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Protein

Phosphoenolpyruvate carboxykinase [ATP]

Gene

pckA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the gluconeogenesis. Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP) through direct phosphoryl transfer between the nucleoside triphosphate and OAA.UniRule annotation3 Publications

Catalytic activityi

ATP + oxaloacetate = ADP + phosphoenolpyruvate + CO2.UniRule annotation1 Publication

Cofactori

Mn2+UniRule annotation5 PublicationsNote: Binds 1 Mn2+ ion per subunit.UniRule annotation5 Publications

Enzyme regulationi

Allosterically activated by calcium. It may represent the only case of a monomeric, allosteric enzyme.4 Publications

Kineticsi

  1. KM=3.8 µM for manganese (at 31 degrees Celsius and pH 7.5)2 Publications
  2. KM=0.11 mM for calcium (at 31 degrees Celsius and pH 7.5)2 Publications
  3. KM=0.31 mM for OAA (at 31 degrees Celsius and pH 7.5)2 Publications
  4. KM=0.51 mM for OAA (at pH 7.5)2 Publications
  5. KM=1.4 mM for magnesium (at 31 degrees Celsius and pH 7.5)2 Publications
  6. KM=11 mM for PEP (at pH 7.5)2 Publications

    Pathway:igluconeogenesis

    This protein is involved in the pathway gluconeogenesis, which is part of Carbohydrate biosynthesis.UniRule annotation
    View all proteins of this organism that are known to be involved in the pathway gluconeogenesis and in Carbohydrate biosynthesis.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei65 – 651SubstrateUniRule annotation1 Publication
    Metal bindingi149 – 1491Calcium; via carbonyl oxygenBy similarity
    Metal bindingi150 – 1501Calcium; via carbonyl oxygenBy similarity
    Metal bindingi152 – 1521Calcium; via carbonyl oxygenBy similarity
    Binding sitei207 – 2071SubstrateUniRule annotation1 Publication
    Metal bindingi213 – 2131ManganeseUniRule annotation1 Publication
    Binding sitei213 – 2131ATPUniRule annotation6 Publications
    Binding sitei213 – 2131SubstrateUniRule annotation1 Publication
    Metal bindingi232 – 2321Manganese; via tele nitrogenUniRule annotation1 Publication
    Binding sitei232 – 2321ATPUniRule annotation6 Publications
    Metal bindingi269 – 2691ManganeseUniRule annotation1 Publication
    Metal bindingi283 – 2831Calcium; via carbonyl oxygenBy similarity
    Binding sitei297 – 2971ATPUniRule annotation6 Publications
    Binding sitei333 – 3331ATPUniRule annotation6 Publications
    Binding sitei333 – 3331SubstrateUniRule annotation1 Publication
    Binding sitei455 – 4551ATPUniRule annotation6 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi248 – 2569ATPUniRule annotation6 Publications
    Nucleotide bindingi449 – 4502ATPUniRule annotation6 Publications

    GO - Molecular functioni

    • ATP binding Source: UniProtKB-HAMAP
    • calcium ion binding Source: EcoCyc
    • magnesium ion binding Source: EcoCyc
    • phosphoenolpyruvate carboxykinase (ATP) activity Source: EcoCyc

    GO - Biological processi

    • gluconeogenesis Source: EcoCyc
    Complete GO annotation...

    Keywords - Molecular functioni

    Decarboxylase, Lyase

    Keywords - Biological processi

    Gluconeogenesis

    Keywords - Ligandi

    ATP-binding, Calcium, Magnesium, Manganese, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:PEPCARBOXYKIN-MONOMER.
    ECOL316407:JW3366-MONOMER.
    MetaCyc:PEPCARBOXYKIN-MONOMER.
    BRENDAi4.1.1.49. 2026.
    UniPathwayiUPA00138.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphoenolpyruvate carboxykinase [ATP]UniRule annotation (EC:4.1.1.49UniRule annotation)
    Short name:
    PCKUniRule annotation
    Short name:
    PEP carboxykinaseUniRule annotation
    Short name:
    PEPCKUniRule annotation
    Gene namesi
    Name:pckAUniRule annotation
    Synonyms:pck
    Ordered Locus Names:b3403, JW3366
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG10688. pck.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi65 – 651R → Q: Slightly lower catalytic efficiency compared to wild-type and the affinity binding for OAA is 330-fold higher than for wild-type. 1 Publication
    Mutagenesisi268 – 2681D → N in PCK51; altered-activity mutant that catalyzes the conversion from oxaloacetate to pyruvate (OAA decarboxylase activity). 1 Publication
    Mutagenesisi284 – 2841G → S in PCK53; shows reduced-activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 540540Phosphoenolpyruvate carboxykinase [ATP]PRO_0000203818Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei87 – 871N6-acetyllysineUniRule annotation1 Publication
    Modified residuei523 – 5231N6-acetyllysineUniRule annotation1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiP22259.
    PRIDEiP22259.

    Expressioni

    Inductioni

    Induced upon entry into stationary phase and by cyclic AMP (cAMP). Repressed by glucose (catabolite repression) and by CsrA.2 Publications

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation9 Publications

    Protein-protein interaction databases

    IntActiP22259. 4 interactions.
    STRINGi511145.b3403.

    Structurei

    Secondary structure

    1
    540
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni5 – 73Combined sources
    Helixi9 – 146Combined sources
    Beta strandi23 – 264Combined sources
    Helixi29 – 379Combined sources
    Helixi43 – 453Combined sources
    Beta strandi47 – 493Combined sources
    Beta strandi55 – 573Combined sources
    Helixi67 – 693Combined sources
    Beta strandi70 – 734Combined sources
    Turni76 – 816Combined sources
    Beta strandi87 – 904Combined sources
    Beta strandi95 – 973Combined sources
    Helixi99 – 11315Combined sources
    Beta strandi118 – 12811Combined sources
    Turni129 – 1313Combined sources
    Beta strandi133 – 1408Combined sources
    Helixi142 – 15110Combined sources
    Helixi157 – 1615Combined sources
    Beta strandi166 – 1727Combined sources
    Turni178 – 1847Combined sources
    Beta strandi186 – 1883Combined sources
    Beta strandi190 – 1945Combined sources
    Turni195 – 1984Combined sources
    Beta strandi199 – 2046Combined sources
    Helixi209 – 22214Combined sources
    Helixi224 – 2263Combined sources
    Beta strandi229 – 2313Combined sources
    Beta strandi233 – 2375Combined sources
    Beta strandi243 – 2475Combined sources
    Helixi254 – 2585Combined sources
    Beta strandi263 – 2697Combined sources
    Beta strandi271 – 2744Combined sources
    Beta strandi277 – 2815Combined sources
    Beta strandi283 – 2886Combined sources
    Turni294 – 2963Combined sources
    Helixi298 – 3025Combined sources
    Beta strandi309 – 3124Combined sources
    Beta strandi314 – 3163Combined sources
    Turni317 – 3193Combined sources
    Beta strandi320 – 3223Combined sources
    Beta strandi333 – 3375Combined sources
    Helixi338 – 3403Combined sources
    Beta strandi341 – 3444Combined sources
    Beta strandi347 – 3526Combined sources
    Beta strandi354 – 3618Combined sources
    Beta strandi370 – 3734Combined sources
    Helixi376 – 38510Combined sources
    Beta strandi387 – 3915Combined sources
    Helixi394 – 3963Combined sources
    Beta strandi401 – 4055Combined sources
    Helixi407 – 4093Combined sources
    Helixi411 – 4133Combined sources
    Helixi418 – 43215Combined sources
    Beta strandi435 – 4406Combined sources
    Beta strandi447 – 4493Combined sources
    Helixi452 – 46312Combined sources
    Helixi466 – 4694Combined sources
    Beta strandi472 – 4754Combined sources
    Turni476 – 4794Combined sources
    Beta strandi480 – 4845Combined sources
    Helixi491 – 4944Combined sources
    Helixi496 – 4994Combined sources
    Beta strandi500 – 5023Combined sources
    Helixi503 – 52119Combined sources
    Helixi522 – 5243Combined sources
    Helixi528 – 5336Combined sources
    Helixi534 – 5363Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AQ2X-ray1.90A1-540[»]
    1AYLX-ray1.80A1-540[»]
    1K3CX-ray2.00A1-540[»]
    1K3DX-ray2.00A1-540[»]
    1OENX-ray1.90A1-538[»]
    1OS1X-ray1.80A1-540[»]
    2OLQX-ray1.94A1-540[»]
    2OLRX-ray1.60A1-540[»]
    2PXZX-ray2.23X1-540[»]
    2PY7X-ray2.20X1-540[»]
    ProteinModelPortaliP22259.
    SMRiP22259. Positions 6-540.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP22259.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the phosphoenolpyruvate carboxykinase [ATP] family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG1866.
    HOGENOMiHOG000271471.
    InParanoidiP22259.
    KOiK01610.
    OMAiRFIVKEP.
    OrthoDBiEOG6DG2RK.
    PhylomeDBiP22259.

    Family and domain databases

    Gene3Di3.40.449.10. 1 hit.
    3.90.228.20. 2 hits.
    HAMAPiMF_00453. PEPCK_ATP.
    InterProiIPR001272. PEP_carboxykinase_ATP.
    IPR013035. PEP_carboxykinase_C.
    IPR008210. PEP_carboxykinase_N.
    IPR015994. PEPCK_ATP_CS.
    [Graphical view]
    PfamiPF01293. PEPCK_ATP. 1 hit.
    [Graphical view]
    PIRSFiPIRSF006294. PEP_crbxkin. 1 hit.
    SUPFAMiSSF68923. SSF68923. 1 hit.
    TIGRFAMsiTIGR00224. pckA. 1 hit.
    PROSITEiPS00532. PEPCK_ATP. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P22259-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MRVNNGLTPQ ELEAYGISDV HDIVYNPSYD LLYQEELDPS LTGYERGVLT
    60 70 80 90 100
    NLGAVAVDTG IFTGRSPKDK YIVRDDTTRD TFWWADKGKG KNDNKPLSPE
    110 120 130 140 150
    TWQHLKGLVT RQLSGKRLFV VDAFCGANPD TRLSVRFITE VAWQAHFVKN
    160 170 180 190 200
    MFIRPSDEEL AGFKPDFIVM NGAKCTNPQW KEQGLNSENF VAFNLTERMQ
    210 220 230 240 250
    LIGGTWYGGE MKKGMFSMMN YLLPLKGIAS MHCSANVGEK GDVAVFFGLS
    260 270 280 290 300
    GTGKTTLSTD PKRRLIGDDE HGWDDDGVFN FEGGCYAKTI KLSKEAEPEI
    310 320 330 340 350
    YNAIRRDALL ENVTVREDGT IDFDDGSKTE NTRVSYPIYH IDNIVKPVSK
    360 370 380 390 400
    AGHATKVIFL TADAFGVLPP VSRLTADQTQ YHFLSGFTAK LAGTERGITE
    410 420 430 440 450
    PTPTFSACFG AAFLSLHPTQ YAEVLVKRMQ AAGAQAYLVN TGWNGTGKRI
    460 470 480 490 500
    SIKDTRAIID AILNGSLDNA ETFTLPMFNL AIPTELPGVD TKILDPRNTY
    510 520 530 540
    ASPEQWQEKA ETLAKLFIDN FDKYTDTPAG AALVAAGPKL
    Length:540
    Mass (Da):59,643
    Last modified:November 1, 1995 - v2
    Checksum:iA744D90899F6A8A5
    GO

    Sequence cautioni

    The sequence AAA24301.1 differs from that shown. Reason: Frameshift at position 456. Translation N-terminally extended.Curated

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti67 – 726PKDKYI → QKISIS in AAA24301 (PubMed:1701430).Curated
    Sequence conflicti192 – 1943AFN → R AA sequence (PubMed:1701430).Curated
    Sequence conflicti197 – 2037ERMQLIG → DRAHAADC AA sequence (PubMed:1701430).Curated
    Sequence conflicti233 – 2331C → S in AAA24301 (PubMed:1701430).Curated
    Sequence conflicti252 – 2521T → N in AAA24301 (PubMed:1701430).Curated
    Sequence conflicti256 – 2605TLSTD → AFPR in AAA24301 (PubMed:1701430).Curated
    Sequence conflicti281 – 2855FEGGC → LKAAG in AAA24301 (PubMed:1701430).Curated
    Sequence conflicti302 – 3076NAIRRD → KLSVVM in AAA24301 (PubMed:1701430).Curated
    Sequence conflicti346 – 3461K → R in AAA24301 (PubMed:1701430).Curated
    Sequence conflicti354 – 3596ATKVIF → GRRLSL in AAA24301 (PubMed:1701430).Curated
    Sequence conflicti363 – 3631D → H in AAA24301 (PubMed:1701430).Curated
    Sequence conflicti446 – 4461T → S in AAA24301 (PubMed:1701430).Curated
    Sequence conflicti449 – 4491R → S in AAA24301 (PubMed:1701430).Curated
    Sequence conflicti460 – 4678DAILNGSL → RRHPQRFV (PubMed:6292200).Curated
    Sequence conflicti499 – 4991T → R (PubMed:6292200).Curated

    Mass spectrometryi

    Molecular mass is 59656 Da from positions 1 - 540. Determined by ESI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M59823 Genomic DNA. Translation: AAA24301.1. Frameshift.
    U18997 Genomic DNA. Translation: AAA58200.1.
    U00096 Genomic DNA. Translation: AAC76428.1.
    AP009048 Genomic DNA. Translation: BAE77888.1.
    J01656 Unassigned RNA. No translation available.
    S76268 Genomic DNA. Translation: AAB33745.2.
    S76269 Genomic DNA. Translation: AAB33746.2.
    U21325 Genomic DNA. Translation: AAA95999.1.
    PIRiF65135.
    RefSeqiNP_417862.1. NC_000913.3.
    WP_001265681.1. NZ_CP010445.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76428; AAC76428; b3403.
    BAE77888; BAE77888; BAE77888.
    GeneIDi945667.
    KEGGieco:b3403.
    PATRICi32122242. VBIEscCol129921_3498.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M59823 Genomic DNA. Translation: AAA24301.1. Frameshift.
    U18997 Genomic DNA. Translation: AAA58200.1.
    U00096 Genomic DNA. Translation: AAC76428.1.
    AP009048 Genomic DNA. Translation: BAE77888.1.
    J01656 Unassigned RNA. No translation available.
    S76268 Genomic DNA. Translation: AAB33745.2.
    S76269 Genomic DNA. Translation: AAB33746.2.
    U21325 Genomic DNA. Translation: AAA95999.1.
    PIRiF65135.
    RefSeqiNP_417862.1. NC_000913.3.
    WP_001265681.1. NZ_CP010445.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AQ2X-ray1.90A1-540[»]
    1AYLX-ray1.80A1-540[»]
    1K3CX-ray2.00A1-540[»]
    1K3DX-ray2.00A1-540[»]
    1OENX-ray1.90A1-538[»]
    1OS1X-ray1.80A1-540[»]
    2OLQX-ray1.94A1-540[»]
    2OLRX-ray1.60A1-540[»]
    2PXZX-ray2.23X1-540[»]
    2PY7X-ray2.20X1-540[»]
    ProteinModelPortaliP22259.
    SMRiP22259. Positions 6-540.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    IntActiP22259. 4 interactions.
    STRINGi511145.b3403.

    Proteomic databases

    PaxDbiP22259.
    PRIDEiP22259.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC76428; AAC76428; b3403.
    BAE77888; BAE77888; BAE77888.
    GeneIDi945667.
    KEGGieco:b3403.
    PATRICi32122242. VBIEscCol129921_3498.

    Organism-specific databases

    EchoBASEiEB0682.
    EcoGeneiEG10688. pck.

    Phylogenomic databases

    eggNOGiCOG1866.
    HOGENOMiHOG000271471.
    InParanoidiP22259.
    KOiK01610.
    OMAiRFIVKEP.
    OrthoDBiEOG6DG2RK.
    PhylomeDBiP22259.

    Enzyme and pathway databases

    UniPathwayiUPA00138.
    BioCyciEcoCyc:PEPCARBOXYKIN-MONOMER.
    ECOL316407:JW3366-MONOMER.
    MetaCyc:PEPCARBOXYKIN-MONOMER.
    BRENDAi4.1.1.49. 2026.

    Miscellaneous databases

    EvolutionaryTraceiP22259.
    PROiP22259.

    Family and domain databases

    Gene3Di3.40.449.10. 1 hit.
    3.90.228.20. 2 hits.
    HAMAPiMF_00453. PEPCK_ATP.
    InterProiIPR001272. PEP_carboxykinase_ATP.
    IPR013035. PEP_carboxykinase_C.
    IPR008210. PEP_carboxykinase_N.
    IPR015994. PEPCK_ATP_CS.
    [Graphical view]
    PfamiPF01293. PEPCK_ATP. 1 hit.
    [Graphical view]
    PIRSFiPIRSF006294. PEP_crbxkin. 1 hit.
    SUPFAMiSSF68923. SSF68923. 1 hit.
    TIGRFAMsiTIGR00224. pckA. 1 hit.
    PROSITEiPS00532. PEPCK_ATP. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Sequence of the pckA gene of Escherichia coli K-12: relevance to genetic and allosteric regulation and homology of E. coli phosphoenolpyruvate carboxykinase with the enzymes from Trypanosoma brucei and Saccharomyces cerevisiae."
      Medina V., Pontarollo R., Glaeske D., Tabel H., Goldie H.
      J. Bacteriol. 172:7151-7156(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, ENZYME REGULATION, COFACTOR, SUBUNIT.
      Strain: K12.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    3. "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.
    4. "Osmoregulation of gene expression. II. DNA sequence of the envZ gene of the ompB operon of Escherichia coli and characterization of its gene product."
      Mizuno T., Wurtzel E.T., Inouye M.
      J. Biol. Chem. 257:13692-13698(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 439-540.
    5. "The global regulatory protein FruR modulates the direction of carbon flow in Escherichia coli."
      Ramseier T.M., Bledig S., Michotey V., Feghali R., Saier M.H. Jr.
      Mol. Microbiol. 16:1157-1169(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-39.
      Strain: K12.
    6. "A mutant phosphoenolpyruvate carboxykinase in Escherichia coli conferring oxaloacetate decarboxylase activity."
      Hou S.-Y., Chao Y.-P., Liao J.C.
      J. Bacteriol. 177:1620-1623(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 242-290, MUTAGENESIS OF ASP-268 AND GLY-284.
    7. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
      Link A.J., Robison K., Church G.M.
      Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-12.
      Strain: K12 / EMG2.
    8. "Allosteric control by calcium and mechanism of desensitization of phosphoenolpyruvate carboxykinase of Escherichia coli."
      Goldie A.H., Sanwal B.D.
      J. Biol. Chem. 255:1399-1405(1980) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
    9. "Regulation of transcription of the Escherichia coli phosphoenolpyruvate carboxykinase locus: studies with pck-lacZ operon fusions."
      Goldie H.
      J. Bacteriol. 159:832-836(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    10. "Control of gluconeogenic growth by pps and pck in Escherichia coli."
      Chao Y.P., Patnaik R., Roof W.D., Young R.F., Liao J.C.
      J. Bacteriol. 175:6939-6944(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN GLUCONEOGENESIS.
    11. "Identification and molecular characterization of csrA, a pleiotropic gene from Escherichia coli that affects glycogen biosynthesis, gluconeogenesis, cell size, and surface properties."
      Romeo T., Gong M., Liu M.-Y., Brun-Zinkernagel A.-M.
      J. Bacteriol. 175:4744-4755(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    12. "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.
    13. "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli."
      Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.
      Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-87 AND LYS-523, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
    14. "Crystal structure of Escherichia coli phosphoenolpyruvate carboxykinase: a new structural family with the P-loop nucleoside triphosphate hydrolase fold."
      Matte A., Goldie H., Sweet R.M., Delbaere L.T.J.
      J. Mol. Biol. 256:126-143(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-538, ENZYME REGULATION, MASS SPECTROMETRY.
    15. "Snapshot of an enzyme reaction intermediate in the structure of the ATP-Mg2+-oxalate ternary complex of Escherichia coli PEP carboxykinase."
      Tari L.W., Matte A., Pugazhenthi U., Goldie H., Delbaere L.T.J.
      Nat. Struct. Biol. 3:355-363(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH ATP AND SUBSTRATE ANALOGS, REACTION MECHANISM.
    16. "Mg(2+)-Mn(2+) clusters in enzyme-catalyzed phosphoryl-transfer reactions."
      Tari L.W., Matte A., Goldie H., Delbaere L.T.
      Nat. Struct. Biol. 4:990-994(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH ATP, MANGANESE AND SUBSTRATE, COFACTOR, SUBUNIT.
    17. "The phosphoryl-transfer mechanism of Escherichia coli phosphoenolpyruvate carboxykinase from the use of AlF(3)."
      Sudom A.M., Prasad L., Goldie H., Delbaere L.T.
      J. Mol. Biol. 314:83-92(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH ATP ANALOGS AND SUBSTRATE, REACTION MECHANISM.
    18. "Mechanisms of activation of phosphoenolpyruvate carboxykinase from Escherichia coli by Ca2+ and of desensitization by trypsin."
      Sudom A., Walters R., Pastushok L., Goldie D., Prasad L., Delbaere L.T., Goldie H.
      J. Bacteriol. 185:4233-4242(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH ATP, CALCIUM AND SUBSTRATE, ENZYME REGULATION, REACTION MECHANISM, SUBUNIT.
    19. Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH ATP, MANGANESE AND SUBSTRATE ANALOGS, MUTAGENESIS OF ARG-65, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES.
    20. "Crystal structure of E. coli phosphoenolpyruvate carboxykinase (PEPCK) complexed with ATP, Mg2+, Mn2+, carbon dioxide and oxaloacetate."
      Delbaere L.T.J., Cotelesage J.J.H., Goldie H.
      Submitted (MAY-2007) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.23 ANGSTROMS) IN COMPLEX WITH ATP, MANGANESE AND SUBSTRATE ANALOGS, COFACTOR.
    21. "Crystal structure of E. coli phosphoenolpyruvate carboxykinase mutant Lys213Ser."
      Delbaere L.T.J., Cotelesage J.J.H., Goldie H.
      Submitted (MAY-2007) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH ATP AND MANGANESE, COFACTOR.

    Entry informationi

    Entry nameiPCKA_ECOLI
    AccessioniPrimary (citable) accession number: P22259
    Secondary accession number(s): Q2M768
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1991
    Last sequence update: November 1, 1995
    Last modified: July 22, 2015
    This is version 149 of the entry and version 2 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, Direct protein sequencing, Reference proteome

    Documents

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

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.