ID A0A0Q9LAJ8_9BACL Unreviewed; 578 AA.
AC A0A0Q9LAJ8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Beta-glucuronidase {ECO:0000313|EMBL:KRE46639.1};
GN ORFNames=ASG81_11345 {ECO:0000313|EMBL:KRE46639.1};
OS Paenibacillus sp. Soil522.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1736388 {ECO:0000313|EMBL:KRE46639.1, ECO:0000313|Proteomes:UP000051180};
RN [1] {ECO:0000313|Proteomes:UP000051180}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil522 {ECO:0000313|Proteomes:UP000051180};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRE46639.1, ECO:0000313|Proteomes:UP000051180}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil522 {ECO:0000313|EMBL:KRE46639.1,
RC ECO:0000313|Proteomes:UP000051180};
RA Schulze-Lefert P.;
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:KRE46639.1}.
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DR EMBL; LMRV01000036; KRE46639.1; -; Genomic_DNA.
DR RefSeq; WP_056633542.1; NZ_LMRV01000036.1.
DR AlphaFoldDB; A0A0Q9LAJ8; -.
DR STRING; 1736388.ASG81_11345; -.
DR OrthoDB; 9762066at2; -.
DR Proteomes; UP000051180; 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 InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR006101; Glyco_hydro_2.
DR InterPro; IPR006103; Glyco_hydro_2_cat.
DR InterPro; IPR006104; Glyco_hydro_2_N.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR10066; BETA-GLUCURONIDASE; 1.
DR PANTHER; PTHR10066:SF67; BETA-GLUCURONIDASE; 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.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT DOMAIN 16..155
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 262..565
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
SQ SEQUENCE 578 AA; 66869 MW; C12F8ADD61F55053 CRC64;
MIRTFQQHRL RKSSLLNGLW DFVFDKNNVG LTEAWHTRFP SDFDQVPVPA CWNNELGKFE
YEGVAWYRTR INCEEAGHLR LLFHAVLGHA DVYWDGEHLG YHFGGYTPFD FTIPNVTAGE
HEIIVRTDST LGRNTIPTHA VDWFHYGGII RPVELQRLDD VSIARMRITY DMTGDSSADV
RIALTLWSMS DASTEVPVSL YRDGELFYSE VVHVPACETV ELNVGQVWTN VKRWEPENPA
LFLIGAVAGN DDMIDRIGFR TVETRNKKIL LNGKELYLQG VNRHEEHPEW GFAFPNKLMT
KDLDIILQMG CNTIRGSHYP QSEYWLDLLD ERGVLFWSEI PIWGACLPAE DTDDPLFVQR
ALTMMDEMIE RDLHHPSILF WSVHNEIDTR SKQAYDLSFK LTELVRGKDQ SRLVAYATMH
PMEDICFGLF DVIGINYYGG WYYGHADFDV MLETFHERCK EYGAENTPVL MTEFGGAGVY
GDSGWEPRLF SEDYQADLIS KALKLFRSDS KISGTYVWQF ADTRADLQSR RAYFRDRARS
FNNKGLVNEY RKPKLAYRVV KGIYTRQSDP YNWGSTLY
//
