P09786 · PHNB_PSEAE
- ProteinAnthranilate synthase component 2, pyocyanine specific
- GenephnB
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids200 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, a precursor for Pseudomonas quinolone signal (2-heptyl-3-hydroxy-4-quinolone; PQS) production which is required to induce the genes for the biosynthesis of the virulence factor pyocyanine (PCN), a characteristic blue-green phenazine pigment produced by P.aeruginosa (PubMed:11591691, PubMed:2153661, PubMed:23449919).
In the first step, the glutamine-binding beta subunit (PhnB) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (PhnA) to produce anthranilate (By similarity).
In the first step, the glutamine-binding beta subunit (PhnB) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (PhnA) to produce anthranilate (By similarity).
Miscellaneous
PhnAB is not feedback inhibited by tryptophan.
Catalytic activity
- chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate + H+
Pathway
Secondary metabolite biosynthesis; pyocyanine biosynthesis.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 56-58 | L-glutamine (UniProtKB | ChEBI) | ||||
Sequence: GPG | ||||||
Active site | 83 | Nucleophile; for GATase activity | ||||
Sequence: C | ||||||
Binding site | 87 | L-glutamine (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 133-134 | L-glutamine (UniProtKB | ChEBI) | ||||
Sequence: SL | ||||||
Active site | 169 | For GATase activity | ||||
Sequence: H | ||||||
Active site | 171 | For GATase activity | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | anthranilate phosphoribosyltransferase activity | |
Molecular Function | anthranilate synthase activity | |
Biological Process | glutamine metabolic process | |
Biological Process | phenazine biosynthetic process | |
Biological Process | tryptophan biosynthetic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameAnthranilate synthase component 2, pyocyanine specific
- EC number
- Short namesAS; ASII
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Pseudomonadales > Pseudomonadaceae > Pseudomonas
Accessions
- Primary accessionP09786
Proteomes
Organism-specific databases
Phenotypes & Variants
Disruption phenotype
Single disruption in strain PA04290 results in decreased pyocyanine synthesis (PubMed:2153661).
Double phnA-phnB deletions are tryptophan prototrophs; they make less PQS (PubMed:23449919).
Double phnA-phnB deletions are tryptophan prototrophs; they make less PQS (PubMed:23449919).
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | 148-149 | in strain: PAC174 | ||||
Sequence: DA → ES | ||||||
Natural variant | 195 | in strain: PAC174 | ||||
Sequence: R → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 2 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000056906 | 1-200 | Anthranilate synthase component 2, pyocyanine specific | |||
Sequence: MRITLLDNFDSFTYNLVEQFCLLGAEVRVMRNDTPLPTIQAALLADGCELLVLSPGPGRPEDAGCMLELLAWARGRLPVLGVCLGHQALALAAGGAVGEARKPLHGKSTSLRFDQRHPLFDGIADLRVARYHSLVVSRLPEGFDCLADADGEIMAMADPRNRQLGLQFHPESILTTHGQRLLENALLWCGALAVRERLRA |
Proteomic databases
Interaction
Subunit
Heterotetramer consisting of two non-identical subunits: a beta subunit (PhnB) and a large alpha subunit (PhnA).
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 2-195 | Glutamine amidotransferase type-1 | ||||
Sequence: RITLLDNFDSFTYNLVEQFCLLGAEVRVMRNDTPLPTIQAALLADGCELLVLSPGPGRPEDAGCMLELLAWARGRLPVLGVCLGHQALALAAGGAVGEARKPLHGKSTSLRFDQRHPLFDGIADLRVARYHSLVVSRLPEGFDCLADADGEIMAMADPRNRQLGLQFHPESILTTHGQRLLENALLWCGALAVR |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length200
- Mass (Da)21,845
- Last updated2000-12-08 v3
- Checksum9D9E218DDE8D7E30
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 195 | in Ref. 1; AAA88449 | ||||
Sequence: R → A |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M15733 EMBL· GenBank· DDBJ | AAA26018.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M33810 EMBL· GenBank· DDBJ | AAA88449.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M33811 EMBL· GenBank· DDBJ | AAA88452.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE004091 EMBL· GenBank· DDBJ | AAG04391.1 EMBL· GenBank· DDBJ | Genomic DNA |