ID A0A1G0QYW3_9BACT Unreviewed; 750 AA.
AC A0A1G0QYW3;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=A2080_09190 {ECO:0000313|EMBL:OGU53057.1};
OS Ignavibacteria bacterium GWC2_36_12.
OC Bacteria; Ignavibacteriota; Ignavibacteria.
OX NCBI_TaxID=1798427 {ECO:0000313|EMBL:OGU53057.1, ECO:0000313|Proteomes:UP000178676};
RN [1] {ECO:0000313|EMBL:OGU53057.1, ECO:0000313|Proteomes:UP000178676}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal, non-reducing beta-D-glucosyl residues
CC with release of beta-D-glucose.; EC=3.2.1.21;
CC Evidence={ECO:0000256|ARBA:ARBA00000448};
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:OGU53057.1}.
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DR EMBL; MGZZ01000033; OGU53057.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G0QYW3; -.
DR STRING; 1798427.A2080_09190; -.
DR Proteomes; UP000178676; 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; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 1.
DR Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR026891; Fn3-like.
DR InterPro; IPR002772; Glyco_hydro_3_C.
DR InterPro; IPR036881; Glyco_hydro_3_C_sf.
DR InterPro; IPR001764; Glyco_hydro_3_N.
DR InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR30620:SF16; LYSOSOMAL BETA GLUCOSIDASE; 1.
DR PANTHER; PTHR30620; PERIPLASMIC BETA-GLUCOSIDASE-RELATED; 1.
DR Pfam; PF14310; Fn3-like; 1.
DR Pfam; PF00933; Glyco_hydro_3; 1.
DR Pfam; PF01915; Glyco_hydro_3_C; 1.
DR PRINTS; PR00133; GLHYDRLASE3.
DR SMART; SM01217; Fn3_like; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT DOMAIN 675..744
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 750 AA; 83824 MW; 636DCE7A10ED6B51 CRC64;
MKYFFSLSCL IIIYLTALGF NNETKKFDAS PVVAEKVKSL LSEMTLEEKV GQMTLITIEA
VSEQQGTKDQ HHVLDDKKLE EAIKKYQVGS IINVFDVSHE IDYWHEIINK IQNFAVNETR
LKIPVLYGID AIHGATYTKG STLFPQGINM AATWNRKLVE KIGEITSYET RASGITWNFY
PVMDIGRQPL WPRLWETYGE DVYLASQIGS SYIKGAQGNN IGAPDKLATC LKHYVGYSFP
VNGRDRTPSW ISERMLREYF LPTFEAGISA GAPSVMVNSG EVDGIPTHSD YHLLTEILRG
ELNFKGIVVS DWEDIKRLYT RDKIAETPKE AVRIAVLAGV DMSMVPKDYS FYEYLLELAK
EGSVPIRRID EAVTRILTVK MELGLFENPF PDPEMKKKLA CDEFTNVNLN AARESIVLTK
NENNVLPLTK KVKVLVTGPT ANMLSVMNGG WTITWQGNEE SLYPKEKNTV LEAIREKIGL
ENVSYVEGCS FDKDINIVDA VKEAKGNDVV VLCLGEPAYC EGEGNITDLT LNSVQLELAK
RIMATGKPVV LVMLEGRPRI ISSIVDGAGA VLTAFLPGME GGNALADIIF GDYSPVGKLS
VTYPKYTNGN TTYDYKPIES FEPNVYDPQW AFGYGLSYTT FGYSNLKIDK AEMKEDEELS
ISVDVTNTGN IASEEVVQLY LSDLYGSVSR PNKQLKGFDR ISLNPGETKT VSFKINKEHL
SFIGRENKRI VEPGEFEVTV NTLKEKFVLK
//
