Detail Information for IndEnz0002002067
IED ID IndEnz0002002067
Enzyme Type ID protease002067
Protein Name Leucine aminopeptidase 2
EC 3.4.11.-
Leucyl aminopeptidase 2
LAP2
Gene Name LAP2
Organism Trichophyton equinum (Horse ringworm fungus)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Onygenales Arthrodermataceae (dermatophytes) Trichophyton Trichophyton equinum (Horse ringworm fungus)
Enzyme Sequence MKSQLLSLAVAVSTISQGVVGQEPFGWPFKPMVTQDDLQNKIKLKDIMAGVEKLQSFSDAHPEKNRVFGGNGHKDTVEWIYNELKATGYYNVKKQEQVHLWSHAEAALSANGKDLKASAMSYSPPANKIMAELVVAKNNGCNATDYPENTQGKIVLIQRGVCSFGEKSSQAGDAKAIGAVVYNNVPGSLAGTLGGLDKRHVPTAGLSQEDGKNLASLVASGKVDVTMNVVSLFENRTTWNVIAETKGGDHNNVVMLGAHSDSVDAGPGINDNGSGSIGIMTVAKALTNFKLNNAVRFAWWTAEEFGLLGSTFYVDSLDDRELHKVKLYLNFDMIGSPNFANQIYDGDGSAYNMTGPAGSAEIEYLFEKFFDDQGLPHQPTAFTGRSDYSAFIKRNVPAGGLFTGAEVVKTPEQVKLFGGEAGVAYDKNYHGKGDTVANINKGAIFLNTRAIAYSVAEYARSLKGFPTRPKTGKRAVNPQYAKMPGGGCGHHTVFM
Enzyme Length 495
Uniprot Accession Number A7UI09
Absorption
Active Site ACT_SITE 303; /note=Proton acceptor; /evidence=ECO:0000250|UniProtKB:P80561
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number 3.4.11.-
Enzyme Function FUNCTION: Extracellular aminopeptidase that releases a wide variety of amino acids from natural peptides and contributes to pathogenicity.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Chain (1); Domain (1); Glycosylation (4); Metal binding (6); Signal peptide (1); Site (1)
Keywords Aminopeptidase;Glycoprotein;Hydrolase;Metal-binding;Metalloprotease;Protease;Secreted;Signal;Virulence;Zinc
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..21; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 53,197
Kinetics
Metal Binding METAL 259; /note=Zinc 1; catalytic; /evidence=ECO:0000250|UniProtKB:P80561; METAL 271; /note=Zinc 1; catalytic; /evidence=ECO:0000250|UniProtKB:P80561; METAL 271; /note=Zinc 2; catalytic; /evidence=ECO:0000250|UniProtKB:P80561; METAL 304; /note=Zinc 2; catalytic; /evidence=ECO:0000250|UniProtKB:P80561; METAL 332; /note=Zinc 1; catalytic; /evidence=ECO:0000250|UniProtKB:P80561; METAL 430; /note=Zinc 2; catalytic; /evidence=ECO:0000250|UniProtKB:P80561
Rhea ID
Cross Reference Brenda