SK2_ORYSJ
ID SK2_ORYSJ Reviewed; 307 AA.
AC Q5NTH3; Q0DDG0;
DT 06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Shikimate kinase 2, chloroplastic;
DE Short=OsSK2;
DE EC=2.7.1.71;
DE Flags: Precursor;
GN Name=SK2; OrderedLocusNames=Os06g0225800, LOC_Os06g12150;
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}.
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DR EMBL; AB188835; BAD83413.1; -; mRNA.
DR EMBL; AP003513; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP008212; BAF19113.2; -; Genomic_DNA.
DR EMBL; AP014962; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015641676.1; XM_015786190.1.
DR AlphaFoldDB; Q5NTH3; -.
DR SMR; Q5NTH3; -.
DR STRING; 4530.OS06T0225800-01; -.
DR PaxDb; Q5NTH3; -.
DR PRIDE; Q5NTH3; -.
DR GeneID; 4340547; -.
DR KEGG; osa:4340547; -.
DR eggNOG; ENOG502QTKR; Eukaryota.
DR HOGENOM; CLU_057607_0_1_1; -.
DR InParanoid; Q5NTH3; -.
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 6.
DR Proteomes; UP000059680; Chromosome 6.
DR Genevisible; Q5NTH3; OS.
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..60
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 61..307
FT /note="Shikimate kinase 2, chloroplastic"
FT /id="PRO_0000421114"
FT REGION 285..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 101..108
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 108
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 126
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 151
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 173
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 212
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 307 AA; 32804 MW; 8F85234E6DFDA2EE CRC64;
MEARAGLAMQ SRAAVGVGAG PGVGRRGRAV IRVGKRPTAA SLRVGGPAGP AAAKPLAPLY
CLKASRGHDS LHNSVDEALL LKRKSEEVLF YLNGRCIYLV GMMGSGKSTV AKILAEVLGY
SFFDSDKLVE QAVGMPSVAQ IFKEHSEAFF RDNESSVLRD LSSMRRLVVA TGGGAVIRPV
NWKYMKKGLS VWLDVPLDAL ARRIAQVGTA SRPLLDQPSS DPYTAAFSKL SMLAEQRGDA
YANADARVSL EEIAAKQGHD DVSKLTPTDI AIEALLKIEN FVTEHSTSSG PVGDLIVDSQ
NRRTKAL
