Detail Information for IndEnz0002002281
IED ID IndEnz0002002281
Enzyme Type ID protease002281
Protein Name Methionine aminopeptidase 1A
MAP 1A
MetAP 1A
EC 3.4.11.18
Peptidase M 1A
Gene Name MAP1A At2g45240 F4L23.25
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 MASESDASSIATLSCARCEKPAHLQCPKCIDLKLPREQASFCTQECFKAAWSSHKSVHVKAQLSSIGDQNSDLISQGWLYCVKKGQARTPKLPHFDWTGPLKQYPISTKRVVPAEIEKPDWAIDGTPKVEPNSDLQHVVEIKTPEQIQRMRETCKIAREVLDAAARVIHPGVTTDEIDRVVHEATIAAGGYPSPLNYYFFPKSCCTSVNEVICHGIPDARKLEDGDIVNVDVTVCYKGCHGDLNETYFVGNVDEASRQLVKCTYECLEKAIAIVKPGVRFREIGEIVNRHATMSGLSVVRSYCGHGIGDLFHCAPNIPHYARNKAVGVMKAGQTFTIEPMINAGGWRDRTWPDGWTAVTADGKRSAQFEHTLLVTETGVEVLTARLPSSPDVYPWLTK
Enzyme Length 398
Uniprot Accession Number Q9SLN5
Absorption
Active Site
Activity Regulation
Binding Site BINDING 214; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_03174; BINDING 312; /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: 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_03174}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Binding site (2); Chain (1); Initiator methionine (1); Metal binding (7); Modified residue (1); Region (1); Sequence conflict (1)
Keywords Acetylation;Aminopeptidase;Cytoplasm;Hydrolase;Metal-binding;Protease;Reference proteome
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03174, ECO:0000269|PubMed:11060042}.
Modified Residue MOD_RES 2; /note=N-acetylalanine; /evidence=ECO:0007744|PubMed:22223895
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 12185496; 15681659; 19855051;
Motif
Gene Encoded By
Mass 43,992
Kinetics
Metal Binding METAL 231; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03174; METAL 242; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03174; METAL 242; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03174; METAL 305; /note=Divalent metal cation 2; catalytic; via tele nitrogen; /evidence=ECO:0000255|HAMAP-Rule:MF_03174; METAL 338; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03174; METAL 369; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03174; METAL 369; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03174
Rhea ID
Cross Reference Brenda