SK1_ARATH
ID SK1_ARATH Reviewed; 303 AA.
AC Q9SJ05; B3DN83; Q3EBW8; Q8GT76;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Shikimate kinase 1, chloroplastic;
DE Short=AtSK1;
DE EC=2.7.1.71;
DE Flags: Precursor;
GN Name=SK1; OrderedLocusNames=At2g21940; ORFNames=F7D8.26;
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 [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 [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA De Los Reyes C., Quan R., Chen H., Bautista V.R., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, GENE FAMILY, NOMENCLATURE, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=19057671; DOI=10.1371/journal.pgen.1000292;
RA Fucile G., Falconer S., Christendat D.;
RT "Evolutionary diversification of plant shikimate kinase gene duplicates.";
RL PLoS Genet. 4:E1000292-E1000292(2008).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND INDUCTION.
RX PubMed=21520319; DOI=10.1002/pro.640;
RA Fucile G., Garcia C., Carlsson J., Sunnerhagen M., Christendat D.;
RT "Structural and biochemical investigation of two Arabidopsis shikimate
RT kinases: the heat-inducible isoform is thermostable.";
RL Protein Sci. 20:1125-1136(2011).
CC -!- FUNCTION: Catalyzes the specific phosphorylation of the 3-hydroxyl
CC group of shikimic acid using ATP as a cosubstrate.
CC {ECO:0000269|PubMed:19057671, ECO:0000269|PubMed:21520319}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + shikimate = 3-phosphoshikimate + ADP + H(+);
CC Xref=Rhea:RHEA:13121, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:36208, ChEBI:CHEBI:145989, ChEBI:CHEBI:456216;
CC EC=2.7.1.71; Evidence={ECO:0000269|PubMed:21520319};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=648 uM for shikimate {ECO:0000269|PubMed:19057671};
CC KM=218 uM for ATP {ECO:0000269|PubMed:19057671};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 5/7.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:21520319}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9SJ05-1; Sequence=Displayed;
CC -!- INDUCTION: By heat stress. {ECO:0000269|PubMed:21520319}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. {ECO:0000269|PubMed:19057671}.
CC -!- MISCELLANEOUS: SK1 forms a homodimer in solution, which may facilitate
CC its relative thermostability when exposed at 37 degrees Celsius.
CC {ECO:0000305|PubMed:21520319}.
CC -!- SIMILARITY: Belongs to the shikimate kinase family. {ECO:0000305}.
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DR EMBL; AC007019; AAD20411.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07240.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07241.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07244.1; -; Genomic_DNA.
DR EMBL; AK118899; BAC43483.2; -; mRNA.
DR EMBL; BT032871; ACD85800.1; -; mRNA.
DR PIR; A84607; A84607.
DR RefSeq; NP_001077938.1; NM_001084469.1. [Q9SJ05-1]
DR RefSeq; NP_179785.2; NM_127763.4. [Q9SJ05-1]
DR RefSeq; NP_973507.2; NM_201778.3. [Q9SJ05-1]
DR AlphaFoldDB; Q9SJ05; -.
DR SMR; Q9SJ05; -.
DR BioGRID; 2083; 1.
DR STRING; 3702.AT2G21940.4; -.
DR iPTMnet; Q9SJ05; -.
DR PaxDb; Q9SJ05; -.
DR ProteomicsDB; 234527; -. [Q9SJ05-1]
DR EnsemblPlants; AT2G21940.1; AT2G21940.1; AT2G21940. [Q9SJ05-1]
DR EnsemblPlants; AT2G21940.2; AT2G21940.2; AT2G21940. [Q9SJ05-1]
DR EnsemblPlants; AT2G21940.5; AT2G21940.5; AT2G21940. [Q9SJ05-1]
DR GeneID; 816730; -.
DR Gramene; AT2G21940.1; AT2G21940.1; AT2G21940. [Q9SJ05-1]
DR Gramene; AT2G21940.2; AT2G21940.2; AT2G21940. [Q9SJ05-1]
DR Gramene; AT2G21940.5; AT2G21940.5; AT2G21940. [Q9SJ05-1]
DR KEGG; ath:AT2G21940; -.
DR Araport; AT2G21940; -.
DR eggNOG; ENOG502S43P; Eukaryota.
DR HOGENOM; CLU_057607_0_1_1; -.
DR InParanoid; Q9SJ05; -.
DR OMA; HASCDEY; -.
DR PhylomeDB; Q9SJ05; -.
DR BioCyc; ARA:AT2G21940-MON; -.
DR BioCyc; MetaCyc:AT2G21940-MON; -.
DR UniPathway; UPA00053; UER00088.
DR PRO; PR:Q9SJ05; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SJ05; baseline and differential.
DR Genevisible; Q9SJ05; AT.
DR GO; GO:0009507; C:chloroplast; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004765; F:shikimate kinase activity; IBA:GO_Central.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00464; SK; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00109; Shikimate_kinase; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR031322; Shikimate/glucono_kinase.
DR InterPro; IPR000623; Shikimate_kinase/TSH1.
DR InterPro; IPR023000; Shikimate_kinase_CS.
DR Pfam; PF01202; SKI; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS01128; SHIKIMATE_KINASE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Amino-acid biosynthesis;
KW Aromatic amino acid biosynthesis; ATP-binding; Chloroplast; Disulfide bond;
KW Kinase; Magnesium; Metal-binding; Nucleotide-binding; Plastid;
KW Reference proteome; Stress response; Transferase; Transit peptide.
FT TRANSIT 1..66
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 67..303
FT /note="Shikimate kinase 1, chloroplastic"
FT /id="PRO_0000002292"
FT BINDING 109..116
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 116
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 134
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 159
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 181
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 220
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT DISULFID 67
FT /note="Interchain"
FT /evidence="ECO:0000255"
FT CONFLICT 229
FT /note="D -> N (in Ref. 3; BAC43483)"
FT /evidence="ECO:0000305"
FT CONFLICT 269
FT /note="N -> D (in Ref. 4; ACD85800)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 303 AA; 33982 MW; B3717FD63F57397D CRC64;
MEAAITQRIQ YPSWVDCRKV ECKPQRGSLR YSQQVKVDRR FRGLSLARLQ PERRNDQRRA
VSPAVSCSDN NSSALLETGS VYPFDEDILK RKAEEVKPYL NGRSMYLVGM MGSGKTTVGK
LMSKVLGYTF FDCDTLIEQA MNGTSVAEIF VHHGENFFRG KETDALKKLS SRYQVVVSTG
GGAVIRPINW KYMHKGISIW LDVPLEALAH RIAAVGTDSR PLLHDESGDA YSVAFKRLSA
IWDERGEAYT NANARVSLEN IAAKRGYKNV SDLTPTEIAI EAFEQVLSFL EKEETMEIPD
GDL
