CPPM_ARATH
ID CPPM_ARATH Reviewed; 339 AA.
AC O49290; Q8LFA2;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Carboxyvinyl-carboxyphosphonate phosphorylmutase, chloroplastic;
DE EC=2.7.8.23;
DE AltName: Full=Carboxyphosphonoenolpyruvate phosphonomutase;
DE Short=CPEP phosphonomutase;
DE Flags: Precursor;
GN OrderedLocusNames=At1g77060; ORFNames=F22K20.14;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=18431481; DOI=10.1371/journal.pone.0001994;
RA Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O., Sun Q.,
RA van Wijk K.J.;
RT "Sorting signals, N-terminal modifications and abundance of the chloroplast
RT proteome.";
RL PLoS ONE 3:E1994-E1994(2008).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-carboxyvinyl carboxyphosphonate + H(+) = 3-
CC (hydrohydroxyphosphoryl)pyruvate + CO2; Xref=Rhea:RHEA:14045,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57999,
CC ChEBI:CHEBI:58348; EC=2.7.8.23;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:18431481}.
CC -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC00621.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AC002291; AAC00621.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002684; AEE35928.1; -; Genomic_DNA.
DR EMBL; AY084963; AAM61524.1; -; mRNA.
DR PIR; E96799; E96799.
DR RefSeq; NP_565148.1; NM_106356.3.
DR AlphaFoldDB; O49290; -.
DR SMR; O49290; -.
DR STRING; 3702.AT1G77060.1; -.
DR PaxDb; O49290; -.
DR PRIDE; O49290; -.
DR ProteomicsDB; 220409; -.
DR EnsemblPlants; AT1G77060.1; AT1G77060.1; AT1G77060.
DR GeneID; 844041; -.
DR Gramene; AT1G77060.1; AT1G77060.1; AT1G77060.
DR KEGG; ath:AT1G77060; -.
DR Araport; AT1G77060; -.
DR TAIR; locus:2025272; AT1G77060.
DR eggNOG; KOG1260; Eukaryota.
DR HOGENOM; CLU_027389_3_1_1; -.
DR InParanoid; O49290; -.
DR OMA; QTELWNK; -.
DR OrthoDB; 1003512at2759; -.
DR PhylomeDB; O49290; -.
DR BioCyc; ARA:AT1G77060-MON; -.
DR PRO; PR:O49290; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O49290; baseline and differential.
DR Genevisible; O49290; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0008807; F:carboxyvinyl-carboxyphosphonate phosphorylmutase activity; IEA:UniProtKB-EC.
DR CDD; cd00377; ICL_PEPM; 1.
DR Gene3D; 3.20.20.60; -; 1.
DR InterPro; IPR039556; ICL/PEPM.
DR InterPro; IPR018523; Isocitrate_lyase_ph_CS.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR SUPFAM; SSF51621; SSF51621; 1.
DR PROSITE; PS00161; ISOCITRATE_LYASE; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Plastid; Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..30
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 31..339
FT /note="Carboxyvinyl-carboxyphosphonate phosphorylmutase,
FT chloroplastic"
FT /id="PRO_0000068822"
SQ SEQUENCE 339 AA; 36566 MW; 871FB6432DC0DB35 CRC64;
MSMLMAVKTT SLCCSSLNLT ASPTFRRNPR AARLVNPTAR IQTRFHRLIE EQGIVLMPGC
YDALSAAIVQ QTGFSAGFIS GYALSASLLG KPDFGLLTPP EMAATARSVC ASAPNIPIIA
DADTGGGNAL NIQRTVKDLI AAGAAGCFLE DQAWPKKCGH MRGKQVIPAE EHAAKIASAR
DAIGDSDFFL VARTDVRATS AKSGLEDAIA RVNLYMEAGA DASFVEAPRD DDELKEIGKR
TKGYRVCNMI EGGVTPLHTP DELKEMGFHL IVHPLTALYA STRALVDVLK TLKENGSTRD
HLQKMATFEE FNSLVDLDSW FELEARYSNL RNALGTTKS
