ID A0A0N0A752_9ACTN Unreviewed; 725 AA.
AC A0A0N0A752;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=ADL04_29150 {ECO:0000313|EMBL:KOV93038.1};
OS Streptomyces sp. NRRL B-3648.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1519493 {ECO:0000313|EMBL:KOV93038.1, ECO:0000313|Proteomes:UP000037702};
RN [1] {ECO:0000313|EMBL:KOV93038.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-3648 {ECO:0000313|EMBL:KOV93038.1};
RA Noorani M.;
RL Submitted (JUL-2015) 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}.
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:KOV93038.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LGDZ01000208; KOV93038.1; -; Genomic_DNA.
DR RefSeq; WP_053711139.1; NZ_LGDZ01000208.1.
DR AlphaFoldDB; A0A0N0A752; -.
DR PATRIC; fig|1519493.3.peg.6200; -.
DR OrthoDB; 9803863at2; -.
DR Proteomes; UP000037702; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0030247; F:polysaccharide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 2.60.40.290; -; 1.
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; IPR001919; CBD2.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR012291; CBM2_carb-bd_dom_sf.
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 InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR30620:SF16; LYSOSOMAL BETA GLUCOSIDASE; 1.
DR PANTHER; PTHR30620; PERIPLASMIC BETA-GLUCOSIDASE-RELATED; 1.
DR Pfam; PF00553; CBM_2; 1.
DR Pfam; PF00933; Glyco_hydro_3; 1.
DR Pfam; PF01915; Glyco_hydro_3_C; 1.
DR PRINTS; PR00133; GLHYDRLASE3.
DR SMART; SM00637; CBD_II; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR PROSITE; PS51173; CBM2; 1.
DR PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU361161};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361161};
KW Reference proteome {ECO:0000313|Proteomes:UP000037702};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..725
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005843672"
FT DOMAIN 624..725
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
SQ SEQUENCE 725 AA; 75381 MW; 2E21B23F2EB577F8 CRC64;
MSLLLARRSP VTALAVCAAA LALTAPAAAA PEPAVAPAAL LPYQDASLPV PDRVTDLLSR
MSLDDKLGQM TQIEKDALVP QSDLAAYRIG SVLSGGDSTV GPNNAQTWAD TYDSLQRTAL
ATPLGIPVIY GIDAVHGHNA VRGATLFPHN IALGATRDPA LVQRIGRAVA EEVSGTGIDW
DFAPCLCVAR DDRWGRTYES YGETPELPSA LTTFITGLQG DALGAGPASV LATAKHYLGD
GGTAGGVDQG DTKASEAELR AVHLPPFKEA VRRGVGAVML SYSSWNGVRS HADRYLVTDV
LKGELGFTGF VVSDWAAVDQ LDGQSGFTGA EIRTAVDAGV DMVMVPHDYK KFLTLLRGEV
TAGRIAVSRI DDANRRILTK KFQLGLFEHP LTDRSYTATV GSAAHRELAR QAVRASQVLL
KNDGGVLPLP KSAKLFVAGK SADDIGNQSG GWTVGWQGRS GPVTDGTTIL QGIRAAVTDP
SRVTYDRYGN GVDSSYRAAV AVVGETPYAE GRGDRPGGLG LDQEDLSTLA RLEASGVPVV
VVLVSGRPLD VSARLPDWKA LLAAWLPGTE GAGVSDVLFG DHAPTGRLPV SWPRTSAQEP
VNDGDGKDPL FPYGYGLTYS GTGPAPVPGT CTARLRTTSS WPGGHQAEVT VENTGSVALT
GWSVDWELGG SRISSLWNGS LGTADGRATV RNAAFNGSLA PGATASFGFT ADGSAGTPAP
HCAGS
//
