ID A0A0M9ACC9_9HYME Unreviewed; 705 AA.
AC A0A0M9ACC9;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Beta-glucuronidase {ECO:0000256|ARBA:ARBA00016205, ECO:0000256|RuleBase:RU361154};
DE EC=3.2.1.31 {ECO:0000256|ARBA:ARBA00012761, ECO:0000256|RuleBase:RU361154};
GN ORFNames=WN51_06672 {ECO:0000313|EMBL:KOX80383.1};
OS Melipona quadrifasciata.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Apidae; Melipona.
OX NCBI_TaxID=166423 {ECO:0000313|EMBL:KOX80383.1, ECO:0000313|Proteomes:UP000053105};
RN [1] {ECO:0000313|EMBL:KOX80383.1, ECO:0000313|Proteomes:UP000053105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0111107301 {ECO:0000313|EMBL:KOX80383.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KOX80383.1};
RA Pan H., Kapheim K.;
RT "The genome of Melipona quadrifasciata.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays an important role in the degradation of dermatan and
CC keratan sulfates. {ECO:0000256|ARBA:ARBA00003025,
CC ECO:0000256|RuleBase:RU361154}.
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 Evidence={ECO:0000256|RuleBase:RU361154};
CC -!- ACTIVITY REGULATION: Inhibited by L-aspartic acid.
CC {ECO:0000256|RuleBase:RU361154}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|RuleBase:RU361154}.
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000256|ARBA:ARBA00004371}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401, ECO:0000256|RuleBase:RU361154}.
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DR EMBL; KQ435701; KOX80383.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M9ACC9; -.
DR STRING; 166423.A0A0M9ACC9; -.
DR OrthoDB; 1847696at2759; -.
DR Proteomes; UP000053105; Unassembled WGS sequence.
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 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361154};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361154};
KW Lysosome {ECO:0000256|RuleBase:RU361154};
KW Reference proteome {ECO:0000313|Proteomes:UP000053105}.
FT DOMAIN 96..272
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 324..378
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 383..678
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
SQ SEQUENCE 705 AA; 81166 MW; D8ACF14AE34A2EC2 CRC64;
MVYMCDTRKR FDALGREVCS RRRAPCQEAD IAVNETLRMW QLVFLLISSA MAGESGPEIE
YPEVPIEYSP LPREEDAPSL LPGMLYPRES ESREVKSLDG MWDFVISPSG DALKGYREAW
FADQLSKVEK VMQMPVPSSY NDITTSRKLR DHIGAVWYQR SFFVPSSWRE QRVFVRFGSV
NYLAQVWIND EFVTNHEMGH LPFEAEISSY LVYGGKNRIT VAVDNTLLQT SVPQGKIIDT
PVDNGTTHLQ TYTFDFFNYA GIHRPVLLHT KPRIYIEDIT VRTGLIGDTG IVKYIIQPAG
LQEHETPICR VSILDAKDIL AVQEPAYGFS GTIKIPFPKL WWPRGMSPNP GYLYTLKVTL
SVANDSKVDV YRLPIGIRTL AWTNTSLLLN DKPIYMRGFG RHEDSILRGR GLDLVTVARD
HELLQWIGAN AYRTSHYPYS DEVLDIADRL GFLIIDECPS VDTENFSPIL LTRHKDSLSE
LIRRDKNRPS VIMWSIANEP RTQLPEAGEY FKQVAHHTKA LDPTRPITIA MARAVQEDKA
GEYLDVISFN RYNAWYNNPG RLDTITSRVI GEAEAWHRKY NKPVLMSEYG ADTMPGLHEL
PEYVWSEEYQ KEVLSKHFIA FDQLRNEGFF IGEFIWNFAD FRTAQTYIRV GGNRKGVFTR
DRQPKMAAFH VRKRYYFLQK ELDGTEIPTD LEDYISLHYS FHSRL
//
