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Protein

Shikimate kinase 2

Gene

aroL

Organism
Dickeya chrysanthemi (Pectobacterium chrysanthemi) (Erwinia chrysanthemi)
Status
Reviewed-Annotation score: -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

Caution

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

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. no protein annotated in this organism
    2. no protein annotated in this organism
    3. no protein annotated in this organism
    4. no protein annotated in this organism
    5. Shikimate kinase 2 (aroL)
    6. no protein annotated in this organism
    7. no protein annotated in this organism
    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

    Keywordsi

    Molecular functionKinase, Transferase
    Biological processAmino-acid biosynthesis, Aromatic amino acid biosynthesis
    LigandATP-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

    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

    Proteomic databases

    PRIDEiP10880

    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
    HAMAPiMF_00109 Shikimate_kinase, 1 hit
    MF_01269 Shikimate_kinase_2, 1 hit
    InterProiView protein in InterPro
    IPR027417 P-loop_NTPase
    IPR031322 Shikimate/glucono_kinase
    IPR000623 Shikimate_kinase/TSH1
    IPR027544 Shikimate_kinase_2
    IPR023000 Shikimate_kinase_CS
    PfamiView protein in Pfam
    PF01202 SKI, 1 hit
    SUPFAMiSSF52540 SSF52540, 1 hit
    PROSITEiView protein in PROSITE
    PS01128 SHIKIMATE_KINASE, 1 hit

    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

    Similar proteinsi

    Entry informationi

    Entry nameiAROL_DICCH
    AccessioniPrimary (citable) accession number: P10880
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: July 1, 1989
    Last modified: May 23, 2018
    This is version 107 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure
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    Main funding by: National Institutes of Health