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Protein

2-heptyl-4(1H)-quinolone synthase PqsD

Gene

pqsD

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Required for the biosynthesis of a number of signaling molecules, such as the quinolone signal 2-heptyl-3-hydroxy-4(1H)-quinolone (PQS), 2-heptyl-4-hydroxyquinoline (HHQ) and 2,4-dihydroxyquinoline (DHQ). These molecules are required for normal biofilm formation. The exact reaction mechanism is still under debate. According to PubMed:18728009, a covalent anthraniloyl-PqsD intermediate is formed, which then condenses with malonyl-CoA or malonyl-acyl carrier protein (malonyl-ACP) to form the short-lived intermediate 3-(2-aminophenyl)-3-oxopropanoyl-CoA. An intramolecular rearrangement of this intermediate can give rise to 2,4-dihydroxyquinoline (DHQ) (in vitro). Alternatively (PubMed:21425231), DHQ and HHQ biosynthesis could proceed via a decarboxylative Claisen condensation of a beta-ketoacid and anthraniloyl-CoA.4 Publications

Catalytic activityi

3-oxodecanoate + anthraniloyl-CoA = CoA + 2-heptyl-4(1H)-quinolone + CO2 + H2O.4 Publications
Malonyl-CoA + anthraniloyl-CoA = 2 CoA + 4-hydroxy-2(1H)-quinolone + CO2.1 Publication3 Publications

Kineticsi

  1. KM=35 µM for anthraniloyl-CoA1 Publication
  2. KM=104 µM for malonyl-CoA1 Publication
  3. KM=48.7 µM for malonyl-CoA1 Publication
  4. KM=18 µM for malonyl-ACP1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei29 – 291Anthraniloyl-CoA1 Publication
    Binding sitei33 – 331Anthraniloyl-CoA1 Publication
    Active sitei113 – 1131Nucleophile2 Publications
    Binding sitei258 – 2581Anthraniloyl-CoA1 Publication

    GO - Molecular functioni

    GO - Biological processi

    • fatty acid biosynthetic process Source: InterPro
    • secondary metabolite biosynthetic process Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-16011.
    BRENDAi2.3.1.230. 5087.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    2-heptyl-4(1H)-quinolone synthase PqsD (EC:2.3.1.2304 Publications)
    Short name:
    PqsD
    Gene namesi
    Name:pqsD
    Ordered Locus Names:PA0999
    OrganismiPseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
    Taxonomic identifieri208964 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
    Proteomesi
    • UP000002438 Componenti: Chromosome

    Organism-specific databases

    PseudoCAPiPA0999.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Disruption phenotypei

    Abolishes the biosynthesis of the signaling molecules 2-heptyl-3-hydroxy-4(1H)-quinolone (PQS), 2-heptyl-4-hydroxyquinoline (HHQ) and 2,4-dihydroxyquinoline (DHQ).1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi113 – 1131C → A: Abolishes enzyme activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 3373372-heptyl-4(1H)-quinolone synthase PqsDPRO_0000110519Add
    BLAST

    Proteomic databases

    PaxDbiP20582.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    STRINGi208964.PA0999.

    Structurei

    Secondary structure

    1
    337
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 128Combined sources
    Beta strandi15 – 195Combined sources
    Helixi20 – 234Combined sources
    Turni24 – 263Combined sources
    Helixi31 – 388Combined sources
    Beta strandi42 – 454Combined sources
    Helixi53 – 6614Combined sources
    Helixi71 – 733Combined sources
    Beta strandi76 – 805Combined sources
    Beta strandi85 – 895Combined sources
    Helixi91 – 999Combined sources
    Beta strandi106 – 1105Combined sources
    Helixi112 – 1143Combined sources
    Helixi115 – 12814Combined sources
    Beta strandi133 – 14210Combined sources
    Helixi144 – 1463Combined sources
    Turni151 – 1533Combined sources
    Helixi154 – 1574Combined sources
    Beta strandi162 – 1709Combined sources
    Beta strandi175 – 18612Combined sources
    Helixi188 – 1936Combined sources
    Beta strandi194 – 1963Combined sources
    Beta strandi203 – 2053Combined sources
    Helixi209 – 2135Combined sources
    Turni214 – 2174Combined sources
    Beta strandi218 – 2214Combined sources
    Helixi223 – 24422Combined sources
    Helixi249 – 2513Combined sources
    Beta strandi253 – 2575Combined sources
    Helixi262 – 27211Combined sources
    Helixi276 – 2783Combined sources
    Helixi283 – 2864Combined sources
    Helixi290 – 2923Combined sources
    Helixi293 – 3019Combined sources
    Helixi302 – 3043Combined sources
    Beta strandi310 – 3178Combined sources
    Turni318 – 3203Combined sources
    Beta strandi321 – 3288Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3H76X-ray1.80A/B2-337[»]
    3H77X-ray1.80A/B2-337[»]
    3H78X-ray1.70A/B2-337[»]
    ProteinModelPortaliP20582.
    SMRiP20582. Positions 2-330.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP20582.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni154 – 1552Anthraniloyl-CoA binding1 Publication
    Regioni221 – 2244Anthraniloyl-CoA binding1 Publication

    Sequence similaritiesi

    Belongs to the FabH family.Curated

    Phylogenomic databases

    eggNOGiENOG4105CCZ. Bacteria.
    COG0332. LUCA.
    HOGENOMiHOG000246674.
    InParanoidiP20582.
    KOiK18003.
    OMAiDIRQQCT.
    PhylomeDBiP20582.

    Family and domain databases

    Gene3Di3.40.47.10. 2 hits.
    InterProiIPR013751. ACP_syn_III.
    IPR013747. ACP_syn_III_C.
    IPR016039. Thiolase-like.
    [Graphical view]
    PfamiPF08545. ACP_syn_III. 1 hit.
    PF08541. ACP_syn_III_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF53901. SSF53901. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P20582-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MGNPILAGLG FSLPKRQVSN HDLVGRINTS DEFIVERTGV RTRYHVEPEQ
    60 70 80 90 100
    AVSALMVPAA RQAIEAAGLL PEDIDLLLVN TLSPDHHDPS QACLIQPLLG
    110 120 130 140 150
    LRHIPVLDIR AQCSGLLYGL QMARGQILAG LARHVLVVCG EVLSKRMDCS
    160 170 180 190 200
    DRGRNLSILL GDGAGAVVVS AGESLEDGLL DLRLGADGNY FDLLMTAAPG
    210 220 230 240 250
    SASPTFLDEN VLREGGGEFL MRGRPMFEHA SQTLVRIAGE MLAAHELTLD
    260 270 280 290 300
    DIDHVICHQP NLRILDAVQE QLGIPQHKFA VTVDRLGNMA SASTPVTLAM
    310 320 330
    FWPDIQPGQR VLVLTYGSGA TWGAALYRKP EEVNRPC
    Length:337
    Mass (Da):36,379
    Last modified:December 8, 2000 - v2
    Checksum:iBB887BAED9C19B92
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE004091 Genomic DNA. Translation: AAG04388.1.
    M33810 Genomic DNA. Translation: AAA88446.1.
    PIRiB83522.
    D35116.
    RefSeqiNP_249690.1. NC_002516.2.
    WP_003112550.1. NZ_ASJY01000132.1.

    Genome annotation databases

    EnsemblBacteriaiAAG04388; AAG04388; PA0999.
    GeneIDi880625.
    KEGGipae:PA0999.
    PATRICi19836288. VBIPseAer58763_1031.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE004091 Genomic DNA. Translation: AAG04388.1.
    M33810 Genomic DNA. Translation: AAA88446.1.
    PIRiB83522.
    D35116.
    RefSeqiNP_249690.1. NC_002516.2.
    WP_003112550.1. NZ_ASJY01000132.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3H76X-ray1.80A/B2-337[»]
    3H77X-ray1.80A/B2-337[»]
    3H78X-ray1.70A/B2-337[»]
    ProteinModelPortaliP20582.
    SMRiP20582. Positions 2-330.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi208964.PA0999.

    Proteomic databases

    PaxDbiP20582.

    Protocols and materials databases

    DNASUi880625.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAG04388; AAG04388; PA0999.
    GeneIDi880625.
    KEGGipae:PA0999.
    PATRICi19836288. VBIPseAer58763_1031.

    Organism-specific databases

    PseudoCAPiPA0999.

    Phylogenomic databases

    eggNOGiENOG4105CCZ. Bacteria.
    COG0332. LUCA.
    HOGENOMiHOG000246674.
    InParanoidiP20582.
    KOiK18003.
    OMAiDIRQQCT.
    PhylomeDBiP20582.

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-16011.
    BRENDAi2.3.1.230. 5087.

    Miscellaneous databases

    EvolutionaryTraceiP20582.

    Family and domain databases

    Gene3Di3.40.47.10. 2 hits.
    InterProiIPR013751. ACP_syn_III.
    IPR013747. ACP_syn_III_C.
    IPR016039. Thiolase-like.
    [Graphical view]
    PfamiPF08545. ACP_syn_III. 1 hit.
    PF08541. ACP_syn_III_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF53901. SSF53901. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiPQSD_PSEAE
    AccessioniPrimary (citable) accession number: P20582
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: December 8, 2000
    Last modified: September 7, 2016
    This is version 108 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.