Q7CQV5 · IAAA_SALTY
- ProteinIsoaspartyl peptidase
- GeneiaaA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids313 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Degrades proteins damaged by L-isoaspartyl residue formation (also known as beta-Asp residues). Degrades L-isoaspartyl-containing di- and tripeptides. Acts best on iso-Asp-Leu, followed by iso-Asp-Ala, -His and to a lesser extent iso-Asp-Lys, -Phe and iso-Asp-Leu-Ala. Does not act on internal iso-Asp bonds (Als-iso-Asp-Leu-Ala). Does not act on alpha-Asp bonds. Has poor L-asparaginase activity.
Catalytic activity
Features
Showing features for site, active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 178-179 | Cleavage; by autolysis | ||||
Sequence: GT | ||||||
Active site | 179 | Nucleophile | ||||
Sequence: T | ||||||
Binding site | 207-210 | substrate | ||||
Sequence: RVGD | ||||||
Binding site | 230-233 | substrate | ||||
Sequence: TGTG |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | asparaginase activity | |
Molecular Function | beta-aspartyl-peptidase activity | |
Biological Process | proteolysis |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameIsoaspartyl peptidase
- EC number
- Alternative names
- Cleaved into 2 chains
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Salmonella
Accessions
- Primary accessionQ7CQV5
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000344061 | 1-178 | Isoaspartyl peptidase subunit alpha | |||
Sequence: MNKAVIAIHGGAGAIARAQMSHEQELRYIQALSEIVESGQKMLEAGDSALDVVTEAVRLLEACPLFNAGIGAVYTRDGTHELDACVMDGNTLKAGAVAGVSHVRHPVLAARLVMERSPHVLMVGEGAENFAFSQGMARVSPDIFSTPARYEQLLAARAAGEMALDHSGAPLDETKKMG | ||||||
Chain | PRO_0000344062 | 179-313 | Isoaspartyl peptidase subunit beta | |||
Sequence: TVGAVARDKFGNLAAATSTGGMTNKLPGRVGDSPLVGAGCYANNASVAVSCTGTGEVFIRTLAAYDIAALMEYGGLSLADACERVVMEKLPALGGSGGLIAVDHEGNVALPFNSEGMYRAWGYAGDTPTTGIYRE |
Post-translational modification
Autocleaved. Generates the alpha and beta subunits. The beta subunit is thought to be responsible for the nucleophile hydrolase activity.
Keywords
- PTM
Proteomic databases
Interaction
Subunit
Heterotetramer of two alpha and two beta chains arranged as a dimer of alpha/beta heterodimers.
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length313
- Mass (Da)32,473
- Last updated2004-07-05 v1
- ChecksumD37BD85830F9D83E
Mass Spectrometry
Isoaspartyl peptidase subunit alpha
Molecular mass is 18,787.4 Da. Determined by MALDI. Subunit alpha.Isoaspartyl peptidase subunit beta
Molecular mass is 13,719.9 Da. Determined by MALDI. Subunit beta.Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE006468 EMBL· GenBank· DDBJ | AAL19783.1 EMBL· GenBank· DDBJ | Genomic DNA |