Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(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)

P00864

- CAPP_ECOLI

UniProt

P00864 - CAPP_ECOLI

Protein

Phosphoenolpyruvate carboxylase

Gene

ppc

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

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

    Catalytic activityi

    Phosphate + oxaloacetate = H2O + phosphoenolpyruvate + HCO3-.

    Cofactori

    Magnesium.By similarity

    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.

    Sites

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

    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

    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 carboxylasePRO_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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00864.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the PEPCase type 1 family.Curated

    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

    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: October 1, 2014
    This is version 139 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