SK2_ARATH
ID SK2_ARATH Reviewed; 300 AA.
AC Q8GY88; Q9SVA4;
DT 06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Shikimate kinase 2, chloroplastic;
DE Short=AtSK2;
DE EC=2.7.1.71;
DE Flags: Precursor;
GN Name=SK2; OrderedLocusNames=At4g39540; ORFNames=F23K16.170;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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;
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 [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 X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 55-300, FUNCTION, CATALYTIC
RP ACTIVITY, ACTIVITY REGULATION, AND SUBUNIT.
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 -!- ACTIVITY REGULATION: Inactivated by heat (37 degrees Celsius).
CC {ECO:0000269|PubMed:21520319}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=422 uM for shikimate {ECO:0000269|PubMed:19057671};
CC KM=246 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: Monomer. {ECO:0000269|PubMed:21520319}.
CC -!- INTERACTION:
CC Q8GY88; Q17TI5: BRX; NbExp=3; IntAct=EBI-1238334, EBI-4426649;
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=Q8GY88-1; Sequence=Displayed;
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. {ECO:0000269|PubMed:19057671}.
CC -!- SIMILARITY: Belongs to the shikimate kinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB44689.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80617.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL078620; CAB44689.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161595; CAB80617.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE87083.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE87084.1; -; Genomic_DNA.
DR EMBL; AK117791; BAC42436.1; -; mRNA.
DR EMBL; BT005291; AAO63355.1; -; mRNA.
DR PIR; T09370; T09370.
DR RefSeq; NP_195664.2; NM_120114.2. [Q8GY88-1]
DR RefSeq; NP_974715.1; NM_202986.2. [Q8GY88-1]
DR PDB; 3NWJ; X-ray; 2.35 A; A/B=55-300.
DR PDBsum; 3NWJ; -.
DR AlphaFoldDB; Q8GY88; -.
DR SMR; Q8GY88; -.
DR BioGRID; 15388; 9.
DR IntAct; Q8GY88; 8.
DR STRING; 3702.AT4G39540.3; -.
DR PaxDb; Q8GY88; -.
DR PRIDE; Q8GY88; -.
DR ProteomicsDB; 234468; -. [Q8GY88-1]
DR EnsemblPlants; AT4G39540.1; AT4G39540.1; AT4G39540. [Q8GY88-1]
DR EnsemblPlants; AT4G39540.2; AT4G39540.2; AT4G39540. [Q8GY88-1]
DR GeneID; 830108; -.
DR Gramene; AT4G39540.1; AT4G39540.1; AT4G39540. [Q8GY88-1]
DR Gramene; AT4G39540.2; AT4G39540.2; AT4G39540. [Q8GY88-1]
DR KEGG; ath:AT4G39540; -.
DR Araport; AT4G39540; -.
DR eggNOG; ENOG502QTKR; Eukaryota.
DR HOGENOM; CLU_057607_0_1_1; -.
DR InParanoid; Q8GY88; -.
DR OMA; EDACHIT; -.
DR PhylomeDB; Q8GY88; -.
DR BioCyc; ARA:AT4G39540-MON; -.
DR BioCyc; MetaCyc:AT4G39540-MON; -.
DR BRENDA; 2.7.1.71; 399.
DR UniPathway; UPA00053; UER00088.
DR PRO; PR:Q8GY88; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8GY88; baseline and differential.
DR Genevisible; Q8GY88; 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; IDA:UniProtKB.
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 GO; GO:0019632; P:shikimate metabolic process; IDA:UniProtKB.
DR CDD; cd00464; SK; 1.
DR DisProt; DP02641; -.
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; 2.
DR PROSITE; PS01128; SHIKIMATE_KINASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Amino-acid biosynthesis;
KW Aromatic amino acid biosynthesis; ATP-binding; Chloroplast; Kinase;
KW Magnesium; Metal-binding; Nucleotide-binding; Plastid; Reference proteome;
KW Transferase; Transit peptide.
FT TRANSIT 1..58
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 59..300
FT /note="Shikimate kinase 2, chloroplastic"
FT /id="PRO_0000421110"
FT BINDING 105..112
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 112
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 130
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 155
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 178
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 217
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT HELIX 83..90
FT /evidence="ECO:0007829|PDB:3NWJ"
FT HELIX 93..96
FT /evidence="ECO:0007829|PDB:3NWJ"
FT STRAND 101..104
FT /evidence="ECO:0007829|PDB:3NWJ"
FT HELIX 111..122
FT /evidence="ECO:0007829|PDB:3NWJ"
FT STRAND 125..128
FT /evidence="ECO:0007829|PDB:3NWJ"
FT HELIX 129..136
FT /evidence="ECO:0007829|PDB:3NWJ"
FT HELIX 142..149
FT /evidence="ECO:0007829|PDB:3NWJ"
FT HELIX 151..168
FT /evidence="ECO:0007829|PDB:3NWJ"
FT STRAND 170..175
FT /evidence="ECO:0007829|PDB:3NWJ"
FT HELIX 178..182
FT /evidence="ECO:0007829|PDB:3NWJ"
FT HELIX 184..190
FT /evidence="ECO:0007829|PDB:3NWJ"
FT STRAND 193..199
FT /evidence="ECO:0007829|PDB:3NWJ"
FT HELIX 202..210
FT /evidence="ECO:0007829|PDB:3NWJ"
FT HELIX 229..247
FT /evidence="ECO:0007829|PDB:3NWJ"
FT STRAND 250..255
FT /evidence="ECO:0007829|PDB:3NWJ"
FT HELIX 256..263
FT /evidence="ECO:0007829|PDB:3NWJ"
FT HELIX 268..270
FT /evidence="ECO:0007829|PDB:3NWJ"
FT HELIX 273..289
FT /evidence="ECO:0007829|PDB:3NWJ"
SQ SEQUENCE 300 AA; 33777 MW; 8868B7DF6FF7D492 CRC64;
MEAATVQRFQ YSSWNDLRNF EGKPRGSLRY NTQRIKEDKR FRVVALTLDK RRDHRLRSVS
DKNSSALLET GSLLHSPFDE EQQILKKKAE EVKPYLNGRS MYLVGMMGSG KTTVGKIMAR
SLGYTFFDCD TLIEQAMKGT SVAEIFEHFG ESVFREKETE ALKKLSLMYH QVVVSTGGGA
VIRPINWKYM HKGISIWLDV PLEALAHRIA AVGTGSRPLL HDDESGDTYT AALNRLSTIW
DARGEAYTKA SARVSLENIT LKLGYRSVSD LTPAEIAIEA FEQVQSYLEK EDGMARPDGL
