT   DOMAIN          12..180
FT                   /note="Glycosyl hydrolases family 2 sugar binding"
FT                   /evidence="ECO:0000259|Pfam:PF02837"
FT   DOMAIN          184..272
FT                   /note="Glycoside hydrolase family 2 immunoglobulin-like
FT                   beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF00703"
FT   DOMAIN          274..593
FT                   /note="Glycoside hydrolase family 2 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF02836"
SQ   SEQUENCE   603 AA;  68461 MW;  B0274EA64B2FF491 CRC64;
     MLRPVETPTR EIKKLDGLWA FSLDRENCGI DQRWWESALQ ESRAIAVPGS FNDQFADADI
     RNYVGNVWYQ REVFIPKGWA GQRIVLRFDA VTHYGKVWVN NQEVMEHQGG YTPFEADVTP
     YVIAGKSVRI TVCVNNELNW QTIPPGMVIT DENGKKKQSY FHDFFNYAGI HRSVMVYTTP
     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
//
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