Detail Information for IndEnz0002002372
IED ID IndEnz0002002372
Enzyme Type ID protease002372
Protein Name Methionine aminopeptidase 2-1
MAP 2-1
MetAP 2-1
EC 3.4.11.18
Peptidase M
Gene Name TSTA_071420
Organism Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006) (Penicillium stipitatum)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Trichocomaceae Talaromyces Talaromyces sect. Talaromyces Talaromyces stipitatus Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006) (Penicillium stipitatum)
Enzyme Sequence MAAQADDELNKLRLNGQNGEAKEQVSASAVDTADNDDSEDDEKEEEGGAEVAATEAAKKKKKRKPKKKKKGGAKKQSSPPRVPVSELFPNNQYPEGEIVEYKDENNYRTTNEEKRYLDRMNNDFLQEYRQGAEVHRQVRQYAQKNIKPGQTLTEIAEGIEDAVRALTGHQGLEEGDNIKGGMGFPCGLSINHCAAHYTPNAGNKMVLQQGDVMKVDFGAHINGRIVDSAFTMTFDPVYDNLLTAVKEATNTGIREAGIDVRMSDIGAAIQEVMESYEVEINGTTYPVKAIRNLNGHNIDQHVIHGGKSVPIVKGGDQTKMEEGEVFAIETFGSTGKGYVREDMETSHYAKAQDAPNVSLRLSSAKNLLNVINKNFGTLPFCRRYLDRLGQDKYLLGLNNLVSAGIVQDYPPLCDIKGSYTAQYEHTIVLRPTVKEVISRGDDY
Enzyme Length 443
Uniprot Accession Number B8LUH2
Absorption
Active Site
Activity Regulation
Binding Site BINDING 196; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; BINDING 304; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_03175
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_03175};
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_03175}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Binding site (2); Chain (1); Compositional bias (3); Metal binding (7); Region (1)
Keywords Aminopeptidase;Cytoplasm;Hydrolase;Metal-binding;Protease;Reference proteome
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03175}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 48,965
Kinetics
Metal Binding METAL 216; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 227; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 227; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 296; /note=Divalent metal cation 2; catalytic; via tele nitrogen; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 329; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 424; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 424; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03175
Rhea ID
Cross Reference Brenda