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Database: UniProt
Entry: C9YXN3_STRSW
LinkDB: C9YXN3_STRSW
Original site: C9YXN3_STRSW 
ID   C9YXN3_STRSW            Unreviewed;       776 AA.
AC   C9YXN3;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN   OrderedLocusNames=SCAB_22731 {ECO:0000313|EMBL:CBG69387.1};
OS   Streptomyces scabiei (strain 87.22).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=680198 {ECO:0000313|EMBL:CBG69387.1, ECO:0000313|Proteomes:UP000001444};
RN   [1] {ECO:0000313|EMBL:CBG69387.1, ECO:0000313|Proteomes:UP000001444}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=87.22 {ECO:0000313|EMBL:CBG69387.1,
RC   ECO:0000313|Proteomes:UP000001444};
RX   PubMed=20064060; DOI=10.1094/MPMI-23-2-0161;
RA   Bignell D.R., Seipke R.F., Huguet-Tapia J.C., Chambers A.H., Parry R.J.,
RA   Loria R.;
RT   "Streptomyces scabies 87-22 contains a coronafacic acid-like biosynthetic
RT   cluster that contributes to plant-microbe interactions.";
RL   Mol. Plant Microbe Interact. 23:161-175(2010).
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};
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DR   EMBL; FN554889; CBG69387.1; -; Genomic_DNA.
DR   RefSeq; WP_010353106.1; NC_013929.1.
DR   AlphaFoldDB; C9YXN3; -.
DR   STRING; 680198.SCAB_22731; -.
DR   CAZy; GH3; Glycoside Hydrolase Family 3.
DR   GeneID; 33083523; -.
DR   KEGG; scb:SCAB_22731; -.
DR   eggNOG; COG1472; Bacteria.
DR   HOGENOM; CLU_004542_5_1_11; -.
DR   Proteomes; UP000001444; Chromosome.
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:CBG69387.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001444}.
FT   DOMAIN          694..764
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   776 AA;  83930 MW;  590EDC6681416742 CRC64;
     MTTTPDTIPN DAGTRRTQGE ARYRDAGLPV EDRVADLLAQ MTLEEKAGQL TQFFYMGTGE
     PIPDDFDIES LPPEHRAFVQ QPHDVEDTVS RGGAGSLLFV KDPALGNRLQ RRAVEDTRLG
     IPLLFGNDVI HGLRTVFPVP IAMAASWDPD AAEAAQVVAA REARAAGIRW TFAPMIDIAR
     DPRWGRMIEG AGEDPVLAAA MAAAQVRGFQ GDLGAESVLA GAKHFLGYGA ARGGRDYDDA
     DISDAELRNV YLPPFRAAIE AGAANVMSAY MDLNGVPASA NRWLLSDLLR DELHFDGWIV
     SDANAVQSLQ TQHFAKDQQD AAVRALNAGL DMEMCTFTPA FDHLPQAVRD GLVAEETLDT
     AVSRVLAVKF RLGLFENPYT DEDAAPAVLN ASAHRDAARD AAERTLVLLK NDAATLPLRP
     EQLTGVAVIG RLADSRRDTL GPWVLDHDTS EAVTILDGLR ARLGDGIRVE YAAGVGAPER
     LHPSPFDVLD PTVVPTPPDL NEDAEIERAV AAARDADVAI VVVGQPQNQI GEKASTSTLD
     LPGRQLEQLQ RVAATGTPVV LVVLSGRPLD LRWADEHVPA IVQAWYPGTR GGEAVASVLV
     GDVSPAGRLP FTWPRHVGQV PLVYSHYRTF APQDQDARYF QEDGAPLYPF GHGLSYATFA
     YTNLRTDRTS MTGGRGTATV SVDVTNTSER DADEVVQLYV HQRYGSSSRP VRELKGFERV
     PVPAGTTTTV SFELGPDQLR YWSAATRTYQ LDATVLDLWV GGSSTAQLTT TLEVTR
//
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