| IED ID | IndEnz0002016647 |
| Enzyme Type ID | protease016647 |
| Protein Name |
Aminopeptidase M1-A EC 3.4.11.2 Alpha-aminoacylpeptide hydrolase |
| Gene Name | Os02g0218200 LOC_Os02g12650 OsJ_05906 P0027A02.7 |
| 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 | MAAAEQSAEQFRGQARLPGFAAPRRYDLRLVPDLDGCAFTGSVDVSVDVTAPTRFLVLNAAELEVSPGGVQFKPHGAEQELHPAEVTNVPEDEILIIRFNEVLPVGEGTLVIAFKGTLNDKMHGFYRSVYELNGEKKNMAVTQFEPADARRCFPCWDEPSFKAIFKITLEVPSETVALSNMPVVEEKVNGLIKAVYFQETPIMSTYLVAVIVGMFDYVEAFTTDGTRVRVYTQVGKSAQGKFALEVAVKTLVLFKEYFAVPYPLPKMDMIAIPDFASGAMENYGLVTYRETALLFDEKHSAAANKQRVAVVVAHELAHQWFGNLVTMEWWTHLWLNEGFATWVSYLAADNFFPEWNVWTQFLEESTTGFKLDALAGSHPIEVDVNHVDEIDEIFDAISYRKGAAVIRMLQSYLGAETFQKSLAAYIEKFAYSNAKTEDLWAALEEGSGEPVKTLMHSWTKQQGYPVVNVKLKDGKLEMEQTQFLSSGAEGVGQWVVPITLCCCSYSRQEKFLFNGKQEDFNLSGLVECQKKEDFWIKLNVNQTGFYRVSYDEELASRLRYAIEANKLSAADRYGVLDDTYALCMAGKQKLVSLLHLIAAYKDETEYTVLARVIDTSLSIVEMVAVAAPEGLGKLKKFLIDFLEPFAQRIGWDAKSGEGHLDALLRGTLLTALAELGHEATINEAVRRFNIFVEDRETPLLPPDVRKAAYVALMQTVNKSNRAGYESLLKIYKETDLSQEKVRILGSLASCPDPDVVRDTLDFMLSPEVRNQDSIFLLRGVGAAGHEVAWTWLKEKWDYISDTFSGTLLTYFVSTTVSPLRTDEMGDDAEEFFKSRTKANIARTVKQSIERVRINAKWVESTRAEANLGNVLKEISHDH |
| Enzyme Length | 878 |
| Uniprot Accession Number | Q6Z6L4 |
| Absorption | |
| Active Site | ACT_SITE 315; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Activity Regulation | |
| Binding Site | BINDING 145; /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 termination (1); Metal binding (3); Motif (1); Region (2); Sequence conflict (2); 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 727..728; /note=Dileucine internalization motif; /evidence=ECO:0000255 |
| Gene Encoded By | |
| Mass | 98,453 |
| Kinetics | |
| Metal Binding | METAL 314; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 318; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 337; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Rhea ID | |
| Cross Reference Brenda |