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P30694 (CAPPA_FLATR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
C4 phosphoenolpyruvate carboxylase
Short name=C4 PEPC
Short name=C4 PEPCase
Short name=ppcA
EC=4.1.1.31
Alternative name(s):
Photosynthetic PEPCase
Gene names
Name:PPCA
OrganismFlaveria trinervia (Clustered yellowtops) (Oedera trinervia)
Taxonomic identifier4227 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › campanulids › Asterales › Asteraceae › Asteroideae › Heliantheae alliance › Tageteae › Flaveria

Protein attributes

Sequence length966 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Forms oxaloacetate through the carboxylation of phosphoenolpyruvate (PEP). Catalyzes the first step of C4 photosynthesis.

Catalytic activity

Phosphate + oxaloacetate = H2O + phosphoenolpyruvate + HCO3-.

Cofactor

Magnesium By similarity.

Enzyme regulation

5 fold activation by the allosteric regulator glucose-6-phosphate. Low sensitivity to inhibition by L-malate. Up-regulated by light-reversible phosphorylation By similarity.

Pathway

Photosynthesis; C4 acid pathway.

Subunit structure

Homotetramer.

Subcellular location

Cytoplasm By similarity.

Tissue specificity

Expressed in mesophyll cells, but not in bundle-sheath, roots, stems and flowers. Ref.1 Ref.7

Domain

Region 2 (296-437) and region 5 (645-966) are involved in the acquisition of C4-specific properties. Region 5 (645-966) is involved in L-malate tolerance.

Miscellaneous

Ser-774 is strongly involved in determining allosteric behavior of C4 PEPC.

Sequence similarities

Belongs to the PEPCase type 1 family.

Biophysicochemical properties

Kinetic parameters:

Vmax=27 µmol/min/mg enzyme Ref.9

Ontologies

Keywords
   Biological processCarbon dioxide fixation
Photosynthesis
   Cellular componentCytoplasm
   LigandMagnesium
   Molecular functionLyase
   PTMPhosphoprotein
   Technical term3D-structure
Allosteric enzyme
Gene Ontology (GO)
   Biological_processC4 photosynthesis

Traceable author statement Ref.8. Source: UniProtKB

tricarboxylic acid cycle

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionphosphoenolpyruvate carboxylase activity

Inferred from direct assay Ref.8. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 966966C4 phosphoenolpyruvate carboxylase
PRO_0000166666

Sites

Active site1721 By similarity
Active site6001 By similarity

Amino acid modifications

Modified residue111Phosphoserine By similarity

Experimental info

Mutagenesis4501R → G: Loss of catalytic activity. Ref.6
Mutagenesis6001K → R or T: Decreased bicarbonate-binding and lower catalytic activity. Ref.5
Mutagenesis7671R → G: Loss of catalytic activity. Ref.6
Mutagenesis7741S → A: Alteration of C4-specific kinetics, but no effect on L-malate tolerance. Ref.8 Ref.10
Mutagenesis8291K → G: Decreased substrate binding and lower catalytic activity. Ref.6
Sequence conflict771E → D in CAA45504. Ref.3
Sequence conflict881T → P in CAA45504. Ref.3
Sequence conflict1111L → V in CAA45504. Ref.3
Sequence conflict1771V → I in CAA45504. Ref.3
Sequence conflict2911N → KH in CAA45504. Ref.3
Sequence conflict3581R → Q in CAA45504. Ref.3
Sequence conflict3971E → K in CAA81072. Ref.4
Sequence conflict4201C → S in CAA45504. Ref.3
Sequence conflict5131K → N in CAA45504. Ref.3

Secondary structure

1 ..................................................................................................................... 966
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P30694 [UniParc].

Last modified February 1, 1996. Version 2.
Checksum: 252F7B674BC94F47

FASTA966110,406
        10         20         30         40         50         60 
MANRNVEKLA SIDAQLRLLV PGKVSEDDKL VEYDALLLDK FLDILQDLHG EDLKEAVQQC 

        70         80         90        100        110        120 
YELSAEYEGK HDPKKLEELG SLLTSLDTGD SIVIAKAFSH MLNLANLAEE LQIAYRRRIK 

       130        140        150        160        170        180 
LKSGDFADEA NATTESDIEE TFKRLVHKLN KSPEEVFDAL KNQTVELVLT AHPTQSVRRS 

       190        200        210        220        230        240 
LLQKHGRIRN CLAQLYAKDI TPDDKQELDE ALHREIQAAF RTDEIRRTPP TPQDEMRAGM 

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

       310        320        330        340        350        360 
DVCLLARMMT SNMYFSQIED LMIEMSMWRC NSELRVRAEE LYRTARKDVK HYIEFWKRIP 

       370        380        390        400        410        420 
PNQPYRVILG DVRDKLYNTR ERSRHLLVDG KSDIPDEAVY TNVEQLLEPL ELCYRSLCDC 

       430        440        450        460        470        480 
GDHVIADGSL LDFLRQVSTF GLSLVKLDIR QESDRHTEVL DAITQHLGIG SYREWSEEKR 

       490        500        510        520        530        540 
QEWLLAELSG KRPLIGPDLP KTEEVKDCLD TFKVLAELPS DCFGAYIISM ATSTSDVLAV 

       550        560        570        580        590        600 
ELLQREYHIK HPLRVVPLFE KLADLEAAPA AMTRLFSMDW YRNRIDGKQE VMIGYSDSGK 

       610        620        630        640        650        660 
DAGRFSAAWQ LYKTQEQIVK IAKEFGVKLV IFHGRGGTVG RGGGPTHLAL LSQPPDTING 

       670        680        690        700        710        720 
SLRVTVQGEV IEQSFGEEHL CFRTLQRFCA ATLEHGMNPP ISPRPEWREL MDQMAVVATE 

       730        740        750        760        770        780 
EYRSVVFKEP RFVEYFRLAT PELEFGRMNI GSRPSKRKPS GGIESLRAIP WIFSWTQTRF 

       790        800        810        820        830        840 
HLPVWLGFGA AFKHAIQKDS KNLQMLQEMY KTWPFFRVTI DLVEMVFAKG NPGIAALNDK 

       850        860        870        880        890        900 
LLVSEDLRPF GESLRANYEE TKNYLLKIAG HKDLLEGDPY LKQGIRLRDP YITTLNVCQA 

       910        920        930        940        950        960 
YTLKRIRDPN YHVTLRPHIS KEYAAEPSKP ADELIHLNPT SEYAPGLEDT LILTMKGIAA 


GMQNTG

« Hide

References

[1]"Multiple cDNAs of phosphoenolpyruvate carboxylase in the C4 dicot Flaveria trinervia."
Poetsch W., Hermans J., Westhoff P.
FEBS Lett. 292:133-136(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Tissue: Leaf.
[2]Poetsch W.
Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[3]"Homologous genes for the C4 isoform of phosphoenolpyruvate carboxylase in a C3 and a C4 Flaveria species."
Hermans J., Westhoff P.
Mol. Gen. Genet. 234:275-284(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]Bauwe H.
Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Leaf.
[5]"Site-directed mutagenesis of Lys600 in phosphoenolpyruvate carboxylase of Flaveria trinervia: its roles in catalytic and regulatory functions."
Gao Y., Woo K.C.
FEBS Lett. 375:95-98(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF LYS-600.
[6]"Site-directed mutagenesis of Flaveria trinervia phosphoenolpyruvate carboxylase: Arg450 and Arg767 are essential for catalytic activity and Lys829 affects substrate binding."
Gao Y., Woo K.C.
FEBS Lett. 392:285-288(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF ARG-450; ARG-767 AND LYS-829.
[7]"The phosphoenolpyruvate carboxylase (ppc) gene family of Flaveria trinervia (C4) and F. pringlei (C3): molecular characterization and expression analysis of the ppcB and ppcC genes."
Ernst K., Westhoff P.
Plant Mol. Biol. 34:427-443(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[8]"Evolution of C4 phosphoenolpyruvate carboxylase in Flaveria, a conserved serine residue in the carboxyl-terminal part of the enzyme is a major determinant for C4-specific characteristics."
Blasing O.E., Westhoff P., Svensson P.
J. Biol. Chem. 275:27917-27923(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION, MUTAGENESIS OF SER-774.
[9]"The non-photosynthetic phosphoenolpyruvate carboxylases of the C4 dicot Flaveria trinervia -- implications for the evolution of C4 photosynthesis."
Blasing O.E., Ernst K., Streubel M., Westhoff P., Svensson P.
Planta 215:448-456(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
[10]"Evolution of C(4) phosphoenolpyruvate carboxylase in Flaveria: determinants for high tolerance towards the inhibitor L-malate."
Jacobs B., Engelmann S., Westhoff P., Gowik U.
Plant Cell Environ. 31:793-803(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION, MUTAGENESIS OF SER-774.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X61304 mRNA. Translation: CAA43601.1.
X64143 Genomic DNA. Translation: CAA45504.1.
Z25853 mRNA. Translation: CAA81072.1.
PIRS18318.
S25082.
S37072.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3ZGEX-ray2.49A/B1-966[»]
ProteinModelPortalP30694.
SMRP30694. Positions 31-966.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00322.

Family and domain databases

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

Entry information

Entry nameCAPPA_FLATR
AccessionPrimary (citable) accession number: P30694
Secondary accession number(s): Q01648, Q42730
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: February 1, 1996
Last modified: May 29, 2013
This is version 78 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents