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P22259

- PCKA_ECOLI

UniProt

P22259 - PCKA_ECOLI

Protein

Phosphoenolpyruvate carboxykinase [ATP]

Gene

pckA

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 141 (01 Oct 2014)
      Sequence version 2 (01 Nov 1995)
      Previous versions | rss
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    Functioni

    Involved in the gluconeogenesis. Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP) through direct phosphoryl transfer between the nucleoside triphosphate and OAA.3 PublicationsUniRule annotation

    Catalytic activityi

    ATP + oxaloacetate = ADP + phosphoenolpyruvate + CO2.1 PublicationUniRule annotation

    Cofactori

    Binds 1 manganese ion per subunit.5 PublicationsUniRule annotation

    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

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei65 – 651Substrate1 PublicationUniRule annotation
    Metal bindingi149 – 1491Calcium; via carbonyl oxygenBy similarity
    Metal bindingi150 – 1501Calcium; via carbonyl oxygenBy similarity
    Metal bindingi152 – 1521Calcium; via carbonyl oxygenBy similarity
    Binding sitei207 – 2071Substrate1 PublicationUniRule annotation
    Metal bindingi213 – 2131Manganese1 PublicationUniRule annotation
    Binding sitei213 – 2131ATP6 PublicationsUniRule annotation
    Binding sitei213 – 2131Substrate1 PublicationUniRule annotation
    Metal bindingi232 – 2321Manganese; via tele nitrogen1 PublicationUniRule annotation
    Binding sitei232 – 2321ATP6 PublicationsUniRule annotation
    Metal bindingi269 – 2691Manganese1 PublicationUniRule annotation
    Metal bindingi283 – 2831Calcium; via carbonyl oxygenBy similarity
    Binding sitei297 – 2971ATP6 PublicationsUniRule annotation
    Binding sitei333 – 3331ATP6 PublicationsUniRule annotation
    Binding sitei333 – 3331Substrate1 PublicationUniRule annotation
    Binding sitei455 – 4551ATP6 PublicationsUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi248 – 2569ATP6 PublicationsUniRule annotation
    Nucleotide bindingi449 – 4502ATP6 PublicationsUniRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-HAMAP
    2. calcium ion binding Source: EcoCyc
    3. magnesium ion binding Source: EcoCyc
    4. phosphoenolpyruvate carboxykinase (ATP) activity Source: EcoCyc

    GO - Biological processi

    1. gluconeogenesis Source: EcoCyc

    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.
    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: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10688. pck.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    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-acetyllysine1 PublicationUniRule annotation
    Modified residuei523 – 5231N6-acetyllysine1 PublicationUniRule annotation

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiP22259.
    PRIDEiP22259.

    PTM databases

    PhosSiteiP0809417.

    Expressioni

    Inductioni

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

    Gene expression databases

    GenevestigatoriP22259.

    Interactioni

    Subunit structurei

    Monomer.9 PublicationsUniRule annotation

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    KOiK01610.
    OMAiGADPEHY.
    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

    MRVNNGLTPQ ELEAYGISDV HDIVYNPSYD LLYQEELDPS LTGYERGVLT    50
    NLGAVAVDTG IFTGRSPKDK YIVRDDTTRD TFWWADKGKG KNDNKPLSPE 100
    TWQHLKGLVT RQLSGKRLFV VDAFCGANPD TRLSVRFITE VAWQAHFVKN 150
    MFIRPSDEEL AGFKPDFIVM NGAKCTNPQW KEQGLNSENF VAFNLTERMQ 200
    LIGGTWYGGE MKKGMFSMMN YLLPLKGIAS MHCSANVGEK GDVAVFFGLS 250
    GTGKTTLSTD PKRRLIGDDE HGWDDDGVFN FEGGCYAKTI KLSKEAEPEI 300
    YNAIRRDALL ENVTVREDGT IDFDDGSKTE NTRVSYPIYH IDNIVKPVSK 350
    AGHATKVIFL TADAFGVLPP VSRLTADQTQ YHFLSGFTAK LAGTERGITE 400
    PTPTFSACFG AAFLSLHPTQ YAEVLVKRMQ AAGAQAYLVN TGWNGTGKRI 450
    SIKDTRAIID AILNGSLDNA ETFTLPMFNL AIPTELPGVD TKILDPRNTY 500
    ASPEQWQEKA ETLAKLFIDN FDKYTDTPAG AALVAAGPKL 540
    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.

    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:
    EMBL
    GenBank
    DDBJ
    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.
    YP_492029.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76428; AAC76428; b3403.
    BAE77888; BAE77888; BAE77888.
    GeneIDi12933187.
    945667.
    KEGGiecj:Y75_p3773.
    eco:b3403.
    PATRICi32122242. VBIEscCol129921_3498.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    PIRi F65135.
    RefSeqi NP_417862.1. NC_000913.3.
    YP_492029.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AQ2 X-ray 1.90 A 1-540 [» ]
    1AYL X-ray 1.80 A 1-540 [» ]
    1K3C X-ray 2.00 A 1-540 [» ]
    1K3D X-ray 2.00 A 1-540 [» ]
    1OEN X-ray 1.90 A 1-538 [» ]
    1OS1 X-ray 1.80 A 1-540 [» ]
    2OLQ X-ray 1.94 A 1-540 [» ]
    2OLR X-ray 1.60 A 1-540 [» ]
    2PXZ X-ray 2.23 X 1-540 [» ]
    2PY7 X-ray 2.20 X 1-540 [» ]
    ProteinModelPortali P22259.
    SMRi P22259. Positions 6-540.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P22259. 4 interactions.
    STRINGi 511145.b3403.

    PTM databases

    PhosSitei P0809417.

    Proteomic databases

    PaxDbi P22259.
    PRIDEi P22259.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76428 ; AAC76428 ; b3403 .
    BAE77888 ; BAE77888 ; BAE77888 .
    GeneIDi 12933187.
    945667.
    KEGGi ecj:Y75_p3773.
    eco:b3403.
    PATRICi 32122242. VBIEscCol129921_3498.

    Organism-specific databases

    EchoBASEi EB0682.
    EcoGenei EG10688. pck.

    Phylogenomic databases

    eggNOGi COG1866.
    HOGENOMi HOG000271471.
    KOi K01610.
    OMAi GADPEHY.
    OrthoDBi EOG6DG2RK.
    PhylomeDBi P22259.

    Enzyme and pathway databases

    UniPathwayi UPA00138 .
    BioCyci EcoCyc:PEPCARBOXYKIN-MONOMER.
    ECOL316407:JW3366-MONOMER.
    MetaCyc:PEPCARBOXYKIN-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P22259.
    PROi P22259.

    Gene expression databases

    Genevestigatori P22259.

    Family and domain databases

    Gene3Di 3.40.449.10. 1 hit.
    3.90.228.20. 2 hits.
    HAMAPi MF_00453. PEPCK_ATP.
    InterProi IPR001272. PEP_carboxykinase_ATP.
    IPR013035. PEP_carboxykinase_C.
    IPR008210. PEP_carboxykinase_N.
    IPR015994. PEPCK_ATP_CS.
    [Graphical view ]
    Pfami PF01293. PEPCK_ATP. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF006294. PEP_crbxkin. 1 hit.
    SUPFAMi SSF68923. SSF68923. 1 hit.
    TIGRFAMsi TIGR00224. pckA. 1 hit.
    PROSITEi PS00532. PEPCK_ATP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 141 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