ID A0A0C5FZ69_9ACTN Unreviewed; 480 AA.
AC A0A0C5FZ69;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Beta-glucosidase {ECO:0000256|ARBA:ARBA00012744, ECO:0000256|RuleBase:RU361175};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744, ECO:0000256|RuleBase:RU361175};
GN ORFNames=TU94_32160 {ECO:0000313|EMBL:AJP05377.1};
OS Streptomyces cyaneogriseus subsp. noncyanogenus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=477245 {ECO:0000313|EMBL:AJP05377.1, ECO:0000313|Proteomes:UP000032234};
RN [1] {ECO:0000313|EMBL:AJP05377.1, ECO:0000313|Proteomes:UP000032234}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NMWT 1 {ECO:0000313|EMBL:AJP05377.1,
RC ECO:0000313|Proteomes:UP000032234};
RA Wang H., Li C., Xiang W., Wang X.;
RT "Genome sequence of thermotolerant Streptomyces cyaneogriseus subsp.
RT Noncyanogenus NMWT1, the producer of nematocidal antibiotics nemadectin.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
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 ECO:0000256|RuleBase:RU361175};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
CC {ECO:0000256|ARBA:ARBA00010838, ECO:0000256|RuleBase:RU361175}.
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DR EMBL; CP010849; AJP05377.1; -; Genomic_DNA.
DR RefSeq; WP_044387069.1; NZ_CP010849.1.
DR AlphaFoldDB; A0A0C5FZ69; -.
DR STRING; 477245.TU94_32160; -.
DR KEGG; scw:TU94_32160; -.
DR PATRIC; fig|477245.3.peg.6853; -.
DR HOGENOM; CLU_001859_1_3_11; -.
DR OrthoDB; 9765195at2; -.
DR Proteomes; UP000032234; Chromosome.
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:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR001360; Glyco_hydro_1.
DR InterPro; IPR018120; Glyco_hydro_1_AS.
DR InterPro; IPR017736; Glyco_hydro_1_beta-glucosidase.
DR InterPro; IPR033132; Glyco_hydro_1_N_CS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR NCBIfam; TIGR03356; BGL; 1.
DR PANTHER; PTHR10353; GLYCOSYL HYDROLASE; 1.
DR PANTHER; PTHR10353:SF36; KLOTHO (MAMMALIAN AGING-ASSOCIATED PROTEIN) HOMOLOG; 1.
DR Pfam; PF00232; Glyco_hydro_1; 1.
DR PRINTS; PR00131; GLHYDRLASE1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR PROSITE; PS00572; GLYCOSYL_HYDROL_F1_1; 1.
DR PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Cellulose degradation {ECO:0000256|ARBA:ARBA00023001};
KW Glycosidase {ECO:0000256|RuleBase:RU361175};
KW Hydrolase {ECO:0000256|RuleBase:RU361175};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023001};
KW Reference proteome {ECO:0000313|Proteomes:UP000032234}.
FT REGION 316..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 179
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-1"
FT ACT_SITE 375
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-1,
FT ECO:0000256|PROSITE-ProRule:PRU10055"
FT BINDING 33
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 134
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 178
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 310
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 422
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 429..430
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
SQ SEQUENCE 480 AA; 52082 MW; 0204C5691EDA70FC CRC64;
MTTTAPPATA RHDALIDRLP PDFRFGAATS AYQIEGAAAE DGRTASIWDT FCRVPGAVHN
GDTGDTACDH YHRMPEDVAL LAALGLDTYR FSVSWPRVQP GGRGPANPAG LGFYDRLVDE
LLARGVTPWL TLYHWDLPQE LQDAGGWPAR DTAHRFADYA ELVHDRLGDR VTHWTTLNEP
FCAAILGHVE GVHAPGGRSL ADGVRAVHHL HLAHGLAVRR LRAAARRPLD LAVSHLLGTS
GPATDSAADR EAARRADAFG FRFYLDPILR GRYPQDLVDD LAEYGVEIPV RDGDLETIAA
PIDTLGVNYY RSMRTSGTDE HGATADADGR PVTRNLPHGG LPVTGLGWEV MPHDLTALLL
RLSHDYPGTP MVVTENGAAY DDHPDAHGFV DDTDRTAYLA AHLAAVAEAR AHGADVRGYF
AWSLLDNFEW AGGYAARFGL VRVDYATQTR TPKRSALWLR DTAHRVRTAG GASGRVGRGT
//
