ID   SK_SOLLC                Reviewed;         300 AA.
AC   Q00497;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Shikimate kinase, chloroplastic;
DE            EC=2.7.1.71;
DE   Flags: Precursor;
GN   Name=SK;
OS   Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC   Solanum subgen. Lycopersicon.
OX   NCBI_TaxID=4081;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR
RP   LOCATION.
RC   STRAIN=cv. UC82B; TISSUE=Leaf;
RX   PubMed=1338949; DOI=10.1111/j.1365-313x.1992.00375.x;
RA   Schmid J., Schaller A., Leibinger U., Boll W., Amrhein N.;
RT   "The in-vitro synthesized tomato shikimate kinase precursor is
RT   enzymatically active and is imported and processed to the mature enzyme by
RT   chloroplasts.";
RL   Plant J. 2:375-383(1992).
CC   -!- FUNCTION: Catalyzes the specific phosphorylation of the 3-hydroxyl
CC       group of shikimic acid using ATP as a cosubstrate.
CC       {ECO:0000269|PubMed:1338949}.
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:1338949};
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   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC       chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC       5/7.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC       {ECO:0000269|PubMed:1338949}.
CC   -!- SIMILARITY: Belongs to the shikimate kinase family. {ECO:0000305}.
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DR   EMBL; X63560; CAA45121.1; -; mRNA.
DR   PIR; S21584; S21584.
DR   RefSeq; NP_001234112.1; NM_001247183.1.
DR   RefSeq; XP_010319693.1; XM_010321391.2.
DR   RefSeq; XP_010319694.1; XM_010321392.2.
DR   AlphaFoldDB; Q00497; -.
DR   SMR; Q00497; -.
DR   STRING; 4081.Solyc04g051860.2.1; -.
DR   PaxDb; Q00497; -.
DR   PRIDE; Q00497; -.
DR   EnsemblPlants; Solyc04g051860.3.1; Solyc04g051860.3.1; Solyc04g051860.3.
DR   GeneID; 544078; -.
DR   Gramene; Solyc04g051860.3.1; Solyc04g051860.3.1; Solyc04g051860.3.
DR   KEGG; sly:544078; -.
DR   eggNOG; ENOG502QTKR; Eukaryota.
DR   HOGENOM; CLU_057607_0_1_1; -.
DR   InParanoid; Q00497; -.
DR   OMA; LKGKCIY; -.
DR   OrthoDB; 1565621at2759; -.
DR   PhylomeDB; Q00497; -.
DR   UniPathway; UPA00053; UER00088.
DR   Proteomes; UP000004994; Chromosome 4.
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   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; ATP-binding;
KW   Chloroplast; Kinase; Magnesium; Metal-binding; Nucleotide-binding; Plastid;
KW   Reference proteome; Transferase; Transit peptide.
FT   TRANSIT         1..65
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           66..300
FT                   /note="Shikimate kinase, chloroplastic"
FT                   /id="PRO_0000002293"
FT   BINDING         111..118
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         118
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         136
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         161
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         183
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         222
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   300 AA;  33720 MW;  9CDAC8136922CCB3 CRC64;
     MEARVSQSLQ LSSWINSDKV VRKPSGLLRF SEKWNEKPRH RVVVSCHLQP RKAAHSDRRV
     QLKVSCSPQN VQASVLESGC FSASIDEIET LKNKAEEVEE YLDGRCVYLV GMMGCGKTTV
     GRILAETLGY SFFDCDRLIE QAVGGITVAE IFELRGESFF RDNETEVLHK LSLMHRLVVS
     TGGGAVVRPI NWRHMHKGIS VWLDVPLEAL AKRITTEGTK SRPLLHEESG DVYDTTLKRL
     TTLMETRGEN YANASARVSL ENIALKREKD VCHITPAEIT LEVLIQIENF LKTQKSVVVL