Detail Information for IndEnz0002003084
IED ID IndEnz0002003084
Enzyme Type ID protease003084
Protein Name Putative Xaa-Pro aminopeptidase FRA1
EC 3.4.11.9
Fe repressor of activation 1
Gene Name FRA1 YLL029W
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 MTSKPSTSDGRAHSISHVPGTHMRGTSASHSPRPFRPCADCTCSPGLLSRQGRRASLFLRQLENSRRSSSMLLNELKGAGGGSSAGNGSVYSCDSLCAVNREVNTTDRLLKLRQEMKKHDLCCYIVPSCDEHQSEYVSLRDQRRAFISGFSGSAGVACITRDLLNFNDDHPDGKSILSTDGRYFNQARQELDYNWTLLRQNEDPITWQEWCVREALEMAKGLGNKEGMVLKIGIDPKLITFNDYVSFRKMIDTKYDAKGKVELVPVEENLVDSIWPDFETLPERPCNDLLLLKYEFHGEEFKDKKEKLLKKLNDKASSATTGRNTFIVVALDEICWLLNLRGSDIDYNPVFFSYVAINEDETILFTNNPFNDDISEYFKINGIEVRPYEQIWEHLTKITSQASSAEHEFLIPDSASWQMVRCLNTSTNANGAIAKKMTAQNFAIIHSPIDVLKSIKNDIEIKNAHKAQVKDAVCLVQYFAWLEQQLVGREALIDEYRAAEKLTEIRKTQRNFMGNSFETISSTGSNAAIIHYSPPVENSSMIDPTKIYLCDSGSQFLEGTTDITRTIHLTKPTKEEMDNYTLVLKGGLALERLIFPENTPGFNIDAIARQFLWSRGLDYKHGTGHGIGSFLNVHEGPMGVGFRPHLMNFPLRAGNIISNEPGYYKDGEYGIRIESDMLIKKATEKGNFLKFENMTVVPYCRKLINTKLLNEEEKTQINEYHARVWRTIVHFLQPQSISYKWLKRETSPL
Enzyme Length 749
Uniprot Accession Number Q07825
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide.; EC=3.4.11.9;
DNA Binding
EC Number 3.4.11.9
Enzyme Function FUNCTION: Involved in the regulation of the iron regulon in responss to decreased mitochondrial iron-sulfur cluster synthesis. {ECO:0000269|PubMed:18281282}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (1); Compositional bias (1); Metal binding (6); Modified residue (3); Region (1)
Keywords Aminopeptidase;Cytoplasm;Direct protein sequencing;Hydrolase;Manganese;Metal-binding;Metalloprotease;Phosphoprotein;Protease;Reference proteome
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
Modified Residue MOD_RES 69; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:19779198"; MOD_RES 92; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:19779198"; MOD_RES 95; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 10487931; 11805837; 11921089; 12140549; 14690591; 15766533; 16554755; 17107617; 17651441; 19536198; 19715344; 20139087; 20522543; 20702584; 21479832; 21840721; 22389494; 22583368; 23457300; 23595675; 23962819; 27693354;
Motif
Gene Encoded By
Mass 84,924
Kinetics
Metal Binding METAL 551; /note=Manganese 2; /evidence=ECO:0000255; METAL 562; /note=Manganese 1; /evidence=ECO:0000255; METAL 562; /note=Manganese 2; /evidence=ECO:0000255; METAL 660; /note=Manganese 1; /evidence=ECO:0000255; METAL 674; /note=Manganese 1; /evidence=ECO:0000255; METAL 674; /note=Manganese 2; /evidence=ECO:0000255
Rhea ID
Cross Reference Brenda