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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)DescriptionActionsGraphical viewLength
    Binding sitei29Anthraniloyl-CoA1 Publication1
    Binding sitei33Anthraniloyl-CoA1 Publication1
    Active sitei113Nucleophile2 Publications1
    Binding sitei258Anthraniloyl-CoA1 Publication1

    GO - Molecular functioni

    GO - Biological processi

    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)DescriptionActionsGraphical viewLength
    Mutagenesisi113C → A: Abolishes enzyme activity. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001105191 – 3372-heptyl-4(1H)-quinolone synthase PqsDAdd BLAST337

    Proteomic databases

    PaxDbiP20582.
    PRIDEiP20582.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    STRINGi208964.PA0999.

    Structurei

    Secondary structure

    1337
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi5 – 12Combined sources8
    Beta strandi15 – 19Combined sources5
    Helixi20 – 23Combined sources4
    Turni24 – 26Combined sources3
    Helixi31 – 38Combined sources8
    Beta strandi42 – 45Combined sources4
    Helixi53 – 66Combined sources14
    Helixi71 – 73Combined sources3
    Beta strandi76 – 80Combined sources5
    Beta strandi85 – 89Combined sources5
    Helixi91 – 99Combined sources9
    Beta strandi106 – 110Combined sources5
    Helixi112 – 114Combined sources3
    Helixi115 – 128Combined sources14
    Beta strandi133 – 142Combined sources10
    Helixi144 – 146Combined sources3
    Turni151 – 153Combined sources3
    Helixi154 – 157Combined sources4
    Beta strandi162 – 170Combined sources9
    Beta strandi175 – 186Combined sources12
    Helixi188 – 193Combined sources6
    Beta strandi194 – 196Combined sources3
    Beta strandi203 – 205Combined sources3
    Helixi209 – 213Combined sources5
    Turni214 – 217Combined sources4
    Beta strandi218 – 221Combined sources4
    Helixi223 – 244Combined sources22
    Helixi249 – 251Combined sources3
    Beta strandi253 – 257Combined sources5
    Helixi262 – 272Combined sources11
    Helixi276 – 278Combined sources3
    Helixi283 – 286Combined sources4
    Helixi290 – 292Combined sources3
    Helixi293 – 301Combined sources9
    Helixi302 – 304Combined sources3
    Beta strandi310 – 317Combined sources8
    Turni318 – 320Combined sources3
    Beta strandi321 – 328Combined sources8

    3D structure databases

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

    Miscellaneous databases

    EvolutionaryTraceiP20582.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni154 – 155Anthraniloyl-CoA binding1 Publication2
    Regioni221 – 224Anthraniloyl-CoA binding1 Publication4

    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
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3H76X-ray1.80A/B2-337[»]
    3H77X-ray1.80A/B2-337[»]
    3H78X-ray1.70A/B2-337[»]
    ProteinModelPortaliP20582.
    SMRiP20582.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi208964.PA0999.

    Proteomic databases

    PaxDbiP20582.
    PRIDEiP20582.

    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: November 2, 2016
    This is version 110 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.