CAPP1_ARATH
ID CAPP1_ARATH Reviewed; 967 AA.
AC Q9MAH0; Q546E4;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 149.
DE RecName: Full=Phosphoenolpyruvate carboxylase 1;
DE Short=AtPPC1 {ECO:0000303|PubMed:19228119};
DE Short=PEPC 1;
DE Short=PEPCase 1;
DE EC=4.1.1.31 {ECO:0000269|PubMed:19228119};
DE AltName: Full=107-kDa PEPC polypeptide;
GN Name=PPC1; Synonyms=p107; OrderedLocusNames=At1g53310; ORFNames=F12M16.21;
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], TISSUE SPECIFICITY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=12805623; DOI=10.1104/pp.102.019653;
RA Sanchez R., Cejudo F.J.;
RT "Identification and expression analysis of a gene encoding a bacterial-type
RT phosphoenolpyruvate carboxylase from Arabidopsis and rice.";
RL Plant Physiol. 132:949-957(2003).
RN [2]
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 [3]
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 [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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11 AND SER-704, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Root;
RX PubMed=18433157; DOI=10.1021/pr8000173;
RA de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT spectrometry and peptide chip analysis.";
RL J. Proteome Res. 7:2458-2470(2008).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, PHOSPHORYLATION AT SER-11, INDUCTION BY
RP PHOSPHATE DEPRIVATION, ACTIVITY REGULATION, SUBUNIT, TISSUE SPECIFICITY,
RP IDENTIFICATION BY MASS SPECTROMETRY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP COFACTOR.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=19228119; DOI=10.1042/bj20082397;
RA Gregory A.L., Hurley B.A., Tran H.T., Valentine A.J., She Y.-M.,
RA Knowles V.L., Plaxton W.C.;
RT "In vivo regulatory phosphorylation of the phosphoenolpyruvate carboxylase
RT AtPPC1 in phosphate-starved Arabidopsis thaliana.";
RL Biochem. J. 420:57-65(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
CC -!- FUNCTION: Through the carboxylation of phosphoenolpyruvate (PEP) it
CC forms oxaloacetate, a four-carbon dicarboxylic acid source for the
CC tricarboxylic acid cycle. Contributes probably to the adaptation to
CC inorganic phosphate (Pi) deprivation. {ECO:0000269|PubMed:19228119}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=oxaloacetate + phosphate = hydrogencarbonate +
CC phosphoenolpyruvate; Xref=Rhea:RHEA:28370, ChEBI:CHEBI:16452,
CC ChEBI:CHEBI:17544, ChEBI:CHEBI:43474, ChEBI:CHEBI:58702; EC=4.1.1.31;
CC Evidence={ECO:0000269|PubMed:19228119};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:28372;
CC Evidence={ECO:0000305|PubMed:19228119};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:19228119};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:19228119};
CC Note=Magnesium. Can also use manganese. {ECO:0000269|PubMed:19228119};
CC -!- ACTIVITY REGULATION: By light-reversible phosphorylation (By
CC similarity). Activated by inorganic phosphate (Pi) deprivation and
CC glucose 6-phosphate. Inhibited by L-malate and L-aspartate.
CC {ECO:0000250, ECO:0000269|PubMed:19228119}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.18 mM for PEP (Phospho-PPC1 at pH 7.3 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:19228119};
CC KM=0.34 mM for PEP (Dephospho-PPC1 at pH 7.3 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:19228119};
CC pH dependence:
CC Optimum pH is 8-9. {ECO:0000269|PubMed:19228119};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:19228119}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in all plant organs, with higher levels
CC in roots. {ECO:0000269|PubMed:12805623, ECO:0000269|PubMed:19228119}.
CC -!- INDUCTION: Upon inorganic phosphate (Pi) deprivation.
CC {ECO:0000269|PubMed:19228119}.
CC -!- PTM: The phosphorylation of Ser-11 is reversibly promoted by inorganic
CC phosphate (Pi) deprivation. Enhanced activity by phosphorylation at pH
CC 7.3 by lowering Km and sensitivity to inhibition by L-malate and L-
CC aspartate, while enhancing activation by glucose 6-phosphate.
CC {ECO:0000269|PubMed:19228119}.
CC -!- SIMILARITY: Belongs to the PEPCase type 1 family. {ECO:0000305}.
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DR EMBL; AJ532901; CAD58725.1; -; mRNA.
DR EMBL; AC008007; AAF69546.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32921.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32922.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32923.1; -; Genomic_DNA.
DR EMBL; AY057507; AAL09748.1; -; mRNA.
DR EMBL; BT000647; AAN18213.1; -; mRNA.
DR PIR; D96573; D96573.
DR RefSeq; NP_001031178.1; NM_001036101.2.
DR RefSeq; NP_001031179.1; NM_001036102.3.
DR RefSeq; NP_175738.1; NM_104209.3.
DR AlphaFoldDB; Q9MAH0; -.
DR SMR; Q9MAH0; -.
DR BioGRID; 26990; 12.
DR IntAct; Q9MAH0; 3.
DR STRING; 3702.AT1G53310.3; -.
DR iPTMnet; Q9MAH0; -.
DR MetOSite; Q9MAH0; -.
DR PaxDb; Q9MAH0; -.
DR PRIDE; Q9MAH0; -.
DR ProteomicsDB; 239179; -.
DR EnsemblPlants; AT1G53310.1; AT1G53310.1; AT1G53310.
DR EnsemblPlants; AT1G53310.2; AT1G53310.2; AT1G53310.
DR EnsemblPlants; AT1G53310.3; AT1G53310.3; AT1G53310.
DR GeneID; 841765; -.
DR Gramene; AT1G53310.1; AT1G53310.1; AT1G53310.
DR Gramene; AT1G53310.2; AT1G53310.2; AT1G53310.
DR Gramene; AT1G53310.3; AT1G53310.3; AT1G53310.
DR KEGG; ath:AT1G53310; -.
DR Araport; AT1G53310; -.
DR TAIR; locus:2009600; AT1G53310.
DR eggNOG; ENOG502QPVS; Eukaryota.
DR HOGENOM; CLU_006557_1_0_1; -.
DR InParanoid; Q9MAH0; -.
DR OMA; HEMYNAW; -.
DR OrthoDB; 775417at2759; -.
DR PhylomeDB; Q9MAH0; -.
DR BRENDA; 4.1.1.31; 399.
DR SABIO-RK; Q9MAH0; -.
DR PRO; PR:Q9MAH0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9MAH0; baseline and differential.
DR Genevisible; Q9MAH0; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IDA:TAIR.
DR GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-KW.
DR GO; GO:0016036; P:cellular response to phosphate starvation; IDA:UniProtKB.
DR GO; GO:0048366; P:leaf development; IMP:TAIR.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR GO; GO:0051262; P:protein tetramerization; IDA:UniProtKB.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR HAMAP; MF_00595; PEPcase_type1; 1.
DR InterPro; IPR021135; PEP_COase.
DR InterPro; IPR022805; PEP_COase_bac/pln-type.
DR InterPro; IPR018129; PEP_COase_Lys_AS.
DR InterPro; IPR033129; PEPCASE_His_AS.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR PANTHER; PTHR30523; PTHR30523; 1.
DR Pfam; PF00311; PEPcase; 1.
DR PRINTS; PR00150; PEPCARBXLASE.
DR SUPFAM; SSF51621; SSF51621; 1.
DR PROSITE; PS00781; PEPCASE_1; 1.
DR PROSITE; PS00393; PEPCASE_2; 1.
PE 1: Evidence at protein level;
KW Allosteric enzyme; Carbon dioxide fixation; Cytoplasm; Lyase; Magnesium;
KW Manganese; Phosphoprotein; Photosynthesis; Reference proteome.
FT CHAIN 1..967
FT /note="Phosphoenolpyruvate carboxylase 1"
FT /id="PRO_0000166657"
FT ACT_SITE 173
FT /evidence="ECO:0000250"
FT ACT_SITE 602
FT /evidence="ECO:0000250"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19228119,
FT ECO:0007744|PubMed:18433157, ECO:0007744|PubMed:19245862,
FT ECO:0007744|PubMed:19376835"
FT MOD_RES 704
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157"
SQ SEQUENCE 967 AA; 110286 MW; BD3E8F98E2046EEE CRC64;
MANRKLEKMA SIDVHLRQLV PGKVSEDDKL VEYDALLLDR FLDILQDLHG EDLRETVQEL
YEHSAEYEGK HEPKKLEELG SVLTSLDPGD SIVIAKAFSH MLNLANLAEE VQIAYRRRIK
KLKKGDFVDE SSATTESDLE ETFKKLVGDL NKSPEEIFDA LKNQTVDLVL TAHPTQSVRR
SLLQKHGRIR DCLAQLYAKD ITPDDKQELD EALQREIQAA FRTDEIKRTP PTPQDEMRAG
MSYFHETIWK GVPKFLRRVD TALKNIGIEE RVPYNAPLIQ FSSWMGGDRD GNPRVTPEVT
RDVCLLARMM AATMYFNQIE DLMFEMSMWR CNDELRARAD EVHANSRKDA AKHYIEFWKS
IPTTEPYRVI LGDVRDKLYH TRERAHQLLS NGHSDVPVEA TFINLEQFLE PLELCYRSLC
SCGDRPIADG SLLDFLRQVS TFGLSLVRLD IRQESDRHTD VLDAITTHLD IGSYREWSEE
RRQEWLLSEL SGKRPLFGSD LPKTEEIADV LDTFHVIAEL PADSFGAYII SMATAPSDVL
AVELLQRECR VKQPLRVVPL FEKLADLEAA PAAVARLFSV DWYKNRINGK QEVMIGYSDS
GKDAGRLSAA WQLYKAQEEL VKVAKEYGVK LTMFHGRGGT VGRGGGPTHL AILSQPPDTI
NGSLRVTVQG EVIEQSFGEE HLCFRTLQRF TAATLEHGMR PPISPKPEWR ALLDEMAVVA
TEEYRSVVFQ EPRFVEYFRL ATPELEYGRM NIGSRPSKRK PSGGIESLRA IPWIFAWTQT
RFHLPVWLGF GSAIRHVIEK DVRNLHMLQD MYQHWPFFRV TIDLIEMVFA KGDPGIAALY
DKLLVSEELW PFGEKLRANF EETKKLILQT AGHKDLLEGD PYLKQRLRLR DSYITTLNVC
QAYTLKRIRD PSYHVTLRPH ISKEIAESSK PAKELIELNP TSEYAPGLED TLILTMKGIA
AGLQNTG
