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Protein

Shikimate kinase

Gene

aroK

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
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.2 Publications

Catalytic activityi

ATP + shikimate = ADP + shikimate 3-phosphate.

Cofactori

Mg2+2 PublicationsNote: Binds 1 Mg2+ ion per subunit.2 Publications

Kineticsi

  1. KM=410 µM for shikimate1 Publication
  2. KM=83 µM for ATP1 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 (LH57_11870), Phospho-2-dehydro-3-deoxyheptonate aldolase AroG (aroG)
    2. 3-dehydroquinate synthase (aroB), 3-dehydroquinate synthase (aroB)
    3. 3-dehydroquinate dehydratase (aroQ), 3-dehydroquinate dehydratase (aroQ)
    4. no protein annotated in this organism
    5. Shikimate kinase (aroK), Shikimate kinase (aroK)
    6. 3-phosphoshikimate 1-carboxyvinyltransferase (aroA), 3-phosphoshikimate 1-carboxyvinyltransferase (aroA)
    7. Chorismate synthase (aroC), 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)DescriptionActionsGraphical viewLength
    Metal bindingi16Magnesium1
    Binding sitei34Substrate1
    Binding sitei58Substrate1
    Binding sitei80Substrate; via amide nitrogen1
    Binding sitei117ATP1
    Binding sitei136Substrate1
    Binding sitei153ATP1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi12 – 17ATP6

    GO - Molecular functioni

    • ATP binding Source: MTBBASE
    • magnesium ion binding Source: MTBBASE
    • shikimate kinase activity Source: MTBBASE

    GO - Biological processi

    • aromatic amino acid family biosynthetic process Source: GO_Central
    • cellular amino acid biosynthetic process Source: UniProtKB-KW
    • chorismate biosynthetic process Source: Reactome
    • growth Source: MTBBASE
    • shikimate metabolic process Source: MTBBASE
    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

    BioCyciMTBH37RV:G185E-6778-MONOMER.
    ReactomeiR-MTU-964903. Chorismate via Shikimate Pathway.
    UniPathwayiUPA00053; UER00088.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Shikimate kinase (EC:2.7.1.71)
    Short name:
    SK
    Gene namesi
    Name:aroK
    Ordered Locus Names:Rv2539c
    ORF Names:MTCY159.17
    OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
    Taxonomic identifieri83332 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
    Proteomesi
    • UP000001584 Componenti: Chromosome

    Organism-specific databases

    TubercuListiRv2539c.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001923931 – 176Shikimate kinaseAdd BLAST176

    Proteomic databases

    PaxDbiP9WPY3.

    Interactioni

    Subunit structurei

    Monomer.7 Publications

    Protein-protein interaction databases

    STRINGi83332.Rv2539c.

    Structurei

    Secondary structure

    1176
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi4 – 8Combined sources5
    Helixi15 – 26Combined sources12
    Beta strandi30 – 32Combined sources3
    Helixi33 – 41Combined sources9
    Helixi45 – 52Combined sources8
    Helixi54 – 71Combined sources18
    Beta strandi74 – 77Combined sources4
    Helixi82 – 84Combined sources3
    Helixi86 – 92Combined sources7
    Beta strandi97 – 101Combined sources5
    Helixi104 – 110Combined sources7
    Turni111 – 113Combined sources3
    Helixi118 – 121Combined sources4
    Beta strandi122 – 124Combined sources3
    Helixi125 – 143Combined sources19
    Beta strandi145 – 149Combined sources5
    Beta strandi151 – 153Combined sources3
    Helixi155 – 163Combined sources9
    Helixi173 – 176Combined sources4

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1L4UX-ray1.80A1-176[»]
    1L4YX-ray2.00A1-176[»]
    1U8AX-ray2.15A1-176[»]
    1WE2X-ray2.30A1-176[»]
    1ZYUX-ray2.90A1-176[»]
    2DFNX-ray1.93A1-176[»]
    2DFTX-ray2.80A/B/C/D1-176[»]
    2G1JX-ray2.00A/B1-176[»]
    2G1KX-ray1.75A1-176[»]
    2IYQX-ray1.80A1-176[»]
    2IYRX-ray1.98A/B1-176[»]
    2IYSX-ray1.40A1-176[»]
    2IYTX-ray1.47A1-176[»]
    2IYUX-ray1.85A1-176[»]
    2IYVX-ray1.35A1-176[»]
    2IYWX-ray1.85A1-176[»]
    2IYXX-ray1.49A1-176[»]
    2IYYX-ray1.62A1-176[»]
    2IYZX-ray2.30A1-176[»]
    3BAFX-ray2.25A1-176[»]
    4BQSX-ray2.15A/B/C1-176[»]
    ProteinModelPortaliP9WPY3.
    SMRiP9WPY3.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni112 – 124LID domainAdd BLAST13

    Domaini

    Consists of three domains: the CORE domain which forms the binding site for nucleotides, the LID domain which closes over the active site upon ATP or shikimate binding, and the substrate-binding domain which functions to recognize and bind shikimate.

    Sequence similaritiesi

    Belongs to the shikimate kinase family.Curated

    Phylogenomic databases

    eggNOGiENOG4105KHV. Bacteria.
    COG0703. LUCA.
    KOiK00891.
    OMAiLYRECAD.
    PhylomeDBiP9WPY3.

    Family and domain databases

    CDDicd00464. SK. 1 hit.
    Gene3Di3.40.50.300. 1 hit.
    HAMAPiMF_00109. Shikimate_kinase. 1 hit.
    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.

    P9WPY3-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MAPKAVLVGL PGSGKSTIGR RLAKALGVGL LDTDVAIEQR TGRSIADIFA
    60 70 80 90 100
    TDGEQEFRRI EEDVVRAALA DHDGVLSLGG GAVTSPGVRA ALAGHTVVYL
    110 120 130 140 150
    EISAAEGVRR TGGNTVRPLL AGPDRAEKYR ALMAKRAPLY RRVATMRVDT
    160 170
    NRRNPGAVVR HILSRLQVPS PSEAAT
    Length:176
    Mass (Da):18,583
    Last modified:April 16, 2014 - v1
    Checksum:i208EE0C38F5186A1
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AL123456 Genomic DNA. Translation: CCP45334.1.
    PIRiG70658.
    RefSeqiNP_217055.1. NC_000962.3.
    WP_003413021.1. NZ_KK339370.1.

    Genome annotation databases

    EnsemblBacteriaiCCP45334; CCP45334; Rv2539c.
    GeneIDi887434.
    KEGGimtu:Rv2539c.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AL123456 Genomic DNA. Translation: CCP45334.1.
    PIRiG70658.
    RefSeqiNP_217055.1. NC_000962.3.
    WP_003413021.1. NZ_KK339370.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1L4UX-ray1.80A1-176[»]
    1L4YX-ray2.00A1-176[»]
    1U8AX-ray2.15A1-176[»]
    1WE2X-ray2.30A1-176[»]
    1ZYUX-ray2.90A1-176[»]
    2DFNX-ray1.93A1-176[»]
    2DFTX-ray2.80A/B/C/D1-176[»]
    2G1JX-ray2.00A/B1-176[»]
    2G1KX-ray1.75A1-176[»]
    2IYQX-ray1.80A1-176[»]
    2IYRX-ray1.98A/B1-176[»]
    2IYSX-ray1.40A1-176[»]
    2IYTX-ray1.47A1-176[»]
    2IYUX-ray1.85A1-176[»]
    2IYVX-ray1.35A1-176[»]
    2IYWX-ray1.85A1-176[»]
    2IYXX-ray1.49A1-176[»]
    2IYYX-ray1.62A1-176[»]
    2IYZX-ray2.30A1-176[»]
    3BAFX-ray2.25A1-176[»]
    4BQSX-ray2.15A/B/C1-176[»]
    ProteinModelPortaliP9WPY3.
    SMRiP9WPY3.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi83332.Rv2539c.

    Proteomic databases

    PaxDbiP9WPY3.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiCCP45334; CCP45334; Rv2539c.
    GeneIDi887434.
    KEGGimtu:Rv2539c.

    Organism-specific databases

    TubercuListiRv2539c.

    Phylogenomic databases

    eggNOGiENOG4105KHV. Bacteria.
    COG0703. LUCA.
    KOiK00891.
    OMAiLYRECAD.
    PhylomeDBiP9WPY3.

    Enzyme and pathway databases

    UniPathwayiUPA00053; UER00088.
    BioCyciMTBH37RV:G185E-6778-MONOMER.
    ReactomeiR-MTU-964903. Chorismate via Shikimate Pathway.

    Family and domain databases

    CDDicd00464. SK. 1 hit.
    Gene3Di3.40.50.300. 1 hit.
    HAMAPiMF_00109. Shikimate_kinase. 1 hit.
    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...

    Entry informationi

    Entry nameiAROK_MYCTU
    AccessioniPrimary (citable) accession number: P9WPY3
    Secondary accession number(s): L0TBI1, P0A4Z2, P95014
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 16, 2014
    Last sequence update: April 16, 2014
    Last modified: November 2, 2016
    This is version 23 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The phosphoryl transfer proceeds by an in-line associative mechanism. The random sequential binding of shikimate and nucleotide is associated with domain movements that suggest a synergic mechanism by which binding of the first substrate may enhance the affinity for the second substrate.
    Was identified as a high-confidence drug target.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
      Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names
    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.