Detail Information for IndEnz0002002358
IED ID IndEnz0002002358
Enzyme Type ID protease002358
Protein Name Methionine aminopeptidase 2-1
MAP 2-1
MetAP 2-1
EC 3.4.11.18
Peptidase M
Gene Name af410 AFUA_8G00410
Organism Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Fumigati Neosartorya fumigata (Aspergillus fumigatus) Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Enzyme Sequence MTVDAPELLEKLRITDAGANGADMSSSTSAAANGTGKEVDDGSDDDGTENPPAVAAEHSTAKKKKNKKRKPKKKQPKVQTDPPSIPLSQLFPNNSYPKGEEVEYKDENRYRTTSEEKRHLDNLNSDFLSDYRQAAEAHRQVRQWAQRNIKPGQTLLEIANGIEESARCLVGHDGLTEGDSLIAGMGFPTGLNIDNIVAHYSPNAGCKTVLAQNNVLKVDIGIHVGGRIVDSAFTMAFDPMYDNLLAAVKDATNTGVREAGIDVRVGELGGYIQEAMESYECEIRGKTYPIKAIRNLCGHTILPYSIHGTKNVPFVKSNDMTKMEEGDVFAIETFGSTGSGRYVEGGEVSHYALRGDADRKDLTLSSARSLLTAIKKNFSTIPFCRRYLDRIGQEKYLLGLNYLVKSGIVEDYPPLNEKPGTYTAQFEHTILLRPTVKEVISRGDDY
Enzyme Length 446
Uniprot Accession Number Q4WAY7
Absorption
Active Site
Activity Regulation
Binding Site BINDING 199; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; BINDING 307; /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) (By similarity). Part of the gene cluster that mediates the biosynthesis of fumagillin, a meroterpenoid that has numerous biological activities including irreversible inhibition of human type 2 methionine aminopeptidase (METAP2) (PubMed:23488861, PubMed:24082142, PubMed:24568283). Since fumagillin is known to inhibit eukaryotic type 2 methionine aminopeptidase, af410 encodes a self-resistant enzyme for A.fumigatus toward fumagillin (PubMed:23488861). {ECO:0000255|HAMAP-Rule:MF_03175, ECO:0000269|PubMed:23488861, ECO:0000269|PubMed:24082142, ECO:0000269|PubMed:24568283}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Binding site (2); Chain (1); Compositional bias (4); Erroneous gene model prediction (1); Metal binding (7); Region (1)
Keywords Aminopeptidase;Cytoplasm;Hydrolase;Metal-binding;Protease;Reference proteome
Interact With
Induction INDUCTION: Expression is controlled by the fumagillin biosynthesis cluster regulator fumR (PubMed:24082142). Expression is also under the control of the developmental and secondary metabolism regulator veA (PubMed:24116213). {ECO:0000269|PubMed:24082142, ECO:0000269|PubMed:24116213}.
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 48,996
Kinetics
Metal Binding METAL 219; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 230; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 230; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 299; /note=Divalent metal cation 2; catalytic; via tele nitrogen; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 332; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 427; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 427; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03175
Rhea ID
Cross Reference Brenda