ID A0A1E7KND7_9ACTN Unreviewed; 727 AA.
AC A0A1E7KND7;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
DE Flags: Fragment;
GN ORFNames=AN218_31535 {ECO:0000313|EMBL:OEV05413.1};
OS Streptomyces nanshensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=518642 {ECO:0000313|EMBL:OEV05413.1, ECO:0000313|Proteomes:UP000176005};
RN [1] {ECO:0000313|EMBL:OEV05413.1, ECO:0000313|Proteomes:UP000176005}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCSIO 10429 {ECO:0000313|EMBL:OEV05413.1,
RC ECO:0000313|Proteomes:UP000176005};
RX PubMed=27446038; DOI=10.3389/fmicb.2016.00998;
RA Tian X., Zhang Z., Yang T., Chen M., Li J., Chen F., Yang J., Li W.,
RA Zhang B., Zhang Z., Wu J., Zhang C., Long L., Xiao J.;
RT "Comparative Genomics Analysis of Streptomyces Species Reveals Their
RT Adaptation to the Marine Environment and Their Diversity at the Genomic
RT Level.";
RL Front. Microbiol. 7:998-998(2016).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal, non-reducing beta-D-glucosyl residues
CC with release of beta-D-glucose.; EC=3.2.1.21;
CC Evidence={ECO:0000256|ARBA:ARBA00000448};
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:OEV05413.1}.
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DR EMBL; LJGW01000679; OEV05413.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E7KND7; -.
DR PATRIC; fig|518642.10.peg.36; -.
DR Proteomes; UP000176005; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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 PANTHER; PTHR30620:SF121; PERIPLASMIC BETA-GLUCOSIDASE; 1.
DR PANTHER; PTHR30620; PERIPLASMIC 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 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.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:OEV05413.1}.
FT DOMAIN 645..716
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OEV05413.1"
SQ SEQUENCE 727 AA; 77190 MW; 30CBFB10CEF191F7 CRC64;
AARGRADARV ERRVRKLLRR MTVEEKFGQL QQLTWNPDTG PGEGQNEKAR EAAAEGRLGS
VLNITGAEEC NELQRYAVEE SRLGIPLVFG LDVIHGFLTT FPVPLAQGAS FDPGVVTADA
EVSAREAASW GVHWTFAPMA DVSREPRWGR IAEGSGEDPY LTAELTAAKV RGYQGEDYSE
KGRLAACAKH FVGYGFPEGG RDYNTVDISE RRLRDIALPP FKAAVDAGVA TVMASFNTVN
GVPAHANRHT LTGILHEDLG FDGFVVGDYN GVQELIPHGV AADGADAAAL ALGAGVDMEM
VSTTYADNGP ELLKSGRIDR QRLDDAVTRI LRVKVRMGLF ENPYTDEDGQ IAEPTAAARR
NAREAAARCA VLLKNDDATL PFGKDLSRLA VVGPLGDDTQ ELHGTWAGPG AGKFPAVSVL
EGVRKAAPDA KVTFARGCDV TGEETGGLSK AVAAVRSADA AVVVVGEKAS HSGEAACRSD
ITLPGVQEEL IRRVAKTGKP FVVVVLAGRP LVLSGVVGHA PAVLAGWHPG LEGGNAVADV
LFGDVNPGGR LPVTFPRAVG QVAEYYAHEN TGRPYEADNK YTSKYLDLAH GPLFPFGHGL
SYTAFAYSRL TLSEQSVSAR SVRDGSATVR ASVTVENTGS RKGDEVVQLY IRDKVASIAQ
PVRRLRGFER ITLDAGESRT VSFELGAADL GFHTNDPSGE LLVEPGEFGV YAGGSSEAEL
HTTLTLT
//
