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Database: UniProt
Entry: A0A0Q4GYH8_9SPHI
LinkDB: A0A0Q4GYH8_9SPHI
Original site: A0A0Q4GYH8_9SPHI 
ID   A0A0Q4GYH8_9SPHI        Unreviewed;       600 AA.
AC   A0A0Q4GYH8;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=Beta-glucuronidase {ECO:0000256|ARBA:ARBA00016205};
DE            EC=3.2.1.31 {ECO:0000256|ARBA:ARBA00012761};
GN   ORFNames=ASE74_15535 {ECO:0000313|EMBL:KQM78118.1};
OS   Pedobacter sp. Leaf216.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Pedobacter.
OX   NCBI_TaxID=1735684 {ECO:0000313|EMBL:KQM78118.1, ECO:0000313|Proteomes:UP000051744};
RN   [1] {ECO:0000313|Proteomes:UP000051744}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf216 {ECO:0000313|Proteomes:UP000051744};
RA   Garrido-Oter R., Mueller D.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000051744}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf216 {ECO:0000313|Proteomes:UP000051744};
RA   Vorholt J.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC       {ECO:0000256|ARBA:ARBA00007401}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KQM78118.1}.
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DR   EMBL; LMKM01000005; KQM78118.1; -; Genomic_DNA.
DR   RefSeq; WP_055904631.1; NZ_LMKM01000005.1.
DR   AlphaFoldDB; A0A0Q4GYH8; -.
DR   STRING; 1735684.ASE74_15535; -.
DR   OrthoDB; 9801077at2; -.
DR   Proteomes; UP000051744; Unassembled WGS sequence.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
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; 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; PS00608; GLYCOSYL_HYDROL_F2_2; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..600
FT                   /note="Beta-glucuronidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006219604"
FT   DOMAIN          35..211
FT                   /note="Glycosyl hydrolases family 2 sugar binding"
FT                   /evidence="ECO:0000259|Pfam:PF02837"
FT   DOMAIN          215..304
FT                   /note="Glycoside hydrolase family 2 immunoglobulin-like
FT                   beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF00703"
FT   DOMAIN          306..547
FT                   /note="Glycoside hydrolase family 2 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF02836"
SQ   SEQUENCE   600 AA;  69349 MW;  23E70F5B947076B8 CRC64;
     MLKTTYSVFL ICFSLLSSIS YGQVTAIQNI QARKIQSLNG KWNYIVDPYE NGYYDYRHEP
     FDQSKTGTGG YFDDKVQKDK SELIEYDFDH SPQMNVPGDW NSQSEKLELY EGNVWLRKKF
     DAKPEKGKRY FVYFAAVNYE AHVYLNGKKL GVHKGGFTPF QFDVTSNLKV GENSIVLKVD
     NIRKQDEIPT VNTDWWNYGG ITRDVFLAEF PDHFINDYKL QLAKGNKNLL NFSVKLADAT
     AGQEITLSIP ELKLEKKYKT DSEGKIADEF TWNNLSLWSP ETPKLYAVNI KTDKENINDK
     IGFRTIQVDG DSILLNGKSV FLRGISLHDE NPLLAGRLRS EGDMRMMLQW AKDMNCNYVR
     LAHYPHNEEM IRLADEMGLL VWAEVPVYWT ISWTNPATYA NAKQQLTDLI VRDKNRASVI
     VWSIGNETPL SDARLSFMSN LAETARTFDD TRLVAAALEV HREGNNIILN DPLGEKIDLV
     SFNEYAGWYW GGNPSEITKY NFDIKYKKPV VITEFGGDAL GGFHADENTR WSEEYQEALY
     KNQITMLSKI GALRGMTPWI LTDFRSPRRQ HPIYQNFWNR KGLIFYVLKD FYDQMQVKYK
//
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