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Protein

Type III pantothenate kinase

Gene

coaX

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

Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis. Can utilize a wide range of phosphoryl donors other than ATP, and does not discriminate between purine- and pyrimidine-based nucleotides or deoxynucleotides. Is responsible for the resistance of P.aeruginosa to the pantothenamide antibiotics, since it cannot bind and phosphorylate these pantothenate analogs.1 Publication

Catalytic activityi

ATP + (R)-pantothenate = ADP + (R)-4'-phosphopantothenate.

Cofactori

K+1 Publication, NH4(+)1 PublicationNote: Monovalent cations. Strong preference for ammonium over potassium.1 Publication

Kineticsi

  1. KM=14 µM for pantothenate1 Publication
  2. KM=20 µM for pantothenate (in the presence of ammonium)1 Publication
  3. KM=7.2 mM for ATP1 Publication
  4. KM=3.2 mM for ATP (in the presence of ammonium)1 Publication

    Pathwayi: coenzyme A biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes CoA from (R)-pantothenate.
    Proteins known to be involved in the 5 steps of the subpathway in this organism are:
    1. Type III pantothenate kinase (coaX)
    2. no protein annotated in this organism
    3. no protein annotated in this organism
    4. Phosphopantetheine adenylyltransferase (coaD)
    5. Dephospho-CoA kinase (coaE)
    This subpathway is part of the pathway coenzyme A biosynthesis, which is itself part of Cofactor biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes CoA from (R)-pantothenate, the pathway coenzyme A biosynthesis and in Cofactor biosynthesis.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei92 – 921Substrate
    Active sitei101 – 1011Proton acceptorSequence analysis
    Metal bindingi121 – 1211Monovalent cationSequence analysis
    Binding sitei124 – 1241ATPSequence analysis
    Binding sitei180 – 1801Substrate

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi6 – 138ATPBy similarity

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Biological processi

    Antibiotic resistance, Coenzyme A biosynthesis

    Keywords - Ligandi

    ATP-binding, Metal-binding, Nucleotide-binding, Potassium

    Enzyme and pathway databases

    BRENDAi2.7.1.33. 5087.
    UniPathwayiUPA00241; UER00352.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Type III pantothenate kinase (EC:2.7.1.33)
    Alternative name(s):
    PanK-III
    Pantothenic acid kinase
    Gene namesi
    Name:coaX
    Synonyms:coaA
    Ordered Locus Names:PA4279
    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

    PseudoCAPiPA4279.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi9 – 91N → G: 96-fold reduction in activity. 1 Publication
    Mutagenesisi13 – 131K → A: 7-fold reduction in activity. 1 Publication
    Mutagenesisi101 – 1011D → A: 5-fold reduction in activity. 1 Publication
    Mutagenesisi121 – 1211D → A: Loss of activity. 1 Publication
    Mutagenesisi156 – 1561H → A: No change in activity. 1 Publication
    Mutagenesisi157 – 1571T → A: 2.5-fold reduction in activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 248248Type III pantothenate kinasePRO_0000267575Add
    BLAST

    Proteomic databases

    PaxDbiQ9HWC1.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    STRINGi208964.PA4279.

    Structurei

    Secondary structure

    248
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi1 – 77Combined sources
    Beta strandi12 – 187Combined sources
    Turni19 – 213Combined sources
    Beta strandi22 – 3110Combined sources
    Helixi32 – 4110Combined sources
    Turni42 – 443Combined sources
    Beta strandi47 – 548Combined sources
    Helixi58 – 7114Combined sources
    Beta strandi83 – 853Combined sources
    Beta strandi92 – 943Combined sources
    Helixi95 – 973Combined sources
    Helixi100 – 11314Combined sources
    Beta strandi117 – 13115Combined sources
    Beta strandi135 – 14410Combined sources
    Helixi146 – 15611Combined sources
    Beta strandi157 – 1593Combined sources
    Helixi164 – 1707Combined sources
    Beta strandi177 – 1793Combined sources
    Helixi180 – 20728Combined sources
    Beta strandi212 – 2176Combined sources
    Helixi220 – 2223Combined sources
    Helixi224 – 2263Combined sources
    Helixi236 – 2449Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2F9TX-ray2.20A/B1-248[»]
    2F9WX-ray1.90A/B1-248[»]
    ProteinModelPortaliQ9HWC1.
    SMRiQ9HWC1. Positions 1-248.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9HWC1.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni99 – 1024Substrate binding

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG4108194. Bacteria.
    COG1521. LUCA.
    HOGENOMiHOG000066026.
    InParanoidiQ9HWC1.
    KOiK03525.
    OMAiFIKWRVI.
    PhylomeDBiQ9HWC1.

    Family and domain databases

    HAMAPiMF_01274. Pantothen_kinase_3. 1 hit.
    InterProiIPR004619. Type_III_PanK.
    [Graphical view]
    PfamiPF03309. Pan_kinase. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR00671. baf. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q9HWC1-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MILELDCGNS LIKWRVIEGA ARSVAGGLAE SDDALVEQLT SQQALPVRAC
    60 70 80 90 100
    RLVSVRSEQE TSQLVARLEQ LFPVSALVAS SGKQLAGVRN GYLDYQRLGL
    110 120 130 140 150
    DRWLALVAAH HLAKKACLVI DLGTAVTSDL VAADGVHLGG YICPGMTLMR
    160 170 180 190 200
    SQLRTHTRRI RYDDAEARRA LASLQPGQAT AEAVERGCLL MLRGFVREQY
    210 220 230 240
    AMACELLGPD CEIFLTGGDA ELVRDELAGA RIMPDLVFVG LALACPIE
    Length:248
    Mass (Da):26,758
    Last modified:March 1, 2001 - v1
    Checksum:i609D37480899DA3B
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE004091 Genomic DNA. Translation: AAG07667.1.
    PIRiH83111.
    RefSeqiNP_252969.1. NC_002516.2.
    WP_003093768.1. NZ_ASJY01000706.1.

    Genome annotation databases

    EnsemblBacteriaiAAG07667; AAG07667; PA4279.
    GeneIDi881667.
    KEGGipae:PA4279.
    PATRICi19843257. VBIPseAer58763_4480.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE004091 Genomic DNA. Translation: AAG07667.1.
    PIRiH83111.
    RefSeqiNP_252969.1. NC_002516.2.
    WP_003093768.1. NZ_ASJY01000706.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2F9TX-ray2.20A/B1-248[»]
    2F9WX-ray1.90A/B1-248[»]
    ProteinModelPortaliQ9HWC1.
    SMRiQ9HWC1. Positions 1-248.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi208964.PA4279.

    Proteomic databases

    PaxDbiQ9HWC1.

    Protocols and materials databases

    DNASUi881667.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAG07667; AAG07667; PA4279.
    GeneIDi881667.
    KEGGipae:PA4279.
    PATRICi19843257. VBIPseAer58763_4480.

    Organism-specific databases

    PseudoCAPiPA4279.

    Phylogenomic databases

    eggNOGiENOG4108194. Bacteria.
    COG1521. LUCA.
    HOGENOMiHOG000066026.
    InParanoidiQ9HWC1.
    KOiK03525.
    OMAiFIKWRVI.
    PhylomeDBiQ9HWC1.

    Enzyme and pathway databases

    UniPathwayiUPA00241; UER00352.
    BRENDAi2.7.1.33. 5087.

    Miscellaneous databases

    EvolutionaryTraceiQ9HWC1.

    Family and domain databases

    HAMAPiMF_01274. Pantothen_kinase_3. 1 hit.
    InterProiIPR004619. Type_III_PanK.
    [Graphical view]
    PfamiPF03309. Pan_kinase. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR00671. baf. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiCOAX_PSEAE
    AccessioniPrimary (citable) accession number: Q9HWC1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 12, 2006
    Last sequence update: March 1, 2001
    Last modified: September 7, 2016
    This is version 91 of the entry and version 1 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. 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.