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P0A796

- PFKA_ECOLI

UniProt

P0A796 - PFKA_ECOLI

Protein

ATP-dependent 6-phosphofructokinase isozyme 1

Gene

pfkA

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 91 (01 Oct 2014)
      Sequence version 1 (07 Jun 2005)
      Previous versions | rss
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    Functioni

    Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.

    Catalytic activityi

    ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate.UniRule annotation

    Cofactori

    Magnesium.

    Enzyme regulationi

    Allosterically activated by ADP and other diphosphonucleosides, and allosterically inhibited by phosphoenolpyruvate.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei12 – 121ATP; via amide nitrogen
    Metal bindingi104 – 1041Magnesium; catalytic1 PublicationUniRule annotation
    Active sitei128 – 1281Proton acceptor2 PublicationsUniRule annotation
    Binding sitei155 – 1551Allosteric activator ADP1 PublicationUniRule annotation
    Binding sitei163 – 1631Substrate; shared with dimeric partner
    Binding sitei212 – 2121Allosteric activator ADPUniRule annotation
    Binding sitei223 – 2231Substrate
    Binding sitei244 – 2441Substrate; shared with dimeric partner

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi73 – 742ATP
    Nucleotide bindingi103 – 1064ATP

    GO - Molecular functioni

    1. 6-phosphofructokinase activity Source: EcoCyc
    2. ATP binding Source: EcoliWiki
    3. GDP binding Source: EcoCyc
    4. identical protein binding Source: EcoliWiki
    5. magnesium ion binding Source: EcoliWiki
    6. ribonucleotide binding Source: EcoliWiki

    GO - Biological processi

    1. carbohydrate phosphorylation Source: GOC
    2. cellular carbohydrate catabolic process Source: EcoliWiki
    3. fructose 6-phosphate metabolic process Source: InterPro
    4. glucose catabolic process Source: EcoliWiki
    5. glycolytic process Source: EcoliWiki

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Biological processi

    Glycolysis

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:6PFK-1-MONOMER.
    ECOL316407:JW3887-MONOMER.
    MetaCyc:6PFK-1-MONOMER.
    SABIO-RKP0A796.
    UniPathwayiUPA00109; UER00182.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    ATP-dependent 6-phosphofructokinase isozyme 1UniRule annotation (EC:2.7.1.11UniRule annotation)
    Short name:
    ATP-PFK 1UniRule annotation
    Short name:
    Phosphofructokinase 1UniRule annotation
    Alternative name(s):
    6-phosphofructokinase isozyme I
    Phosphohexokinase 1UniRule annotation
    Gene namesi
    Name:pfkAUniRule annotation
    Ordered Locus Names:b3916, JW3887
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10699. pfkA.

    Subcellular locationi

    GO - Cellular componenti

    1. 6-phosphofructokinase complex Source: EcoliWiki
    2. cytoplasm Source: EcoliWiki

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi128 – 1281D → S: 18000-fold reduction of catalytic rate. 1 Publication
    Mutagenesisi172 – 1721R → S: 3.4-fold reduction in turnover numbers. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 320320ATP-dependent 6-phosphofructokinase isozyme 1PRO_0000111950Add
    BLAST

    Proteomic databases

    PaxDbiP0A796.
    PRIDEiP0A796.

    2D gel databases

    SWISS-2DPAGEP0A796.

    Expressioni

    Gene expression databases

    GenevestigatoriP0A796.

    Interactioni

    Subunit structurei

    Homotetramer.1 PublicationUniRule annotation

    Protein-protein interaction databases

    DIPiDIP-35841N.
    IntActiP0A796. 7 interactions.
    MINTiMINT-1322275.
    STRINGi511145.b3916.

    Structurei

    Secondary structure

    1
    320
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 96
    Helixi17 – 3014
    Beta strandi34 – 396
    Helixi41 – 466
    Beta strandi50 – 534
    Helixi56 – 583
    Helixi75 – 784
    Helixi80 – 9213
    Beta strandi97 – 1026
    Helixi104 – 11512
    Beta strandi120 – 1256
    Helixi140 – 16122
    Beta strandi164 – 1696
    Helixi176 – 1849
    Beta strandi188 – 1914
    Helixi199 – 21113
    Beta strandi217 – 22610
    Helixi228 – 23912
    Beta strandi243 – 2475
    Helixi249 – 2535
    Helixi259 – 27719
    Beta strandi282 – 2887
    Beta strandi291 – 2966
    Helixi297 – 3037
    Helixi310 – 31910

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1PFKX-ray2.40A/B1-320[»]
    2PFKX-ray2.40A/B/C/D1-320[»]
    ProteinModelPortaliP0A796.
    SMRiP0A796. Positions 1-320.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A796.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni22 – 265Allosteric activator ADP binding; shared with dimeric partner
    Regioni55 – 606Allosteric activator ADP binding; shared with dimeric partner
    Regioni126 – 1283Substrate binding
    Regioni170 – 1723Substrate binding
    Regioni186 – 1883Allosteric activator ADP binding
    Regioni214 – 2163Allosteric activator ADP binding
    Regioni250 – 2534Substrate binding

    Sequence similaritiesi

    Belongs to the phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Prokaryotic clade "B1" sub-subfamily.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0205.
    HOGENOMiHOG000248870.
    KOiK00850.
    OMAiGFGGRCV.
    OrthoDBiEOG644ZRM.
    PhylomeDBiP0A796.

    Family and domain databases

    HAMAPiMF_00339. Phosphofructokinase_I_B1.
    InterProiIPR012003. ATP_PFK_prok.
    IPR012828. PFKA_ATP.
    IPR022953. Phosphofructokinase.
    IPR015912. Phosphofructokinase_CS.
    IPR000023. Phosphofructokinase_dom.
    [Graphical view]
    PfamiPF00365. PFK. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000532. ATP_PFK_prok. 1 hit.
    PRINTSiPR00476. PHFRCTKINASE.
    SUPFAMiSSF53784. SSF53784. 1 hit.
    TIGRFAMsiTIGR02482. PFKA_ATP. 1 hit.
    PROSITEiPS00433. PHOSPHOFRUCTOKINASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P0A796-1 [UniParc]FASTAAdd to Basket

    « Hide

    MIKKIGVLTS GGDAPGMNAA IRGVVRSALT EGLEVMGIYD GYLGLYEDRM    50
    VQLDRYSVSD MINRGGTFLG SARFPEFRDE NIRAVAIENL KKRGIDALVV 100
    IGGDGSYMGA MRLTEMGFPC IGLPGTIDND IKGTDYTIGF FTALSTVVEA 150
    IDRLRDTSSS HQRISVVEVM GRYCGDLTLA AAIAGGCEFV VVPEVEFSRE 200
    DLVNEIKAGI AKGKKHAIVA ITEHMCDVDE LAHFIEKETG RETRATVLGH 250
    IQRGGSPVPY DRILASRMGA YAIDLLLAGY GGRCVGIQNE QLVHHDIIDA 300
    IENMKRPFKG DWLDCAKKLY 320
    Length:320
    Mass (Da):34,842
    Last modified:June 7, 2005 - v1
    Checksum:iD03D79F6A5536A41
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti74 – 741F → C in CAA26356. (PubMed:3158524)Curated
    Sequence conflicti103 – 1042GD → DG in CAA26356. (PubMed:3158524)Curated
    Sequence conflicti163 – 1631R → P in CAA26356. (PubMed:3158524)Curated
    Sequence conflicti317 – 3193KKL → EKM in CAA26356. (PubMed:3158524)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X02519 Genomic DNA. Translation: CAA26356.1.
    L19201 Genomic DNA. Translation: AAB03048.1.
    U00096 Genomic DNA. Translation: AAC76898.1.
    AP009048 Genomic DNA. Translation: BAE77394.1.
    PIRiG65197. KIECFA.
    RefSeqiNP_418351.1. NC_000913.3.
    YP_491535.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76898; AAC76898; b3916.
    BAE77394; BAE77394; BAE77394.
    GeneIDi12932230.
    948412.
    KEGGiecj:Y75_p3271.
    eco:b3916.
    PATRICi32123343. VBIEscCol129921_4032.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X02519 Genomic DNA. Translation: CAA26356.1 .
    L19201 Genomic DNA. Translation: AAB03048.1 .
    U00096 Genomic DNA. Translation: AAC76898.1 .
    AP009048 Genomic DNA. Translation: BAE77394.1 .
    PIRi G65197. KIECFA.
    RefSeqi NP_418351.1. NC_000913.3.
    YP_491535.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1PFK X-ray 2.40 A/B 1-320 [» ]
    2PFK X-ray 2.40 A/B/C/D 1-320 [» ]
    ProteinModelPortali P0A796.
    SMRi P0A796. Positions 1-320.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-35841N.
    IntActi P0A796. 7 interactions.
    MINTi MINT-1322275.
    STRINGi 511145.b3916.

    2D gel databases

    SWISS-2DPAGE P0A796.

    Proteomic databases

    PaxDbi P0A796.
    PRIDEi P0A796.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76898 ; AAC76898 ; b3916 .
    BAE77394 ; BAE77394 ; BAE77394 .
    GeneIDi 12932230.
    948412.
    KEGGi ecj:Y75_p3271.
    eco:b3916.
    PATRICi 32123343. VBIEscCol129921_4032.

    Organism-specific databases

    EchoBASEi EB0693.
    EcoGenei EG10699. pfkA.

    Phylogenomic databases

    eggNOGi COG0205.
    HOGENOMi HOG000248870.
    KOi K00850.
    OMAi GFGGRCV.
    OrthoDBi EOG644ZRM.
    PhylomeDBi P0A796.

    Enzyme and pathway databases

    UniPathwayi UPA00109 ; UER00182 .
    BioCyci EcoCyc:6PFK-1-MONOMER.
    ECOL316407:JW3887-MONOMER.
    MetaCyc:6PFK-1-MONOMER.
    SABIO-RK P0A796.

    Miscellaneous databases

    EvolutionaryTracei P0A796.
    PROi P0A796.

    Gene expression databases

    Genevestigatori P0A796.

    Family and domain databases

    HAMAPi MF_00339. Phosphofructokinase_I_B1.
    InterProi IPR012003. ATP_PFK_prok.
    IPR012828. PFKA_ATP.
    IPR022953. Phosphofructokinase.
    IPR015912. Phosphofructokinase_CS.
    IPR000023. Phosphofructokinase_dom.
    [Graphical view ]
    Pfami PF00365. PFK. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000532. ATP_PFK_prok. 1 hit.
    PRINTSi PR00476. PHFRCTKINASE.
    SUPFAMi SSF53784. SSF53784. 1 hit.
    TIGRFAMsi TIGR02482. PFKA_ATP. 1 hit.
    PROSITEi PS00433. PHOSPHOFRUCTOKINASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence and high-level expression of the major Escherichia coli phosphofructokinase."
      Hellinga H.W., Evans P.R.
      Eur. J. Biochem. 149:363-373(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Mutations in the active site of Escherichia coli phosphofructokinase."
      Hellinga H.W., Evans P.R.
      Nature 327:437-439(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION, ACTIVE SITE, MUTAGENESIS OF ASP-128 AND ARG-172.
    3. "Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes."
      Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.
      Nucleic Acids Res. 21:3391-3398(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    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].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    6. "A role of RnlA in the RNase LS activity from Escherichia coli."
      Otsuka Y., Koga M., Iwamoto A., Yonesaki T.
      Genes Genet. Syst. 82:291-299(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-8.
      Strain: K12.
    7. "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.
    8. "Crystal structure of the complex of phosphofructokinase from Escherichia coli with its reaction products."
      Shirakihara Y., Evans P.R.
      J. Mol. Biol. 204:973-994(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH MAGNESIUM; ADP; FRUCTOSE 1,6-BISPHOSPHATE AND ALLOSTERIC ACTIVATOR, ACTIVE SITE.
    9. "Crystal structure of unliganded phosphofructokinase from Escherichia coli."
      Rypniewski W.R., Evans P.R.
      J. Mol. Biol. 207:805-821(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).

    Entry informationi

    Entry nameiPFKA_ECOLI
    AccessioniPrimary (citable) accession number: P0A796
    Secondary accession number(s): P06998, Q2M8L2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1988
    Last sequence update: June 7, 2005
    Last modified: October 1, 2014
    This is version 91 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