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
//