ID F4QGH5_9CAUL Unreviewed; 635 AA.
AC F4QGH5;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=ABI_20970 {ECO:0000313|EMBL:EGF93656.1};
OS Asticcacaulis biprosthecium C19.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Asticcacaulis.
OX NCBI_TaxID=715226 {ECO:0000313|EMBL:EGF93656.1, ECO:0000313|Proteomes:UP000006512};
RN [1] {ECO:0000313|Proteomes:UP000006512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C19 {ECO:0000313|Proteomes:UP000006512};
RA Brown P.J.B., Buechlein A., Hemmerich C., Brun Y.V.;
RT "Draft genome sequence of Brevundimonas diminuta.";
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC {ECO:0000256|ARBA:ARBA00005336, ECO:0000256|RuleBase:RU361161}.
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DR EMBL; GL883077; EGF93656.1; -; Genomic_DNA.
DR RefSeq; WP_006272857.1; NZ_GL883077.1.
DR AlphaFoldDB; F4QGH5; -.
DR STRING; 715226.ABI_20970; -.
DR eggNOG; COG1472; Bacteria.
DR HOGENOM; CLU_004542_9_3_5; -.
DR OrthoDB; 9781691at2; -.
DR Proteomes; UP000006512; 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 InterPro; IPR019800; Glyco_hydro_3_AS.
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 PANTHER; PTHR30620:SF77; BETA-GLUCOSIDASE BOGH3B-LIKE; 1.
DR PANTHER; PTHR30620; PERIPLASMIC BETA-GLUCOSIDASE-RELATED; 1.
DR Pfam; PF00933; Glyco_hydro_3; 1.
DR Pfam; PF01915; Glyco_hydro_3_C; 1.
DR PRINTS; PR00133; GLHYDRLASE3.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
DR PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361161};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361161};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..635
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003320225"
FT DOMAIN 57..374
FT /note="Glycoside hydrolase family 3 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00933"
FT DOMAIN 411..612
FT /note="Glycoside hydrolase family 3 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01915"
SQ SEQUENCE 635 AA; 67031 MW; 819C4AE66BA83353 CRC64;
MSLLSTVARI ALVSILFAST PALAKEPLTD WPHITSAIPQ DAATEAKIAK MVAGMSLRDK
VAQMTQVEIK TVTPQDIRTY QFGSVLNGGG SWPNMDKYAT AKDWVAMADS FHAQAKIPLL
WGTDAVHGHS NVVGATLFPH NIGLGAARDP ELIGDIAAAT GKAVRATGVN WAFAPTLAVV
EDGRWGRTYE GFSSDPQLIH DYARAYVDGM QGNFQGPGNI VATAKHYIGD GGTAQGIDQG
ITPASEAELI NVHAQGYFGA LEAGVQTVMV SYSSWTDTGT GKAYGKMHGN GYLVNDVLKG
KMGFDGFVIS DWNAIEQIPG CTKDRCPQAI NAGVDMIMVP FDWKAFIDNT VADVEIGDIP
MSRIDDAVTR ILRVKMRAGL FGAKPSASPY AGKPQALQAR DLARRAVAET LVLLKNEGGL
PLKAGAKILV VGKSANNMAN QSGGWSITWQ GTETSNADYP VGDSLLTAIK ATNTGGTVTY
SAAGADVDVS QFDVVVAVIG ETPYAEGKGD IKPDQSLAHS DRYPEDIAAL NAVSGKGKPV
VTVFESGRTV YANDLINASD AFVAAWLPGT EGKGVTDVLF GQKDFKGVLP FAWPGAPCEG
RTLFPAGYGL SYTNQATVTT LEFIETPGCP HAQSH
//