Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Phosphoenolpyruvate carboxylase 1

Gene

PPC1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Through the carboxylation of phosphoenolpyruvate (PEP) it forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle. Contributes probably to the adaptation to inorganic phosophate (Pi) deprivation.1 Publication

Catalytic activityi

Phosphate + oxaloacetate = H2O + phosphoenolpyruvate + HCO3-.

Cofactori

Mg2+1 Publication, Mn2+1 PublicationNote: Magnesium. Can also use manganese.1 Publication

Enzyme regulationi

By light-reversible phosphorylation (By similarity). Activated by inorganic phosophate (Pi) deprivation and glucose 6-phosphate. Inhibited by L-malate and L-aspartate.By similarity1 Publication

Kineticsi

  1. KM=0.18 mM for PEP (Phospho-PPC1 at pH 7.3 and 25 degrees Celsius)1 Publication
  2. KM=0.34 mM for PEP (Dephospho-PPC1 at pH 7.3 and 25 degrees Celsius)1 Publication

    pH dependencei

    Optimum pH is 8-9.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei173 – 1731By similarity
    Active sitei602 – 6021By similarity

    GO - Molecular functioni

    • phosphoenolpyruvate carboxylase activity Source: TAIR

    GO - Biological processi

    • carbon fixation Source: UniProtKB-KW
    • cellular response to phosphate starvation Source: UniProtKB
    • leaf development Source: TAIR
    • photosynthesis Source: UniProtKB-KW
    • protein tetramerization Source: UniProtKB
    • tricarboxylic acid cycle Source: InterPro
    Complete GO annotation...

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Carbon dioxide fixation, Photosynthesis

    Keywords - Ligandi

    Magnesium, Manganese

    Enzyme and pathway databases

    BioCyciARA:GQT-2761-MONOMER.
    ARA:GQT-2762-MONOMER.
    BRENDAi4.1.1.31. 399.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphoenolpyruvate carboxylase 1 (EC:4.1.1.31)
    Short name:
    AtPPC1
    Short name:
    PEPC 1
    Short name:
    PEPCase 1
    Alternative name(s):
    107-kDa PEPC polypeptide
    Gene namesi
    Name:PPC1
    Synonyms:p107
    Ordered Locus Names:At1g53310
    ORF Names:F12M16.21
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548 Componenti: Chromosome 1

    Organism-specific databases

    TAIRiAT1G53310.

    Subcellular locationi

    GO - Cellular componenti

    • apoplast Source: TAIR
    • cytosol Source: TAIR
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 967967Phosphoenolpyruvate carboxylase 1PRO_0000166657Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei11 – 111Phosphoserine4 Publications
    Modified residuei704 – 7041Phosphoserine1 Publication

    Post-translational modificationi

    Ubiquitinated.1 Publication
    The phosphorylation of Ser-11 is reversibly promoted by inorganic phosophate (Pi) deprivation. Enhanced activity by phosphorylation at pH 7.3 by lowering Km and sensitivity to inhibition by L-malate and L-aspartate, while enhancing activation by glucose 6-phosphate.1 Publication

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiQ9MAH0.
    PRIDEiQ9MAH0.

    Expressioni

    Tissue specificityi

    Expressed in all plant organs, with higher levels in roots.2 Publications

    Inductioni

    Upon inorganic phosophate (Pi) deprivation.1 Publication

    Interactioni

    Subunit structurei

    Homotetramer.1 Publication

    Protein-protein interaction databases

    BioGridi26990. 4 interactions.
    IntActiQ9MAH0. 2 interactions.
    STRINGi3702.AT1G53310.1.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9MAH0.
    SMRiQ9MAH0. Positions 6-967.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the PEPCase type 1 family.Curated

    Phylogenomic databases

    eggNOGiCOG2352.
    HOGENOMiHOG000238648.
    InParanoidiQ9MAH0.
    KOiK01595.
    OMAiHISKEIA.
    PhylomeDBiQ9MAH0.

    Family and domain databases

    HAMAPiMF_00595. PEPcase_type1.
    InterProiIPR021135. PEP_COase.
    IPR018129. PEP_COase_AS.
    IPR022805. PEP_COase_bac/pln-type.
    IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
    [Graphical view]
    PfamiPF00311. PEPcase. 1 hit.
    [Graphical view]
    PRINTSiPR00150. PEPCARBXLASE.
    SUPFAMiSSF51621. SSF51621. 2 hits.
    PROSITEiPS00781. PEPCASE_1. 1 hit.
    PS00393. PEPCASE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9MAH0-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MANRKLEKMA SIDVHLRQLV PGKVSEDDKL VEYDALLLDR FLDILQDLHG
    60 70 80 90 100
    EDLRETVQEL YEHSAEYEGK HEPKKLEELG SVLTSLDPGD SIVIAKAFSH
    110 120 130 140 150
    MLNLANLAEE VQIAYRRRIK KLKKGDFVDE SSATTESDLE ETFKKLVGDL
    160 170 180 190 200
    NKSPEEIFDA LKNQTVDLVL TAHPTQSVRR SLLQKHGRIR DCLAQLYAKD
    210 220 230 240 250
    ITPDDKQELD EALQREIQAA FRTDEIKRTP PTPQDEMRAG MSYFHETIWK
    260 270 280 290 300
    GVPKFLRRVD TALKNIGIEE RVPYNAPLIQ FSSWMGGDRD GNPRVTPEVT
    310 320 330 340 350
    RDVCLLARMM AATMYFNQIE DLMFEMSMWR CNDELRARAD EVHANSRKDA
    360 370 380 390 400
    AKHYIEFWKS IPTTEPYRVI LGDVRDKLYH TRERAHQLLS NGHSDVPVEA
    410 420 430 440 450
    TFINLEQFLE PLELCYRSLC SCGDRPIADG SLLDFLRQVS TFGLSLVRLD
    460 470 480 490 500
    IRQESDRHTD VLDAITTHLD IGSYREWSEE RRQEWLLSEL SGKRPLFGSD
    510 520 530 540 550
    LPKTEEIADV LDTFHVIAEL PADSFGAYII SMATAPSDVL AVELLQRECR
    560 570 580 590 600
    VKQPLRVVPL FEKLADLEAA PAAVARLFSV DWYKNRINGK QEVMIGYSDS
    610 620 630 640 650
    GKDAGRLSAA WQLYKAQEEL VKVAKEYGVK LTMFHGRGGT VGRGGGPTHL
    660 670 680 690 700
    AILSQPPDTI NGSLRVTVQG EVIEQSFGEE HLCFRTLQRF TAATLEHGMR
    710 720 730 740 750
    PPISPKPEWR ALLDEMAVVA TEEYRSVVFQ EPRFVEYFRL ATPELEYGRM
    760 770 780 790 800
    NIGSRPSKRK PSGGIESLRA IPWIFAWTQT RFHLPVWLGF GSAIRHVIEK
    810 820 830 840 850
    DVRNLHMLQD MYQHWPFFRV TIDLIEMVFA KGDPGIAALY DKLLVSEELW
    860 870 880 890 900
    PFGEKLRANF EETKKLILQT AGHKDLLEGD PYLKQRLRLR DSYITTLNVC
    910 920 930 940 950
    QAYTLKRIRD PSYHVTLRPH ISKEIAESSK PAKELIELNP TSEYAPGLED
    960
    TLILTMKGIA AGLQNTG
    Length:967
    Mass (Da):110,286
    Last modified:October 1, 2000 - v1
    Checksum:iBD3E8F98E2046EEE
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AJ532901 mRNA. Translation: CAD58725.1.
    AC008007 Genomic DNA. Translation: AAF69546.1.
    CP002684 Genomic DNA. Translation: AEE32921.1.
    CP002684 Genomic DNA. Translation: AEE32922.1.
    CP002684 Genomic DNA. Translation: AEE32923.1.
    AY057507 mRNA. Translation: AAL09748.1.
    BT000647 mRNA. Translation: AAN18213.1.
    PIRiD96573.
    RefSeqiNP_001031178.1. NM_001036101.1.
    NP_001031179.1. NM_001036102.2.
    NP_175738.1. NM_104209.2.
    UniGeneiAt.23221.

    Genome annotation databases

    EnsemblPlantsiAT1G53310.1; AT1G53310.1; AT1G53310.
    AT1G53310.2; AT1G53310.2; AT1G53310.
    AT1G53310.3; AT1G53310.3; AT1G53310.
    GeneIDi841765.
    KEGGiath:AT1G53310.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AJ532901 mRNA. Translation: CAD58725.1.
    AC008007 Genomic DNA. Translation: AAF69546.1.
    CP002684 Genomic DNA. Translation: AEE32921.1.
    CP002684 Genomic DNA. Translation: AEE32922.1.
    CP002684 Genomic DNA. Translation: AEE32923.1.
    AY057507 mRNA. Translation: AAL09748.1.
    BT000647 mRNA. Translation: AAN18213.1.
    PIRiD96573.
    RefSeqiNP_001031178.1. NM_001036101.1.
    NP_001031179.1. NM_001036102.2.
    NP_175738.1. NM_104209.2.
    UniGeneiAt.23221.

    3D structure databases

    ProteinModelPortaliQ9MAH0.
    SMRiQ9MAH0. Positions 6-967.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi26990. 4 interactions.
    IntActiQ9MAH0. 2 interactions.
    STRINGi3702.AT1G53310.1.

    Proteomic databases

    PaxDbiQ9MAH0.
    PRIDEiQ9MAH0.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblPlantsiAT1G53310.1; AT1G53310.1; AT1G53310.
    AT1G53310.2; AT1G53310.2; AT1G53310.
    AT1G53310.3; AT1G53310.3; AT1G53310.
    GeneIDi841765.
    KEGGiath:AT1G53310.

    Organism-specific databases

    GeneFarmi5060. 479.
    TAIRiAT1G53310.

    Phylogenomic databases

    eggNOGiCOG2352.
    HOGENOMiHOG000238648.
    InParanoidiQ9MAH0.
    KOiK01595.
    OMAiHISKEIA.
    PhylomeDBiQ9MAH0.

    Enzyme and pathway databases

    BioCyciARA:GQT-2761-MONOMER.
    ARA:GQT-2762-MONOMER.
    BRENDAi4.1.1.31. 399.

    Miscellaneous databases

    PROiQ9MAH0.

    Family and domain databases

    HAMAPiMF_00595. PEPcase_type1.
    InterProiIPR021135. PEP_COase.
    IPR018129. PEP_COase_AS.
    IPR022805. PEP_COase_bac/pln-type.
    IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
    [Graphical view]
    PfamiPF00311. PEPcase. 1 hit.
    [Graphical view]
    PRINTSiPR00150. PEPCARBXLASE.
    SUPFAMiSSF51621. SSF51621. 2 hits.
    PROSITEiPS00781. PEPCASE_1. 1 hit.
    PS00393. PEPCASE_2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Identification and expression analysis of a gene encoding a bacterial-type phosphoenolpyruvate carboxylase from Arabidopsis and rice."
      Sanchez R., Cejudo F.J.
      Plant Physiol. 132:949-957(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, NOMENCLATURE.
      Strain: cv. Columbia.
    2. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
      Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
      , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
      Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    3. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
      Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
      , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
      Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.
    5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11 AND SER-704, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Root.
    6. "In vivo regulatory phosphorylation of the phosphoenolpyruvate carboxylase AtPPC1 in phosphate-starved Arabidopsis thaliana."
      Gregory A.L., Hurley B.A., Tran H.T., Valentine A.J., She Y.-M., Knowles V.L., Plaxton W.C.
      Biochem. J. 420:57-65(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION AT SER-11, INDUCTION BY PHOSPHATE DEPRIVATION, ENZYME REGULATION, SUBUNIT, TISSUE SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR.
      Strain: cv. Columbia and cv. Landsberg erecta.
    7. "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis thaliana."
      Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E., Rathjen J.P., Peck S.C.
      J. Proteomics 72:439-451(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: cv. Columbia.
    8. "Tandem affinity purification and mass spectrometric analysis of ubiquitylated proteins in Arabidopsis."
      Saracco S.A., Hansson M., Scalf M., Walker J.M., Smith L.M., Vierstra R.D.
      Plant J. 59:344-358(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS].
    9. "Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks."
      Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S.
      Plant Physiol. 150:889-903(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiCAPP1_ARATH
    AccessioniPrimary (citable) accession number: Q9MAH0
    Secondary accession number(s): Q546E4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 2002
    Last sequence update: October 1, 2000
    Last modified: June 24, 2015
    This is version 112 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Allosteric enzyme, Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.