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Database: UniProt/SWISS-PROT
Entry: CAPP1_ARATH
LinkDB: CAPP1_ARATH
Original site: 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   16-JAN-2019, entry version 134.
DE   RecName: Full=Phosphoenolpyruvate carboxylase 1;
DE            Short=AtPPC1;
DE            Short=PEPC 1;
DE            Short=PEPCase 1;
DE            EC=4.1.1.31;
DE   AltName: Full=107-kDa PEPC polypeptide;
GN   Name=PPC1; Synonyms=p107; OrderedLocusNames=At1g53310;
GN   ORFNames=F12M16.21;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   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
RT   bacterial-type phosphoenolpyruvate carboxylase from Arabidopsis and
RT   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.,
RA   White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
RA   Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
RA   Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
RA   Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
RA   Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
RA   Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
RA   Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
RA   Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
RA   Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
RA   Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
RA   Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
RA   Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
RA   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.,
RA   Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis
RT   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
RT   reference 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.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., 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.,
RA   Lorkovic Z.J., Barta A., Lecourieux D., Verhounig A., Jonak C.,
RA   Hirt H.;
RT   "Site-specific phosphorylation profiling of Arabidopsis proteins by
RT   mass spectrometry and peptide chip analysis.";
RL   J. Proteome Res. 7:2458-2470(2008).
RN   [6]
RP   FUNCTION, PHOSPHORYLATION AT SER-11, INDUCTION BY PHOSPHATE
RP   DEPRIVATION, ACTIVITY REGULATION, SUBUNIT, TISSUE SPECIFICITY,
RP   IDENTIFICATION BY MASS SPECTROMETRY, BIOPHYSICOCHEMICAL PROPERTIES,
RP   AND 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
RT   carboxylase 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
RP   BY 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.,
RA   Andreasson E., Rathjen J.P., Peck S.C.;
RT   "Phosphoproteomic analysis of nuclei-enriched fractions from
RT   Arabidopsis thaliana.";
RL   J. Proteomics 72:439-451(2009).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, AND IDENTIFICATION
RP   BY 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)
CC       it forms oxaloacetate, a four-carbon dicarboxylic acid source for
CC       the tricarboxylic acid cycle. Contributes probably to the
CC       adaptation to inorganic phosphate (Pi) deprivation.
CC       {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;
CC         EC=4.1.1.31;
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.
CC       {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
CC         Celsius) {ECO:0000269|PubMed:19228119};
CC         KM=0.34 mM for PEP (Dephospho-PPC1 at pH 7.3 and 25 degrees
CC         Celsius) {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
CC       levels in roots. {ECO:0000269|PubMed:12805623,
CC       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
CC       inorganic phosphate (Pi) deprivation. Enhanced activity by
CC       phosphorylation at pH 7.3 by lowering Km and sensitivity to
CC       inhibition by L-malate and L-aspartate, while enhancing activation
CC       by glucose 6-phosphate. {ECO:0000269|PubMed:19228119}.
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family. {ECO:0000305}.
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   UniGene; At.23221; -.
DR   ProteinModelPortal; Q9MAH0; -.
DR   SMR; Q9MAH0; -.
DR   BioGrid; 26990; 6.
DR   IntAct; Q9MAH0; 3.
DR   STRING; 3702.AT1G53310.1; -.
DR   iPTMnet; Q9MAH0; -.
DR   PaxDb; Q9MAH0; -.
DR   PRIDE; Q9MAH0; -.
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; ENOG410IEAR; Eukaryota.
DR   eggNOG; COG2352; LUCA.
DR   HOGENOM; HOG000238648; -.
DR   InParanoid; Q9MAH0; -.
DR   KO; K01595; -.
DR   OMA; RMFHEMY; -.
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; IDA:TAIR.
DR   GO; GO:0009507; C:chloroplast; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IDA: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; Complete proteome;
KW   Cytoplasm; Lyase; Magnesium; Manganese; Phosphoprotein;
KW   Photosynthesis; Reference proteome.
FT   CHAIN         1    967       Phosphoenolpyruvate carboxylase 1.
FT                                /FTId=PRO_0000166657.
FT   ACT_SITE    173    173       {ECO:0000250}.
FT   ACT_SITE    602    602       {ECO:0000250}.
FT   MOD_RES      11     11       Phosphoserine.
FT                                {ECO:0000244|PubMed:18433157,
FT                                ECO:0000244|PubMed:19245862,
FT                                ECO:0000244|PubMed:19376835,
FT                                ECO:0000269|PubMed:19228119}.
FT   MOD_RES     704    704       Phosphoserine.
FT                                {ECO:0000244|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
//
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