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
//