Detail Information for IndEnz0002002349
IED ID IndEnz0002002349
Enzyme Type ID protease002349
Protein Name Methionine aminopeptidase 1
MAP 1
MetAP 1
EC 3.4.11.18
Peptidase M 1
Gene Name MAP1 YLR244C L9672.12
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces Saccharomyces cerevisiae (Baker's yeast) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Enzyme Sequence MSTATTTVTTSDQASHPTKIYCSGLQCGRETSSQMKCPVCLKQGIVSIFCDTSCYENNYKAHKALHNAKDGLEGAYDPFPKFKYSGKVKASYPLTPRRYVPEDIPKPDWAANGLPVSEQRNDRLNNIPIYKKDQIKKIRKACMLGREVLDIAAAHVRPGITTDELDEIVHNETIKRGAYPSPLNYYNFPKSLCTSVNEVICHGVPDKTVLKEGDIVNLDVSLYYQGYHADLNETYYVGENISKEALNTTETSRECLKLAIKMCKPGTTFQELGDHIEKHATENKCSVVRTYCGHGVGEFFHCSPNIPHYAKNRTPGVMKPGMVFTIEPMINEGTWKDMTWPDDWTSTTQDGKLSAQFEHTLLVTEHGVEILTARNKKSPGGPRQRIK
Enzyme Length 387
Uniprot Accession Number Q01662
Absorption
Active Site
Activity Regulation ACTIVITY REGULATION: In contract to the MetAP 2 isoform, is not inhibited by the fungal metabolite fumagillin, an antiangiogenic drug. {ECO:0000269|PubMed:9177176}.
Binding Site BINDING 202; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_03174; BINDING 301; /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). Plays the major role in N-terminal methionine removal. Less efficient when the second residue is Val. {ECO:0000255|HAMAP-Rule:MF_03174, ECO:0000269|PubMed:11811952, ECO:0000269|PubMed:11968008, ECO:0000269|PubMed:12874831, ECO:0000269|PubMed:7862096}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Binding site (2); Chain (1); Initiator methionine (1); Metal binding (7); Modified residue (1); Mutagenesis (3); Propeptide (1); Region (1)
Keywords Acetylation;Aminopeptidase;Cytoplasm;Direct protein sequencing;Hydrolase;Metal-binding;Protease;Reference proteome;Zinc
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm.
Modified Residue MOD_RES 2; /note=N-acetylserine; /evidence=ECO:0007744|PubMed:22814378
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 10224104; 10515904; 10727764; 12144506; 14563547; 14676204; 15210064; 15547949; 16386852; 16554755; 16917013; 17229726; 18205808; 18719252; 18998772; 19536198; 20934449; 21124907; 21655302; 21936842; 22350874; 2246265; 23586741; 25710965; 26195668; 26335097; 26777405; 27693354; 7644482; 8618900;
Motif
Gene Encoded By
Mass 43,373
Kinetics BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.68 mM for a Met-Ala-Ser peptide {ECO:0000269|PubMed:10075912, ECO:0000269|PubMed:7862096}; KM=6.56 mM for a Met-Gly-Met-Met peptide {ECO:0000269|PubMed:10075912, ECO:0000269|PubMed:7862096}; KM=139 uM for a Met-Ala-Ser-Trp peptide {ECO:0000269|PubMed:10075912, ECO:0000269|PubMed:7862096}; Note=kcat is 1173, 1416 and 507 min(-1) with a Met-Ala-Ser, a Met-Gly-Met-Met and a Met-Ala-Ser-Trp peptide substrate, respectively.;
Metal Binding METAL 219; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03174; METAL 230; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03174; METAL 230; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03174; METAL 294; /note=Divalent metal cation 2; catalytic; via tele nitrogen; /evidence=ECO:0000255|HAMAP-Rule:MF_03174; METAL 327; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03174; METAL 358; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03174; METAL 358; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03174
Rhea ID
Cross Reference Brenda