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Q9MAH0 (CAPP1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphoenolpyruvate carboxylase 1

Short name=AtPPC1
Short name=PEPC 1
Short name=PEPCase 1
EC=4.1.1.31
Alternative name(s):
107-kDa PEPC polypeptide
Gene names
Name:PPC1
Synonyms:p107
Ordered Locus Names:At1g53310
ORF Names:F12M16.21
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length967 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6

Catalytic activity

Phosphate + oxaloacetate = H2O + phosphoenolpyruvate + HCO3-. HAMAP-Rule MF_00595

Cofactor

Magnesium. Can also use manganese. Ref.6

Enzyme regulation

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

Subunit structure

Homotetramer. Ref.6

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00595.

Tissue specificity

Expressed in all plant organs, with higher levels in roots. Ref.1 Ref.6

Induction

Upon inorganic phosophate (Pi) deprivation. Ref.6

Post-translational modification

Ubiquitinated. HAMAP-Rule MF_00595

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. HAMAP-Rule MF_00595

Sequence similarities

Belongs to the PEPCase type 1 family.

Biophysicochemical properties

Kinetic parameters:

KM=0.18 mM for PEP (Phospho-PPC1 at pH 7.3 and 25 degrees Celsius) Ref.6

KM=0.34 mM for PEP (Dephospho-PPC1 at pH 7.3 and 25 degrees Celsius)

pH dependence:

Optimum pH is 8-9.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 967967Phosphoenolpyruvate carboxylase 1 HAMAP-Rule MF_00595
PRO_0000166657

Sites

Active site1731 By similarity
Active site6021 By similarity

Amino acid modifications

Modified residue111Phosphoserine Ref.5 Ref.6 Ref.7 Ref.9
Modified residue7041Phosphoserine Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q9MAH0 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: BD3E8F98E2046EEE

FASTA967110,286
        10         20         30         40         50         60 
MANRKLEKMA SIDVHLRQLV PGKVSEDDKL VEYDALLLDR FLDILQDLHG EDLRETVQEL 

        70         80         90        100        110        120 
YEHSAEYEGK HEPKKLEELG SVLTSLDPGD SIVIAKAFSH MLNLANLAEE VQIAYRRRIK 

       130        140        150        160        170        180 
KLKKGDFVDE SSATTESDLE ETFKKLVGDL NKSPEEIFDA LKNQTVDLVL TAHPTQSVRR 

       190        200        210        220        230        240 
SLLQKHGRIR DCLAQLYAKD ITPDDKQELD EALQREIQAA FRTDEIKRTP PTPQDEMRAG 

       250        260        270        280        290        300 
MSYFHETIWK GVPKFLRRVD TALKNIGIEE RVPYNAPLIQ FSSWMGGDRD GNPRVTPEVT 

       310        320        330        340        350        360 
RDVCLLARMM AATMYFNQIE DLMFEMSMWR CNDELRARAD EVHANSRKDA AKHYIEFWKS 

       370        380        390        400        410        420 
IPTTEPYRVI LGDVRDKLYH TRERAHQLLS NGHSDVPVEA TFINLEQFLE PLELCYRSLC 

       430        440        450        460        470        480 
SCGDRPIADG SLLDFLRQVS TFGLSLVRLD IRQESDRHTD VLDAITTHLD IGSYREWSEE 

       490        500        510        520        530        540 
RRQEWLLSEL SGKRPLFGSD LPKTEEIADV LDTFHVIAEL PADSFGAYII SMATAPSDVL 

       550        560        570        580        590        600 
AVELLQRECR VKQPLRVVPL FEKLADLEAA PAAVARLFSV DWYKNRINGK QEVMIGYSDS 

       610        620        630        640        650        660 
GKDAGRLSAA WQLYKAQEEL VKVAKEYGVK LTMFHGRGGT VGRGGGPTHL AILSQPPDTI 

       670        680        690        700        710        720 
NGSLRVTVQG EVIEQSFGEE HLCFRTLQRF TAATLEHGMR PPISPKPEWR ALLDEMAVVA 

       730        740        750        760        770        780 
TEEYRSVVFQ EPRFVEYFRL ATPELEYGRM NIGSRPSKRK PSGGIESLRA IPWIFAWTQT 

       790        800        810        820        830        840 
RFHLPVWLGF GSAIRHVIEK DVRNLHMLQD MYQHWPFFRV TIDLIEMVFA KGDPGIAALY 

       850        860        870        880        890        900 
DKLLVSEELW PFGEKLRANF EETKKLILQT AGHKDLLEGD PYLKQRLRLR DSYITTLNVC 

       910        920        930        940        950        960 
QAYTLKRIRD PSYHVTLRPH ISKEIAESSK PAKELIELNP TSEYAPGLED TLILTMKGIA 


AGLQNTG 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]"Site-specific phosphorylation profiling of Arabidopsis proteins by mass spectrometry and peptide chip analysis."
de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E., Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J., Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.
J. Proteome Res. 7:2458-2470(2008) [PubMed] [Europe PMC] [Abstract]
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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRD96573.
RefSeqNP_001031178.1. NM_001036101.1.
NP_001031179.1. NM_001036102.2.
NP_175738.1. NM_104209.2.
UniGeneAt.23221.

3D structure databases

ProteinModelPortalQ9MAH0.
SMRQ9MAH0. Positions 6-967.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid26990. 4 interactions.
IntActQ9MAH0. 2 interactions.

Proteomic databases

PaxDbQ9MAH0.
PRIDEQ9MAH0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G53310.1; AT1G53310.1; AT1G53310.
AT1G53310.2; AT1G53310.2; AT1G53310.
AT1G53310.3; AT1G53310.3; AT1G53310.
GeneID841765.
KEGGath:AT1G53310.

Organism-specific databases

GeneFarm5060. 479.
TAIRAT1G53310.

Phylogenomic databases

eggNOGCOG2352.
HOGENOMHOG000238648.
InParanoidQ9MAH0.
KOK01595.
OMAEYETKHD.
PhylomeDBQ9MAH0.

Enzyme and pathway databases

BioCycARA:GQT-2761-MONOMER.
ARA:GQT-2762-MONOMER.
BRENDA4.1.1.31. 399.

Gene expression databases

ArrayExpressQ9MAH0.
GenevestigatorQ9MAH0.

Family and domain databases

HAMAPMF_00595. PEPcase_type1.
InterProIPR021135. PEP_COase.
IPR018129. PEP_COase_AS.
IPR022805. PEP_COase_bac/pln-type.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
[Graphical view]
PfamPF00311. PEPcase. 1 hit.
[Graphical view]
PRINTSPR00150. PEPCARBXLASE.
SUPFAMSSF51621. SSF51621. 2 hits.
PROSITEPS00781. PEPCASE_1. 1 hit.
PS00393. PEPCASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCAPP1_ARATH
AccessionPrimary (citable) accession number: Q9MAH0
Secondary accession number(s): Q546E4
Entry history
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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names