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Database: UniProt
Entry: A0A494WEY3_9SPHN
LinkDB: A0A494WEY3_9SPHN
Original site: A0A494WEY3_9SPHN 
ID   A0A494WEY3_9SPHN        Unreviewed;       795 AA.
AC   A0A494WEY3;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN   ORFNames=SAMIE_1030210 {ECO:0000313|EMBL:BBD99520.1};
OS   Sphingobium amiense.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=135719 {ECO:0000313|EMBL:BBD99520.1, ECO:0000313|Proteomes:UP000279959};
RN   [1] {ECO:0000313|EMBL:BBD99520.1, ECO:0000313|Proteomes:UP000279959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16289 {ECO:0000313|EMBL:BBD99520.1,
RC   ECO:0000313|Proteomes:UP000279959};
RA   Ootsuka M., Nishizawa T., Ohta H.;
RT   "Complete Genome Sequence of the Nonylphenol-Degrading Bacterium
RT   Sphingobium amiense DSM 16289T.";
RL   Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC       {ECO:0000256|ARBA:ARBA00005336, ECO:0000256|RuleBase:RU361161}.
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DR   EMBL; AP018664; BBD99520.1; -; Genomic_DNA.
DR   RefSeq; WP_066700699.1; NZ_AP018664.1.
DR   AlphaFoldDB; A0A494WEY3; -.
DR   KEGG; sami:SAMIE_1030210; -.
DR   Proteomes; UP000279959; Chromosome.
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; IPR019800; Glyco_hydro_3_AS.
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   PANTHER; PTHR42715; BETA-GLUCOSIDASE; 1.
DR   PANTHER; PTHR42715:SF28; BETA-GLUCOSIDASE-RELATED; 1.
DR   Pfam; PF00933; Glyco_hydro_3; 1.
DR   Pfam; PF01915; Glyco_hydro_3_C; 1.
DR   PRINTS; PR00133; GLHYDRLASE3.
DR   SMART; SM01217; Fn3_like; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF56988; Anthrax protective antigen; 1.
DR   SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
DR   PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
DR   PROSITE; PS51820; PA14; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361161};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361161};
KW   Reference proteome {ECO:0000313|Proteomes:UP000279959}.
FT   DOMAIN          388..538
FT                   /note="PA14"
FT                   /evidence="ECO:0000259|PROSITE:PS51820"
SQ   SEQUENCE   795 AA;  84710 MW;  6D7746D2FCA7D3D9 CRC64;
     MTDTLTLEEQ LAMTAGAAMW STVGYEKAGI PALSMADGPM GIASGRVDER DIALLTPCPT
     ALGASWDVEL NARVGALVGG EAIRMGVDMV LAPNVNLARS PLAGRAFEYF SEEPVLAGVL
     GAAWTTGLQS TGTASVVKHL VCNDSETDRD RMNAVVDERT LREVYLLPFE LCAQAGAGGM
     LAAYNRVNGD WCAEQHHVLT TIVKGEWAYP GLIMSDWFGT HSTAATLHAG LDLEMPGPAR
     FLGFRANEAL AKGDLDTGRI RDAAARVTRA ALRFRQDKTA PIVGRDADNL LVEAAAAGFV
     MLRNEGGLLP LVPGRDRHIA IIGPNAAAPC YQGGTFAKIA VSPQAARPLE AIMARFADHA
     RVDYEPGVDP QPRLPSMPVT PCRDLGDGFA SGMTIDYYDG QQADARLIAS ETRDTNSLVW
     FAGVHDDVAM LGQPARIVAR GIFRAEQDGD HIFYLGATGP VVMRVDGAEV LAQQEPIPSS
     DVMGKLKSGD ARSVSLALRA GQEAAVEVEF TYDPARVHGL WYGIRRPDTP EAMLARAVAL
     AGQADAVILM VGETSDASVE SKDRGDTHLP AEQIALIEAV TAANPRTAVV ANVGHAFDTR
     WEDRAAALLI AWYPGEGFGE AIAQVLAGDR EPGGRMPVAI AREESDYPAF SLTPDANGDL
     AYAEGTRIGY RGMADPRHTL GEGSGYADIA LLAARVELGD DGGLVVRATV ENRSDRAGSD
     VIQIYRRAPE LALCGFAKAH LAPGERRDIL IPIARRRLQS WRDGWVDIEN PGLFAGRSAR
     DIAFDLSLPA LEPIA
//
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