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Q5GM68 (CAPP2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 77. 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 2

Short name=AtPPC2
Short name=PEPC 2
Short name=PEPCase 2
EC=4.1.1.31
Gene names
Name:PPC2
Ordered Locus Names:At2g42600
ORF Names:F14N22.13
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length963 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. HAMAP-Rule MF_00595

Catalytic activity

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

Cofactor

Magnesium By similarity. HAMAP-Rule MF_00595

Enzyme regulation

By light-reversible phosphorylation By similarity. HAMAP-Rule MF_00595

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_00595

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00595.

Tissue specificity

Expressed in all plant organs, with higher levels in stems and leaves. Ref.1

Post-translational modification

Ubiquitinated. HAMAP-Rule MF_00595

Sequence similarities

Belongs to the PEPCase type 1 family.

Sequence caution

The sequence AAD22994.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 963963Phosphoenolpyruvate carboxylase 2 HAMAP-Rule MF_00595
PRO_0000166658

Sites

Active site1721 By similarity
Active site5991 By similarity

Amino acid modifications

Modified residue111Phosphoserine By similarity
Modified residue7011Phosphoserine Ref.5

Experimental info

Sequence conflict4531E → D in AAP43628. Ref.2
Sequence conflict4561S → T in AAP43628. Ref.2
Sequence conflict7701W → R in CAD58726. Ref.1
Sequence conflict7991S → N in AAP43628. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q5GM68 [UniParc].

Last modified August 30, 2005. Version 2.
Checksum: D2F000BC8087D845

FASTA963109,753
        10         20         30         40         50         60 
MAARNLEKMA SIDAQLRLLA PGKVSEDDKL IEYDALLLDR FLDILQDLHG EDVREFVQEC 

        70         80         90        100        110        120 
YEVAADYDGN RNTEKLEELG NMLTSLDPGD SIVVTKSFSN MLSLANLAEE VQIAYRRRIK 

       130        140        150        160        170        180 
KLKKGDFADE ASATTESDIE ETLKRLLQLN KTPEEVFDAL KNQTVDLVLT AHPTQSVRRS 

       190        200        210        220        230        240 
LLQKFGRIRD CLTQLYAKDI TPDDKQELDE ALQREIQAAF RTDEIRRTPP TPQDEMRAGM 

       250        260        270        280        290        300 
SYFHETIWKG VPKFLRRVDT ALKNIGINER VPYNAPLIQF SSWMGGDRDG NPRVTPEVTR 

       310        320        330        340        350        360 
DVCLLARMMA ANLYFSQIED LMFEMSMWRC NEELRVRAER QRCAKRDAKH YIEFWKQIPA 

       370        380        390        400        410        420 
NEPYRAILGD VRDKLYNTRE RARQLLSSGV SDVPEDAVFT SVDQFLEPLE LCYRSLCDCG 

       430        440        450        460        470        480 
DRPIADGSLL DFLRQVSTFG LALVKLDIRQ ESERHSDVLD AITTHLGIGS YKEWSEDKRQ 

       490        500        510        520        530        540 
EWLLSELSGK RPLFGPDLPK TEEVADVLDT FKVISELPSD SFGAYIISMA TAPSDVLAVE 

       550        560        570        580        590        600 
LLQRECGITD PLRVVPLFEK LADLESAPAA VARLFSIEWY RNRINGKQEV MIGYSDSGKD 

       610        620        630        640        650        660 
AGRLSAAWQL YKTQEELVKV AKEYGVKLTM FHGRGGTVGR GGGPTHLAIL SQPPDTIHGQ 

       670        680        690        700        710        720 
LRVTVQGEVI EQSFGEEHLC FRTLQRFTAA TLEHGMHPPV SPKPEWRVLM DEMAIIATEE 

       730        740        750        760        770        780 
YRSVVFKEPR FVEYFRLATP ELEYGRMNIG SRPSKRKPSG GIESLRAIPW IFAWTQTRFH 

       790        800        810        820        830        840 
LPVWLGFGGA FKRVIQKDSK NLNMLKEMYN QWPFFRVTID LVEMVFAKGD PGIAALYDRL 

       850        860        870        880        890        900 
LVSEELQPFG EQLRVNYQET RRLLLQVAGH KDILEGDPYL RQRLQLRDPY ITTLNVCQAY 

       910        920        930        940        950        960 
TLKQIRDPSF HVKVRPHLSK DYMESSPAAE LVKLNPKSEY APGLEDTVIL TMKGIAAGMQ 


NTG 

« 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]"Cloning of Arabidopsis guard cell PEP carboxylase."
Zanor M.I., Plesch G., Mueller-Roeber B.
Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana."
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. expand/collapse author list , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.
Nature 402:761-768(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[4]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
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-701, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Root.
[6]"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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ532902 mRNA. Translation: CAD58726.1.
AY210895 mRNA. Translation: AAP43628.1.
AC007087 Genomic DNA. Translation: AAD22994.1. Sequence problems.
CP002685 Genomic DNA. Translation: AEC10145.1.
CP002685 Genomic DNA. Translation: AEC10146.1.
PIRH84855.
RefSeqNP_850372.4. NM_180041.4.
NP_850373.4. NM_180042.5.
UniGeneAt.14366.

3D structure databases

ProteinModelPortalQ5GM68.
SMRQ5GM68. Positions 6-963.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid4197. 2 interactions.
STRING3702.AT2G42600.2-P.

Proteomic databases

PaxDbQ5GM68.
PRIDEQ5GM68.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT2G42600.1; AT2G42600.1; AT2G42600.
AT2G42600.2; AT2G42600.2; AT2G42600.
GeneID818860.
KEGGath:AT2G42600.

Organism-specific databases

GeneFarm5061. 479.
TAIRAT2G42600.

Phylogenomic databases

eggNOGCOG2352.
HOGENOMHOG000238648.
InParanoidQ5GM68.
KOK01595.
OMAYNAPIIQ.
PhylomeDBQ5GM68.

Enzyme and pathway databases

BioCycARA:GQT-2357-MONOMER.
BRENDA4.1.1.31. 399.

Gene expression databases

ArrayExpressQ5GM68.
GenevestigatorQ5GM68.

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. 1 hit.
PROSITEPS00781. PEPCASE_1. 1 hit.
PS00393. PEPCASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCAPP2_ARATH
AccessionPrimary (citable) accession number: Q5GM68
Secondary accession number(s): Q8GVE9, Q9SIN0
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: August 30, 2005
Last modified: May 14, 2014
This is version 77 of the entry and version 2 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