IED ID | IndEnz0002002352 |
Enzyme Type ID | protease002352 |
Protein Name |
Methionine aminopeptidase 2A MAP 2A MetAP 2A EC 3.4.11.18 Peptidase M |
Gene Name | MAP2A At2g44180 F6E13.31 |
Organism | Arabidopsis thaliana (Mouse-ear cress) |
Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae rosids malvids Brassicales Brassicaceae Camelineae Arabidopsis Arabidopsis thaliana (Mouse-ear cress) |
Enzyme Sequence | MAIGNPEVATMGKENTEAESSNGNESQLSSDLTKSLDLAEVKEDEKDNNQEEEDGLKAEASTKKKKKKSKSKKKKSSLQQTDPPSIPVLELFPSGDFPQGEIQQYNDDNLWRTTSEEKREMERLQKPIYNSLRQAAEVHRQVRKYMRSILKPGMLMIDLCETLENTVRKLISENGLQAGIAFPTGCSLNNVAAHWTPNSGDKTVLQYDDVMKLDFGTHIDGHIVDSAFTVAFNPMFDPLLAASRDATYTGIKEAGVDVRLCDVGAAVQEVMESYEVEINGKVYQVKSIRNLNGHSIGRYQIHAEKSVPNVRGGEQTKMEEGELYAIETFGSTGKGYVREDLECSHYMKNYDVGHVPLRLPRAKQLLATINKNFSTLAFCRRYLDRLGETKYLMALKNLCDSGIIEPCPPVCDVKGSYISQFEHTILLRPTCKEIISKGDDY |
Enzyme Length | 441 |
Uniprot Accession Number | Q9FV49 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | BINDING 194; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; BINDING 302; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_03175 |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.; EC=3.4.11.18; Evidence={ECO:0000255|HAMAP-Rule:MF_03175}; |
DNA Binding | |
EC Number | 3.4.11.18 |
Enzyme Function | FUNCTION: Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). {ECO:0000255|HAMAP-Rule:MF_03175}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Binding site (2); Chain (1); Compositional bias (2); Metal binding (7); Region (1); Sequence conflict (2) |
Keywords | Aminopeptidase;Cytoplasm;Hydrolase;Metal-binding;Protease;Reference proteome |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03175, ECO:0000269|PubMed:11060042}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 12185496; 15681659; 18650403; |
Motif | |
Gene Encoded By | |
Mass | 49,395 |
Kinetics | |
Metal Binding | METAL 214; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 225; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 225; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 294; /note=Divalent metal cation 2; catalytic; via tele nitrogen; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 327; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 422; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 422; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03175 |
Rhea ID | |
Cross Reference Brenda |