Detail Information for IndEnz0011000244
IED ID IndEnz0011000244
Enzyme Type ID glucanase000244
Protein Name Glucan endo-1,3-beta-glucosidase, acidic isoform PR-Q'
EC 3.2.1.39
1-
3
-beta-glucan endohydrolase
1-
3
-beta-glucanase
Beta-1,3-endoglucanase
PR-35
Gene Name
Organism Nicotiana tabacum (Common tobacco)
Taxonomic Lineage cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae asterids lamiids Solanales Solanaceae Nicotianoideae Nicotianeae Nicotiana Nicotiana tabacum (Common tobacco)
Enzyme Sequence MAHLIVTLLLLSVLTLATLDFTGAQAGVCYGRQGNGLPSPADVVSLCNRNNIRRMRIYDPDQPTLEALRGSNIELMLGVPNPDLENVAASQANADTWVQNNVRNYGNVKFRYIAVGNEVSPLNENSKYVPVLLNAMRNIQTAISGAGLGNQIKVSTAIETGLTTDTSPPSNGRFKDDVRQFIEPIINFLVTNRAPLLVNLYPYFAIANNADIKLEYALFTSSEVVVNDNGRGYRNLFDAILDATYSALEKASGSSLEIVVSESGWPSAGAGQLTSIDNARTYNNNLISHVKGGSPKRPSGPIETYVFALFDEDQKDPEIEKHFGLFSANMQPKYQISFN
Enzyme Length 339
Uniprot Accession Number P36401
Absorption
Active Site ACT_SITE 118; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:O22317; ACT_SITE 262; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:O22317
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans.; EC=3.2.1.39;
DNA Binding
EC Number 3.2.1.39
Enzyme Function FUNCTION: Implicated in the defense of plants against pathogens.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (2); Chain (1); Erroneous initiation (1); Modified residue (1); Sequence conflict (1); Signal peptide (1)
Keywords Apoplast;Direct protein sequencing;Glycosidase;Hydrolase;Plant defense;Pyrrolidone carboxylic acid;Reference proteome;Secreted;Signal
Interact With
Induction INDUCTION: Accumulates following infection.
Subcellular Location SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast.
Modified Residue MOD_RES 25; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000250|UniProtKB:P15797
Post Translational Modification PTM: The N-terminus is blocked.
Signal Peptide SIGNAL 1..24; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 36,995
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda