Detail Information for IndEnz0002002300
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