ID S6IFM1_9PSED Unreviewed; 879 AA.
AC S6IFM1;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=CFII64_18618 {ECO:0000313|EMBL:EPJ79897.1};
OS Pseudomonas sp. CFII64.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=911242 {ECO:0000313|EMBL:EPJ79897.1, ECO:0000313|Proteomes:UP000014850};
RN [1] {ECO:0000313|EMBL:EPJ79897.1, ECO:0000313|Proteomes:UP000014850}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFII64 {ECO:0000313|EMBL:EPJ79897.1,
RC ECO:0000313|Proteomes:UP000014850};
RA Feris K.P., Lalor S.J.;
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC {ECO:0000256|ARBA:ARBA00005336}.
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:EPJ79897.1}.
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DR EMBL; ATLO01000042; EPJ79897.1; -; Genomic_DNA.
DR AlphaFoldDB; S6IFM1; -.
DR PATRIC; fig|911242.4.peg.3694; -.
DR Proteomes; UP000014850; 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:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 1.
DR Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR026891; Fn3-like.
DR InterPro; IPR002772; Glyco_hydro_3_C.
DR InterPro; IPR036881; Glyco_hydro_3_C_sf.
DR InterPro; IPR001764; Glyco_hydro_3_N.
DR InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR037524; PA14/GLEYA.
DR InterPro; IPR011658; PA14_dom.
DR PANTHER; PTHR42715; BETA-GLUCOSIDASE; 1.
DR PANTHER; PTHR42715:SF28; BETA-GLUCOSIDASE-RELATED; 1.
DR Pfam; PF14310; Fn3-like; 1.
DR Pfam; PF00933; Glyco_hydro_3; 1.
DR Pfam; PF01915; Glyco_hydro_3_C; 1.
DR Pfam; PF07691; PA14; 1.
DR PRINTS; PR00133; GLHYDRLASE3.
DR SMART; SM01217; Fn3_like; 1.
DR SMART; SM00758; PA14; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF56988; Anthrax protective antigen; 1.
DR PROSITE; PS51820; PA14; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT DOMAIN 394..548
FT /note="PA14"
FT /evidence="ECO:0000259|PROSITE:PS51820"
FT REGION 847..879
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 879 AA; 95730 MW; CD1092B8D57DC2EC CRC64;
MAQQTLSQMT LEEKFSYISG TGGWDVKPLP RFNLPQILGA DGGLGVRYTN QGNDQGVVYP
SGPNLAATFN LRRAVDFGRA LGYDTATGGY HYITGPGMNM YRMPYGGRNF EYLTGEDPFL
GASMAPAVIN GIQSRGIWAD AKHFAANDQE TNRFVLDQSM PERVLREMTM PPFESASKNG
KVALMMCSFQ KVNGEFVCEN SHLLRDILKQ GWGYQGFVQS DYGAVVNGLN AAQGGTDIEM
LFGVQMNSTT LTPYIESGVL SVATIDDKVL RILRQIYLFD FDTYVPSTAH DMDNPASNQA
ALNVAREGIV LLKNKDNFLP LDRNVVRKIA VVGVLGKYAP PIGFGSAYVS ARNYISEVSG
MRQVASNAQV TFLDSLSLDP QAAVWTHLDS DGTTSVPGMT AEYFTNPDWS GTPAATRTET
YVDLNWDSDE NLPTDGNDRN TSIRWSGRIT PTISGEHVFK VRADGLIRLR INGQQILDNG
DGEPLPNNPI PPTIPAYTKY TLEAGQTYDV MLEYSRRPAY VASLGGYTGV RFSWASLVAP
DDIASYDAVV VAAGNSNEYE GEGWDHMFEL PEYQGQMIQS IAAQNPKTIV ALHGGTGLKV
SDWVDQVSGL LHAFYPGQNG GQALAEIIFG RVNPSAKLPI SLERDIQDNP LFSYFPQFDN
EGVITQTSYA NDLLSGYRGY EKKGTTPLYP FGYGLSYTQF SYSGIRITPA VALGNTPVQV
SFDITNTGQR AGAEVAQLYV GQRNPRLERP IKELKGYQKV FLQPGERQRV TIELNGRSLA
YYNPATSNWV IDGDTFDIGV GAASNDIRLR TRLLSPYRQS LSVANSNPLP PTVVTATKVT
ARQLAMNGND DQASGDGLDT PVPAPVTPPG NGNSGGSTQ
//