ID A0A0Q7BAI4_9ACTN Unreviewed; 812 AA.
AC A0A0Q7BAI4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Beta-glucosidase {ECO:0000313|EMBL:KQW45085.1};
GN ORFNames=ASC77_20105 {ECO:0000313|EMBL:KQW45085.1};
OS Nocardioides sp. Root1257.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1736439 {ECO:0000313|EMBL:KQW45085.1, ECO:0000313|Proteomes:UP000051939};
RN [1] {ECO:0000313|EMBL:KQW45085.1, ECO:0000313|Proteomes:UP000051939}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1257 {ECO:0000313|EMBL:KQW45085.1,
RC ECO:0000313|Proteomes:UP000051939};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQW45085.1, ECO:0000313|Proteomes:UP000051939}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1257 {ECO:0000313|EMBL:KQW45085.1,
RC ECO:0000313|Proteomes:UP000051939};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQW45085.1}.
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DR EMBL; LMDV01000012; KQW45085.1; -; Genomic_DNA.
DR RefSeq; WP_056158142.1; NZ_LMDV01000012.1.
DR AlphaFoldDB; A0A0Q7BAI4; -.
DR STRING; 1736439.ASC77_20105; -.
DR OrthoDB; 9803863at2; -.
DR Proteomes; UP000051939; 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 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; PS51820; PA14; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000051939}.
FT DOMAIN 403..555
FT /note="PA14"
FT /evidence="ECO:0000259|PROSITE:PS51820"
SQ SEQUENCE 812 AA; 86351 MW; D35D98522056C736 CRC64;
MPSLDLPALV SRLSLEQKVR LLTGADFWAL YDEPAIGLRR MVTSDGPAGV RGELWDERDP
STNIPSPTAI AASWDPELTA TLGRLLAHEA RRKGVDVVLA PTVNLHRSPY GGRHFECLSE
DPVLTGSIGA ALVEGLQSQG VAATVKHFVA NDSETDRLTY DARVDERTLR ELYLAPFETI
VRDAGAWSVM AAYNSVDGAT MTESPMLRAI LHEEWGFDGV IMTDWYAGRS TEAAARGALD
LIMPGPTGPW REALVDAVRE QRVDEADIDA KVLRLLGLAT RVGALADGPE AQPVEPWTDA
ESDALVQRAA AAGFVLVRNA PVGDAPVLPV RPGIKRVAVI GPNAREARFL GGGSALVFPP
ATVSPLAGLL AALGPDVEVT YCLGARGHER VSAADPALLT TPGGEPGIRV EFRGAGGEVL
GADRRLGSAF NWNNAFEGVD PALITEIALD VVVTADQSGE YRIGASGVGR YRLRLDDHPA
FDELLELPPG ADPVEGLMRP PQEWATVALT AGQQVRVSLV HVVKDHTADE DLLVSMQLAV
DCTVEDDDAS LAHAVADAAA ADLAVVVVGT TEEVESEGFD RTSLALPGRQ DELVHRVAAA
RPETVVVVNA GAPVLMPWRD EVAATLLAWF PGQEFGGALA DVLLGRVEPG GRLPTTWPAS
EDAALPSTTP VDGRLDYTEG LHVGYRRFLR DGVEPAYWFG HGLGYTTWTY DDLVVTGTDV
AVTVTNTGDR PGRELVQVYL ARPDSAVERP VRWLVGHAWV EAGPGAGATA RIGVPARAFE
HWSDGGWVRE PGAFTVEVGR SAADIVLSAE VG
//
