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Database: UniProt
Entry: A0A3M0HUP5_9ACTN
LinkDB: A0A3M0HUP5_9ACTN
Original site: A0A3M0HUP5_9ACTN 
ID   A0A3M0HUP5_9ACTN        Unreviewed;       454 AA.
AC   A0A3M0HUP5;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 17.
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=CTZ28_43605 {ECO:0000313|EMBL:RMB79818.1};
OS   Streptomyces shenzhenensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=943815 {ECO:0000313|EMBL:RMB79818.1, ECO:0000313|Proteomes:UP000270471};
RN   [1] {ECO:0000313|EMBL:RMB79818.1, ECO:0000313|Proteomes:UP000270471}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=193 {ECO:0000313|EMBL:RMB79818.1,
RC   ECO:0000313|Proteomes:UP000270471};
RA   Siqueira K.A., Liotti R.G., Mendes T.A.O., Soares M.A.;
RT   "Draft genome of actinobacteria isolated from guarana (Paullinia cupana
RT   (Mart.) Ducke.";
RL   Submitted (NOV-2017) 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:RMB79818.1}.
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DR   EMBL; PENI01000053; RMB79818.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3M0HUP5; -.
DR   OrthoDB; 9765195at2; -.
DR   Proteomes; UP000270471; 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:UP000270471}.
FT   ACT_SITE        170
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-1"
FT   ACT_SITE        355
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-1"
FT   BINDING         24
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT   BINDING         125
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT   BINDING         169
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT   BINDING         297
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT   BINDING         402
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT   BINDING         409..410
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
SQ   SEQUENCE   454 AA;  50462 MW;  03C48CC5A21AC5B4 CRC64;
     MSDRIDLAAL PHDFLWGTAT SAYQIEGAVA EDGRTPSIWD TFSHTPGRID NGDHGDVACD
     HYHRWREDID LMRRLGTNAY RLSIAWPRVL PGGDGPVNPE GLAFYDQLVD ALLEAGITPS
     VTLYHWDLPQ VLQDRGGWPE RDTAEHFAAY AQAVAARLGD RVHHWATLNE PSCSAWIGHL
     EGTMAPGLTD LTAAVRASYH LLLGHGLAVQ ALRAAAPDAE IGIVNNLSTV RPAGDRPEDE
     AAARRHDGHV NRWWLDPVHG CGFPADMREV YGVDLPERPG DLETIAAPLD WLGLNYYFPA
     QVTDDPAGPA PHARSVRRPG VPRTGMDWEI DASGIETLLL RLTHEYGARR IYVTENGCAY
     PDVIRPDGTV DDPERQDYLV EHLAACASAA RKGAPLAGYF AWSLLDNFEW AYGYDKRFGL
     VHVDYRTQQR TIKNTGHRYT DIIHHHRTQS HHTT
//
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