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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 (NM75_10300), Shikimate kinase (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)DescriptionActionsGraphical viewLength
    Metal bindingi16Magnesium1
    Metal bindingi32Magnesium1
    Binding sitei34SubstrateCurated1
    Binding sitei58SubstrateCurated1
    Binding sitei79Substrate; via amide nitrogenBy similarity1
    Binding sitei120ATPBy similarity1
    Binding sitei139SubstrateCurated1
    Binding sitei155ATP1

    Regions

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

    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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesPectobacteriaceaeDickeya

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi13C → S: 66% of wild-type activity. Increase in substrates affinity. 1 Publication1
    Mutagenesisi15K → M: Loss of activity. Increased thermostability. 1 Publication1
    Mutagenesisi34D → N: Loss of activity. 1 Publication1
    Mutagenesisi162C → S: No effect on activity and substrates affinity. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001923831 – 173Shikimate kinase 2Add BLAST173

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Structurei

    Secondary structure

    1173
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi5 – 9Combined sources5
    Helixi15 – 26Combined sources12
    Beta strandi29 – 32Combined sources4
    Helixi33 – 41Combined sources9
    Helixi45 – 68Combined sources24
    Beta strandi71 – 76Combined sources6
    Helixi81 – 83Combined sources3
    Helixi85 – 94Combined sources10
    Beta strandi95 – 101Combined sources7
    Helixi104 – 115Combined sources12
    Helixi125 – 146Combined sources22
    Beta strandi148 – 152Combined sources5
    Helixi157 – 167Combined sources11

    3D structure databases

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

    Miscellaneous databases

    EvolutionaryTraceiP10880.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni112 – 126LID domainAdd BLAST15

    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

    CDDicd00464. SK. 1 hit.
    Gene3Di3.40.50.300. 1 hit.
    HAMAPiMF_00109. Shikimate_kinase. 1 hit.
    MF_01269. Shikimate_kinase_2. 1 hit.
    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
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1E6CX-ray1.80A/B1-173[»]
    1SHKX-ray1.90A/B1-173[»]
    2SHKX-ray2.60A/B1-173[»]
    ProteinModelPortaliP10880.
    SMRiP10880.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Enzyme and pathway databases

    UniPathwayiUPA00053; UER00088.
    SABIO-RKP10880.

    Miscellaneous databases

    EvolutionaryTraceiP10880.

    Family and domain databases

    CDDicd00464. SK. 1 hit.
    Gene3Di3.40.50.300. 1 hit.
    HAMAPiMF_00109. Shikimate_kinase. 1 hit.
    MF_01269. Shikimate_kinase_2. 1 hit.
    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...

    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: November 2, 2016
    This is version 101 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.