| IED ID | IndEnz0002002300 |
| Enzyme Type ID | protease002300 |
| Protein Name |
Methionine aminopeptidase 1D, chloroplastic/mitochondrial MAP 1D MetAP 1D EC 3.4.11.18 Peptidase M 1D |
| Gene Name | MAP1D At4g37040 C7A10.320 |
| 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 | MAGVKSLQPRLISSFLGNNSIRSTQPLIHLFRFDLGRRHVSMQLSRTFSGLTDLLFNRRNEDEVIDGKRKRLRPGNVSPRRPVPGHITKPPYVDSLQAPGISSGLEVHDKKGIECMRASGILAARVRDYAGTLVKPGVTTDEIDEAVHNMIIENGAYPSPLGYGGFPKSVCTSVNECICHGIPDSRPLEDGDIINIDVTVYLNGYHGDTSATFFCGNVDEKAKKLVEVTKESLDKAISICGPGVEYKKIGKVIHDLADKHKYGVVRQFVGHGVGSVFHADPVVLHFRNNEAGRMVLNQTFTIEPMLTIGSRNPIMWDDNWTVVTEDASLSAQFEHTILITKDGAEILTKC |
| Enzyme Length | 350 |
| Uniprot Accession Number | Q9FV50 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 180; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_03174; BINDING 278; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_03174 |
| 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_03174}; |
| DNA Binding | |
| EC Number | 3.4.11.18 |
| Enzyme Function | FUNCTION: 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_03174}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Binding site (2); Chain (1); Erroneous gene model prediction (2); Metal binding (7); Modified residue (1); Region (1); Transit peptide (1) |
| Keywords | Acetylation;Aminopeptidase;Chloroplast;Hydrolase;Metal-binding;Mitochondrion;Plastid;Protease;Reference proteome;Transit peptide |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255|HAMAP-Rule:MF_03174, ECO:0000269|PubMed:11060042}. Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03174, ECO:0000269|PubMed:11060042}. |
| Modified Residue | MOD_RES 50; /note=N-acetylglycine; /evidence=ECO:0007744|PubMed:22223895 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 12185496; 15681659; 18431481; 18650403; 20733066; |
| Motif | |
| Gene Encoded By | |
| Mass | 38,532 |
| Kinetics | |
| Metal Binding | METAL 197; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03174; METAL 208; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03174; METAL 208; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03174; METAL 271; /note=Divalent metal cation 2; catalytic; via tele nitrogen; /evidence=ECO:0000255|HAMAP-Rule:MF_03174; METAL 303; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03174; METAL 334; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03174; METAL 334; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03174 |
| Rhea ID | |
| Cross Reference Brenda |