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P00864 (CAPP_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 138. Feed History...

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

Names and origin

Protein namesRecommended name:
Phosphoenolpyruvate carboxylase

Short name=PEPC
Short name=PEPCase
EC=4.1.1.31
Gene names
Name:ppc
Synonyms:glu
Ordered Locus Names:b3956, JW3928
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length883 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

The enzyme has distinct binding sites for each of the allosteric effectors such as acetyl-CoA, fructose 1,6-bisphosphate, guanosine 3'-diphosphate 5'-diphosphate, long chain fatty acids, and L-aspartate. HAMAP-Rule MF_00595

Subunit structure

Homotetramer.

Sequence similarities

Belongs to the PEPCase type 1 family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

uvrAP0A6981EBI-1133741,EBI-552091

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 883883Phosphoenolpyruvate carboxylase HAMAP-Rule MF_00595
PRO_0000166592

Sites

Active site1381
Active site5461 By similarity

Experimental info

Mutagenesis1381H → N: Loss of activity. Ref.8
Mutagenesis5791H → N: 29% of wild-type activity. Ref.7
Mutagenesis5791H → P: 5.4% of wild-type activity. Ref.7
Mutagenesis5871R → S: Loss of activity. Ref.9

Secondary structure

..................................................................................................................... 883
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00864 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 2620A776CF1F2EBC

FASTA88399,063
        10         20         30         40         50         60 
MNEQYSALRS NVSMLGKVLG ETIKDALGEH ILERVETIRK LSKSSRAGND ANRQELLTTL 

        70         80         90        100        110        120 
QNLSNDELLP VARAFSQFLN LANTAEQYHS ISPKGEAASN PEVIARTLRK LKNQPELSED 

       130        140        150        160        170        180 
TIKKAVESLS LELVLTAHPT EITRRTLIHK MVEVNACLKQ LDNKDIADYE HNQLMRRLRQ 

       190        200        210        220        230        240 
LIAQSWHTDE IRKLRPSPVD EAKWGFAVVE NSLWQGVPNY LRELNEQLEE NLGYKLPVEF 

       250        260        270        280        290        300 
VPVRFTSWMG GDRDGNPNVT ADITRHVLLL SRWKATDLFL KDIQVLVSEL SMVEATPELL 

       310        320        330        340        350        360 
ALVGEEGAAE PYRYLMKNLR SRLMATQAWL EARLKGEELP KPEGLLTQNE ELWEPLYACY 

       370        380        390        400        410        420 
QSLQACGMGI IANGDLLDTL RRVKCFGVPL VRIDIRQEST RHTEALGELT RYLGIGDYES 

       430        440        450        460        470        480 
WSEADKQAFL IRELNSKRPL LPRNWQPSAE TREVLDTCQV IAEAPQGSIA AYVISMAKTP 

       490        500        510        520        530        540 
SDVLAVHLLL KEAGIGFAMP VAPLFETLDD LNNANDVMTQ LLNIDWYRGL IQGKQMVMIG 

       550        560        570        580        590        600 
YSDSAKDAGV MAASWAQYQA QDALIKTCEK AGIELTLFHG RGGSIGRGGA PAHAALLSQP 

       610        620        630        640        650        660 
PGSLKGGLRV TEQGEMIRFK YGLPEITVSS LSLYTGAILE ANLLPPPEPK ESWRRIMDEL 

       670        680        690        700        710        720 
SVISCDVYRG YVRENKDFVP YFRSATPEQE LGKLPLGSRP AKRRPTGGVE SLRAIPWIFA 

       730        740        750        760        770        780 
WTQNRLMLPA WLGAGTALQK VVEDGKQSEL EAMCRDWPFF STRLGMLEMV FAKADLWLAE 

       790        800        810        820        830        840 
YYDQRLVDKA LWPLGKELRN LQEEDIKVVL AIANDSHLMA DLPWIAESIQ LRNIYTDPLN 

       850        860        870        880 
VLQAELLHRS RQAEKEGQEP DPRVEQALMV TIAGIAAGMR NTG 

« Hide

References

« Hide 'large scale' references
[1]"The primary structure of phosphoenolpyruvate carboxylase of Escherichia coli. Nucleotide sequence of the ppc gene and deduced amino acid sequence."
Fujita N., Miwa T., Ishijima S., Izui K., Katsuki H.
J. Biochem. 95:909-916(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes."
Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.
Nucleic Acids Res. 21:5408-5417(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"Structural and biochemical characterization of the Escherichia coli argE gene product."
Meinnel T., Schmitt E., Mechulam Y., Blanquet S.
J. Bacteriol. 174:2323-2331(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-37.
Strain: K12.
[6]"Promoter analysis of the phosphoenolpyruvate carboxylase gene of Escherichia coli."
Izui K., Miwa T., Kajitani M., Fujita N., Sabe H., Ishihama I., Katsuki H.
Nucleic Acids Res. 13:59-71(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-41.
[7]"Site-directed mutagenesis of phosphoenolpyruvate carboxylase from E. coli: the role of His579 in the catalytic and regulatory functions."
Terada K., Murata T., Izui K.
J. Biochem. 109:49-54(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF HIS-579.
[8]"Site-directed mutagenesis of the conserved histidine residue of phosphoenolpyruvate carboxylase. His138 is essential for the second partial reaction."
Terada K., Izui K.
Eur. J. Biochem. 202:797-803(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF HIS-138.
[9]"Catalytic role of an arginine residue in the highly conserved and unique sequence of phosphoenolpyruvate carboxylase."
Yano M., Terada K., Umiji K., Izui K.
J. Biochem. 117:1196-1200(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF ARG-587.
[10]"First crystallization of a phosphoenolpyruvate carboxylase from Escherichia coli."
Inoue M., Hayashi M., Sugimoto M., Harada S., Kai Y., Kasai N., Terada K., Izui K.
J. Mol. Biol. 208:509-510(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: CRYSTALLIZATION.
[11]"Escherichia coli proteome analysis using the gene-protein database."
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY 2D-GEL.
[12]"Three-dimensional structure of phosphoenolpyruvate carboxylase: a proposed mechanism for allosteric inhibition."
Kai Y., Matsumura H., Inoue T., Terada K., Nagara Y., Yoshinaga T., Kihara A., Tsumura K., Izui K.
Proc. Natl. Acad. Sci. U.S.A. 96:823-828(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X05903 Genomic DNA. Translation: CAA29332.1.
X55417 Genomic DNA. No translation available.
U00006 Genomic DNA. Translation: AAC43062.1.
U00096 Genomic DNA. Translation: AAC76938.1.
AP009048 Genomic DNA. Translation: BAE77355.1.
X01700 Genomic DNA. Translation: CAA25847.1.
PIRQYEC. A01083.
RefSeqNP_418391.1. NC_000913.3.
YP_491496.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FIYX-ray2.80A1-883[»]
1JQNX-ray2.35A1-883[»]
1QB4X-ray2.60A1-883[»]
ProteinModelPortalP00864.
SMRP00864. Positions 4-883.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-10538N.
IntActP00864. 3 interactions.
STRING511145.b3956.

Proteomic databases

PaxDbP00864.
PRIDEP00864.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76938; AAC76938; b3956.
BAE77355; BAE77355; BAE77355.
GeneID12933655.
948457.
KEGGecj:Y75_p3232.
eco:b3956.
PATRIC32123433. VBIEscCol129921_4077.

Organism-specific databases

EchoBASEEB0749.
EcoGeneEG10756. ppc.

Phylogenomic databases

eggNOGCOG2352.
HOGENOMHOG000238648.
KOK01595.
OMAELSTISC.
OrthoDBEOG6TJ7T8.
PhylomeDBP00864.

Enzyme and pathway databases

BioCycEcoCyc:PEPCARBOX-MONOMER.
ECOL316407:JW3928-MONOMER.
MetaCyc:PEPCARBOX-MONOMER.

Gene expression databases

GenevestigatorP00864.

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...

Other

EvolutionaryTraceP00864.
PROP00864.

Entry information

Entry nameCAPP_ECOLI
AccessionPrimary (citable) accession number: P00864
Secondary accession number(s): Q2M8Q1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: May 14, 2014
This is version 138 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene