ID A0A1G9YXF6_9ACTN Unreviewed; 478 AA.
AC A0A1G9YXF6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=SAMN05444921_12010 {ECO:0000313|EMBL:SDN13852.1};
OS Streptomyces wuyuanensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1196353 {ECO:0000313|EMBL:SDN13852.1, ECO:0000313|Proteomes:UP000199063};
RN [1] {ECO:0000313|Proteomes:UP000199063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.7042 {ECO:0000313|Proteomes:UP000199063};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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 ---------------------------------------------------------------------------
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; FNHI01000020; SDN13852.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G9YXF6; -.
DR STRING; 1196353.SAMN05444921_12010; -.
DR OrthoDB; 9765195at2; -.
DR Proteomes; UP000199063; 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};
KW Hydrolase {ECO:0000256|RuleBase:RU361175};
KW Reference proteome {ECO:0000313|Proteomes:UP000199063}.
FT REGION 312..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 172
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-1"
FT ACT_SITE 377
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-1"
FT BINDING 26
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 127
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 171
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 303
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 424
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 431..432
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
SQ SEQUENCE 478 AA; 52068 MW; 0AE0A37080C0BA88 CRC64;
MPQAEAPAAL TFPSSFTWGT ATAAYQIEGA ATLDGRTPSI WDTYSRTPGR VRNGDTGDVA
TDHYHRWRED VAIMADLGVG AYRFSLAWPR IQPTGRGPSV QKGLDFYRRL TDELLEKNIQ
PVATLYHWDL PQELEDAGGW PERATAERFA EYAGLAAEAL GDRVRTWITL NEPWCSAFLG
YASGVHAPGR TDPVAALRAA HHLNLGHGKA VQALRANLPA DAQVSVTLNI HHVRPRSGAE
EDVDAARRID ALANRVFTGP MLQGAYPEDL LRDTASLTDW SFVKDGDLEE IAQPLDFLGV
NYYTPTLVSG GAAETSHGSD GHGNSAHSPW PGADGVSFHL PPGSTTAMGW AVDPTGLYDL
LVRLKDDFPR LPLMITENGA AFDDYVNPEG EVNDPDRIAY LQGHLAAVHR AIEAGADVRG
YFLWSLLDNF EWGYGYSKRF GAVYVDYPTG KRIPKASARW YGGVARTGLL PAPDSDQG
//
