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P0A799

- PGK_ECOLI

UniProt

P0A799 - PGK_ECOLI

Protein

Phosphoglycerate kinase

Gene

pgk

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 87 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei36 – 361SubstrateBy similarity
    Binding sitei113 – 1131SubstrateBy similarity
    Binding sitei146 – 1461SubstrateBy similarity
    Binding sitei197 – 1971ATPBy similarity
    Binding sitei314 – 3141ATPBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi340 – 3434ATPBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. phosphoglycerate kinase activity Source: EcoCyc

    GO - Biological processi

    1. glycolytic process Source: EcoCyc

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Biological processi

    Glycolysis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:PGK.
    ECOL316407:JW2893-MONOMER.
    MetaCyc:PGK.
    SABIO-RKP0A799.
    UniPathwayiUPA00109; UER00185.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphoglycerate kinase (EC:2.7.2.3)
    Gene namesi
    Name:pgk
    Ordered Locus Names:b2926, JW2893
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10703. pgk.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 387386Phosphoglycerate kinasePRO_0000145941Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei84 – 841N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiP0A799.
    PRIDEiP0A799.

    2D gel databases

    SWISS-2DPAGEP0A799.

    PTM databases

    PhosSiteiP0810419.

    Expressioni

    Gene expression databases

    GenevestigatoriP0A799.

    Interactioni

    Subunit structurei

    Monomer.

    Protein-protein interaction databases

    DIPiDIP-36163N.
    IntActiP0A799. 15 interactions.
    MINTiMINT-1229247.
    STRINGi511145.b2926.

    Structurei

    Secondary structure

    1
    387
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi6 – 83
    Beta strandi15 – 195
    Beta strandi30 – 323
    Helixi35 – 4915
    Beta strandi53 – 575
    Helixi70 – 723
    Helixi75 – 8410
    Beta strandi89 – 935
    Beta strandi106 – 1094
    Helixi112 – 1143
    Turni116 – 1216
    Helixi123 – 1319
    Beta strandi134 – 1385
    Helixi141 – 1433
    Turni149 – 1535
    Helixi154 – 1574
    Beta strandi158 – 1636
    Helixi165 – 17814
    Beta strandi182 – 19211
    Turni194 – 1974
    Helixi198 – 2058
    Beta strandi209 – 2157
    Helixi216 – 2249
    Helixi236 – 2383
    Helixi239 – 2468
    Beta strandi255 – 26612
    Beta strandi270 – 2734
    Helixi274 – 2763
    Beta strandi282 – 2865
    Helixi288 – 30013
    Beta strandi302 – 3087
    Helixi316 – 3183
    Helixi320 – 33112
    Beta strandi332 – 3387
    Helixi341 – 35010
    Helixi353 – 3553
    Beta strandi356 – 3594
    Helixi364 – 3707
    Helixi376 – 3849

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1ZMRX-ray2.40A1-387[»]
    ProteinModelPortaliP0A799.
    SMRiP0A799. Positions 2-387.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A799.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni21 – 233Substrate bindingBy similarity
    Regioni59 – 624Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the phosphoglycerate kinase family.Curated

    Phylogenomic databases

    eggNOGiCOG0126.
    HOGENOMiHOG000227107.
    KOiK00927.
    OMAiAGHPVGK.
    OrthoDBiEOG64N9Z0.
    PhylomeDBiP0A799.

    Family and domain databases

    Gene3Di3.40.50.1260. 1 hit.
    3.40.50.1270. 1 hit.
    HAMAPiMF_00145. Phosphoglyc_kinase.
    InterProiIPR001576. Phosphoglycerate_kinase.
    IPR015901. Phosphoglycerate_kinase_C.
    IPR015911. Phosphoglycerate_kinase_CS.
    IPR015824. Phosphoglycerate_kinase_N.
    [Graphical view]
    PANTHERiPTHR11406. PTHR11406. 1 hit.
    PfamiPF00162. PGK. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000724. Pgk. 1 hit.
    PRINTSiPR00477. PHGLYCKINASE.
    SUPFAMiSSF53748. SSF53748. 1 hit.
    PROSITEiPS00111. PGLYCERATE_KINASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P0A799-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSVIKMTDLD LAGKRVFIRA DLNVPVKDGK VTSDARIRAS LPTIELALKQ    50
    GAKVMVTSHL GRPTEGEYNE EFSLLPVVNY LKDKLSNPVR LVKDYLDGVD 100
    VAEGELVVLE NVRFNKGEKK DDETLSKKYA ALCDVFVMDA FGTAHRAQAS 150
    THGIGKFADV ACAGPLLAAE LDALGKALKE PARPMVAIVG GSKVSTKLTV 200
    LDSLSKIADQ LIVGGGIANT FIAAQGHDVG KSLYEADLVD EAKRLLTTCN 250
    IPVPSDVRVA TEFSETAPAT LKSVNDVKAD EQILDIGDAS AQELAEILKN 300
    AKTILWNGPV GVFEFPNFRK GTEIVANAIA DSEAFSIAGG GDTLAAIDLF 350
    GIADKISYIS TGGGAFLEFV EGKVLPAVAM LEERAKK 387
    Length:387
    Mass (Da):41,118
    Last modified:January 23, 2007 - v2
    Checksum:iFAD7D66D100514B2
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X14436 Genomic DNA. Translation: CAA32604.1.
    U28377 Genomic DNA. Translation: AAA69093.1.
    U00096 Genomic DNA. Translation: AAC75963.1.
    AP009048 Genomic DNA. Translation: BAE76990.1.
    PIRiS04733. TVECG.
    RefSeqiNP_417401.1. NC_000913.3.
    YP_491126.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75963; AAC75963; b2926.
    BAE76990; BAE76990; BAE76990.
    GeneIDi12933840.
    947414.
    KEGGiecj:Y75_p2857.
    eco:b2926.
    PATRICi32121266. VBIEscCol129921_3021.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X14436 Genomic DNA. Translation: CAA32604.1 .
    U28377 Genomic DNA. Translation: AAA69093.1 .
    U00096 Genomic DNA. Translation: AAC75963.1 .
    AP009048 Genomic DNA. Translation: BAE76990.1 .
    PIRi S04733. TVECG.
    RefSeqi NP_417401.1. NC_000913.3.
    YP_491126.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1ZMR X-ray 2.40 A 1-387 [» ]
    ProteinModelPortali P0A799.
    SMRi P0A799. Positions 2-387.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-36163N.
    IntActi P0A799. 15 interactions.
    MINTi MINT-1229247.
    STRINGi 511145.b2926.

    PTM databases

    PhosSitei P0810419.

    2D gel databases

    SWISS-2DPAGE P0A799.

    Proteomic databases

    PaxDbi P0A799.
    PRIDEi P0A799.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC75963 ; AAC75963 ; b2926 .
    BAE76990 ; BAE76990 ; BAE76990 .
    GeneIDi 12933840.
    947414.
    KEGGi ecj:Y75_p2857.
    eco:b2926.
    PATRICi 32121266. VBIEscCol129921_3021.

    Organism-specific databases

    EchoBASEi EB0697.
    EcoGenei EG10703. pgk.

    Phylogenomic databases

    eggNOGi COG0126.
    HOGENOMi HOG000227107.
    KOi K00927.
    OMAi AGHPVGK.
    OrthoDBi EOG64N9Z0.
    PhylomeDBi P0A799.

    Enzyme and pathway databases

    UniPathwayi UPA00109 ; UER00185 .
    BioCyci EcoCyc:PGK.
    ECOL316407:JW2893-MONOMER.
    MetaCyc:PGK.
    SABIO-RK P0A799.

    Miscellaneous databases

    EvolutionaryTracei P0A799.
    PROi P0A799.

    Gene expression databases

    Genevestigatori P0A799.

    Family and domain databases

    Gene3Di 3.40.50.1260. 1 hit.
    3.40.50.1270. 1 hit.
    HAMAPi MF_00145. Phosphoglyc_kinase.
    InterProi IPR001576. Phosphoglycerate_kinase.
    IPR015901. Phosphoglycerate_kinase_C.
    IPR015911. Phosphoglycerate_kinase_CS.
    IPR015824. Phosphoglycerate_kinase_N.
    [Graphical view ]
    PANTHERi PTHR11406. PTHR11406. 1 hit.
    Pfami PF00162. PGK. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000724. Pgk. 1 hit.
    PRINTSi PR00477. PHGLYCKINASE.
    SUPFAMi SSF53748. SSF53748. 1 hit.
    PROSITEi PS00111. PGLYCERATE_KINASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification, molecular cloning and sequence analysis of a gene cluster encoding the class II fructose 1,6-bisphosphate aldolase, 3-phosphoglycerate kinase and a putative second glyceraldehyde 3-phosphate dehydrogenase of Escherichia coli."
      Alefounder P.R., Perham R.N.
      Mol. Microbiol. 3:723-732(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12 / CS520.
    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. "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 2-24.
      Strain: K12 / EMG2.
    5. Frutiger S., Hughes G.J., Pasquali C., Hochstrasser D.F.
      Submitted (FEB-1996) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-12.
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    6. Cited for: PROTEIN SEQUENCE OF 2-5.
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    7. "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-84, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.

    Entry informationi

    Entry nameiPGK_ECOLI
    AccessioniPrimary (citable) accession number: P0A799
    Secondary accession number(s): P11665, Q2M9R6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 7, 2005
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 87 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, 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