IED ID | IndEnz0002004059 |
Enzyme Type ID | protease004059 |
Protein Name |
ATP synthase subunit gamma, chloroplastic F-ATPase gamma subunit Cleaved into: Inceptin Fragment |
Gene Name | |
Organism | Vigna unguiculata (Cowpea) |
Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae rosids fabids Fabales Fabaceae Papilionoideae 50 kb inversion clade NPAAA clade indigoferoid/millettioid clade Phaseoleae Vigna Vigna unguiculata (Cowpea) |
Enzyme Sequence | DPLYTKFVSLVKSDPVIHTLLPLSPKGEICDINGVCVDAAEDEFFRLTTKEGKLTVERDVVRTKTTDYSPILQFEQDPVQILDALLPLYLNSQILRALQESLASELAARMSAMSNAAA |
Enzyme Length | 118 |
Uniprot Accession Number | Q2LGZ2 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | |
Enzyme Function | FUNCTION: Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex. {ECO:0000269|PubMed:16720701}.; FUNCTION: Inceptin is a proteolytic fragment produced by insect larvae that previously ingested the protein. This peptide mediate plant perception of herbivory through the induction of volatile, phenylpropanoid and protease inhibitor defenses such as ethylene, jasmonic acid and salicylic acid for example. {ECO:0000269|PubMed:16720701}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Chain (1); Disulfide bond (1); Non-terminal residue (2); Peptide (1) |
Keywords | ATP synthesis;CF(1);Chloroplast;Direct protein sequencing;Disulfide bond;Hydrogen ion transport;Ion transport;Membrane;Plastid;Thylakoid;Transport |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 13,024 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |