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Protein

Shikimate kinase 2

Gene

aroL

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.2 Publications

Catalytic activityi

ATP + shikimate = ADP + shikimate 3-phosphate.

Cofactori

Mg2+1 PublicationNote: Binds 1 Mg2+ ion per subunit.1 Publication

Kineticsi

  1. KM=200 µM for shikimate1 Publication
  2. KM=160 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, 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 bindingi16 – 161MagnesiumBy similarity
    Metal bindingi32 – 321MagnesiumBy similarity
    Binding sitei34 – 341SubstrateBy similarity
    Binding sitei58 – 581SubstrateBy similarity
    Binding sitei79 – 791Substrate; via amide nitrogenBy similarity
    Binding sitei120 – 1201ATPBy similarity
    Binding sitei139 – 1391SubstrateBy similarity

    Regions

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

    GO - Molecular functioni

    • ATP binding Source: UniProtKB-HAMAP
    • magnesium ion binding Source: EcoCyc
    • metal ion binding Source: EcoCyc
    • shikimate kinase activity Source: EcoCyc

    GO - Biological processi

    • aromatic amino acid family biosynthetic process Source: EcoliWiki
    • chorismate biosynthetic process Source: UniProtKB-UniPathway
    • shikimate metabolic process Source: GO_Central
    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:AROL-MONOMER.
    ECOL316407:JW0379-MONOMER.
    MetaCyc:AROL-MONOMER.
    SABIO-RKP0A6E1.
    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
    Ordered Locus Names:b0388, JW0379
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG10082. aroL.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methionineiRemoved2 Publications
    Chaini2 – 174173Shikimate kinase 2PRO_0000192378Add
    BLAST

    Proteomic databases

    PaxDbiP0A6E1.
    PRIDEiP0A6E1.

    Expressioni

    Inductioni

    Expressed under the control of TyrR and TrpR repressors.3 Publications

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Protein-protein interaction databases

    BioGridi4259831. 2 interactions.
    IntActiP0A6E1. 3 interactions.
    STRINGi511145.b0388.

    Structurei

    3D structure databases

    ProteinModelPortaliP0A6E1.
    SMRiP0A6E1. Positions 1-168.
    ModBaseiSearch...
    MobiDBiSearch...

    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.By similarity

    Sequence similaritiesi

    Belongs to the shikimate kinase family. AroL subfamily.Curated

    Phylogenomic databases

    eggNOGiENOG4105KHV. Bacteria.
    COG0703. LUCA.
    HOGENOMiHOG000032568.
    InParanoidiP0A6E1.
    KOiK00891.
    OMAiIFLVGPR.
    OrthoDBiEOG6SJJGD.
    PhylomeDBiP0A6E1.

    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.

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

    P0A6E1-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MTQPLFLIGP RGCGKTTVGM ALADSLNRRF VDTDQWLQSQ LNMTVAEIVE
    60 70 80 90 100
    REEWAGFRAR ETAALEAVTA PSTVIATGGG IILTEFNRHF MQNNGIVVYL
    110 120 130 140 150
    CAPVSVLVNR LQAAPEEDLR PTLTGKPLSE EVQEVLEERD ALYREVAHII
    160 170
    IDATNEPSQV ISEIRSALAQ TINC
    Length:174
    Mass (Da):19,151
    Last modified:January 23, 2007 - v3
    Checksum:iFCB8D86F6DD55347
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X04064 Genomic DNA. Translation: CAA27696.1.
    M13045 Genomic DNA. Translation: AAA83833.1.
    U73857 Genomic DNA. Translation: AAB18112.1.
    U00096 Genomic DNA. Translation: AAC73491.1.
    AP009048 Genomic DNA. Translation: BAE76169.1.
    PIRiA90333. KIECS.
    RefSeqiNP_414922.1. NC_000913.3.
    WP_000193393.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC73491; AAC73491; b0388.
    BAE76169; BAE76169; BAE76169.
    GeneIDi945031.
    KEGGiecj:JW0379.
    eco:b0388.
    PATRICi32115917. VBIEscCol129921_0400.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X04064 Genomic DNA. Translation: CAA27696.1.
    M13045 Genomic DNA. Translation: AAA83833.1.
    U73857 Genomic DNA. Translation: AAB18112.1.
    U00096 Genomic DNA. Translation: AAC73491.1.
    AP009048 Genomic DNA. Translation: BAE76169.1.
    PIRiA90333. KIECS.
    RefSeqiNP_414922.1. NC_000913.3.
    WP_000193393.1. NZ_LN832404.1.

    3D structure databases

    ProteinModelPortaliP0A6E1.
    SMRiP0A6E1. Positions 1-168.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4259831. 2 interactions.
    IntActiP0A6E1. 3 interactions.
    STRINGi511145.b0388.

    Proteomic databases

    PaxDbiP0A6E1.
    PRIDEiP0A6E1.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC73491; AAC73491; b0388.
    BAE76169; BAE76169; BAE76169.
    GeneIDi945031.
    KEGGiecj:JW0379.
    eco:b0388.
    PATRICi32115917. VBIEscCol129921_0400.

    Organism-specific databases

    EchoBASEiEB0080.
    EcoGeneiEG10082. aroL.

    Phylogenomic databases

    eggNOGiENOG4105KHV. Bacteria.
    COG0703. LUCA.
    HOGENOMiHOG000032568.
    InParanoidiP0A6E1.
    KOiK00891.
    OMAiIFLVGPR.
    OrthoDBiEOG6SJJGD.
    PhylomeDBiP0A6E1.

    Enzyme and pathway databases

    UniPathwayiUPA00053; UER00088.
    BioCyciEcoCyc:AROL-MONOMER.
    ECOL316407:JW0379-MONOMER.
    MetaCyc:AROL-MONOMER.
    SABIO-RKP0A6E1.

    Miscellaneous databases

    PROiP0A6E1.

    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

    « Hide 'large scale' publications
    1. "The cloning and expression of the aroL gene from Escherichia coli K12. Purification and complete amino acid sequence of shikimate kinase II, the aroL-gene product."
      Millar G., Lewendon A., Hunter M.G., Coggins J.R.
      Biochem. J. 237:427-437(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-25, FUNCTION, SUBUNIT.
      Strain: K12.
    2. "Nucleotide sequence of the transcription unit containing the aroL and aroM genes from Escherichia coli K-12."
      Defeyter R.C., Davidson B.E., Pittard J.
      J. Bacteriol. 165:233-239(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    3. "Sequence of minutes 4-25 of Escherichia coli."
      Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
      Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    5. "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.
    6. "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: PROTEIN SEQUENCE OF 2-9, FUNCTION, COFACTOR, KINETIC PARAMETERS.
      Strain: K12.
    7. "Genetic and molecular analysis of aroL, the gene for shikimate kinase II in Escherichia coli K-12."
      DeFeyter R.C., Pittard J.
      J. Bacteriol. 165:226-232(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
      Strain: K12.
    8. "Synergism between the Trp repressor and Tyr repressor in repression of the aroL promoter of Escherichia coli K-12."
      Heatwole V.M., Somerville R.L.
      J. Bacteriol. 174:331-335(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
      Strain: K12.
    9. "Regulation of aroL expression by TyrR protein and Trp repressor in Escherichia coli K-12."
      Lawley B., Pittard A.J.
      J. Bacteriol. 176:6921-6930(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
      Strain: K12.

    Entry informationi

    Entry nameiAROL_ECOLI
    AccessioniPrimary (citable) accession number: P0A6E1
    Secondary accession number(s): P08329, Q2MC37
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: January 23, 2007
    Last modified: January 20, 2016
    This is version 88 of the entry and version 3 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

    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. 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.