| IED ID | IndEnz0002014569 |
| Enzyme Type ID | protease014569 |
| Protein Name |
Aminopeptidase M1-C EC 3.4.11.2 Alpha-aminoacylpeptide hydrolase |
| Gene Name | Os09g0362500 LOC_Os09g19790 OJ1506_A04.10 |
| 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 | MAPAPAPAGSADQFRGQARLPRFAAPRRYELRLRPDLDACVFTGDASVVVDVSAPTRFLVLNAADLAVDRASIRFQGLAPTEVSLFEDDEILVLEFDGELPLGEGVLAMDFNGTLNDQMRGFYRSKYEYKGETKNMAVTQFEAVDARRCFPCWDEPAFKAKFKLTLEVPSELVALSNMPVACETIAGPIKTIHYEESPLMSTYLVAIVVGLFDYVEGVTSEGNKVRVYTQVGKSSQGKFALDIGVKSLNFYKDYFDTPYPLPKLDMVAIPDFAAGAMENYGLVTYREVSLLFDEQSSSASFKQNVAITVAHELAHQWFGNLVTMEWWTHLWLNEGFATWMSHLSVDSFFPQWNIWTQFLDSTTSALKLDSQAESHPIEVEIHHASEVDEIFDAISYDKGASVIRMLQSYLGAERFQKALTSYIKKYAYSNAKTEDLWAVLEEVSGEPVKDLMTTWTKQQGYPVISVKLKGHDLELEQDQFLLNGTSGAGIWIVPITLGCCSHDKQKRLLLKHKHDNIKAIVSQCDSRQKGGNFWIKLNIDETGFYRVKYDDELTAALRNALQAKKLSLMDEIGIVDDAHALSIACKQTLSSLLHLLYAFRDEADYSVLSHINSVTSSVAKISIDATPDLAGDIKQLFIKLLLPPAKKLGWDPKDGESHLNAMLRPMLLVALVQLGHDKTINEGFRRFQIFFDDRNTSLLTPDTRKAAYLSVMHNVSSTNRSGYDALLKVYRKSAEGEEKLRVLGTLSSCQDKDIVLESLNLIFTDEVRNQDAYRVLGGVIIEARETAWSWLKENWDRISEAFSGSSLISDFIRSIVTLFTSKEKEAEISQFFATRTKPGYERTLKQSLERVLINARWIEGIRGEAKLAQTVHELLHKP |
| Enzyme Length | 878 |
| Uniprot Accession Number | Q0J2B5 |
| Absorption | |
| Active Site | ACT_SITE 312; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Activity Regulation | |
| Binding Site | BINDING 142; /note=Substrate; /evidence=ECO:0000250 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa- from a peptide, amide or arylamide. Xaa is preferably Ala, but may be most amino acids including Pro (slow action). When a terminal hydrophobic residue is followed by a prolyl residue, the two may be released as an intact Xaa-Pro dipeptide.; EC=3.4.11.2; |
| DNA Binding | |
| EC Number | 3.4.11.2 |
| Enzyme Function | |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Binding site (1); Chain (1); Erroneous gene model prediction (1); Metal binding (3); Motif (1); Region (2); Sequence conflict (1); Site (1) |
| Keywords | Aminopeptidase;Cytoplasm;Endoplasmic reticulum;Hydrolase;Membrane;Metal-binding;Metalloprotease;Microsome;Protease;Reference proteome;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Microsome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=The dileucine internalization motif may be involved in intracellular sequestration. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 726..727; /note=Dileucine internalization motif; /evidence=ECO:0000255 |
| Gene Encoded By | |
| Mass | 98,683 |
| Kinetics | |
| Metal Binding | METAL 311; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 315; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 334; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Rhea ID | |
| Cross Reference Brenda |