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Protein

Shikimate kinase 1

Gene

aroK

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.1 Publication

Catalytic activityi

ATP + shikimate = ADP + shikimate 3-phosphate.

Cofactori

Mg2+CuratedNote: Binds 1 Mg2+ ion per subunit.Curated

Kineticsi

  1. KM=20 mM for shikimate1 Publication

    Pathwayi: chorismate biosynthesis

    This protein is involved in step 5 of the subpathway that synthesizes chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate.
    Proteins known to be involved in the 7 steps of the subpathway in this organism are:
    1. Phospho-2-dehydro-3-deoxyheptonate aldolase, Tyr-sensitive (aroF), Phospho-2-dehydro-3-deoxyheptonate aldolase, Trp-sensitive (aroH), Phospho-2-dehydro-3-deoxyheptonate aldolase, Phe-sensitive (aroG)
    2. 3-dehydroquinate synthase (aroB)
    3. 3-dehydroquinate dehydratase (aroD)
    4. Quinate/shikimate dehydrogenase (ydiB), Shikimate dehydrogenase (NADP(+)) (aroE)
    5. Shikimate kinase 2 (aroL), Shikimate kinase 1 (aroK)
    6. 3-phosphoshikimate 1-carboxyvinyltransferase (aroA)
    7. Chorismate synthase (aroC)
    This subpathway is part of the pathway chorismate biosynthesis, which is itself part of Metabolic intermediate biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate, the pathway chorismate biosynthesis and in Metabolic intermediate biosynthesis.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi18 – 181MagnesiumBy similarity
    Binding sitei36 – 361SubstrateBy similarity
    Binding sitei60 – 601SubstrateBy similarity
    Binding sitei82 – 821Substrate; via amide nitrogenBy similarity
    Binding sitei120 – 1201ATPBy similarity
    Binding sitei140 – 1401SubstrateBy similarity
    Binding sitei157 – 1571ATPBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi14 – 196ATPBy similarity

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Biological processi

    Amino-acid biosynthesis, Aromatic amino acid biosynthesis

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:AROK-MONOMER.
    ECOL316407:JW5947-MONOMER.
    UniPathwayiUPA00053; UER00088.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Shikimate kinase 1 (EC:2.7.1.71)
    Short name:
    SK 1
    Alternative name(s):
    Shikimate kinase I
    Short name:
    SKI
    Gene namesi
    Name:aroK
    Ordered Locus Names:b3390, JW5947
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG10081. aroK.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: EcoCyc
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methionineiRemoved2 Publications
    Chaini2 – 173172Shikimate kinase 1PRO_0000192377Add
    BLAST

    Proteomic databases

    EPDiP0A6D7.
    PaxDbiP0A6D7.
    PRIDEiP0A6D7.

    2D gel databases

    SWISS-2DPAGEP0A6D7.

    Expressioni

    Inductioni

    Constitutively expressed.

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Protein-protein interaction databases

    BioGridi4259297. 192 interactions.
    DIPiDIP-48271N.
    IntActiP0A6D7. 1 interaction.
    MINTiMINT-1299909.
    STRINGi511145.b3390.

    Structurei

    Secondary structure

    1
    173
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi7 – 104Combined sources
    Helixi17 – 2711Combined sources
    Beta strandi31 – 344Combined sources
    Helixi35 – 439Combined sources
    Helixi47 – 7125Combined sources
    Beta strandi73 – 797Combined sources
    Helixi84 – 863Combined sources
    Helixi88 – 9710Combined sources
    Beta strandi98 – 1036Combined sources
    Helixi107 – 1115Combined sources
    Beta strandi123 – 1264Combined sources
    Helixi130 – 14718Combined sources
    Beta strandi149 – 1524Combined sources
    Helixi159 – 17012Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1KAGX-ray2.05A/B1-173[»]
    ProteinModelPortaliP0A6D7.
    SMRiP0A6D7. Positions 3-171.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A6D7.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni116 – 12712Lid domainAdd
    BLAST

    Domaini

    The LID domain closes over the active site upon ATP binding.

    Sequence similaritiesi

    Belongs to the shikimate kinase family.Curated

    Phylogenomic databases

    eggNOGiENOG4105KHV. Bacteria.
    COG0703. LUCA.
    HOGENOMiHOG000032568.
    InParanoidiP0A6D7.
    KOiK00891.
    OMAiFEQHGEA.
    OrthoDBiEOG6SJJGD.
    PhylomeDBiP0A6D7.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    HAMAPiMF_00109. Shikimate_kinase.
    InterProiIPR027417. P-loop_NTPase.
    IPR031322. Shikimate/glucono_kinase.
    IPR000623. Shikimate_kinase/TSH1.
    IPR023000. Shikimate_kinase_CS.
    [Graphical view]
    PfamiPF01202. SKI. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    PROSITEiPS01128. SHIKIMATE_KINASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P0A6D7-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MAEKRNIFLV GPMGAGKSTI GRQLAQQLNM EFYDSDQEIE KRTGADVGWV
    60 70 80 90 100
    FDLEGEEGFR DREEKVINEL TEKQGIVLAT GGGSVKSRET RNRLSARGVV
    110 120 130 140 150
    VYLETTIEKQ LARTQRDKKR PLLHVETPPR EVLEALANER NPLYEEIADV
    160 170
    TIRTDDQSAK VVANQIIHML ESN
    Length:173
    Mass (Da):19,538
    Last modified:January 23, 2007 - v2
    Checksum:i5681B562B5CD4674
    GO

    Sequence cautioni

    The sequence AAA58187.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
    The sequence AAC36834.1 differs from that shown. Reason: Frameshift at position 98. Curated
    The sequence CAA79665.1 differs from that shown. Reason: Frameshift at position 98. Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M76389 Unassigned DNA. Translation: AAC36834.1. Frameshift.
    X80167 Genomic DNA. Translation: CAA56448.1.
    L39822 Genomic DNA. Translation: AAB59099.1.
    Z19601 Genomic DNA. Translation: CAA79665.1. Frameshift.
    U18997 Genomic DNA. Translation: AAA58187.1. Different initiation.
    U00096 Genomic DNA. Translation: AAC76415.2.
    AP009048 Genomic DNA. Translation: BAE77901.1.
    PIRiA65134.
    RefSeqiWP_000818618.1. NZ_LN832404.1.
    YP_026215.2. NC_000913.3.

    Genome annotation databases

    EnsemblBacteriaiAAC76415; AAC76415; b3390.
    BAE77901; BAE77901; BAE77901.
    GeneIDi2847759.
    KEGGiecj:JW5947.
    eco:b3390.
    PATRICi32122212. VBIEscCol129921_3483.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M76389 Unassigned DNA. Translation: AAC36834.1. Frameshift.
    X80167 Genomic DNA. Translation: CAA56448.1.
    L39822 Genomic DNA. Translation: AAB59099.1.
    Z19601 Genomic DNA. Translation: CAA79665.1. Frameshift.
    U18997 Genomic DNA. Translation: AAA58187.1. Different initiation.
    U00096 Genomic DNA. Translation: AAC76415.2.
    AP009048 Genomic DNA. Translation: BAE77901.1.
    PIRiA65134.
    RefSeqiWP_000818618.1. NZ_LN832404.1.
    YP_026215.2. NC_000913.3.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1KAGX-ray2.05A/B1-173[»]
    ProteinModelPortaliP0A6D7.
    SMRiP0A6D7. Positions 3-171.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4259297. 192 interactions.
    DIPiDIP-48271N.
    IntActiP0A6D7. 1 interaction.
    MINTiMINT-1299909.
    STRINGi511145.b3390.

    2D gel databases

    SWISS-2DPAGEP0A6D7.

    Proteomic databases

    EPDiP0A6D7.
    PaxDbiP0A6D7.
    PRIDEiP0A6D7.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC76415; AAC76415; b3390.
    BAE77901; BAE77901; BAE77901.
    GeneIDi2847759.
    KEGGiecj:JW5947.
    eco:b3390.
    PATRICi32122212. VBIEscCol129921_3483.

    Organism-specific databases

    EchoBASEiEB0079.
    EcoGeneiEG10081. aroK.

    Phylogenomic databases

    eggNOGiENOG4105KHV. Bacteria.
    COG0703. LUCA.
    HOGENOMiHOG000032568.
    InParanoidiP0A6D7.
    KOiK00891.
    OMAiFEQHGEA.
    OrthoDBiEOG6SJJGD.
    PhylomeDBiP0A6D7.

    Enzyme and pathway databases

    UniPathwayiUPA00053; UER00088.
    BioCyciEcoCyc:AROK-MONOMER.
    ECOL316407:JW5947-MONOMER.

    Miscellaneous databases

    EvolutionaryTraceiP0A6D7.
    PROiP0A6D7.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    HAMAPiMF_00109. Shikimate_kinase.
    InterProiIPR027417. P-loop_NTPase.
    IPR031322. Shikimate/glucono_kinase.
    IPR000623. Shikimate_kinase/TSH1.
    IPR023000. Shikimate_kinase_CS.
    [Graphical view]
    PfamiPF01202. SKI. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    PROSITEiPS01128. SHIKIMATE_KINASE. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Identification of the gene (aroK) encoding shikimic acid kinase I of Escherichia coli."
      Lobner-Olesen A., Boye E., Marinus M.G.
      J. Bacteriol. 174:525-529(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
      Strain: K12.
    2. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "The gene (aroK) encoding shikimate kinase I from Escherichia coli."
      Griffin H.G., Gasson M.J.
      DNA Seq. 5:195-197(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    4. "A reassessment of the relationship between aroK- and aroL-encoded shikimate kinase enzymes of Escherichia coli."
      Whipp M.J., Pittard A.J.
      J. Bacteriol. 177:1627-1629(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    5. "Characterization of three genes in the dam-containing operon of Escherichia coli."
      Lyngstadaas A., Lobner-Olesen A., Boye E.
      Mol. Gen. Genet. 247:546-554(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    7. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    8. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
      Link A.J., Robison K., Church G.M.
      Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-13.
      Strain: K12 / EMG2.
    9. Cited for: PROTEIN SEQUENCE OF 2-5.
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    10. "Purification and properties of shikimate kinase II from Escherichia coli K-12."
      DeFeyter R.C., Pittard J.
      J. Bacteriol. 165:331-333(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: KINETIC PARAMETERS.
      Strain: K12.
    11. "Crystal structure of the Escherichia coli shikimate kinase I (AroK) that confers sensitivity to mecillinam."
      Romanowski M.J., Burley S.K.
      Proteins 47:558-562(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS), SUBUNIT.

    Entry informationi

    Entry nameiAROK_ECOLI
    AccessioniPrimary (citable) accession number: P0A6D7
    Secondary accession number(s): P24167
    , P78113, Q2M755, Q8X4S0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 7, 2005
    Last sequence update: January 23, 2007
    Last modified: April 13, 2016
    This is version 98 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Two isozymes have been found in E.coli. AroK has 100-fold lower affinity for shikimate than AroL, suggesting that AroL is the dominant enzyme in the biosynthesis of the aromatic amino acids, with AroK playing a secondary role and possibly participating in an as yet unidentified cellular process.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. 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.