ID A0A1I4V4G0_9PSEU Unreviewed; 812 AA.
AC A0A1I4V4G0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Beta-glucosidase {ECO:0000313|EMBL:SFM96079.1};
GN ORFNames=SAMN05421805_10214 {ECO:0000313|EMBL:SFM96079.1};
OS Saccharopolyspora antimicrobica.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharopolyspora.
OX NCBI_TaxID=455193 {ECO:0000313|EMBL:SFM96079.1, ECO:0000313|Proteomes:UP000199398};
RN [1] {ECO:0000313|EMBL:SFM96079.1, ECO:0000313|Proteomes:UP000199398}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CPCC 201259 {ECO:0000313|EMBL:SFM96079.1,
RC ECO:0000313|Proteomes:UP000199398};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FOUP01000002; SFM96079.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I4V4G0; -.
DR STRING; 455193.SAMN05421805_10214; -.
DR Proteomes; UP000199398; 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; 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:SF10; BETA-GLUCOSIDASE F-RELATED; 1.
DR Pfam; PF14310; Fn3-like; 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; 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|RuleBase:RU361161};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361161}.
FT DOMAIN 391..542
FT /note="PA14"
FT /evidence="ECO:0000259|PROSITE:PS51820"
SQ SEQUENCE 812 AA; 86237 MW; F654E251033DCD05 CRC64;
MVDHDAAIAA ALAELDLDAK ARLLAGQGMW SLPALPEIGL APLVMSDGPI GVRGVRWSAS
DPSIALPSPT ALAATWDPEL ARRAGHLLAQ EAQRKGVHVL LAPTVNLHRS PLGGRHFECY
SEDPHLTGEI GTGYVRGVQE GGVGTTVKHF VANDAETERF TVDNIVGERA LRELYLAPFE
AIVKQARPWG VMAAYNSVNG PTMTEHARLQ NEVLRGEWGF DGCIVSDWFA ARHTARAIRG
GLDIAMPGPR TVYGEALAAA VRAGEVEESL VDGAVRNVLR LAARVGALEG VPAAVPPEQR
PDRIDGHALA REIAHRAFVL VRNENRALPL EPSADVAVIG RAARDARVLG GGSAQVFPDR
VVSPLDGLRA ALPDVTFAVG TEINDELTAA GTGFALRAVV RDADGRVLGE ETLPNGMVQW
HGDFPEGVRY DELHSVEITG TFTPQDSGPH TFGTKGLGGF ELTVAGAVVF GGEHSADGRD
PFDVFFEAPV PRAEVELTAG EAVEVSLVNV VPKITASLDS VAVGLAHRGP RRDAEELLDE
AVAAARAAGT AIVVVATTDR VESEGFDRAS LRLPGRQDEL VRRVAAVNPN TVVVVNSGSP
VEMPWRDDVA AILLSWFPGQ EAGAALADVL LGVEEPGGRL PTTWPTRLAD APVTRVAPTD
GELHYDEGVF IGYRAWQRAG TAPAYCFGHG LGYTDWHYES AELTAPEGPD ELARLTVRVR
NTGDRAGREV VQVYLAVPEA DSVERPARRL AGFASVTAEP GATAEATVVL PRRAAEIWDE
SAGSWRLVPG TYTAETGHSL DDVRLHTPVD AA
//
