ID A0A4R6JAY7_9ACTN Unreviewed; 778 AA.
AC A0A4R6JAY7;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 12.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=C8E87_8311 {ECO:0000313|EMBL:TDO32839.1};
OS Actinoplanes brasiliensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=52695 {ECO:0000313|EMBL:TDO32839.1, ECO:0000313|Proteomes:UP000294901};
RN [1] {ECO:0000313|EMBL:TDO32839.1, ECO:0000313|Proteomes:UP000294901}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43805 {ECO:0000313|EMBL:TDO32839.1,
RC ECO:0000313|Proteomes:UP000294901};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (MAR-2019) 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:TDO32839.1}.
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DR EMBL; SNWR01000002; TDO32839.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4R6JAY7; -.
DR Proteomes; UP000294901; 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 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.
PE 3: Inferred from homology;
KW Glycosidase {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..778
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038554504"
FT DOMAIN 668..777
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT REGION 652..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 778 AA; 80371 MW; 09DCC895F5115E31 CRC64;
MPVRFVRTTL ILAGLLAVTA PVSAAQASTA TRLGAQASTA TRLGAHASTA TRLGAETLTA
TRLAGQGATA SDSLAGSGLA SRAAAAALPY QDPGLPVSAR VDDLVSRMTL DDKIGQMVQS
ERGTTSAADV TSFRVGSILS GGGSAPANNT PAGWSDMYDD YQRAALATPL QIPILYGIDA
VHGNNNVPGS TIFPHNIGLG ATRDPALVER IGRATADEVK GAGLDWTFAP CVCVARNDRW
GRTYESYGEK PEIASSMTTI VDGLQDADVL ATAKHYVGDG GTTGGVDQGN TQISEAELRA
VHLPPFRAAV ERGVASVMVS FSSFNGVKVH GHKYLVTDVL KGELGFAGFV VSDWAGIDQI
DGRPGFTQAE IATAVNAGLD MAMVPTDWKT FVGHLRAAVQ AGQIPMSRID DANRRILTQK
FAFGLFEKPY AERGFASTVG SAEHRALARQ AVRQSQVLLK NAGNVLPLAK SGGKIFVAGK
SADDLGNQSG GWTVSWQGSS GNIIAGTSIL AGIRAAAGNG TTVTYNRDGV GIDNSYRAAV
AVIGETPYAE GEGDRTGSMG LDSTDLNTLS RLRAAGVPVI VVLVSGRPLD IGSEIGNWNA
LLAAWLPGSE GAGVADVLFG DYAPTGKLPV TWMQSASQQP INDGDGKTPL FPYGHGLTYD
GGPDPDPDPE PSSSCRVKYT TNDWNTGFTG TVSVTNTGST PVSPWTLTWS FTGGQTITQA
WSARVTQSGS AVTASGESWS STLAPGASAS FGFNGSHPGT NPRPAAFALN GATCTTES
//
