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P0AD61

- KPYK1_ECOLI

UniProt

P0AD61 - KPYK1_ECOLI

Protein

Pyruvate kinase I

Gene

pykF

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 90 (01 Oct 2014)
      Sequence version 1 (06 Dec 2005)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    ATP + pyruvate = ADP + phosphoenolpyruvate.

    Cofactori

    Magnesium.
    Potassium.

    Enzyme regulationi

    Belongs to type I PK; fructose 1,6-bisphosphate-activated.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei32 – 321SubstrateBy similarity
    Metal bindingi34 – 341PotassiumBy similarity
    Metal bindingi36 – 361PotassiumBy similarity
    Metal bindingi66 – 661PotassiumBy similarity
    Metal bindingi67 – 671Potassium; via carbonyl oxygenBy similarity
    Sitei220 – 2201Transition state stabilizerBy similarity
    Metal bindingi222 – 2221MagnesiumBy similarity
    Binding sitei245 – 2451Substrate; via amide nitrogenBy similarity
    Metal bindingi246 – 2461MagnesiumBy similarity
    Binding sitei246 – 2461Substrate; via amide nitrogenBy similarity
    Binding sitei278 – 2781SubstrateBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. magnesium ion binding Source: InterPro
    3. potassium ion binding Source: InterPro
    4. pyruvate kinase activity Source: UniProtKB-EC

    GO - Biological processi

    1. glycolytic process Source: UniProtKB-UniPathway
    2. response to heat Source: EcoCyc

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Biological processi

    Glycolysis

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Potassium, Pyruvate

    Enzyme and pathway databases

    BioCyciEcoCyc:PKI-MONOMER.
    ECOL316407:JW1666-MONOMER.
    MetaCyc:PKI-MONOMER.
    SABIO-RKP0AD61.
    UniPathwayiUPA00109; UER00188.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Pyruvate kinase I (EC:2.7.1.40)
    Alternative name(s):
    PK-1
    Gene namesi
    Name:pykF
    Ordered Locus Names:b1676, JW1666
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10804. pykF.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: UniProtKB
    2. membrane Source: UniProtKB

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 470470Pyruvate kinase IPRO_0000112069Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei76 – 761N6-acetyllysine1 Publication
    Modified residuei319 – 3191N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiP0AD61.
    PRIDEiP0AD61.

    2D gel databases

    SWISS-2DPAGEP0AD61.

    PTM databases

    PhosSiteiP0810429.

    Expressioni

    Gene expression databases

    GenevestigatoriP0AD61.

    Interactioni

    Subunit structurei

    Homotetramer.

    Protein-protein interaction databases

    DIPiDIP-36221N.
    IntActiP0AD61. 21 interactions.
    STRINGi511145.b1676.

    Structurei

    Secondary structure

    1
    470
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 96
    Helixi12 – 143
    Helixi17 – 2610
    Beta strandi28 – 347
    Helixi40 – 5718
    Beta strandi62 – 665
    Beta strandi72 – 743
    Helixi78 – 803
    Beta strandi83 – 853
    Beta strandi90 – 956
    Beta strandi105 – 1095
    Helixi113 – 1164
    Beta strandi122 – 1254
    Turni126 – 1294
    Beta strandi130 – 1389
    Beta strandi141 – 1466
    Beta strandi150 – 1523
    Beta strandi157 – 1593
    Helixi172 – 18413
    Beta strandi187 – 1937
    Helixi197 – 20812
    Turni209 – 2113
    Beta strandi216 – 2216
    Helixi224 – 2285
    Helixi230 – 2367
    Beta strandi237 – 2437
    Helixi244 – 2507
    Helixi253 – 27018
    Beta strandi273 – 2775
    Beta strandi278 – 2814
    Helixi282 – 2854
    Helixi292 – 30413
    Beta strandi307 – 3115
    Helixi313 – 3164
    Helixi322 – 33615
    Helixi355 – 36814
    Beta strandi372 – 3776
    Beta strandi379 – 3813
    Helixi382 – 3887
    Beta strandi393 – 4019
    Helixi403 – 4086
    Helixi409 – 4113
    Beta strandi415 – 4195
    Helixi426 – 43914
    Beta strandi441 – 4433
    Beta strandi448 – 4536
    Beta strandi455 – 4573
    Beta strandi464 – 4696

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1E0TX-ray1.80A/B/C/D1-470[»]
    1E0UX-ray2.80A/B/C/D1-470[»]
    1PKYX-ray2.50A/B/C/D1-470[»]
    ProteinModelPortaliP0AD61.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0AD61.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the pyruvate kinase family.Curated

    Phylogenomic databases

    eggNOGiCOG0469.
    HOGENOMiHOG000021559.
    KOiK00873.
    OMAiCIVENAG.
    OrthoDBiEOG6GBMB0.
    PhylomeDBiP0AD61.

    Family and domain databases

    Gene3Di2.40.33.10. 1 hit.
    3.20.20.60. 2 hits.
    3.40.1380.20. 1 hit.
    InterProiIPR001697. Pyr_Knase.
    IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
    IPR011037. Pyrv_Knase-like_insert_dom.
    IPR015794. Pyrv_Knase_a/b.
    IPR018209. Pyrv_Knase_AS.
    IPR015793. Pyrv_Knase_brl.
    IPR015795. Pyrv_Knase_C.
    IPR015806. Pyrv_Knase_insert_dom.
    [Graphical view]
    PANTHERiPTHR11817. PTHR11817. 1 hit.
    PfamiPF00224. PK. 1 hit.
    PF02887. PK_C. 1 hit.
    [Graphical view]
    PRINTSiPR01050. PYRUVTKNASE.
    SUPFAMiSSF50800. SSF50800. 1 hit.
    SSF51621. SSF51621. 2 hits.
    SSF52935. SSF52935. 1 hit.
    TIGRFAMsiTIGR01064. pyruv_kin. 1 hit.
    PROSITEiPS00110. PYRUVATE_KINASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P0AD61-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKKTKIVCTI GPKTESEEML AKMLDAGMNV MRLNFSHGDY AEHGQRIQNL    50
    RNVMSKTGKT AAILLDTKGP EIRTMKLEGG NDVSLKAGQT FTFTTDKSVI 100
    GNSEMVAVTY EGFTTDLSVG NTVLVDDGLI GMEVTAIEGN KVICKVLNNG 150
    DLGENKGVNL PGVSIALPAL AEKDKQDLIF GCEQGVDFVA ASFIRKRSDV 200
    IEIREHLKAH GGENIHIISK IENQEGLNNF DEILEASDGI MVARGDLGVE 250
    IPVEEVIFAQ KMMIEKCIRA RKVVITATQM LDSMIKNPRP TRAEAGDVAN 300
    AILDGTDAVM LSGESAKGKY PLEAVSIMAT ICERTDRVMN SRLEFNNDNR 350
    KLRITEAVCR GAVETAEKLD APLIVVATQG GKSARAVRKY FPDATILALT 400
    TNEKTAHQLV LSKGVVPQLV KEITSTDDFY RLGKELALQS GLAHKGDVVV 450
    MVSGALVPSG TTNTASVHVL 470
    Length:470
    Mass (Da):50,729
    Last modified:December 6, 2005 - v1
    Checksum:iE29BF01B90327D8B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti44 – 441G → S AA sequence (PubMed:1859631)Curated
    Sequence conflicti379 – 3791Q → N AA sequence (PubMed:2653362)Curated
    Sequence conflicti401 – 4011T → D AA sequence (PubMed:2653362)Curated
    Sequence conflicti451 – 47020MVSGA…SVHVL → YGFWCTGTERHY(PubMed:2674937)CuratedAdd
    BLAST
    Sequence conflicti451 – 47020MVSGA…SVHVL → YGFWCTGTERHY(PubMed:9097039)CuratedAdd
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M24636 Genomic DNA. Translation: AAA24392.1.
    U68703 Genomic DNA. Translation: AAB47952.1.
    U00096 Genomic DNA. Translation: AAC74746.1.
    AP009048 Genomic DNA. Translation: BAA15445.2.
    PIRiD64925.
    RefSeqiNP_416191.1. NC_000913.3.
    YP_489938.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC74746; AAC74746; b1676.
    BAA15445; BAA15445; BAA15445.
    GeneIDi12931281.
    946179.
    KEGGiecj:Y75_p1651.
    eco:b1676.
    PATRICi32118658. VBIEscCol129921_1747.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M24636 Genomic DNA. Translation: AAA24392.1 .
    U68703 Genomic DNA. Translation: AAB47952.1 .
    U00096 Genomic DNA. Translation: AAC74746.1 .
    AP009048 Genomic DNA. Translation: BAA15445.2 .
    PIRi D64925.
    RefSeqi NP_416191.1. NC_000913.3.
    YP_489938.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1E0T X-ray 1.80 A/B/C/D 1-470 [» ]
    1E0U X-ray 2.80 A/B/C/D 1-470 [» ]
    1PKY X-ray 2.50 A/B/C/D 1-470 [» ]
    ProteinModelPortali P0AD61.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-36221N.
    IntActi P0AD61. 21 interactions.
    STRINGi 511145.b1676.

    PTM databases

    PhosSitei P0810429.

    2D gel databases

    SWISS-2DPAGE P0AD61.

    Proteomic databases

    PaxDbi P0AD61.
    PRIDEi P0AD61.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC74746 ; AAC74746 ; b1676 .
    BAA15445 ; BAA15445 ; BAA15445 .
    GeneIDi 12931281.
    946179.
    KEGGi ecj:Y75_p1651.
    eco:b1676.
    PATRICi 32118658. VBIEscCol129921_1747.

    Organism-specific databases

    EchoBASEi EB0797.
    EcoGenei EG10804. pykF.

    Phylogenomic databases

    eggNOGi COG0469.
    HOGENOMi HOG000021559.
    KOi K00873.
    OMAi CIVENAG.
    OrthoDBi EOG6GBMB0.
    PhylomeDBi P0AD61.

    Enzyme and pathway databases

    UniPathwayi UPA00109 ; UER00188 .
    BioCyci EcoCyc:PKI-MONOMER.
    ECOL316407:JW1666-MONOMER.
    MetaCyc:PKI-MONOMER.
    SABIO-RK P0AD61.

    Miscellaneous databases

    EvolutionaryTracei P0AD61.
    PROi P0AD61.

    Gene expression databases

    Genevestigatori P0AD61.

    Family and domain databases

    Gene3Di 2.40.33.10. 1 hit.
    3.20.20.60. 2 hits.
    3.40.1380.20. 1 hit.
    InterProi IPR001697. Pyr_Knase.
    IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
    IPR011037. Pyrv_Knase-like_insert_dom.
    IPR015794. Pyrv_Knase_a/b.
    IPR018209. Pyrv_Knase_AS.
    IPR015793. Pyrv_Knase_brl.
    IPR015795. Pyrv_Knase_C.
    IPR015806. Pyrv_Knase_insert_dom.
    [Graphical view ]
    PANTHERi PTHR11817. PTHR11817. 1 hit.
    Pfami PF00224. PK. 1 hit.
    PF02887. PK_C. 1 hit.
    [Graphical view ]
    PRINTSi PR01050. PYRUVTKNASE.
    SUPFAMi SSF50800. SSF50800. 1 hit.
    SSF51621. SSF51621. 2 hits.
    SSF52935. SSF52935. 1 hit.
    TIGRFAMsi TIGR01064. pyruv_kin. 1 hit.
    PROSITEi PS00110. PYRUVATE_KINASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Direct genomic sequencing of bacterial DNA: the pyruvate kinase I gene of Escherichia coli."
      Ohara O., Dorit R.L., Gilbert W.
      Proc. Natl. Acad. Sci. U.S.A. 86:6883-6887(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Analysis of the boundaries of Salmonella pathogenicity island 2 and the corresponding chromosomal region of Escherichia coli K-12."
      Hensel M., Shea J.E., Baeumler A.J., Gleeson C., Blattner F.R., Holden D.W.
      J. Bacteriol. 179:1105-1111(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    5. "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], SEQUENCE REVISION TO 451-470.
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    6. "Bacterial pyruvate kinases have a shorter N-terminal domain."
      Valentini G., Stoppini M., Speranza M.L., Malcovati M., Ferri G.
      Biol. Chem. Hoppe-Seyler 372:91-93(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-48.
    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 1-11.
      Strain: K12 / EMG2.
    8. "Primary structure of three peptides at the catalytic and allosteric sites of the fructose-1,6-bisphosphate-activated pyruvate kinase from Escherichia coli."
      Speranza M.L., Valentini G., Iadarola P., Stoppini M., Malcovati M., Ferri G.
      Biol. Chem. Hoppe-Seyler 370:211-216(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 293-319; 369-385 AND 389-404.
    9. "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.
    10. "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-76 AND LYS-319, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
    11. "Crystal structure of Escherichia coli pyruvate kinase type I: molecular basis of the allosteric transition."
      Mattevi A., Valentini G., Rizzi M., Speranza M.L., Bolognesi M., Coda A.
      Structure 3:729-741(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
    12. Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).

    Entry informationi

    Entry nameiKPYK1_ECOLI
    AccessioniPrimary (citable) accession number: P0AD61
    Secondary accession number(s): P14178
    , P76921, P78165, P78231
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 6, 2005
    Last sequence update: December 6, 2005
    Last modified: October 1, 2014
    This is version 90 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, 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