ID   BGLR_PONAB              Reviewed;         651 AA.
AC   Q5R5N6; Q5R8A1;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 2.
DT   22-FEB-2023, entry version 78.
DE   RecName: Full=Beta-glucuronidase;
DE            EC=3.2.1.31;
DE   Flags: Precursor;
GN   Name=GUSB;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex, and Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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 {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family. {ECO:0000305}.
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DR   EMBL; CR859852; CAH92009.1; -; mRNA.
DR   EMBL; CR860821; CAH92930.1; -; mRNA.
DR   RefSeq; NP_001126724.1; NM_001133252.1.
DR   RefSeq; NP_001128846.1; NM_001135374.1.
DR   AlphaFoldDB; Q5R5N6; -.
DR   SMR; Q5R5N6; -.
DR   STRING; 9601.ENSPPYP00000019644; -.
DR   CAZy; GH2; Glycoside Hydrolase Family 2.
DR   GlyCosmos; Q5R5N6; 5 sites, No reported glycans.
DR   GeneID; 100173726; -.
DR   GeneID; 100189763; -.
DR   KEGG; pon:100173726; -.
DR   CTD; 2990; -.
DR   eggNOG; KOG2024; Eukaryota.
DR   InParanoid; Q5R5N6; -.
DR   OrthoDB; 1847696at2759; -.
DR   Proteomes; UP000001595; Unplaced.
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; Reference proteome; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000250"
FT   CHAIN           23..651
FT                   /note="Beta-glucuronidase"
FT                   /id="PRO_0000231039"
FT   ACT_SITE        451
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        173
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        190
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        272
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        420
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        631
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        4
FT                   /note="G -> R (in Ref. 1; CAH92009)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        69
FT                   /note="R -> Q (in Ref. 1; CAH92930)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        370
FT                   /note="F -> I (in Ref. 1; CAH92009)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        406
FT                   /note="E -> G (in Ref. 1; CAH92930)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        460
FT                   /note="G -> D (in Ref. 1; CAH92009)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   651 AA;  74772 MW;  A3170629BE393917 CRC64;
     MARGSAVAWA AFGPLLWGCA LGLQGGMLYP QESRSRERKE LDGLWSFRAD FSDNRRRGFE
     EQWYRRPLRE SGPTLDMPVP SSFNDISQDW RLRHFVGWVW YEREVILPER WTQDLHTRVV
     LRIGSAHSYA IVWVNGVDTL EHEGGYLPFE ADISNLVQVG PLPSRLRITI AINNTLTPTT
     LPPGTIQYMN DTSKYPKGYF VQNTYFDFFN YAGLQRSVLL YTTPTTYIDD ITVTTGVEQD
     SGLVNYQISV KGSNLFELEA RLLDAENKVV ANGTGTQGQL KVPGASLWWP YLMHERPAYL
     YSLEVRLTAQ TSLGPVSDFY SLPVGIRTVA VTESQFLING KPFYFHGVNK HEDADIRGKG
     FDWPLLVKDF NLLRWLGANA FRTSHYPYAE EVLQMCDRHG IVVIDECPGV GLALPQFFNN
     VSLHHHMRVM EEVVRRDKNH PAVVMWSVAN EPASHLESAG YYLKMVIAHT KALDPSRPVT
     FVSNSNYAAD KGAPYVDVIC LNSYYSWYHD YGHLELIQLQ LATQFENWYK KYQKPIIQSE
     YGAETIAGFH QDPPLMFTEE YQKSLLEQYH LGLDQKRRKY VVGELIWNFA DFMTEQSLTR
     VLGNKKGIFT RQRQPKSAAF LLRERYWKIA NETRYPHSVA KSQCLENSPF T
//