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Q9MAH0

- CAPP1_ARATH

UniProt

Q9MAH0 - CAPP1_ARATH

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Protein
Phosphoenolpyruvate carboxylase 1
Gene
PPC1, p107, At1g53310, F12M16.21
Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - 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-.UniRule annotation

Cofactori

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.1 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)

pH dependencei

Optimum pH is 8-9.

Sites

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

GO - Molecular functioni

  1. phosphoenolpyruvate carboxylase activity Source: UniProtKB-EC
  2. protein binding Source: TAIR

GO - Biological processi

  1. carbon fixation Source: UniProtKB-KW
  2. cellular response to phosphate starvation Source: UniProtKB
  3. photosynthesis Source: UniProtKB-KW
  4. protein tetramerization Source: UniProtKB
  5. 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: Chromosome 1

Organism-specific databases

TAIRiAT1G53310.

Subcellular locationi

Cytoplasm By similarity UniRule annotation

GO - Cellular componenti

  1. apoplast Source: TAIR
  2. cytosol Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

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

Amino acid modifications

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

Post-translational modificationi

Ubiquitinated.UniRule annotation
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.UniRule annotation

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

Gene expression databases

ArrayExpressiQ9MAH0.
GenevestigatoriQ9MAH0.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

BioGridi26990. 4 interactions.
IntActiQ9MAH0. 2 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ9MAH0.
SMRiQ9MAH0. Positions 6-967.

Family & Domainsi

Sequence similaritiesi

Belongs to the PEPCase type 1 family.

Phylogenomic databases

eggNOGiCOG2352.
HOGENOMiHOG000238648.
InParanoidiQ9MAH0.
KOiK01595.
OMAiEYETKHD.
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

MANRKLEKMA SIDVHLRQLV PGKVSEDDKL VEYDALLLDR FLDILQDLHG    50
EDLRETVQEL YEHSAEYEGK HEPKKLEELG SVLTSLDPGD SIVIAKAFSH 100
MLNLANLAEE VQIAYRRRIK KLKKGDFVDE SSATTESDLE ETFKKLVGDL 150
NKSPEEIFDA LKNQTVDLVL TAHPTQSVRR SLLQKHGRIR DCLAQLYAKD 200
ITPDDKQELD EALQREIQAA FRTDEIKRTP PTPQDEMRAG MSYFHETIWK 250
GVPKFLRRVD TALKNIGIEE RVPYNAPLIQ FSSWMGGDRD GNPRVTPEVT 300
RDVCLLARMM AATMYFNQIE DLMFEMSMWR CNDELRARAD EVHANSRKDA 350
AKHYIEFWKS IPTTEPYRVI LGDVRDKLYH TRERAHQLLS NGHSDVPVEA 400
TFINLEQFLE PLELCYRSLC SCGDRPIADG SLLDFLRQVS TFGLSLVRLD 450
IRQESDRHTD VLDAITTHLD IGSYREWSEE RRQEWLLSEL SGKRPLFGSD 500
LPKTEEIADV LDTFHVIAEL PADSFGAYII SMATAPSDVL AVELLQRECR 550
VKQPLRVVPL FEKLADLEAA PAAVARLFSV DWYKNRINGK QEVMIGYSDS 600
GKDAGRLSAA WQLYKAQEEL VKVAKEYGVK LTMFHGRGGT VGRGGGPTHL 650
AILSQPPDTI NGSLRVTVQG EVIEQSFGEE HLCFRTLQRF TAATLEHGMR 700
PPISPKPEWR ALLDEMAVVA TEEYRSVVFQ EPRFVEYFRL ATPELEYGRM 750
NIGSRPSKRK PSGGIESLRA IPWIFAWTQT RFHLPVWLGF GSAIRHVIEK 800
DVRNLHMLQD MYQHWPFFRV TIDLIEMVFA KGDPGIAALY DKLLVSEELW 850
PFGEKLRANF EETKKLILQT AGHKDLLEGD PYLKQRLRLR DSYITTLNVC 900
QAYTLKRIRD PSYHVTLRPH ISKEIAESSK PAKELIELNP TSEYAPGLED 950
TLILTMKGIA AGLQNTG 967
Length:967
Mass (Da):110,286
Last modified:October 1, 2000 - v1
Checksum:iBD3E8F98E2046EEE
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
PIRi D96573.
RefSeqi NP_001031178.1. NM_001036101.1.
NP_001031179.1. NM_001036102.2.
NP_175738.1. NM_104209.2.
UniGenei At.23221.

3D structure databases

ProteinModelPortali Q9MAH0.
SMRi Q9MAH0. Positions 6-967.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 26990. 4 interactions.
IntActi Q9MAH0. 2 interactions.

Proteomic databases

PaxDbi Q9MAH0.
PRIDEi Q9MAH0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT1G53310.1 ; AT1G53310.1 ; AT1G53310 .
AT1G53310.2 ; AT1G53310.2 ; AT1G53310 .
AT1G53310.3 ; AT1G53310.3 ; AT1G53310 .
GeneIDi 841765.
KEGGi ath:AT1G53310.

Organism-specific databases

GeneFarmi 5060. 479.
TAIRi AT1G53310.

Phylogenomic databases

eggNOGi COG2352.
HOGENOMi HOG000238648.
InParanoidi Q9MAH0.
KOi K01595.
OMAi EYETKHD.
PhylomeDBi Q9MAH0.

Enzyme and pathway databases

BioCyci ARA:GQT-2761-MONOMER.
ARA:GQT-2762-MONOMER.
BRENDAi 4.1.1.31. 399.

Gene expression databases

ArrayExpressi Q9MAH0.
Genevestigatori Q9MAH0.

Family and domain databases

HAMAPi MF_00595. PEPcase_type1.
InterProi IPR021135. PEP_COase.
IPR018129. PEP_COase_AS.
IPR022805. PEP_COase_bac/pln-type.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
[Graphical view ]
Pfami PF00311. PEPcase. 1 hit.
[Graphical view ]
PRINTSi PR00150. PEPCARBXLASE.
SUPFAMi SSF51621. SSF51621. 2 hits.
PROSITEi PS00781. PEPCASE_1. 1 hit.
PS00393. PEPCASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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 11, 2014
This is version 104 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