ID A0A0M8V6H5_9ACTN Unreviewed; 824 AA.
AC A0A0M8V6H5;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Beta-glucosidase {ECO:0000313|EMBL:KOV59429.1};
GN ORFNames=ADL01_35935 {ECO:0000313|EMBL:KOV59429.1};
OS Streptomyces sp. NRRL WC-3618.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1519490 {ECO:0000313|EMBL:KOV59429.1, ECO:0000313|Proteomes:UP000037738};
RN [1] {ECO:0000313|EMBL:KOV59429.1, ECO:0000313|Proteomes:UP000037738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL WC-3618 {ECO:0000313|EMBL:KOV59429.1,
RC ECO:0000313|Proteomes:UP000037738};
RA Noorani M.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC {ECO:0000256|ARBA:ARBA00005336, ECO:0000256|RuleBase:RU361161}.
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:KOV59429.1}.
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DR EMBL; LGDW01000472; KOV59429.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M8V6H5; -.
DR PATRIC; fig|1519490.3.peg.7834; -.
DR Proteomes; UP000037738; 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 InterPro; IPR011658; PA14_dom.
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 Pfam; PF07691; PA14; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000037738}.
FT DOMAIN 390..550
FT /note="PA14"
FT /evidence="ECO:0000259|PROSITE:PS51820"
SQ SEQUENCE 824 AA; 88449 MW; 24517581C682E535 CRC64;
MRAWVVEGAL ARMDLDTKAR LIAGQDMWSL PAVPAVGLRS VVMSDGPIGV RGTRWSPDDP
SVALPSPTAL AATWDPELAH RAGRLLAHEA RRKGVDVLLA PTVNLHRTPL GGRHFECFSE
DPLLTGVIGA AYVRGVQDGG VGTTVKHFVA NESETERFTL DARVGERALR ELYLAPFEHI
VTHAGPWGVM SAYNGVNGAT MTENHRLQNE VLRGEWGFDG VIVSDWMAAR DTVRAAEGGL
DIAMPGPKTV YGAALADAVR DGRVAERTLD AAVRRVLRLA ARVGALDGAP PAGTSGAEEI
DGRALAREIA RRSFVLLKNH PAPDGGAVLP LNRDALRRVA LIGDTARHAR VMGGGSATVF
PEHVVSPLAG LRRALPPAVE LVHAQGADPR TRLAPAAEYF TLRSRYRDED GNVLAELPQP
DGQVMTVGSL PTGVTARQLH SVDITGSFTP DRSGTHTFGV TGFGSYTLDV AGHRLAEDVC
VPDSDDPFLA FTNPSERRFT VELTAAETVE VAFRFVPFTK GMDDNIAALA FGLGHRPPTA
TDEELIEEAV AVAAASDVAV IVVATTEETE SEGFDRASLK LPGHQDELVR RVAEANPRTV
VVVNTGSPVE MPWRDEVAAV LLGWFPGQEA GHALADVLLG AEEPGGRLPT TWPAAMTDYP
VLDTEPVDGL LTYDEDVFIG YRAWARQDTP PAYWFGHGLG YTDWAYEEAA FTPAPPGAHE
LGTLRVRVRN TGGRPGREVV QVYLEPADTA TADAAECPRR RLAGFATAQA APGRTTVVEI
PVPRRAAQIW DAELDAWHTV QGRYRLRAGR SYPDLRVEAA CDAL
//