ID A0A0Q7K4S6_9ACTN Unreviewed; 483 AA.
AC A0A0Q7K4S6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=ASD06_07655 {ECO:0000313|EMBL:KQX66233.1};
OS Angustibacter sp. Root456.
OC Bacteria; Actinomycetota; Actinomycetes; Kineosporiales; Kineosporiaceae.
OX NCBI_TaxID=1736539 {ECO:0000313|EMBL:KQX66233.1, ECO:0000313|Proteomes:UP000051170};
RN [1] {ECO:0000313|EMBL:KQX66233.1, ECO:0000313|Proteomes:UP000051170}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root456 {ECO:0000313|EMBL:KQX66233.1,
RC ECO:0000313|Proteomes:UP000051170};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQX66233.1, ECO:0000313|Proteomes:UP000051170}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root456 {ECO:0000313|EMBL:KQX66233.1,
RC ECO:0000313|Proteomes:UP000051170};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQX66233.1}.
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DR EMBL; LMER01000015; KQX66233.1; -; Genomic_DNA.
DR RefSeq; WP_056676158.1; NZ_LMER01000015.1.
DR AlphaFoldDB; A0A0Q7K4S6; -.
DR STRING; 1736539.ASD06_07655; -.
DR OrthoDB; 9765195at2; -.
DR Proteomes; UP000051170; 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:UP000051170}.
FT ACT_SITE 172
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-1"
FT ACT_SITE 387
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-1"
FT BINDING 22
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 312
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 434
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 441..442
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
SQ SEQUENCE 483 AA; 52963 MW; AC8C9183DAF9F38E CRC64;
MAQNTRQFPE DFLWGSATAS YQIEGAVAEG GRTPSIWDTF SHTPGKVANG DTGDVADDHY
HRFREDVAIM RDLGLRSYRF SVAWPRITPQ VTPDALGPVN DEGLDFYRAL VAELVAAGIE
PAVTLYHWDL PQALEDAGGW AERRTAERFA EYAAVVARAL SPQVDTFITL NEPWCSAYLG
YASGVHAPGR QDPASALAAV HHLNLAHGLA TSAIRAAVPS ARVALTLNLA WVHAPDGTAY
SDELLASSEG DRDAVRRIDG LQNRVFLDPV MSGRYPADVQ HDTAGVTDWS FVRDGDLELV
HQVPDVLGLN YYSPTLVRRW DGSSPRQTAD GHDASAASPW IACDDVEFPE QPGQHTDMGW
AIDPRGMTEL LLRLHRDYPG VELMVTENGA AFPDQVSDDG AVHDPARIDY LDQHLAAVLD
AIHAGAPVRG YYLWSLLDNF EWSFGYSKRF GVVHVDYDTQ ARTIKDSGRW YAKVVASGEL
PTA
//
