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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//