ISPE_ARATH
ID ISPE_ARATH Reviewed; 383 AA.
AC O81014; Q9GI18;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=4-diphosphocytidyl-2-C-methyl-D-erythritol kinase, chloroplastic;
DE EC=2.7.1.148;
DE AltName: Full=4-(cytidine-5'-diphospho)-2-C-methyl-D-erythritol kinase;
DE Short=CDPMEK;
DE Short=CMEK;
DE AltName: Full=Protein PIGMENT DEFECTIVE 277;
DE Flags: Precursor;
GN Name=ISPE; Synonyms=CMK, PDE227; OrderedLocusNames=At2g26930;
GN ORFNames=F12C20.3;
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 [MRNA].
RC STRAIN=cv. Columbia;
RA Okada K., Kawaide H., Kuzuyama T., Takagi M., Seto H., Kamiya Y.;
RT "4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Wungsintaweekul J., Rohdich F.;
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
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 [5]
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 [6]
RP INDUCTION.
RX PubMed=15863698; DOI=10.1104/pp.104.058735;
RA Hsieh M.H., Goodman H.M.;
RT "The Arabidopsis IspH homolog is involved in the plastid nonmevalonate
RT pathway of isoprenoid biosynthesis.";
RL Plant Physiol. 138:641-653(2005).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=18236010; DOI=10.1007/s11103-008-9297-5;
RA Hsieh M.H., Chang C.Y., Hsu S.J., Chen J.J.;
RT "Chloroplast localization of methylerythritol 4-phosphate pathway enzymes
RT and regulation of mitochondrial genes in ispD and ispE albino mutants in
RT Arabidopsis.";
RL Plant Mol. Biol. 66:663-673(2008).
CC -!- FUNCTION: Enzyme of the plastid non-mevalonate pathway for isoprenoid
CC biosynthesis that catalyzes the phosphorylation of the position 2
CC hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol. Is
CC essential for chloroplast development. {ECO:0000269|PubMed:18236010}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-CDP-2-C-methyl-D-erythritol + ATP = 4-CDP-2-C-methyl-D-
CC erythritol 2-phosphate + ADP + H(+); Xref=Rhea:RHEA:18437,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57823,
CC ChEBI:CHEBI:57919, ChEBI:CHEBI:456216; EC=2.7.1.148;
CC -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis
CC via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-
CC phosphate: step 3/6.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000305|PubMed:18236010}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, stems, flowers and siliques.
CC {ECO:0000269|PubMed:18236010}.
CC -!- INDUCTION: Circadian-regulated with a peak in the late period of the
CC light phase. {ECO:0000269|PubMed:15863698,
CC ECO:0000269|PubMed:18236010}.
CC -!- DISRUPTION PHENOTYPE: Albino phenotype and seedling lethal when
CC homozygous. The phenotype is caused by an early arrest in chloroplast
CC differentiation. {ECO:0000269|PubMed:18236010}.
CC -!- SIMILARITY: Belongs to the GHMP kinase family. IspE subfamily.
CC {ECO:0000305}.
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DR EMBL; AB037877; BAB21593.1; -; mRNA.
DR EMBL; AF288615; AAG01340.1; -; mRNA.
DR EMBL; AC005168; AAC32234.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07908.1; -; Genomic_DNA.
DR EMBL; AY136394; AAM97060.1; -; mRNA.
DR EMBL; BT000208; AAN15527.1; -; mRNA.
DR PIR; T02642; T02642.
DR RefSeq; NP_180261.1; NM_128250.4.
DR AlphaFoldDB; O81014; -.
DR SMR; O81014; -.
DR BioGRID; 2586; 1.
DR STRING; 3702.AT2G26930.1; -.
DR ChEMBL; CHEMBL1293253; -.
DR PaxDb; O81014; -.
DR PRIDE; O81014; -.
DR ProteomicsDB; 250640; -.
DR EnsemblPlants; AT2G26930.1; AT2G26930.1; AT2G26930.
DR GeneID; 817234; -.
DR Gramene; AT2G26930.1; AT2G26930.1; AT2G26930.
DR KEGG; ath:AT2G26930; -.
DR Araport; AT2G26930; -.
DR TAIR; locus:2039503; AT2G26930.
DR eggNOG; ENOG502QT9C; Eukaryota.
DR HOGENOM; CLU_053057_0_0_1; -.
DR InParanoid; O81014; -.
DR OMA; ACDALWG; -.
DR OrthoDB; 1256281at2759; -.
DR PhylomeDB; O81014; -.
DR BioCyc; ARA:AT2G26930-MON; -.
DR UniPathway; UPA00056; UER00094.
DR PRO; PR:O81014; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O81014; baseline and differential.
DR Genevisible; O81014; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR GO; GO:0050515; F:4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase activity; ISS:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019288; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:InterPro.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.70.890; -; 1.
DR HAMAP; MF_00061; IspE; 1.
DR InterPro; IPR013750; GHMP_kinase_C_dom.
DR InterPro; IPR036554; GHMP_kinase_C_sf.
DR InterPro; IPR006204; GHMP_kinase_N_dom.
DR InterPro; IPR004424; IspE.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR PANTHER; PTHR43527:SF2; PTHR43527:SF2; 1.
DR Pfam; PF08544; GHMP_kinases_C; 1.
DR Pfam; PF00288; GHMP_kinases_N; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55060; SSF55060; 1.
DR TIGRFAMs; TIGR00154; ispE; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Chloroplast; Isoprene biosynthesis; Kinase;
KW Nucleotide-binding; Plastid; Reference proteome; Transferase;
KW Transit peptide.
FT TRANSIT 1..72
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 73..383
FT /note="4-diphosphocytidyl-2-C-methyl-D-erythritol kinase,
FT chloroplastic"
FT /id="PRO_0000016479"
FT BINDING 165..175
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 11
FT /note="T -> A (in Ref. 2; AAG01340)"
FT /evidence="ECO:0000305"
FT CONFLICT 109
FT /note="D -> G (in Ref. 2; AAG01340)"
FT /evidence="ECO:0000305"
FT CONFLICT 272
FT /note="E -> K (in Ref. 2; AAG01340)"
FT /evidence="ECO:0000305"
FT CONFLICT 346
FT /note="N -> D (in Ref. 2; AAG01340)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 383 AA; 42043 MW; 7CBF500239AE138D CRC64;
MATASPPFIS TLSFTHSSFK TSSSSSFSPK LLRPLLSFSV KASRKQVEIV FDPDERLNKI
GDDVDKEAPL SRLKLFSPCK INVFLRITGK REDGFHDLAS LFHVISLGDT IKFSLSPSKS
KDRLSTNVQG VPVDGRNLII KALNLYRKKT GSNRFFWIHL DKKVPTGAGL GGGSSNAATA
LWAANELNGG LVTENELQDW SSEIGSDIPF FFSHGAAYCT GRGEIVQDLP PPFPLDLPMV
LIKPREACST AEVYKRLRLD QTSNINPLTL LENVTSNGVS QSICVNDLEP PAFSVLPSLK
RLKQRIIASG RGEYDAVFMS GSGSTIIGIG SPDPPQFIYD DEEYKNVFLS EANFMTREAN
EWYKEPASAN ATTSSAESRM DFQ
