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Protein

Homoserine kinase

Gene

HSK

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate. Is specific for L-homoserine and cannot use other substrates such D-serine, L-serine, D-threonine and L-threonine, galactose or D-homoserine in vitro. Required for susceptibility to the downy mildew pathogen Hyaloperonospora parasitica.4 Publications

Catalytic activityi

ATP + L-homoserine = ADP + O-phospho-L-homoserine.

Kineticsi

  1. KM=0.40 mM for L-homoserine1 Publication
  2. KM=0.32 mM for ATP1 Publication

    Pathwayi

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi143 – 15412ATPSequence AnalysisAdd
    BLAST

    GO - Molecular functioni

    • ATP binding Source: UniProtKB-KW
    • homoserine kinase activity Source: TAIR

    GO - Biological processi

    • defense response Source: UniProtKB-KW
    • methionine biosynthetic process Source: TAIR
    • response to bacterium Source: TAIR
    • response to fungus Source: TAIR
    • threonine biosynthetic process Source: TAIR
    Complete GO annotation...

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Biological processi

    Amino-acid biosynthesis, Plant defense, Threonine biosynthesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-1961.
    BRENDAi2.7.1.39. 399.
    UniPathwayiUPA00050; UER00064.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Homoserine kinase (EC:2.7.1.39)
    Alternative name(s):
    Protein DOWNY MILDEW RESISTANT 1
    Gene namesi
    Name:HSK
    Synonyms:DMR1
    Ordered Locus Names:At2g17265
    ORF Names:F5J6.24
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548 Componenti: Chromosome 2

    Organism-specific databases

    TAIRiAT2G17265.

    Subcellular locationi

    GO - Cellular componenti

    • chloroplast Source: TAIR
    • chloroplast stroma Source: TAIR
    Complete GO annotation...

    Keywords - Cellular componenti

    Chloroplast, Plastid

    Pathology & Biotechi

    Disruption phenotypei

    No visible phenotype under normal growth conditions, but mutant plant accumulate homoserine and show reduced susceptibility to the downy mildew pathogen Hyaloperonospora parasitica.3 Publications

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi46 – 461E → K in dmr1-2; loss of function. 1 Publication
    Mutagenesisi118 – 1181G → R in dmr1-6; loss of function. 1 Publication
    Mutagenesisi180 – 1801G → D in dmr1-5; loss of function. 1 Publication
    Mutagenesisi202 – 2021G → R in dmr1-4; loss of function. 1 Publication
    Mutagenesisi241 – 2411M → K in dmr1-3; loss of function. 1 Publication
    Mutagenesisi267 – 2671A → V in dmr1-1; loss of function. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3434ChloroplastSequence AnalysisAdd
    BLAST
    Chaini35 – 370336Homoserine kinasePRO_0000428662Add
    BLAST

    Proteomic databases

    PRIDEiQ8L7R2.
    ProMEXiQ8L7R2.

    Expressioni

    Gene expression databases

    GenevestigatoriQ8L7R2.

    Interactioni

    Protein-protein interaction databases

    STRINGi3702.AT2G17265.1-P.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8L7R2.
    SMRiQ8L7R2. Positions 53-365.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi153 – 16210Poly-Ala

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    HOGENOMiHOG000247197.
    InParanoidiQ8L7R2.
    KOiK00872.
    OMAiGFDDWLW.
    PhylomeDBiQ8L7R2.

    Family and domain databases

    Gene3Di3.30.230.10. 1 hit.
    3.30.70.890. 1 hit.
    HAMAPiMF_00384. Homoser_kinase.
    InterProiIPR013750. GHMP_kinase_C_dom.
    IPR006204. GHMP_kinase_N_dom.
    IPR006203. GHMP_knse_ATP-bd_CS.
    IPR000870. Homoserine_kinase.
    IPR020568. Ribosomal_S5_D2-typ_fold.
    IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
    [Graphical view]
    PfamiPF08544. GHMP_kinases_C. 1 hit.
    PF00288. GHMP_kinases_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000676. Homoser_kin. 1 hit.
    SUPFAMiSSF54211. SSF54211. 1 hit.
    SSF55060. SSF55060. 1 hit.
    TIGRFAMsiTIGR00191. thrB. 1 hit.
    PROSITEiPS00627. GHMP_KINASES_ATP. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q8L7R2-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MASLCFQSPS KPISYFQPKS NPSPPLFAKV SVFRCRASVQ TLVAVEPEPV
    60 70 80 90 100
    FVSVKTFAPA TVANLGPGFD FLGCAVDGLG DHVTLRVDPS VRAGEVSISE
    110 120 130 140 150
    ITGTTTKLST NPLRNCAGIA AIATMKMLGI RSVGLSLDLH KGLPLGSGLG
    160 170 180 190 200
    SSAASAAAAA VAVNEIFGRK LGSDQLVLAG LESEAKVSGY HADNIAPAIM
    210 220 230 240 250
    GGFVLIRNYE PLDLKPLRFP SDKDLFFVLV SPDFEAPTKK MRAALPTEIP
    260 270 280 290 300
    MVHHVWNSSQ AAALVAAVLE GDAVMLGKAL SSDKIVEPTR APLIPGMEAV
    310 320 330 340 350
    KKAALEAGAF GCTISGAGPT AVAVIDSEEK GQVIGEKMVE AFWKVGHLKS
    360 370
    VASVKKLDNV GARLVNSVSR
    Length:370
    Mass (Da):38,529
    Last modified:October 1, 2002 - v1
    Checksum:i50FB7315AF061889
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti32 – 321V → F in BAC42512 (PubMed:11910074).Curated
    Sequence conflicti218 – 2181R → K in AAD33097 (PubMed:10562426).Curated
    Sequence conflicti233 – 2331D → E in AAD33097 (PubMed:10562426).Curated
    Sequence conflicti359 – 3591N → K in AAD33097 (PubMed:10562426).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF082525 mRNA. Translation: AAD33097.1.
    CP002685 Genomic DNA. Translation: AEC06605.1.
    AK117871 mRNA. Translation: BAC42512.2.
    AY128313 mRNA. Translation: AAM91516.1.
    BT001174 mRNA. Translation: AAN65061.1.
    RefSeqiNP_179318.1. NM_127281.1.
    UniGeneiAt.10492.
    At.26823.

    Genome annotation databases

    EnsemblPlantsiAT2G17265.1; AT2G17265.1; AT2G17265.
    GeneIDi816232.
    KEGGiath:AT2G17265.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF082525 mRNA. Translation: AAD33097.1.
    CP002685 Genomic DNA. Translation: AEC06605.1.
    AK117871 mRNA. Translation: BAC42512.2.
    AY128313 mRNA. Translation: AAM91516.1.
    BT001174 mRNA. Translation: AAN65061.1.
    RefSeqiNP_179318.1. NM_127281.1.
    UniGeneiAt.10492.
    At.26823.

    3D structure databases

    ProteinModelPortaliQ8L7R2.
    SMRiQ8L7R2. Positions 53-365.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi3702.AT2G17265.1-P.

    Proteomic databases

    PRIDEiQ8L7R2.
    ProMEXiQ8L7R2.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblPlantsiAT2G17265.1; AT2G17265.1; AT2G17265.
    GeneIDi816232.
    KEGGiath:AT2G17265.

    Organism-specific databases

    TAIRiAT2G17265.

    Phylogenomic databases

    HOGENOMiHOG000247197.
    InParanoidiQ8L7R2.
    KOiK00872.
    OMAiGFDDWLW.
    PhylomeDBiQ8L7R2.

    Enzyme and pathway databases

    UniPathwayiUPA00050; UER00064.
    BioCyciMetaCyc:MONOMER-1961.
    BRENDAi2.7.1.39. 399.

    Miscellaneous databases

    PROiQ8L7R2.

    Gene expression databases

    GenevestigatoriQ8L7R2.

    Family and domain databases

    Gene3Di3.30.230.10. 1 hit.
    3.30.70.890. 1 hit.
    HAMAPiMF_00384. Homoser_kinase.
    InterProiIPR013750. GHMP_kinase_C_dom.
    IPR006204. GHMP_kinase_N_dom.
    IPR006203. GHMP_knse_ATP-bd_CS.
    IPR000870. Homoserine_kinase.
    IPR020568. Ribosomal_S5_D2-typ_fold.
    IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
    [Graphical view]
    PfamiPF08544. GHMP_kinases_C. 1 hit.
    PF00288. GHMP_kinases_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000676. Homoser_kin. 1 hit.
    SUPFAMiSSF54211. SSF54211. 1 hit.
    SSF55060. SSF55060. 1 hit.
    TIGRFAMsiTIGR00191. thrB. 1 hit.
    PROSITEiPS00627. GHMP_KINASES_ATP. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Identification of the gene encoding homoserine kinase from Arabidopsis thaliana and characterization of the recombinant enzyme derived from the gene."
      Lee M., Leustek T.
      Arch. Biochem. Biophys. 372:135-142(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
      Strain: cv. Columbia.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    3. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.
    5. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
      Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
      , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
      Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.
    6. "Identification of arabidopsis loci required for susceptibility to the downy mildew pathogen Hyaloperonospora parasitica."
      Van Damme M., Andel A., Huibers R.P., Panstruga R., Weisbeek P.J., Van den Ackerveken G.
      Mol. Plant Microbe Interact. 18:583-592(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    7. "Methionine and threonine synthesis are limited by homoserine availability and not the activity of homoserine kinase in Arabidopsis thaliana."
      Lee M., Martin M.N., Hudson A.O., Lee J., Muhitch M.J., Leustek T.
      Plant J. 41:685-696(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    8. Cited for: FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF GLU-46; GLY-118; GLY-180; GLY-202; MET-241 AND ALA-267.

    Entry informationi

    Entry nameiKHSE_ARATH
    AccessioniPrimary (citable) accession number: Q8L7R2
    Secondary accession number(s): Q7FLV1, Q9XEE0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 16, 2014
    Last sequence update: October 1, 2002
    Last modified: May 27, 2015
    This is version 110 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    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 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.