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Q8L7R2 (KHSE_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Homoserine kinase

EC=2.7.1.39
Alternative name(s):
Protein DOWNY MILDEW RESISTANT 1
Gene names
Name:HSK
Synonyms:DMR1
Ordered Locus Names:At2g17265
ORF Names:F5J6.24
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length370 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.6 Ref.7 Ref.8

Catalytic activity

ATP + L-homoserine = ADP + O-phospho-L-homoserine. HAMAP-Rule MF_00384

Pathway

Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 4/5. HAMAP-Rule MF_00384

Subcellular location

Plastidchloroplast stroma Potential HAMAP-Rule MF_00384.

Disruption phenotype

No visible phenotype under normal growth conditions, but mutant plant accumulate homoserine and show reduced susceptibility to the downy mildew pathogen Hyaloperonospora parasitica. Ref.6 Ref.7 Ref.8

Sequence similarities

Belongs to the GHMP kinase family. Homoserine kinase subfamily.

Biophysicochemical properties

Kinetic parameters:

KM=0.40 mM for L-homoserine Ref.1

KM=0.32 mM for ATP

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3434Chloroplast Potential
Chain35 – 370336Homoserine kinase HAMAP-Rule MF_00384
PRO_0000428662

Regions

Nucleotide binding143 – 15412ATP Potential
Compositional bias153 – 16210Poly-Ala HAMAP-Rule MF_00384

Experimental info

Mutagenesis461E → K in dmr1-2; loss of function. Ref.8
Mutagenesis1181G → R in dmr1-6; loss of function. Ref.8
Mutagenesis1801G → D in dmr1-5; loss of function. Ref.8
Mutagenesis2021G → R in dmr1-4; loss of function. Ref.8
Mutagenesis2411M → K in dmr1-3; loss of function. Ref.8
Mutagenesis2671A → V in dmr1-1; loss of function. Ref.8
Sequence conflict321V → F in BAC42512. Ref.4
Sequence conflict2181R → K in AAD33097. Ref.1
Sequence conflict2331D → E in AAD33097. Ref.1
Sequence conflict3591N → K in AAD33097. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q8L7R2 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 50FB7315AF061889

FASTA37038,529
        10         20         30         40         50         60 
MASLCFQSPS KPISYFQPKS NPSPPLFAKV SVFRCRASVQ TLVAVEPEPV FVSVKTFAPA 

        70         80         90        100        110        120 
TVANLGPGFD FLGCAVDGLG DHVTLRVDPS VRAGEVSISE ITGTTTKLST NPLRNCAGIA 

       130        140        150        160        170        180 
AIATMKMLGI RSVGLSLDLH KGLPLGSGLG SSAASAAAAA VAVNEIFGRK LGSDQLVLAG 

       190        200        210        220        230        240 
LESEAKVSGY HADNIAPAIM GGFVLIRNYE PLDLKPLRFP SDKDLFFVLV SPDFEAPTKK 

       250        260        270        280        290        300 
MRAALPTEIP MVHHVWNSSQ AAALVAAVLE GDAVMLGKAL SSDKIVEPTR APLIPGMEAV 

       310        320        330        340        350        360 
KKAALEAGAF GCTISGAGPT AVAVIDSEEK GQVIGEKMVE AFWKVGHLKS VASVKKLDNV 

       370 
GARLVNSVSR 

« Hide

References

« Hide 'large scale' references
[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]"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana."
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. expand/collapse author list , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.
Nature 402:761-768(1999) [PubMed] [Europe PMC] [Abstract]
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]"Functional annotation of a full-length Arabidopsis cDNA collection."
Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T., Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K., Shinagawa A., Shinozaki K.
Science 296:141-145(2002) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"Downy mildew resistance in Arabidopsis by mutation of HOMOSERINE KINASE."
van Damme M., Zeilmaker T., Elberse J., Andel A., de Sain-van der Velden M., van den Ackerveken G.
Plant Cell 21:2179-2189(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF GLU-46; GLY-118; GLY-180; GLY-202; MET-241 AND ALA-267.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_179318.1. NM_127281.1.
UniGeneAt.10492.
At.26823.

3D structure databases

SMRQ8L7R2. Positions 52-328.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING3702.AT2G17265.1-P.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT2G17265.1; AT2G17265.1; AT2G17265.
GeneID816232.
KEGGath:AT2G17265.

Organism-specific databases

TAIRAT2G17265.

Phylogenomic databases

InParanoidQ8L7R2.
KOK00872.
OMALHEPYRW.
PhylomeDBQ8L7R2.
ProtClustDBPLN02451.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-1961.
UniPathwayUPA00050; UER00064.

Gene expression databases

GenevestigatorQ8L7R2.

Family and domain databases

Gene3D3.30.230.10. 1 hit.
3.30.70.890. 1 hit.
HAMAPMF_00384. Homoser_kinase.
InterProIPR013750. 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]
PfamPF08544. GHMP_kinases_C. 1 hit.
PF00288. GHMP_kinases_N. 1 hit.
[Graphical view]
PIRSFPIRSF000676. Homoser_kin. 1 hit.
SUPFAMSSF54211. SSF54211. 1 hit.
SSF55060. SSF55060. 1 hit.
TIGRFAMsTIGR00191. thrB. 1 hit.
PROSITEPS00627. GHMP_KINASES_ATP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROQ8L7R2.

Entry information

Entry nameKHSE_ARATH
AccessionPrimary (citable) accession number: Q8L7R2
Secondary accession number(s): Q7FLV1, Q9XEE0
Entry history
Integrated into UniProtKB/Swiss-Prot: April 16, 2014
Last sequence update: October 1, 2002
Last modified: April 16, 2014
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names