ID A0A3N6GYK2_9ACTN Unreviewed; 467 AA.
AC A0A3N6GYK2;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Beta-glucosidase {ECO:0000256|ARBA:ARBA00012744, ECO:0000256|RuleBase:RU361175};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744, ECO:0000256|RuleBase:RU361175};
GN ORFNames=EES45_15410 {ECO:0000313|EMBL:RPK79411.1};
OS Streptomyces sp. ADI97-07.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1522762 {ECO:0000313|EMBL:RPK79411.1, ECO:0000313|Proteomes:UP000281409};
RN [1] {ECO:0000313|EMBL:RPK79411.1, ECO:0000313|Proteomes:UP000281409}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ADI97-07 {ECO:0000313|EMBL:RPK79411.1,
RC ECO:0000313|Proteomes:UP000281409};
RA Guerrero-Garzon J.F., Zehl M., Urban E., Schneider O., Ruckert C.,
RA Busche T., Kalinowski J., Zotchev S.B.;
RT "Streptomyces spp. from the marine sponge Antho dichothoma: analyses of
RT secondary metabolite biosynthesis gene clusters and some of their
RT products.";
RL Submitted (NOV-2018) 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 ECO:0000256|RuleBase:RU361175};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
CC {ECO:0000256|RuleBase:RU361175}.
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:RPK79411.1}.
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DR EMBL; RPGY01000079; RPK79411.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N6GYK2; -.
DR Proteomes; UP000281409; Unassembled WGS sequence.
DR GO; GO:0008422; F:beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR001360; Glyco_hydro_1.
DR InterPro; IPR017736; Glyco_hydro_1_beta-glucosidase.
DR InterPro; IPR033132; Glyco_hydro_1_N_CS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR NCBIfam; TIGR03356; BGL; 1.
DR PANTHER; PTHR10353; GLYCOSYL HYDROLASE; 1.
DR PANTHER; PTHR10353:SF36; KLOTHO (MAMMALIAN AGING-ASSOCIATED PROTEIN) HOMOLOG; 1.
DR Pfam; PF00232; Glyco_hydro_1; 1.
DR PRINTS; PR00131; GLHYDRLASE1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU361175, ECO:0000313|EMBL:RPK79411.1};
KW Hydrolase {ECO:0000256|RuleBase:RU361175, ECO:0000313|EMBL:RPK79411.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000281409}.
FT ACT_SITE 176
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-1"
FT ACT_SITE 371
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-1"
FT BINDING 30
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 131
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 175
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 307
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 418
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 425..426
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
SQ SEQUENCE 467 AA; 50898 MW; FEB7B3ABF6AF240E CRC64;
MTAVDARPDT VAGLRFPTGF RWGTATAAYQ IEGAATEGGR TESIWDTFSR TPGKVRNGDT
GDIAADHLHR MPQDVALMKD LGVTDYRFSV SWPRVQPTGR GPAVEHGLDF YRRLVDELLA
AGIRPVATLY HWDLPQELED AGGWPERDTA QRFADYAGLV ARALGDRVAT WTTLNEPWCA
AFLGYGNGVH APGRTSDVAA LRAAHHLNLA HGSATGVLRS LLPASAEVSL TLNLHALRPL
ADTPADHDAV RRIDAVANRL FLDPVFHGRL PQDLVQDTAA VTDWSFVRDG DLEVVSAPLD
SLGINYYSPS VVSAGASESP SPWAGAEKHV AFTPADGPRT AMDWPVDADG LYELLTRLRD
DLPGLPLMVT ENGAAYDDYA DPSGQVHDPE RVAYLDAHLS AVHRAIGDGV DVRGYFLWSL
LDNFEWAYGY GKRFGIVHVD FASQRRTPKD SARWYADVIA RGGIDRP
//
