IED Industry Enzyme Database

Detail Information for IndEnz0011000042
IED ID IndEnz0011000042
Enzyme Type ID glucanase000042
Protein Name Beta-glucosidase 7
Os3bglu7
EC 3.2.1.21
Gene Name BGLU7 BGLU1 Os03g0703000 LOC_Os03g49600 OSJNBa0004L11.16
Organism Oryza sativa subsp. japonica (Rice)
Taxonomic Lineage cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae Liliopsida Petrosaviidae commelinids Poales Poaceae BOP clade Oryzoideae Oryzeae Oryzinae Oryza Oryza sativa (Rice) Oryza sativa subsp. japonica (Rice)
Enzyme Sequence MAARRANCALVLVLALALLAARDAGAAAVPKPNWLGGLSRAAFPKRFVFGTATSAYQVEGMAASGGRGPSIWDAFAHTPGNVAGNQNGDVATDQYHRYKEDVNLMKSLNFDAYRFSISWSRIFPDGEGRVNQEGVAYYNNLINYLLQKGITPYVNLYHYDLPLALEKKYGGWLNAKMADLFTEYADFCFKTFGNRVKHWFTFNEPRIVALLGYDQGTNPPKRCTKCAAGGNSATEPYIVAHNFLLSHAAAVARYRTKYQAAQQGKVGIVLDFNWYEALSNSTEDQAAAQRARDFHIGWYLDPLINGHYPQIMQDLVKDRLPKFTPEQARLVKGSADYIGINQYTASYMKGQQLMQQTPTSYSADWQVTYVFAKNGKPIGPQANSNWLYIVPWGMYGCVNYIKQKYGNPTVVITENGMDQPANLSRDQYLRDTTRVHFYRSYLTQLKKAIDEGANVAGYFAWSLLDNFEWLSGYTSKFGIVYVDFNTLERHPKASAYWFRDMLKH
Enzyme Length 504
Uniprot Accession Number Q75I93
Absorption
Active Site ACT_SITE 204; /note=Proton donor; /evidence=ECO:0000269|PubMed:25252199; ACT_SITE 414; /note=Nucleophile; /evidence=ECO:0000269|PubMed:25252199
Activity Regulation
Binding Site BINDING 57; /note="Substrate"; /evidence="ECO:0000269|PubMed:18308333, ECO:0000269|PubMed:20884352, ECO:0000269|PubMed:25252199, ECO:0007744|PDB:2RGM, ECO:0007744|PDB:3AHT, ECO:0007744|PDB:3F5J, ECO:0007744|PDB:3F5K, ECO:0007744|PDB:3F5L, ECO:0007744|PDB:4QLK"; BINDING 158; /note="Substrate"; /evidence="ECO:0000269|PubMed:20884352, ECO:0000269|PubMed:25252199, ECO:0007744|PDB:3AHT, ECO:0007744|PDB:3F5J, ECO:0007744|PDB:3F5K, ECO:0007744|PDB:3F5L, ECO:0007744|PDB:4QLK"; BINDING 203; /note="Substrate"; /evidence="ECO:0000269|PubMed:18308333, ECO:0000269|PubMed:20884352, ECO:0000269|PubMed:25252199, ECO:0007744|PDB:2RGM, ECO:0007744|PDB:3F5K, ECO:0007744|PDB:3F5L, ECO:0007744|PDB:4QLK"; BINDING 343; /note="Substrate"; /evidence="ECO:0000269|PubMed:18308333, ECO:0000269|PubMed:20884352, ECO:0000269|PubMed:25252199, ECO:0007744|PDB:2RGM, ECO:0007744|PDB:3AHT, ECO:0007744|PDB:3F5K, ECO:0007744|PDB:3F5L, ECO:0007744|PDB:4QLK"; BINDING 461; /note="Substrate"; /evidence="ECO:0000305, ECO:0007744|PDB:3SCW"
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.; EC=3.2.1.21; Evidence={ECO:0000269|PubMed:14692878};
DNA Binding
EC Number 3.2.1.21
Enzyme Function FUNCTION: Hydrolyzes p-nitrophenyl beta-D-glucoside, p-nitrophenyl beta-D-mannoside, p-nitrophenyl beta-D-galactoside, p-nitrophenyl beta-D-xyloside, p-nitrophenyl beta-D-fucoside, p-nitrophenyl beta-L-arabinoside, oligosaccharides, pyridoxine beta-D-glucoside and the cyanogenic glucosides amygdalin, prunasin and dhurrin. Possesses pyridoxine transglucosylation activity. {ECO:0000269|PubMed:14692878, ECO:0000269|PubMed:18308333, ECO:0000269|PubMed:19766588}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (2); Beta strand (18); Binding site (5); Chain (1); Disulfide bond (1); Erroneous gene model prediction (4); Glycosylation (2); Helix (24); Mutagenesis (4); Region (1); Sequence conflict (1); Signal peptide (1); Turn (4)
Keywords 3D-structure;Disulfide bond;Glycoprotein;Glycosidase;Hydrolase;Reference proteome;Secreted;Signal
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..26; /evidence=ECO:0000255
Structure 3D X-ray crystallography (22)
Cross Reference PDB 2RGL; 2RGM; 3AHT; 3AHV; 3F4V; 3F5J; 3F5K; 3F5L; 3SCN; 3SCO; 3SCP; 3SCQ; 3SCR; 3SCS; 3SCT; 3SCU; 3SCV; 3SCW; 4QLJ; 4QLK; 4QLL; 7BZM;
Mapped Pubmed ID 16880561; 32549280;
Motif
Gene Encoded By
Mass 56,872
Kinetics BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.2 mM for p-nitrophenyl beta-D-glucoside (at pH 5.0) {ECO:0000269|PubMed:14692878, ECO:0000269|PubMed:18308333, ECO:0000269|PubMed:19766588}; KM=0.23 mM for p-nitrophenyl beta-D-fucoside (at pH 5.0) {ECO:0000269|PubMed:14692878, ECO:0000269|PubMed:18308333, ECO:0000269|PubMed:19766588}; KM=3.2 mM for p-nitrophenyl beta-D-galactoside (at pH 5.0) {ECO:0000269|PubMed:14692878, ECO:0000269|PubMed:18308333, ECO:0000269|PubMed:19766588}; KM=1.3 mM for p-nitrophenyl beta-D-mannoside (at pH 5.0) {ECO:0000269|PubMed:14692878, ECO:0000269|PubMed:18308333, ECO:0000269|PubMed:19766588}; KM=1.3 mM for p-nitrophenyl beta-D-xyloside (at pH 5.0) {ECO:0000269|PubMed:14692878, ECO:0000269|PubMed:18308333, ECO:0000269|PubMed:19766588}; KM=1.2 mM for p-nitrophenyl beta-L-arabinoside (at pH 5.0) {ECO:0000269|PubMed:14692878, ECO:0000269|PubMed:18308333, ECO:0000269|PubMed:19766588}; KM=0.78 mM for p-nitrophenyl beta-D-cellobioside (at pH 5.0) {ECO:0000269|PubMed:14692878, ECO:0000269|PubMed:18308333, ECO:0000269|PubMed:19766588}; KM=22 mM for cellobiose (at pH 5.0) {ECO:0000269|PubMed:14692878, ECO:0000269|PubMed:18308333, ECO:0000269|PubMed:19766588}; KM=0.22 mM for cellotriose (at pH 5.0) {ECO:0000269|PubMed:14692878, ECO:0000269|PubMed:18308333, ECO:0000269|PubMed:19766588}; KM=0.28 mM for cellotetraose (at pH 5.0) {ECO:0000269|PubMed:14692878, ECO:0000269|PubMed:18308333, ECO:0000269|PubMed:19766588}; KM=0.24 mM for cellopentaose (at pH 5.0) {ECO:0000269|PubMed:14692878, ECO:0000269|PubMed:18308333, ECO:0000269|PubMed:19766588}; KM=0.22 mM for cellohexaose (at pH 5.0) {ECO:0000269|PubMed:14692878, ECO:0000269|PubMed:18308333, ECO:0000269|PubMed:19766588}; KM=2.05 mM for laminaribiose (at pH 5.0) {ECO:0000269|PubMed:14692878, ECO:0000269|PubMed:18308333, ECO:0000269|PubMed:19766588}; KM=1.92 mM for laminaritriose (at pH 5.0) {ECO:0000269|PubMed:14692878, ECO:0000269|PubMed:18308333, ECO:0000269|PubMed:19766588}; KM=13.9 mM for sophorose (at pH 5.0) {ECO:0000269|PubMed:14692878, ECO:0000269|PubMed:18308333, ECO:0000269|PubMed:19766588}; KM=38.3 mM for gentiobiose (at pH 5.0) {ECO:0000269|PubMed:14692878, ECO:0000269|PubMed:18308333, ECO:0000269|PubMed:19766588};
Metal Binding
Rhea ID
Cross Reference Brenda 3.2.1.21;