IED ID | IndEnz0011000184 |
Enzyme Type ID | glucanase000184 |
Protein Name |
Probable aspartic proteinase GIP2 EC 3.4.23.- Glucanase inhibitor protein 2 NbGIP2 |
Gene Name | GIP2 Niben101Scf03191g04002 |
Organism | Nicotiana benthamiana |
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 benthamiana |
Enzyme Sequence | MASSCCLHAILLCSLLFITSTTAQSETSFRPKGLILPITKDALTLQYLTQIQQRTPLVPVSLTLDLGGQFLWVDCDQGYVSSTYRPARCRSAQCSLAGAGSGCGQCFSPPKPGCNNNTCGLLPDNTITRTATSGELASDTVQVQSSNGKNPGRHVSDKDFLFVCGSTFLLEGLASGVKGMAGLGRTRISLPSQFSAEFSFPRKFAVCLSSSTNSKGVVLFGDGPYTFLPNREFANNDFSYTPLFINPVSTASAFSSREPSSEYFIGVKSIKINEKVVPINTTLLSIDNQGVGGTKISTVNPYTILETSIYNAVTNFFVKELVNITRVASVAPFRACFDSRNIASTRVGPAVPSIDLVLQNENVFWRIFGANSMVQVSENVLCLGFVDGGVSPRTSIVVGGYTIEDNLLQFDLARSRLGFTSSILFRQTTCANFNFTSIA |
Enzyme Length | 439 |
Uniprot Accession Number | P0DO21 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | 3.4.23.- |
Enzyme Function | FUNCTION: Involved in plant defense against Phytophtora parasitica (PubMed:28082413). Contributes positively to Nicotiana resistance against P.parasitica (PubMed:28082413). Binds the P.parasitica xyloglucanase XEG1 and inhibits its cell wall degrading enzyme activity and its contribution as P.parasitica virulence factor (PubMed:28082413). XEG1 acts as an important virulence factor during P.parasitica infection but also acts as a pathogen-associated molecular pattern (PAMP) in Nictotiana species, where it can trigger defense responses including cell death (PubMed:28082413). {ECO:0000269|PubMed:28082413}.; FUNCTION: (Microbial infection) Possesses stronger binding affinity with XLP1, a truncated paralog of P.parasitica XEG1 which has no enzyme activity. Is impaired in its inhibitor activity towards the P.parasitica xyloglucanase XEG1 when hijacked by XLP1 binding. {ECO:0000269|PubMed:28082413}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Chain (1); Domain (1); Glycosylation (4); Signal peptide (1) |
Keywords | Apoplast;Aspartyl protease;Glycoprotein;Hydrolase;Plant defense;Protease;Secreted;Signal |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast {ECO:0000305|PubMed:28082413}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..23; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 47,214 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |