Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Shikimate kinase 2

Gene

aroL

Organism
Dickeya chrysanthemi (Pectobacterium chrysanthemi) (Erwinia chrysanthemi)
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+1 PublicationNote: Binds 1 Mg2+ ion per subunit.1 Publication

Enzyme regulationi

Inhibited by chloride and sulfate ions.1 Publication

Kineticsi

  1. KM=310 µM for shikimate1 Publication
  2. KM=620 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 (NM75_08005), Phospho-2-dehydro-3-deoxyheptonate aldolase (NM75_16595), Phospho-2-dehydro-3-deoxyheptonate aldolase (NM75_12555)
    2. 3-dehydroquinate synthase (aroB)
    3. 3-dehydroquinate dehydratase (aroQ)
    4. Shikimate dehydrogenase (NADP(+)) (aroE)
    5. Shikimate kinase 2 (aroL), Shikimate kinase 1 (aroK), Shikimate kinase 2 (aroL)
    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 bindingi16 – 161Magnesium
    Metal bindingi32 – 321Magnesium
    Binding sitei34 – 341SubstrateCurated
    Binding sitei58 – 581SubstrateCurated
    Binding sitei79 – 791Substrate; via amide nitrogenBy similarity
    Binding sitei120 – 1201ATPBy similarity
    Binding sitei139 – 1391SubstrateCurated
    Binding sitei155 – 1551ATP

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi12 – 176ATP

    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

    SABIO-RKP10880.
    UniPathwayiUPA00053; UER00088.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Shikimate kinase 2 (EC:2.7.1.71)
    Short name:
    SK 2
    Alternative name(s):
    Shikimate kinase II
    Short name:
    SKII
    Gene namesi
    Name:aroL
    Synonyms:aroM
    OrganismiDickeya chrysanthemi (Pectobacterium chrysanthemi) (Erwinia chrysanthemi)
    Taxonomic identifieri556 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeDickeya

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi13 – 131C → S: 66% of wild-type activity. Increase in substrates affinity. 1 Publication
    Mutagenesisi15 – 151K → M: Loss of activity. Increased thermostability. 1 Publication
    Mutagenesisi34 – 341D → N: Loss of activity. 1 Publication
    Mutagenesisi162 – 1621C → S: No effect on activity and substrates affinity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 173173Shikimate kinase 2PRO_0000192383Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Structurei

    Secondary structure

    1
    173
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 95Combined sources
    Helixi15 – 2612Combined sources
    Beta strandi29 – 324Combined sources
    Helixi33 – 419Combined sources
    Helixi45 – 6824Combined sources
    Beta strandi71 – 766Combined sources
    Helixi81 – 833Combined sources
    Helixi85 – 9410Combined sources
    Beta strandi95 – 1017Combined sources
    Helixi104 – 11512Combined sources
    Helixi125 – 14622Combined sources
    Beta strandi148 – 1525Combined sources
    Helixi157 – 16711Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1E6CX-ray1.80A/B1-173[»]
    1SHKX-ray1.90A/B1-173[»]
    2SHKX-ray2.60A/B1-173[»]
    ProteinModelPortaliP10880.
    SMRiP10880. Positions 1-170.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP10880.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni112 – 12615LID domainAdd
    BLAST

    Domaini

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

    Sequence similaritiesi

    Belongs to the shikimate kinase family. AroL subfamily.Curated

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    HAMAPiMF_00109. Shikimate_kinase.
    MF_01269. Shikimate_kinase_2.
    InterProiIPR027417. P-loop_NTPase.
    IPR031322. Shikimate/glucono_kinase.
    IPR000623. Shikimate_kinase/TSH1.
    IPR027544. Shikimate_kinase_2.
    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.

    P10880-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MTEPIFMVGA RGCGKTTVGR ELARALGYEF VDTDIFMQHT SGMTVADVVA
    60 70 80 90 100
    AEGWPGFRRR ESEALQAVAT PNRVVATGGG MVLLEQNRQF MRAHGTVVYL
    110 120 130 140 150
    FAPAEELALR LQASPQAHQR PTLTGRPIAE EMEAVLRERE ALYQDVAHYV
    160 170
    VDATQPPAAI VCELMQTMRL PAA
    Length:173
    Mass (Da):18,956
    Last modified:July 1, 1989 - v1
    Checksum:iAE28692D0B25B577
    GO

    Mass spectrometryi

    Molecular mass is 18955 Da from positions 1 - 173. Determined by ESI. 1 Publication
    Molecular mass is 18824 Da from positions 2 - 173. Determined by ESI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X14777 Genomic DNA. Translation: CAA32883.1.
    PIRiS09613.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X14777 Genomic DNA. Translation: CAA32883.1.
    PIRiS09613.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1E6CX-ray1.80A/B1-173[»]
    1SHKX-ray1.90A/B1-173[»]
    2SHKX-ray2.60A/B1-173[»]
    ProteinModelPortaliP10880.
    SMRiP10880. Positions 1-170.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Enzyme and pathway databases

    UniPathwayiUPA00053; UER00088.
    SABIO-RKP10880.

    Miscellaneous databases

    EvolutionaryTraceiP10880.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    HAMAPiMF_00109. Shikimate_kinase.
    MF_01269. Shikimate_kinase_2.
    InterProiIPR027417. P-loop_NTPase.
    IPR031322. Shikimate/glucono_kinase.
    IPR000623. Shikimate_kinase/TSH1.
    IPR027544. Shikimate_kinase_2.
    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

    1. "Nucleotide sequence of an Erwinia chrysanthemi gene encoding shikimate kinase."
      Minton N.P., Whitehead P.J., Atkinson T., Gilbert H.J.
      Nucleic Acids Res. 17:1769-1769(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Crystallization and preliminary X-ray crystallographic analysis of shikimate kinase from Erwinia chrysanthemi."
      Krell T., Coyle J.E., Horsburgh M.J., Coggins J.R., Lapthorn A.J.
      Acta Crystallogr. D 53:612-614(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: CRYSTALLIZATION, MASS SPECTROMETRY, SUBUNIT.
    3. "Effects of salts on the function and conformational stability of shikimate kinase."
      Cerasoli E., Kelly S.M., Coggins J.R., Lapthorn A.J., Clarke D.T., Price N.C.
      Biochim. Biophys. Acta 1648:43-54(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION, EFFECTS OF SALTS.
    4. "The three-dimensional structure of shikimate kinase."
      Krell T., Coggins J.R., Lapthorn A.J.
      J. Mol. Biol. 278:983-997(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF NATIVE PROTEIN AND COMPLEX WITH MG-ADP, COFACTOR.
      Strain: NCPPB 1066.
    5. "Biochemical and X-ray crystallographic studies on shikimate kinase: the important structural role of the P-loop lysine."
      Krell T., Maclean J., Boam D.J., Cooper A., Resmini M., Brocklehurst K., Kelly S.M., Price N.C., Lapthorn A.J., Coggins J.R.
      Protein Sci. 10:1137-1149(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANT MET-15, FUNCTION, KINETIC PARAMETERS, MUTAGENESIS OF CYS-13; LYS-15; ASP-34 AND CYS-162.

    Entry informationi

    Entry nameiAROL_DICCH
    AccessioniPrimary (citable) accession number: P10880
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: July 1, 1989
    Last modified: October 14, 2015
    This is version 98 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Caution

    It is uncertain whether the initial Met is cleaved or not.Curated

    Keywords - Technical termi

    3D-structure

    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.