IED ID | IndEnz0002016717 |
Enzyme Type ID | protease016717 |
Protein Name |
Aminopeptidase T AP-T EC 3.4.11.- Heat-stable aminopeptidase |
Gene Name | TTHA1152 |
Organism | Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) |
Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Deinococcus-Thermus Deinococci Thermales Thermaceae Thermus Thermus thermophilus Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) |
Enzyme Sequence | MDAFKRNLEKLAELAIRVGLNLEKGQEVIATAPIEAVDFVRLLAEKAYREGASLFTVIYGDQELARKRLALAPEEGLDKAPAWLYEGMARAFREGAARLAVSGSDPKALEGLPPEKVGRAQKANARAYKPALEAITEFVTNWTIVPFAHPGWARAVFPGLPEEEAVRRLWEAIFQATRADQEDPIAAWEAHNRALHEKVAYLNARRFHALHFKGPGTDLVVGLAEGHLWQGGATATKGGRLCNPNLPTEEVFTAPHRERVEGVVRASRPLALGGTLVEGIFARFERGFAVEVRAEKGEEVLRRLLDTDEGARRLGEVALVPADNPIAKTGLVFFDTLFDENAASHIAFGQAYQENLEGRPSGEAFRKRGGNESLVHVDWMIGSEEMDVDGLYEDGTRTPLMRRGRWVV |
Enzyme Length | 408 |
Uniprot Accession Number | P42778 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | 3.4.11.- |
Enzyme Function | FUNCTION: Metal-dependent exopeptidase. {ECO:0000269|PubMed:16242715}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Chain (1); Metal binding (8) |
Keywords | 3D-structure;Aminopeptidase;Cobalt;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Zinc |
Interact With | |
Induction | |
Subcellular Location | |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | X-ray crystallography (1) |
Cross Reference PDB | 2AYI; |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 45,018 |
Kinetics | |
Metal Binding | METAL 250; /note=Divalent metal cation 1; /evidence=ECO:0000305|PubMed:16242715; METAL 316; /note=Divalent metal cation 1; /evidence=ECO:0000305|PubMed:16242715; METAL 316; /note=Divalent metal cation 2; /evidence=ECO:0000305|PubMed:16242715; METAL 340; /note=Divalent metal cation 1; /evidence=ECO:0000305|PubMed:16242715; METAL 340; /note=Divalent metal cation 2; /evidence=ECO:0000305|PubMed:16242715; METAL 345; /note=Divalent metal cation 1; /evidence=ECO:0000305|PubMed:16242715; METAL 376; /note=Divalent metal cation 2; /evidence=ECO:0000305|PubMed:16242715; METAL 378; /note=Divalent metal cation 2; /evidence=ECO:0000305|PubMed:16242715 |
Rhea ID | |
Cross Reference Brenda |