Detail Information for IndEnz0002002335
IED ID IndEnz0002002335
Enzyme Type ID protease002335
Protein Name Methionine aminopeptidase 1
MAP 1
MetAP 1
EC 3.4.11.18
Peptidase M 1
Gene Name fma1 SPBC3E7.10
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota Taphrinomycotina Schizosaccharomycetes Schizosaccharomycetales Schizosaccharomycetaceae Schizosaccharomyces Schizosaccharomyces pombe (Fission yeast) Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Enzyme Sequence MATEIAKHICCGIDCNNEADRLQCPKCLNDGVKSYFCGQECFRNSWNIHKHLHRPPNVEKREDGTYNPFPKFHFAGSLKPVYPLSPIRKVPPHIKRPDYAKTGVSRSEQIEGRSFKLKRLTPKEQEGMRKVCRLGREVLDAAAAAVRPGTTTDELDSIVHNACIERDCFPSTLNYYAFPKSVCTSVNEIICHGIPDQRPLEDGDIVNIDVSLYHNGFHGDLNETYYVGDKAKANPDLVCLVENTRIALDKAIAAVKPGVLFQEFGNIIEKHTNSITEKQISVVRTYCGHGINQLFHCSPSIPHYSHNKAPGIARPGMTFTIEPMLTLGPARDITWPDDWTSSTASGRCSAQFEHTLLVTETGCEVLTARLPNSPGGPLK
Enzyme Length 379
Uniprot Accession Number O59730
Absorption
Active Site
Activity Regulation
Binding Site BINDING 192; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_03174; BINDING 296; /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); Metal binding (7); Modified residue (1); Region (1)
Keywords Aminopeptidase;Cytoplasm;Hydrolase;Metal-binding;Nucleus;Phosphoprotein;Protease;Reference proteome
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03174, ECO:0000269|PubMed:16823372}. Nucleus, nucleolus {ECO:0000269|PubMed:16823372}.
Modified Residue MOD_RES 373; /note=Phosphoserine; /evidence=ECO:0000269|PubMed:18257517
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 16491466; 18684775; 20473289; 23697806; 24763107; 29996109; 30647105; 30726745; 32062975;
Motif
Gene Encoded By
Mass 42,139
Kinetics
Metal Binding METAL 209; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03174; METAL 220; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03174; METAL 220; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03174; METAL 289; /note=Divalent metal cation 2; catalytic; via tele nitrogen; /evidence=ECO:0000255|HAMAP-Rule:MF_03174; METAL 322; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03174; METAL 353; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03174; METAL 353; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03174
Rhea ID
Cross Reference Brenda