SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P00864

- CAPP_ECOLI

UniProt

P00864 - CAPP_ECOLI

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Phosphoenolpyruvate carboxylase

Gene
ppc, glu, b3956, JW3928
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.UniRule annotation

Catalytic activityi

Phosphate + oxaloacetate = H2O + phosphoenolpyruvate + HCO3-.UniRule annotation

Cofactori

Magnesium By similarity.UniRule annotation

Enzyme regulationi

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.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei138 – 1381
Active sitei546 – 5461 By similarity

GO - Molecular functioni

  1. magnesium ion binding Source: UniProtKB-HAMAP
  2. phosphoenolpyruvate carboxylase activity Source: EcoCyc

GO - Biological processi

  1. carbon fixation Source: UniProtKB-HAMAP
  2. oxaloacetate metabolic process Source: UniProtKB-HAMAP
  3. tricarboxylic acid cycle Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Carbon dioxide fixation

Keywords - Ligandi

Magnesium

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoenolpyruvate carboxylase (EC:4.1.1.31)
Short name:
PEPC
Short name:
PEPCase
Gene namesi
Name:ppc
Synonyms:glu
Ordered Locus Names:b3956, JW3928
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10756. ppc.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: EcoCyc
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi138 – 1381H → N: Loss of activity. 1 Publication
Mutagenesisi579 – 5791H → N: 29% of wild-type activity. 1 Publication
Mutagenesisi579 – 5791H → P: 5.4% of wild-type activity. 1 Publication
Mutagenesisi587 – 5871R → S: Loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 883883Phosphoenolpyruvate carboxylaseUniRule annotationPRO_0000166592Add
BLAST

Proteomic databases

PaxDbiP00864.
PRIDEiP00864.

Expressioni

Gene expression databases

GenevestigatoriP00864.

Interactioni

Subunit structurei

Homotetramer.

Binary interactionsi

WithEntry#Exp.IntActNotes
uvrAP0A6981EBI-1133741,EBI-552091

Protein-protein interaction databases

DIPiDIP-10538N.
IntActiP00864. 3 interactions.
STRINGi511145.b3956.

Structurei

Secondary structure

1
883
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 2621
Turni27 – 293
Helixi30 – 4617
Helixi50 – 6112
Helixi65 – 9127
Turni93 – 964
Helixi102 – 11211
Helixi119 – 1279
Beta strandi131 – 1355
Beta strandi143 – 1453
Helixi148 – 16114
Helixi168 – 18720
Helixi198 – 21114
Helixi213 – 23119
Beta strandi243 – 2475
Turni249 – 2513
Helixi261 – 28929
Helixi297 – 3037
Beta strandi307 – 3104
Helixi311 – 33424
Helixi349 – 36517
Helixi369 – 3724
Helixi375 – 38511
Turni386 – 3894
Beta strandi390 – 3989
Helixi399 – 41214
Helixi418 – 4203
Helixi423 – 43513
Helixi449 – 46315
Beta strandi468 – 4758
Helixi480 – 49112
Turni492 – 4943
Beta strandi501 – 5055
Helixi508 – 52316
Helixi525 – 5306
Turni531 – 5333
Beta strandi534 – 5396
Helixi541 – 5488
Helixi550 – 57122
Beta strandi574 – 5796
Helixi584 – 5863
Helixi589 – 5979
Turni601 – 6066
Beta strandi608 – 6125
Helixi614 – 6163
Helixi617 – 6215
Helixi624 – 64320
Helixi651 – 67222
Helixi678 – 6858
Helixi688 – 6936
Beta strandi697 – 6993
Helixi709 – 7113
Helixi714 – 72310
Helixi728 – 7303
Turni731 – 7333
Helixi734 – 7429
Turni743 – 7453
Helixi747 – 75610
Helixi758 – 77316
Helixi776 – 78611
Turni789 – 7913
Helixi792 – 81221
Turni818 – 8214
Helixi823 – 85634
Helixi862 – 87918

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FIYX-ray2.80A1-883[»]
1JQNX-ray2.35A1-883[»]
1QB4X-ray2.60A1-883[»]
ProteinModelPortaliP00864.
SMRiP00864. Positions 4-883.

Miscellaneous databases

EvolutionaryTraceiP00864.

Family & Domainsi

Sequence similaritiesi

Belongs to the PEPCase type 1 family.

Phylogenomic databases

eggNOGiCOG2352.
HOGENOMiHOG000238648.
KOiK01595.
OMAiELSTISC.
OrthoDBiEOG6TJ7T8.
PhylomeDBiP00864.

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. 1 hit.
PROSITEiPS00781. PEPCASE_1. 1 hit.
PS00393. PEPCASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P00864-1 [UniParc]FASTAAdd to Basket

« Hide

MNEQYSALRS NVSMLGKVLG ETIKDALGEH ILERVETIRK LSKSSRAGND    50
ANRQELLTTL QNLSNDELLP VARAFSQFLN LANTAEQYHS ISPKGEAASN 100
PEVIARTLRK LKNQPELSED TIKKAVESLS LELVLTAHPT EITRRTLIHK 150
MVEVNACLKQ LDNKDIADYE HNQLMRRLRQ LIAQSWHTDE IRKLRPSPVD 200
EAKWGFAVVE NSLWQGVPNY LRELNEQLEE NLGYKLPVEF VPVRFTSWMG 250
GDRDGNPNVT ADITRHVLLL SRWKATDLFL KDIQVLVSEL SMVEATPELL 300
ALVGEEGAAE PYRYLMKNLR SRLMATQAWL EARLKGEELP KPEGLLTQNE 350
ELWEPLYACY QSLQACGMGI IANGDLLDTL RRVKCFGVPL VRIDIRQEST 400
RHTEALGELT RYLGIGDYES WSEADKQAFL IRELNSKRPL LPRNWQPSAE 450
TREVLDTCQV IAEAPQGSIA AYVISMAKTP SDVLAVHLLL KEAGIGFAMP 500
VAPLFETLDD LNNANDVMTQ LLNIDWYRGL IQGKQMVMIG YSDSAKDAGV 550
MAASWAQYQA QDALIKTCEK AGIELTLFHG RGGSIGRGGA PAHAALLSQP 600
PGSLKGGLRV TEQGEMIRFK YGLPEITVSS LSLYTGAILE ANLLPPPEPK 650
ESWRRIMDEL SVISCDVYRG YVRENKDFVP YFRSATPEQE LGKLPLGSRP 700
AKRRPTGGVE SLRAIPWIFA WTQNRLMLPA WLGAGTALQK VVEDGKQSEL 750
EAMCRDWPFF STRLGMLEMV FAKADLWLAE YYDQRLVDKA LWPLGKELRN 800
LQEEDIKVVL AIANDSHLMA DLPWIAESIQ LRNIYTDPLN VLQAELLHRS 850
RQAEKEGQEP DPRVEQALMV TIAGIAAGMR NTG 883
Length:883
Mass (Da):99,063
Last modified:July 21, 1986 - v1
Checksum:i2620A776CF1F2EBC
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiA01083. QYEC.
RefSeqiNP_418391.1. NC_000913.3.
YP_491496.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76938; AAC76938; b3956.
BAE77355; BAE77355; BAE77355.
GeneIDi12933655.
948457.
KEGGiecj:Y75_p3232.
eco:b3956.
PATRICi32123433. VBIEscCol129921_4077.

Cross-referencesi

Web resourcesi

Worthington enzyme manual

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
PIRi A01083. QYEC.
RefSeqi NP_418391.1. NC_000913.3.
YP_491496.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1FIY X-ray 2.80 A 1-883 [» ]
1JQN X-ray 2.35 A 1-883 [» ]
1QB4 X-ray 2.60 A 1-883 [» ]
ProteinModelPortali P00864.
SMRi P00864. Positions 4-883.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-10538N.
IntActi P00864. 3 interactions.
STRINGi 511145.b3956.

Proteomic databases

PaxDbi P00864.
PRIDEi P00864.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC76938 ; AAC76938 ; b3956 .
BAE77355 ; BAE77355 ; BAE77355 .
GeneIDi 12933655.
948457.
KEGGi ecj:Y75_p3232.
eco:b3956.
PATRICi 32123433. VBIEscCol129921_4077.

Organism-specific databases

EchoBASEi EB0749.
EcoGenei EG10756. ppc.

Phylogenomic databases

eggNOGi COG2352.
HOGENOMi HOG000238648.
KOi K01595.
OMAi ELSTISC.
OrthoDBi EOG6TJ7T8.
PhylomeDBi P00864.

Enzyme and pathway databases

BioCyci EcoCyc:PEPCARBOX-MONOMER.
ECOL316407:JW3928-MONOMER.
MetaCyc:PEPCARBOX-MONOMER.

Miscellaneous databases

EvolutionaryTracei P00864.
PROi P00864.

Gene expression databases

Genevestigatori P00864.

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. 1 hit.
PROSITEi PS00781. PEPCASE_1. 1 hit.
PS00393. PEPCASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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).

Entry informationi

Entry nameiCAPP_ECOLI
AccessioniPrimary (citable) accession number: P00864
Secondary accession number(s): Q2M8Q1
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Allosteric enzyme, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi