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Database: UniProt
Entry: A0A0K8P3N6_IDESA
LinkDB: A0A0K8P3N6_IDESA
Original site: A0A0K8P3N6_IDESA 
ID   A0A0K8P3N6_IDESA        Unreviewed;       455 AA.
AC   A0A0K8P3N6;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 26.
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=ISF6_3113 {ECO:0000313|EMBL:GAP37258.1};
OS   Ideonella sakaiensis (strain NBRC 110686 / TISTR 2288 / 201-F6).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sphaerotilaceae; Ideonella.
OX   NCBI_TaxID=1547922 {ECO:0000313|EMBL:GAP37258.1, ECO:0000313|Proteomes:UP000037660};
RN   [1] {ECO:0000313|Proteomes:UP000037660}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 110686 / TISTR 2288 / 201-F6
RC   {ECO:0000313|Proteomes:UP000037660};
RA   Yoshida S., Hiraga K., Takehana T., Taniguchi I., Yamaji H., Maeda Y.,
RA   Toyohara K., Miyamoto K., Kimura Y., Oda K.;
RT   "Discovery of a poly(ethylene terephthalate assimilation.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:GAP37258.1, ECO:0000313|Proteomes:UP000037660}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 110686 / TISTR 2288 / 201-F6
RC   {ECO:0000313|Proteomes:UP000037660};
RX   PubMed=26965627; DOI=10.1126/science.aad6359;
RA   Yoshida S., Hiraga K., Takehana T., Taniguchi I., Yamaji H., Maeda Y.,
RA   Toyohara K., Miyamoto K., Kimura Y., Oda K.;
RT   "A bacterium that degrades and assimilates poly(ethylene terephthalate).";
RL   Science 351:1196-1199(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|RuleBase:RU361175};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
CC       {ECO:0000256|RuleBase:RU361175}.
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:GAP37258.1}.
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DR   EMBL; BBYR01000044; GAP37258.1; -; Genomic_DNA.
DR   RefSeq; WP_054021202.1; NZ_BBYR01000044.1.
DR   AlphaFoldDB; A0A0K8P3N6; -.
DR   STRING; 1547922.ISF6_3113; -.
DR   OMA; HLPGTTY; -.
DR   OrthoDB; 9765195at2; -.
DR   Proteomes; UP000037660; 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:0030245; P:cellulose catabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR001360; Glyco_hydro_1.
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; LACTASE-LIKE PROTEIN; 1.
DR   Pfam; PF00232; Glyco_hydro_1; 1.
DR   PRINTS; PR00131; GLHYDRLASE1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 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, ECO:0000313|EMBL:GAP37258.1};
KW   Hydrolase {ECO:0000256|RuleBase:RU361175, ECO:0000313|EMBL:GAP37258.1};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037660}.
FT   ACT_SITE        171
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-1"
FT   ACT_SITE        351
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-1"
FT   BINDING         25
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT   BINDING         126
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT   BINDING         170
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT   BINDING         299
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT   BINDING         397
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT   BINDING         404..405
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
SQ   SEQUENCE   455 AA;  50360 MW;  350792486663BF82 CRC64;
     MDLPVDPLHR FPEDFVWGVA TSAFQIEGSA RADGKGPSIW DRFCERPGAI ADGSHGEVAC
     DHVQRWREDL DLVAALGVDA YRFSVSWPRV QPQGQGAWND RGLDFYERLV DGLLARGVRP
     YLTLNHWDLP DALQQRGGWA ARDTVHRFVD YALGLQARLG DRVAAITTHN EPWVIATLGH
     EWGSFAPGLK DRATAVQVSH HLLLSHGLAL QALRAAGCRA RLGIVLNLAP VHAATRSAAD
     RVQARIDDGR LVRWYMDPLF HGRYPDDVLE HLGADAPRTE PGDLAAIATP MDFLGINYYS
     RSVASADGSW QAGRSGLALT DMGWEVYPTG LTELLLRLHR DWPVPPLYVK ENGAAFRDEC
     VDGRVHDAER VAYLAAHIAA VGAALAAGVP VAGYMVWSLL DNFEWTSGYA KRFGLVHVDY
     ATQRRTLKDS ARWYRDFLRR QRALRSSPAA EPALA
//
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