Q8AAN6 · Q8AAN6_BACTN
- ProteinPhenylacetate-coenzyme A ligase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids435 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score2/5
Function
function
Catalyzes the activation of phenylacetic acid (PA) to phenylacetyl-CoA (PA-CoA).
Catalytic activity
- 2-phenylacetate + ATP + CoA = AMP + diphosphate + phenylacetyl-CoA
Pathway
Aromatic compound metabolism; phenylacetate degradation.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 94 | ADP 1 (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 165 | CoA (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 166 | CoA (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 190 | CoA (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 214 | ADP 2 (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 214 | ADP 1 (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 214 | AMP 2 (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 214 | AMP 1 (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 235 | ADP 2 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 235 | ADP 1 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 235 | AMP 2 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 235 | AMP 1 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 236 | ADP 1 (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 236 | ADP 2 (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 236 | AMP 1 (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 236 | AMP 2 (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 238 | ADP 1 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 238 | AMP 1 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 240 | ADP 3 (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 240 | ADP 1 (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 240 | ADP 2 (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 240 | AMP 2 (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 240 | AMP 1 (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 251 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 258 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 304 | ADP 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 304 | ADP 3 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 304 | ADP 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 304 | AMP 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 304 | AMP 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 313 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 315 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 328 | ADP 2 (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 328 | ADP 1 (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 328 | ADP 3 (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 328 | AMP 2 (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 328 | AMP 1 (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 336 | CoA (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 339 | ADP 2 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 339 | ADP 3 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 339 | AMP 2 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 407 | CoA (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 424 | ADP 1 (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 424 | AMP 1 (UniProtKB | ChEBI) | ||||
Sequence: K |
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 | |||
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Aspect | Term | |
---|---|---|
Molecular Function | metal ion binding | |
Molecular Function | nucleotide binding | |
Molecular Function | phenylacetate-CoA ligase activity | |
Biological Process | phenylacetate catabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePhenylacetate-coenzyme A ligase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Bacteroidota > Bacteroidia > Bacteroidales > Bacteroidaceae > Bacteroides
Accessions
- Primary accessionQ8AAN6
Proteomes
PTM/Processing
Proteomic databases
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 93-287 | AMP-dependent synthetase/ligase | ||||
Sequence: SSGTTGNPTVIVHSQHDLDSWANLVARCLYMVGIRKTDVFQNSSGYGMFTGGLGFQYGAERLGCLTVPAAAGNSKRQIKFISDFKTTALHAIPSYAIRLAEVFQEEGIDPRETTLKTLVIGAEPHTDEQRRKIERMLNVKAYNSFGMTEMNGPGVAFECQEQNGMHFWEDCYLVEIIDPETGEPVPEGEIGELVL | ||||||
Domain | 337-432 | AMP-dependent ligase C-terminal | ||||
Sequence: GVNIFPMQVEKILVQFPELGSNYLITLETVNNQDEMIVEVELSDLSTDNYIELEKIRRDIIRQLKDEILVTPKVKLVKKGSLPQSEGKAVRVKDLR |
Sequence similarities
Belongs to the phenylacetyl-CoA ligase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length435
- Mass (Da)49,380
- Last updated2003-06-01 v1
- Checksum50F97E048724D7A2
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE015928 EMBL· GenBank· DDBJ | AAO75535.1 EMBL· GenBank· DDBJ | Genomic DNA |