KHSE_ARATH
ID KHSE_ARATH Reviewed; 370 AA.
AC Q8L7R2; Q7FLV1; Q9XEE0;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Homoserine kinase {ECO:0000303|PubMed:15703056};
DE EC=2.7.1.39 {ECO:0000305|PubMed:15703056};
DE AltName: Full=Protein DOWNY MILDEW RESISTANT 1;
DE Flags: Precursor;
GN Name=HSK; Synonyms=DMR1; OrderedLocusNames=At2g17265; ORFNames=F5J6.24;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=cv. Columbia;
RX PubMed=10562426; DOI=10.1006/abbi.1999.1481;
RA Lee M., Leustek T.;
RT "Identification of the gene encoding homoserine kinase from Arabidopsis
RT thaliana and characterization of the recombinant enzyme derived from the
RT gene.";
RL Arch. Biochem. Biophys. 372:135-142(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15986928; DOI=10.1094/mpmi-18-0583;
RA Van Damme M., Andel A., Huibers R.P., Panstruga R., Weisbeek P.J.,
RA Van den Ackerveken G.;
RT "Identification of arabidopsis loci required for susceptibility to the
RT downy mildew pathogen Hyaloperonospora parasitica.";
RL Mol. Plant Microbe Interact. 18:583-592(2005).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=15703056; DOI=10.1111/j.1365-313x.2004.02329.x;
RA Lee M., Martin M.N., Hudson A.O., Lee J., Muhitch M.J., Leustek T.;
RT "Methionine and threonine synthesis are limited by homoserine availability
RT and not the activity of homoserine kinase in Arabidopsis thaliana.";
RL Plant J. 41:685-696(2005).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLU-46; GLY-118;
RP GLY-180; GLY-202; MET-241 AND ALA-267.
RX PubMed=19622802; DOI=10.1105/tpc.109.066811;
RA van Damme M., Zeilmaker T., Elberse J., Andel A.,
RA de Sain-van der Velden M., van den Ackerveken G.;
RT "Downy mildew resistance in Arabidopsis by mutation of HOMOSERINE KINASE.";
RL Plant Cell 21:2179-2189(2009).
CC -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of L-homoserine
CC to L-homoserine phosphate (PubMed:15703056). Is specific for L-
CC homoserine and cannot use other substrates such D-serine, L-serine, D-
CC threonine and L-threonine, galactose or D-homoserine in vitro. Required
CC for susceptibility to the downy mildew pathogen Hyaloperonospora
CC parasitica. {ECO:0000269|PubMed:10562426, ECO:0000269|PubMed:15703056,
CC ECO:0000269|PubMed:15986928, ECO:0000269|PubMed:19622802,
CC ECO:0000305|PubMed:15703056}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-homoserine = ADP + H(+) + O-phospho-L-homoserine;
CC Xref=Rhea:RHEA:13985, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57476, ChEBI:CHEBI:57590, ChEBI:CHEBI:456216;
CC EC=2.7.1.39; Evidence={ECO:0000305|PubMed:15703056};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13986;
CC Evidence={ECO:0000305|PubMed:15703056};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.40 mM for L-homoserine {ECO:0000269|PubMed:10562426};
CC KM=0.32 mM for ATP {ECO:0000269|PubMed:10562426};
CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC from L-aspartate: step 4/5.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plant accumulate homoserine and show reduced
CC susceptibility to the downy mildew pathogen Hyaloperonospora
CC parasitica. {ECO:0000269|PubMed:15703056, ECO:0000269|PubMed:15986928,
CC ECO:0000269|PubMed:19622802}.
CC -!- SIMILARITY: Belongs to the GHMP kinase family. Homoserine kinase
CC subfamily. {ECO:0000305}.
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DR EMBL; AF082525; AAD33097.1; -; mRNA.
DR EMBL; CP002685; AEC06605.1; -; Genomic_DNA.
DR EMBL; AK117871; BAC42512.2; -; mRNA.
DR EMBL; AY128313; AAM91516.1; -; mRNA.
DR EMBL; BT001174; AAN65061.1; -; mRNA.
DR RefSeq; NP_179318.1; NM_127281.2.
DR AlphaFoldDB; Q8L7R2; -.
DR SMR; Q8L7R2; -.
DR STRING; 3702.AT2G17265.1; -.
DR PaxDb; Q8L7R2; -.
DR PRIDE; Q8L7R2; -.
DR ProMEX; Q8L7R2; -.
DR ProteomicsDB; 250688; -.
DR EnsemblPlants; AT2G17265.1; AT2G17265.1; AT2G17265.
DR GeneID; 816232; -.
DR Gramene; AT2G17265.1; AT2G17265.1; AT2G17265.
DR KEGG; ath:AT2G17265; -.
DR Araport; AT2G17265; -.
DR TAIR; locus:2827533; AT2G17265.
DR eggNOG; KOG1537; Eukaryota.
DR HOGENOM; CLU_041243_1_0_1; -.
DR InParanoid; Q8L7R2; -.
DR OMA; CANRIPH; -.
DR OrthoDB; 793380at2759; -.
DR PhylomeDB; Q8L7R2; -.
DR BioCyc; MetaCyc:MON-1961; -.
DR BRENDA; 2.7.1.39; 399.
DR SABIO-RK; Q8L7R2; -.
DR UniPathway; UPA00050; UER00064.
DR PRO; PR:Q8L7R2; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8L7R2; baseline and differential.
DR Genevisible; Q8L7R2; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004413; F:homoserine kinase activity; IDA:TAIR.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0009086; P:methionine biosynthetic process; TAS:TAIR.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0048573; P:photoperiodism, flowering; IMP:TAIR.
DR GO; GO:0009617; P:response to bacterium; IGI:TAIR.
DR GO; GO:0009620; P:response to fungus; IGI:TAIR.
DR GO; GO:0009088; P:threonine biosynthetic process; TAS:TAIR.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.70.890; -; 1.
DR HAMAP; MF_00384; Homoser_kinase; 1.
DR InterPro; IPR013750; GHMP_kinase_C_dom.
DR InterPro; IPR036554; GHMP_kinase_C_sf.
DR InterPro; IPR006204; GHMP_kinase_N_dom.
DR InterPro; IPR006203; GHMP_knse_ATP-bd_CS.
DR InterPro; IPR000870; Homoserine_kinase.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR Pfam; PF08544; GHMP_kinases_C; 1.
DR Pfam; PF00288; GHMP_kinases_N; 1.
DR PIRSF; PIRSF000676; Homoser_kin; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55060; SSF55060; 1.
DR TIGRFAMs; TIGR00191; thrB; 1.
DR PROSITE; PS00627; GHMP_KINASES_ATP; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; ATP-binding; Chloroplast; Kinase;
KW Nucleotide-binding; Plant defense; Plastid; Reference proteome;
KW Threonine biosynthesis; Transferase; Transit peptide.
FT TRANSIT 1..34
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 35..370
FT /note="Homoserine kinase"
FT /id="PRO_0000428662"
FT BINDING 143..154
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MUTAGEN 46
FT /note="E->K: In dmr1-2; loss of function."
FT /evidence="ECO:0000269|PubMed:19622802"
FT MUTAGEN 118
FT /note="G->R: In dmr1-6; loss of function."
FT /evidence="ECO:0000269|PubMed:19622802"
FT MUTAGEN 180
FT /note="G->D: In dmr1-5; loss of function."
FT /evidence="ECO:0000269|PubMed:19622802"
FT MUTAGEN 202
FT /note="G->R: In dmr1-4; loss of function."
FT /evidence="ECO:0000269|PubMed:19622802"
FT MUTAGEN 241
FT /note="M->K: In dmr1-3; loss of function."
FT /evidence="ECO:0000269|PubMed:19622802"
FT MUTAGEN 267
FT /note="A->V: In dmr1-1; loss of function."
FT /evidence="ECO:0000269|PubMed:19622802"
FT CONFLICT 32
FT /note="V -> F (in Ref. 4; BAC42512)"
FT /evidence="ECO:0000305"
FT CONFLICT 218
FT /note="R -> K (in Ref. 1; AAD33097)"
FT /evidence="ECO:0000305"
FT CONFLICT 233
FT /note="D -> E (in Ref. 1; AAD33097)"
FT /evidence="ECO:0000305"
FT CONFLICT 359
FT /note="N -> K (in Ref. 1; AAD33097)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 370 AA; 38529 MW; 50FB7315AF061889 CRC64;
MASLCFQSPS KPISYFQPKS NPSPPLFAKV SVFRCRASVQ TLVAVEPEPV FVSVKTFAPA
TVANLGPGFD FLGCAVDGLG DHVTLRVDPS VRAGEVSISE ITGTTTKLST NPLRNCAGIA
AIATMKMLGI RSVGLSLDLH KGLPLGSGLG SSAASAAAAA VAVNEIFGRK LGSDQLVLAG
LESEAKVSGY HADNIAPAIM GGFVLIRNYE PLDLKPLRFP SDKDLFFVLV SPDFEAPTKK
MRAALPTEIP MVHHVWNSSQ AAALVAAVLE GDAVMLGKAL SSDKIVEPTR APLIPGMEAV
KKAALEAGAF GCTISGAGPT AVAVIDSEEK GQVIGEKMVE AFWKVGHLKS VASVKKLDNV
GARLVNSVSR
