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PSEAE:PQSD

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Species (Taxon ID) Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG12228). (208964)
Gene Name(s) pqsD
Protein Name(s) 2-heptyl-4(1H)-quinolone synthase PqsD

PqsD

External Links
UniProt P20582
EMBL AE004091
M33810
PIR B83522
D35116
RefSeq NP_249690.1
PDB 3H76
3H77
3H78
PDBsum 3H76
3H77
3H78
ProteinModelPortal P20582
SMR P20582
STRING 208964.PA0999
DNASU 880625
EnsemblBacteria AAG04388
GeneID 880625
KEGG pae:PA0999
PATRIC 19836288
PseudoCAP PA0999
eggNOG COG0332
HOGENOM HOG000246674
InParanoid P20582
KO K18003
OMA PATACMV
OrthoDB EOG6J74XN
PhylomeDB P20582
BioCyc MetaCyc:MONOMER-16011
EvolutionaryTrace P20582
Proteomes UP000002438
GO GO:0005737
GO:0004315
GO:0016746
GO:0006633
GO:0044550
Gene3D 3.40.47.10
InterPro IPR013751
IPR013747
IPR016039
IPR016038
Pfam PF08545
PF08541
SUPFAM SSF53901

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0004315

3-oxoacyl-[acyl-carrier-protein] synthase activity

PMID:18728009[1]

ECO:0000314

F

Figure 2 shows DHQ formation by PqsD in Vitro. Mutant strains showed PqsD was a part of DHQ synthesis in vivo and was further tested in vitro. Anthraniloyl-CoA was produced in situ by PqsA and reacted with malonyl-CoA (a product of PqsD) to form DHQ as supported by TLC and LC-MS. These tests confirm DHQ formation when compared against the DHQ standard. Figure 7 shows the proposed mechanism for DHQ synthesis with the products of the Pqs gene.

complete
CACAO 7692

enables

GO:0016746

transferase activity, transferring acyl groups

PMID:18728009[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0044550

secondary metabolite biosynthetic process

PMID:18728009[1]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0044550

secondary metabolite biosynthetic process

PMID:12426334[2]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0016746

transferase activity, transferring acyl groups

PMID:18728009[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0003824

catalytic activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR016039

F

Seeded From UniProt

complete

enables

GO:0004315

3-oxoacyl-[acyl-carrier-protein] synthase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR013751

F

Seeded From UniProt

complete

involved_in

GO:0006633

fatty acid biosynthetic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR013751

P

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0963
UniProtKB-SubCell:SL-0086

C

Seeded From UniProt

complete

enables

GO:0016740

transferase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0808

F

Seeded From UniProt

complete

enables

GO:0016746

transferase activity, transferring acyl groups

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0012

F

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. 1.0 1.1 1.2 1.3 Zhang, YM et al. (2008) PqsD is responsible for the synthesis of 2,4-dihydroxyquinoline, an extracellular metabolite produced by Pseudomonas aeruginosa. J. Biol. Chem. 283 28788-94 PubMed GONUTS page
  2. Gallagher, LA et al. (2002) Functions required for extracellular quinolone signaling by Pseudomonas aeruginosa. J. Bacteriol. 184 6472-80 PubMed GONUTS page