ID W2F0T9_9ACTN Unreviewed; 775 AA.
AC W2F0T9;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=MPTA5024_03465 {ECO:0000313|EMBL:ETK37505.1};
OS Microbispora sp. ATCC PTA-5024.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Microbispora.
OX NCBI_TaxID=316330 {ECO:0000313|EMBL:ETK37505.1, ECO:0000313|Proteomes:UP000018869};
RN [1] {ECO:0000313|EMBL:ETK37505.1, ECO:0000313|Proteomes:UP000018869}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC PTA-5024 {ECO:0000313|EMBL:ETK37505.1,
RC ECO:0000313|Proteomes:UP000018869};
RX PubMed=24459268;
RA Sosio M., Gallo G., Pozzi R., Serina S., Monciardini P., Bera A.,
RA Stegmann E., Weber T.;
RT "Draft Genome Sequence of the Microbispora sp. Strain ATCC-PTA-5024,
RT Producing the Lantibiotic NAI-107.";
RL Genome Announc. 2:e01198-13(2014).
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 -!- 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:ETK37505.1}.
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DR EMBL; AWEV01000026; ETK37505.1; -; Genomic_DNA.
DR AlphaFoldDB; W2F0T9; -.
DR STRING; 316330.MPTA5024_03465; -.
DR PATRIC; fig|316330.3.peg.676; -.
DR HOGENOM; CLU_004542_9_3_11; -.
DR OrthoDB; 9803863at2; -.
DR Proteomes; UP000018869; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0030247; F:polysaccharide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 2.60.40.290; -; 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 InterPro; IPR001919; CBD2.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR012291; CBM2_carb-bd_dom_sf.
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 PANTHER; PTHR30620:SF16; LYSOSOMAL BETA GLUCOSIDASE; 1.
DR PANTHER; PTHR30620; PERIPLASMIC BETA-GLUCOSIDASE-RELATED; 1.
DR Pfam; PF00553; CBM_2; 1.
DR Pfam; PF00933; Glyco_hydro_3; 1.
DR Pfam; PF01915; Glyco_hydro_3_C; 1.
DR PRINTS; PR00133; GLHYDRLASE3.
DR SMART; SM00637; CBD_II; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR PROSITE; PS51173; CBM2; 1.
DR PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 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:UP000018869};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..775
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039492247"
FT DOMAIN 666..775
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT REGION 614..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..668
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 775 AA; 80539 MW; F62751B8C43B31F7 CRC64;
MASRLRLLWT TAVVPLLVAA LAVTVTVNRD EARAADAPYK DPSLPVATRV NDLLSRMSLD
DKVGQMTQAE RGVLSNASDV ATYRLGSILS GGGSAPSPNT ASSWADMYDN FQRQALATPL
GIPMIYGSDA VHGHNNVAGA TIFPHNIGLG ATRDSDLVRR IGTATAEEVS GTGVDWTFAP
CVCVARNDRW GRTYESYSED PQVVSQMTTI IDGLQKAGSA SIMATAKHYM GDGGTTGGKD
QGNTELSEAD LRAIHLAPYR AAVQRNVASV MVSYSSWNGA KMHGNKYLIT DVLKGELGFS
GFVVTDWAGI DQLDGQSGFT ASEITTAINA GVDMVMVPND FKTFISLLRS EVQAGRIPMS
RIDDANRRIL TKKFEYGLFE HPLTDRSYTS TVGSSAHRAL AREAVRKSLV LLKNAGNVLP
LAKSGGKIFV AGKDADDIGN QSGGWTISWQ GSSGATTTGT TILQGIRAAV GSGAQVSYSR
DGSGIDSSYR AAIAVVGETP YAEGQGDRPG SMSLDSTDLS TLQRLKASGV PLVVVLVSGR
PLDIAAQLDQ WNALVAAWLP GTEGAGVADV LFGDYAPTGK LPMTWMRSAD QEPINAGDGK
QALFEFGYGL TYAGPSPSPS PSPSPSPSPS PSPSPSPSPS PSPSPSPSPS PSPSPSPSPS
PSPSPSPSPG GTCTVAYKPN DWGGGFTADV TITNRSSSTV NGWTLQWSFG GTQKITNAWN
ATVTQSGQQV TAKNLSYNGT IGSGGTASFG FQATYSGANP APAAFTLNGA ACAAG
//
