ID   BGLR_CHLAE              Reviewed;         648 AA.
AC   O77695;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   22-FEB-2023, entry version 92.
DE   RecName: Full=Beta-glucuronidase;
DE            EC=3.2.1.31;
DE   Flags: Precursor; Fragment;
GN   Name=GUSB;
OS   Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Chlorocebus.
OX   NCBI_TaxID=9534;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Vervoort R.;
RT   "Partial cDNA sequence of Cercopithecus aethiops (COS7 cell) beta-
RT   glucuronidase.";
RL   Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Plays an important role in the degradation of dermatan and
CC       keratan sulfates. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a beta-D-glucuronoside + H2O = an alcohol + D-glucuronate;
CC         Xref=Rhea:RHEA:17633, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879,
CC         ChEBI:CHEBI:58720, ChEBI:CHEBI:83411; EC=3.2.1.31;
CC   -!- ACTIVITY REGULATION: Inhibited by L-aspartic acid. {ECO:0000250}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Lysosome.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family. {ECO:0000305}.
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DR   EMBL; AF084552; AAC34593.1; -; mRNA.
DR   AlphaFoldDB; O77695; -.
DR   SMR; O77695; -.
DR   CAZy; GH2; Glycoside Hydrolase Family 2.
DR   GlyCosmos; O77695; 4 sites, No reported glycans.
DR   GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0004566; F:beta-glucuronidase 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   2: Evidence at transcript level;
KW   Glycoprotein; Glycosidase; Hydrolase; Lysosome; Signal.
FT   SIGNAL          <1..19
FT                   /evidence="ECO:0000250"
FT   CHAIN           20..648
FT                   /note="Beta-glucuronidase"
FT                   /id="PRO_0000012159"
FT   ACT_SITE        448
FT                   /note="Proton donor"
FT   CARBOHYD        170
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        269
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        417
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        628
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   NON_TER         1
SQ   SEQUENCE   648 AA;  74632 MW;  D4BB309C0D9F38D4 CRC64;
     GLAMAWAVLG PLLWGCALAL QGGMLYPRES QSRERKELDG LWSFRADFSD NRRRGFEEQW
     YRRPLRESGP TLDMPVPSSF NDISQDWRLR HFVGWVWYER EVILPERWTQ DLSTRVVLRI
     GSAHAYAIVW VNGVHTLEHE GGYLPFEADI SNLVQVGPLS SHVRITIAIN NTLTSTTLPP
     GTIQYLTDIS KYPKGYFIQN TYFDFFNYAG LQRSVLLYTT PTAYIDDITV TTGVEHDTGL
     VNYQISVKGS NLFELEVRLL DAENKLVANG TGIQGQLKVP GARLWWPYLM HERPAYLYSL
     EVRLTAQTSL GPVSDFYTLP VGIRTVAVTE SQFLINGKPF YFHGVNKHED ADIRGKGFDW
     PLLVKDFNLL RWLGANAFRT SHYPYAEEVL QMCDRYGIVV IDECPGVGLA LPQFFNNVSL
     QNHMRVMEEV VRRDKNHPAV VMWSVANEPA SHLESAGYYL KMVITHTKAL DPSRPVTFVT
     NSNYAADKGA PYVDVICLNS YYSWYHDYGH LELIQRQLTT QFENWYKTYQ KPIIQSEYGA
     ETIVGFHQDP PLMFTEEYQK SLLEQYHVVL DQKRRKYVVG ELIWNFADFM TEQSPTRVLG
     NKKGVFTRQR QPKSAAFLLR ERYWKIANET RYPHSIAKSQ CLENSPFT
//