ID A0A0N1AFJ4_9PROT Unreviewed; 454 AA.
AC A0A0N1AFJ4;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=IP80_10150 {ECO:0000313|EMBL:KPF48562.1};
OS beta proteobacterium AAP65.
OC Bacteria; Pseudomonadota; Betaproteobacteria.
OX NCBI_TaxID=1523424 {ECO:0000313|EMBL:KPF48562.1, ECO:0000313|Proteomes:UP000037849};
RN [1] {ECO:0000313|EMBL:KPF48562.1, ECO:0000313|Proteomes:UP000037849}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AAP65 {ECO:0000313|EMBL:KPF48562.1,
RC ECO:0000313|Proteomes:UP000037849};
RA Zeng Y., Feng F., Liu Y., Koblizek M.;
RT "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as
RT Revealed by High-throughput Strain Identification and Genome Sequencing.";
RL Submitted (AUG-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:KPF48562.1}.
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DR EMBL; LJHW01000017; KPF48562.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N1AFJ4; -.
DR STRING; 1523424.IP80_10150; -.
DR PATRIC; fig|1523424.3.peg.633; -.
DR OrthoDB; 9765195at2; -.
DR Proteomes; UP000037849; 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:UP000037849}.
FT ACT_SITE 174
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-1"
FT ACT_SITE 361
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-1"
FT BINDING 28
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 129
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 173
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 408
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 415..416
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
SQ SEQUENCE 454 AA; 50030 MW; 933599D99FABC7F8 CRC64;
MSHTLPPWPA RSAFPPGFLF GAATSAFQIE GGVATEGRGA SWWDRYTHLP GRIRDGRHAD
TACDHHRLWR EDLDLMQRLG LQAYRFSIAW PRVLPMGRGA ANEAGLAFYD RLVDGLLARG
IVPYATLYHW DLPLALADAG GWQSRDTAAA LADYAALVVQ RLGDRVQHWA TLNEPRCCAW
VGHFEGRHAP GLQGDLRATL AAVHHQLLGH GLAVQAMRAA RPTAQLGLVL DLKPHLPASG
HADDVAAARR GDGVFNRCLL DPVFHASYPA DVVQACAAEM PEIRSGDMAT IATPIDELGI
NYYTRAVVAH DASRPWPSLR EERVPGVHHS TMGWEDWPEG LEQTLLRVQR EYAPKAVYIA
ENGAAEPDEV STDGLVHDPA RQHYLRGHVQ ACARALAQGV PLQAYLAWSL MDNFEWGRGY
TQRFGLVHVD FETQQRRVKN SGADYAAFIA SPRA
//
