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SK1_ORYSJ
ID   SK1_ORYSJ               Reviewed;         308 AA.
AC   Q5NTH4; Q0DXJ9;
DT   06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Shikimate kinase 1, chloroplastic;
DE            Short=OsSK1;
DE            EC=2.7.1.71;
DE   Flags: Precursor;
GN   Name=SK1; OrderedLocusNames=Os02g0749300, LOC_Os02g51410;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
RP   LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15891897; DOI=10.1007/s00425-005-1559-8;
RA   Kasai K., Kanno T., Akita M., Ikejiri-Kanno Y., Wakasa K., Tozawa Y.;
RT   "Identification of three shikimate kinase genes in rice: characterization
RT   of their differential expression during panicle development and of the
RT   enzymatic activities of the encoded proteins.";
RL   Planta 222:438-447(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
CC   -!- FUNCTION: Catalyzes the specific phosphorylation of the 3-hydroxyl
CC       group of shikimic acid using ATP as a cosubstrate.
CC       {ECO:0000269|PubMed:15891897}.
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:15891897};
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:0000305|PubMed:15891897}.
CC   -!- TISSUE SPECIFICITY: Expressed in panicles.
CC       {ECO:0000269|PubMed:15891897}.
CC   -!- INDUCTION: By chitin oligosaccharide elicitor.
CC       {ECO:0000269|PubMed:15891897}.
CC   -!- SIMILARITY: Belongs to the shikimate kinase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAF10039.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AB188834; BAD83412.1; -; mRNA.
DR   EMBL; AP005848; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AP008208; BAF10039.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AP014958; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_015626759.1; XM_015771273.1.
DR   AlphaFoldDB; Q5NTH4; -.
DR   SMR; Q5NTH4; -.
DR   STRING; 4530.OS02T0749300-01; -.
DR   PaxDb; Q5NTH4; -.
DR   PRIDE; Q5NTH4; -.
DR   GeneID; 4330732; -.
DR   KEGG; osa:4330732; -.
DR   eggNOG; ENOG502QTKR; Eukaryota.
DR   InParanoid; Q5NTH4; -.
DR   OrthoDB; 1565621at2759; -.
DR   BRENDA; 2.7.1.71; 4460.
DR   PlantReactome; R-OSA-1119430; Chorismate biosynthesis.
DR   UniPathway; UPA00053; UER00088.
DR   Proteomes; UP000000763; Chromosome 2.
DR   Proteomes; UP000059680; Chromosome 2.
DR   GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR   GO; GO:0009536; C:plastid; IDA:Gramene.
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; IDA:Gramene.
DR   GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IDA:Gramene.
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   GO; GO:0019632; P:shikimate metabolic process; IDA:UniProtKB.
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..62
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           63..308
FT                   /note="Shikimate kinase 1, chloroplastic"
FT                   /id="PRO_0000421113"
FT   BINDING         103..110
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         110
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         128
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         153
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         175
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         214
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   308 AA;  33310 MW;  D8A4FDB1CE88EA3E CRC64;
     MEAGVGLALQ SRAAGFGGSD RRRSALYGGE GRARIGSLRV AEPAVAKAAV WARGSKPVAP
     LRAKKSSGGH ETLHNSVDEA LLLKRKSEEV LFYLNGRCIY LVGMMGSGKS TVGKIMSEVL
     GYSFFDSDKL VEQAVGMPSV AQIFKVHSEA FFRDNESSVL RDLSSMKRLV VATGGGAVIR
     PVNWKYMKKG LSVWLDVPLD ALARRIAKVG TASRPLLDQP SGDPYTMAFS KLSMLAEQRG
     DAYANADVRV SLEEIASKQG HDDVSKLTPT DIAIESFHKI ENFVIEHTVD NPVGDSQADS
     RAQRIQTL
 
 
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