ID E2AGJ7_CAMFO Unreviewed; 670 AA.
AC E2AGJ7;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 52.
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=EAG_01784 {ECO:0000313|EMBL:EFN67454.1};
OS Camponotus floridanus (Florida carpenter ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Formicinae; Camponotus.
OX NCBI_TaxID=104421 {ECO:0000313|Proteomes:UP000000311};
RN [1] {ECO:0000313|EMBL:EFN67454.1, ECO:0000313|Proteomes:UP000000311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C129 {ECO:0000313|Proteomes:UP000000311};
RX PubMed=20798317; DOI=10.1126/science.1192428;
RA Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA Wang J., Liebig J.;
RT "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT saltator.";
RL Science 329:1068-1071(2010).
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; GL439316; EFN67454.1; -; Genomic_DNA.
DR RefSeq; XP_019883360.1; XM_020027801.1.
DR RefSeq; XP_019883361.1; XM_020027802.1.
DR AlphaFoldDB; E2AGJ7; -.
DR STRING; 104421.E2AGJ7; -.
DR EnsemblMetazoa; XM_020027801.2; XP_019883360.1; LOC105252146.
DR EnsemblMetazoa; XM_020027802.2; XP_019883361.1; LOC105252146.
DR GeneID; 105252146; -.
DR InParanoid; E2AGJ7; -.
DR OMA; VFSQHFK; -.
DR OrthoDB; 1847696at2759; -.
DR Proteomes; UP000000311; 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:UP000000311};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..670
FT /note="Beta-glucuronidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003156735"
FT DOMAIN 61..236
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 288..342
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 347..642
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
SQ SEQUENCE 670 AA; 76980 MW; 8F142C2F67591453 CRC64;
MWHLIFLLIG SAMAGESGPE SPTDFFDATI KIEAPLPYED AFPIPLPGLL YPRESESREV
RSLDGLWDFA VSEGDALRGY REGWYALDLS KASEVMKMPV PSSYNDITTS RNLRDHVGAV
WYQRTFFVPS FWRDQRVFVR FGSVNYLAQV WINGVLVTNH EMGHLPFEGE LSSYLTFGAE
NRITVAVDNT LLQTSVPQGK IVEMVTDNGT AHMQTYTFDF FNYAGIHRSV LLYTTPRVYV
EDISVRTSLI GEMGIVKYII QPNGLREGEI PICMVSLYDA EQNLAINEPV EGLSGTLKVP
FVKLWWPRGM DSKPGYLYTL EVKLWVENDT KVDIYRLPIG IRTLAWTNTS LLLNDRPVYM
RGFGKHEDSA IRGRGFDLVT SVRDHELLQW VGANAYRTSH YPYSDEVLDM ADRLGFLIID
ECPSVDTENF SPSLLSRHKD SLSELIRRDK NRPSVIMWSL ANEPRTQLAE ADEYFKQIAQ
HTKAIDPTRP VTIALARAVQ EDKAGQFLDV ISFNRYNAWY SNPGRIDMIN DRVYEEAEAW
HKKYNKPVLI SEYGADTMPG LHELPEYVWS EEYQKELLSK HFEAFDRLRH EGYFIGEFIW
NFADFRTAQT YTRVGGNRKG IFTRDRQPKM AAHHVRKRYH ALAVELDGVQ IPGEVEDYYI
SSYYSSHSEL
//
