A0R3F9 · PAT_MYCS2
- ProteinAcetyltransferase Pat
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids333 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes specifically the acetylation of the epsilon-amino group of a highly conserved lysine residue in acetyl-CoA synthetase (ACS) and of the universal stress protein (USP) MSMEG_4207. Acetylation results in the inactivation of ACS activity and could be important for mycobacteria to adjust to environmental changes.
Cofactor
Activity regulation
Allosterically regulated by cAMP.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
3.1 μM | acetyl-CoA (with ACS as substrate) | |||||
10 μM | acetyl-CoA (with USP as substrate) | |||||
10.2 μM | ACS | |||||
335 μM | USP |
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 85-88 | 3',5'-cyclic AMP (UniProtKB | ChEBI); allosteric activator | ||||
Sequence: GEIA | ||||||
Binding site | 95-96 | 3',5'-cyclic AMP (UniProtKB | ChEBI); allosteric activator | ||||
Sequence: RT | ||||||
Binding site | 135 | 3',5'-cyclic AMP (UniProtKB | ChEBI); allosteric activator | ||||
Sequence: R | ||||||
Binding site | 211 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 237-239 | substrate | ||||
Sequence: FTV | ||||||
Binding site | 245-250 | substrate | ||||
Sequence: GRGIGS | ||||||
Binding site | 276 | substrate | ||||
Sequence: N | ||||||
Binding site | 285 | substrate | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | metal ion binding | |
Molecular Function | N-acetyltransferase activity |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAcetyltransferase Pat
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Mycobacteriales > Mycobacteriaceae > Mycolicibacterium
Accessions
- Primary accessionA0R3F9
Proteomes
Phenotypes & Variants
Disruption phenotype
Disruption of this gene abolishes acetylation of USP.
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 95 | No increase in the rate of acetylation in the presence of cAMP, presumably because of its inability to bind cAMP. | ||||
Sequence: R → K | ||||||
Mutagenesis | 234 | Shows a lower rate of acetylation of USP in the absence of cAMP than the wild-type protein, but in the presence of cAMP, an increase in the rate of acetyltransferase activity is observed. | ||||
Sequence: E → A |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000420361 | 1-333 | Acetyltransferase Pat | |||
Sequence: MAELTEVRAADLAALEFFTGCRPSALEPLATQLRPLKAEPGQVLIRQGDPALTFMLIESGRVQVSHAVADGPPIVLDIEPGLIIGEIALLRDAPRTATVVAAEPVIGWVGDRDAFDTILHLPGMFDRLVRIARQRLAAFITPIPVQVRTGEWFYLRPVLPGDVERTLNGPVEFSSETLYRRFQSVRKPTRALLEYLFEVDYADHFVWVMTEGALGPVIADARFVREGHNATMAEVAFTVGDDYQGRGIGSFLMGALIVSANYVGVQRFNARVLTDNMAMRKIMDRLGAVWVREDLGVVMTEVDVPPVDTVPFEPELIDQIRDATRKVIRAVSQ |
Proteomic databases
Interaction
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 153-317 | N-acetyltransferase | ||||
Sequence: FYLRPVLPGDVERTLNGPVEFSSETLYRRFQSVRKPTRALLEYLFEVDYADHFVWVMTEGALGPVIADARFVREGHNATMAEVAFTVGDDYQGRGIGSFLMGALIVSANYVGVQRFNARVLTDNMAMRKIMDRLGAVWVREDLGVVMTEVDVPPVDTVPFEPELI |
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length333
- Mass (Da)36,848
- Last updated2007-01-09 v1
- ChecksumC6CCBC36F639C945
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000480 EMBL· GenBank· DDBJ | ABK70370.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP001663 EMBL· GenBank· DDBJ | AFP41750.1 EMBL· GenBank· DDBJ | Genomic DNA |