ID Q2PBR7_STRSZ Unreviewed; 594 AA.
AC Q2PBR7;
DT 07-FEB-2006, integrated into UniProtKB/TrEMBL.
DT 07-FEB-2006, sequence version 1.
DT 24-JAN-2024, entry version 71.
DE RecName: Full=Beta-glucuronidase {ECO:0000256|ARBA:ARBA00016205};
DE EC=3.2.1.31 {ECO:0000256|ARBA:ARBA00012761};
GN Name=gusA {ECO:0000313|EMBL:CAI72019.1};
OS Streptococcus equi subsp. zooepidemicus.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=40041 {ECO:0000313|EMBL:CAI72019.1};
RN [1] {ECO:0000313|EMBL:CAI72019.1}
RP NUCLEOTIDE SEQUENCE.
RA Krahulec J., Szemes T., Krahulcova J.;
RT "Bioinformatics Characterization of Potential New Beta-Glucuronidase from
RT Streptococcus equi subsp. Zooepidemicus.";
RL Mol. Biotechnol. 44:232-241(2010).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401, ECO:0000256|RuleBase:RU361154}.
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DR EMBL; AJ890474; CAI72019.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2PBR7; -.
DR SMR; Q2PBR7; -.
DR CAZy; GH2; Glycoside Hydrolase Family 2.
DR BRENDA; 3.2.1.31; 5960.
DR GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
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 14..175
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 177..269
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 271..586
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
SQ SEQUENCE 594 AA; 68143 MW; 2B7CA96C40BAC5CB CRC64;
MLYPILTKTR KIYDLGGLWQ FKLGDHNPQE LLASDELMVV PTSFNDVVVD KDKRNYIGDF
WYERFVDVPD LAADEELVLR FGSVTHNATV YVASFRAHKG GFTPFEVLVP EDLYRDSRIK
VSVCANNILD YTSLPVGNYS EELQEDGSIK KVVKENFDFF NYAGIHRPVK LMVRPKCHIS
DITITSDLSE DMTSALVKVS VETSAAVDEV KVTILDEEHR LVAKVVDGKA RLDSVRLWEV
LDAYLYTAHV ELIVDGNVVD SYDESFGVRS IAVEEGQFLL NGKPVYFKGF GKHEDTFING
RGLNEAANLM DMNLLKELGA NSFRTSHYPY SEEMMRLADR MGILVIDEIP AVGLFQNFTA
SLDLSPKDNG TWSVMKTKEA HEQAICELVK RDKNHPSVVM WVVANEPASH EEGAHEYFEP
LIALYKALDP QQRPVTLVNL LLATPDRDKV MDLVDVISLN RYYAWYVDHG DLIKGEVGLR
QELLEWQKKF PNKPILMTEY GADTLPGLHS MWDIPYTEEF QCRFYEMSHR VFDEIPNLVG
EQVWNFADFE TNLMIFRIQG NHKGLFSRNR QPKHVVGLFK ERWNTIPHYN YKKK
//
