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Database: UniProt
Entry: A0A1Q6FX92_9BACT
LinkDB: A0A1Q6FX92_9BACT
Original site: A0A1Q6FX92_9BACT 
ID   A0A1Q6FX92_9BACT        Unreviewed;       605 AA.
AC   A0A1Q6FX92;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Beta-glucuronidase {ECO:0000313|EMBL:OKZ03409.1};
GN   ORFNames=BHV65_03460 {ECO:0000313|EMBL:OKZ03409.1};
OS   Alistipes sp. 58_9_plus.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae;
OC   Alistipes.
OX   NCBI_TaxID=1896970 {ECO:0000313|EMBL:OKZ03409.1, ECO:0000313|Proteomes:UP000186889};
RN   [1] {ECO:0000313|EMBL:OKZ03409.1, ECO:0000313|Proteomes:UP000186889}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=58_9_plus {ECO:0000313|EMBL:OKZ03409.1};
RX   PubMed=27819664; DOI=10.1038/nbt.3704;
RA   Brown C.T., Olm M.R., Thomas B.C., Banfield J.F.;
RT   "Measurement of bacterial replication rates in microbial communities.";
RL   Nat. Biotechnol. 34:1256-1263(2016).
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:OKZ03409.1}.
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DR   EMBL; MNQG01000025; OKZ03409.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q6FX92; -.
DR   Proteomes; UP000186889; 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; 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; PTHR42732; BETA-GALACTOSIDASE; 1.
DR   PANTHER; PTHR42732:SF3; HYDROLASE-RELATED; 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   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   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..605
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012298940"
FT   DOMAIN          38..157
FT                   /note="Glycosyl hydrolases family 2 sugar binding"
FT                   /evidence="ECO:0000259|Pfam:PF02837"
FT   DOMAIN          202..297
FT                   /note="Glycoside hydrolase family 2 immunoglobulin-like
FT                   beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF00703"
FT   DOMAIN          301..462
FT                   /note="Glycoside hydrolase family 2 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF02836"
SQ   SEQUENCE   605 AA;  68484 MW;  46199A547BAC9C19 CRC64;
     MKSRLLIVVA ALLFSTAIGA QPRAEYPRPQ FERADWVNLN GEWSFALDLS DSGRDRDFYN
     SKGFEQRITV PFAPESKLSG IGYTDFINSV WYQRMIQIPS AWQGKRVKLN FGAVYYESEV
     YIDGRFVGRH YGGSDSFAFD ITDFVGDGKE HSIVVHAESD LRSGTQPGGK QSTNYYSYGC
     SYTRTTGIWQ TVWMEAVDDM ALERVQVVTD IDNEQIVVIP TYYNVAGGNT LSVEVRDGGK
     VVAHAESAAV QGVPVVVALK KAKLWSPESP FLYDVVYEVK DAEGKTLDRV DAYVGMRKVH
     IDGNKIYLNN KPYYQRLVLD QGFYPDGIWT APSDEALKHD IEMSKAAGFN GARLHQKVFE
     ERFHYWADKL GYIVWGEMAS WDKDFNSVAA ARNFLSEWGN IVVRDRNHPA LIVWTPFNEE
     FGVPSNEAGR FLTDVYNETR RLDPTRPVNT VSGGIYVISD FCTAHCYEQD GARLHSMLFD
     GEKFYQPQGP NGGFDRAIRK LYYDGSLPYL LDEFGGIKCA ETQPEGGNSW GYGNAAPTRE
     DFYTRLEALV KAIVDHSDKI CGFCYTQLTD VEQEQNGVYY YDRGEKFDMG RVKAIFQMKA
     EGYEQ
//
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