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P52034

- PFKA_DROME

UniProt

P52034 - PFKA_DROME

Protein

ATP-dependent 6-phosphofructokinase

Gene

Pfk

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 2 (16 Aug 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.2 PublicationsUniRule annotation

    Catalytic activityi

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

    Cofactori

    Magnesium.UniRule annotation

    Enzyme regulationi

    Allosterically activated by ADP, AMP, or fructose 2,6-bisphosphate, and allosterically inhibited by ATP or citrate.UniRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei27 – 271ATP; via amide nitrogenUniRule annotation
    Metal bindingi121 – 1211Magnesium; catalyticUniRule annotation
    Active sitei168 – 1681Proton acceptorUniRule annotation
    Binding sitei203 – 2031Substrate; shared with dimeric partnerUniRule annotation
    Binding sitei266 – 2661SubstrateUniRule annotation
    Binding sitei294 – 2941Substrate; shared with dimeric partnerUniRule annotation
    Binding sitei480 – 4801Allosteric activator fructose 2,6-bisphosphateUniRule annotation
    Binding sitei575 – 5751Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partnerUniRule annotation
    Binding sitei638 – 6381Allosteric activator fructose 2,6-bisphosphateUniRule annotation
    Binding sitei664 – 6641Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partnerUniRule annotation
    Binding sitei745 – 7451Allosteric activator fructose 2,6-bisphosphateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi90 – 912ATPUniRule annotation
    Nucleotide bindingi120 – 1234ATPUniRule annotation

    GO - Molecular functioni

    1. 6-phosphofructokinase activity Source: FlyBase
    2. ATP binding Source: UniProtKB-KW
    3. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. carbohydrate phosphorylation Source: GOC
    2. fructose 6-phosphate metabolic process Source: InterPro
    3. glycolytic process Source: FlyBase

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Biological processi

    Glycolysis

    Keywords - Ligandi

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

    Enzyme and pathway databases

    ReactomeiREACT_206319. Glycolysis.
    UniPathwayiUPA00109; UER00182.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    ATP-dependent 6-phosphofructokinaseUniRule annotation (EC:2.7.1.11UniRule annotation)
    Short name:
    ATP-PFKUniRule annotation
    Short name:
    PhosphofructokinaseUniRule annotation
    Alternative name(s):
    PhosphohexokinaseUniRule annotation
    Gene namesi
    Name:Pfk
    ORF Names:CG4001
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 2R

    Organism-specific databases

    FlyBaseiFBgn0003071. Pfk.

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. 6-phosphofructokinase complex Source: FlyBase

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 788788ATP-dependent 6-phosphofructokinasePRO_0000112031Add
    BLAST

    Proteomic databases

    PaxDbiP52034.

    Expressioni

    Tissue specificityi

    Nearly 90% of the PFK activity in adults is localized to the thorax.1 Publication

    Gene expression databases

    BgeeiP52034.

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation

    Protein-protein interaction databases

    BioGridi61888. 2 interactions.
    MINTiMINT-928619.

    Structurei

    3D structure databases

    ProteinModelPortaliP52034.
    SMRiP52034. Positions 18-766.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 392392N-terminal catalytic PFK domain 1Add
    BLAST
    Regioni166 – 1683Substrate bindingUniRule annotation
    Regioni210 – 2123Substrate bindingUniRule annotation
    Regioni300 – 3034Substrate bindingUniRule annotation
    Regioni393 – 41018Interdomain linkerAdd
    BLAST
    Regioni411 – 788378C-terminal regulatory PFK domain 2Add
    BLAST
    Regioni537 – 5415Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation
    Regioni582 – 5843Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation
    Regioni670 – 6734Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation

    Sequence similaritiesi

    Belongs to the phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Eukaryotic two domain clade "E" sub-subfamily.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0205.
    GeneTreeiENSGT00390000013209.
    HOGENOMiHOG000148827.
    InParanoidiP52034.
    KOiK00850.
    OMAiVYHMASK.
    OrthoDBiEOG7ZSHV5.
    PhylomeDBiP52034.

    Family and domain databases

    HAMAPiMF_03184. Phosphofructokinase_I_E.
    InterProiIPR009161. 6-phosphofructokinase_euk.
    IPR022953. Phosphofructokinase.
    IPR015912. Phosphofructokinase_CS.
    IPR000023. Phosphofructokinase_dom.
    [Graphical view]
    PfamiPF00365. PFK. 2 hits.
    [Graphical view]
    PIRSFiPIRSF000533. ATP_PFK_euk. 1 hit.
    PRINTSiPR00476. PHFRCTKINASE.
    SUPFAMiSSF53784. SSF53784. 2 hits.
    TIGRFAMsiTIGR02478. 6PF1K_euk. 1 hit.
    PROSITEiPS00433. PHOSPHOFRUCTOKINASE. 2 hits.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform B (identifier: P52034-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MNSEINQRFL ARGSQKDKGL AVFTSGGDSQ GMNAAVRACV RMAIYLGCKV    50
    YFIREGYQGM VDGGDCIQEA NWASVSSIIH RGGTIIGSAR CQDFRERQGR 100
    LKAANNLIQR GITNLVVIGG DGSLTGANLF RQEWSSLLDE LVKNKTITTE 150
    QQEKFNVLHI VGLVGSIDND FCGTDMTIGT DTALHRIIEA IDAISSTAYS 200
    HQRTFIMEVM GRHCGYLALV GGLACEADFI FIPEMPPKVD WPDRLCSQLA 250
    QERSAGQRLN IVIVAEGAMD REGHPITAED VKKVIDERLK HDARITVLGH 300
    VQRGGNPSAF DRILACRMGA EATLALMEAT KDSVPVVISL DGNQAVRVPL 350
    MECVERTQAV AKAMAEKRWA DAVKLRGRSF ERNLETYKML TRLKPPKENF 400
    DADGKGIEGY RLAVMHIGAP ACGMNAAVRS FVRNAIYRGD VVYGINDGVE 450
    GLIAGNVREL GWSDVSGWVG QGGAYLGTKR TLPEGKFKEI AARLKEFKIQ 500
    GLLIIGGFES YHAAGQIADQ RDNYPQFCIP IVVIPSTISN NVPGTEFSLG 550
    CDTGLNEITE ICDRIRQSAQ GTKRRVFVIE TMGGYCGYLA TLAGLAGGAD 600
    AAYIYEEKFS IKDLQQDVYH MASKMAEGVS RGLILRNEKA SENYSTDFIY 650
    RLYSEEGKGL FTCRMNILGH MQQGGSPTPF DRNMGTKMAA KCVDWLAAQI 700
    KANIDANGVV NCKSPDTATL LGIVSRQYRF SPLVDLIAET NFDQRIPKKQ 750
    WWLRLRPLLR ILAKHDSAYE EEGMYITVEE ECDTDAVA 788
    Length:788
    Mass (Da):86,648
    Last modified:August 16, 2005 - v2
    Checksum:iBE45A03013299B75
    GO
    Isoform A (identifier: P52034-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-15: MNSEINQRFLARGSQ → MHSIKFRVFT...IDFVHPVKPF

    Note: No experimental confirmation available.

    Show »
    Length:950
    Mass (Da):105,187
    Checksum:i28BD631321945759
    GO
    Isoform C (identifier: P52034-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         219-250: LVGGLACEADFIFIPEMPPKVDWPDRLCSQLA → ISAAIATEADFMFIPEEPVSVNWKDEICVKLH

    Note: No experimental confirmation available.

    Show »
    Length:788
    Mass (Da):86,720
    Checksum:iD4E991EADAD0B084
    GO

    Sequence cautioni

    The sequence AAN71109.1 differs from that shown. Reason: Frameshift at position 218.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti68 – 703QEA → RKS in AAA62385. (PubMed:7929140)Curated
    Sequence conflicti80 – 9213HRGGT…SARCQ → PFVGWHHPLLRPLP(PubMed:7929140)CuratedAdd
    BLAST
    Sequence conflicti130 – 1312FR → LP in AAA62385. (PubMed:7929140)Curated
    Sequence conflicti160 – 1612IV → ML in AAA62385. (PubMed:7929140)Curated
    Sequence conflicti190 – 19910AIDAISSTAY → QSKAKVQSPVQPN in AAA62385. (PubMed:7929140)Curated
    Sequence conflicti209 – 2124VMGR → GQVS in AAA62385. (PubMed:7929140)Curated
    Sequence conflicti228 – 25225DFIFI…QLAQE → IHIHPNAPGRLGQTGSALSW TQ in AAA62385. (PubMed:7929140)CuratedAdd
    BLAST
    Sequence conflicti313 – 3131I → F in AAA62385. (PubMed:7929140)Curated
    Sequence conflicti322 – 3254ATLA → PLWP in AAA62385. (PubMed:7929140)Curated
    Sequence conflicti360 – 3612VA → G in AAA62385. (PubMed:7929140)Curated
    Sequence conflicti374 – 3752KL → NV in AAA62385. (PubMed:7929140)Curated
    Sequence conflicti455 – 4551G → R in AAA62385. (PubMed:7929140)Curated
    Sequence conflicti478 – 4781T → S in AAA62385. (PubMed:7929140)Curated
    Sequence conflicti522 – 5265DNYPQ → TTTHS in AAA62385. (PubMed:7929140)Curated
    Sequence conflicti590 – 5912AT → PP in AAA62385. (PubMed:7929140)Curated
    Sequence conflicti613 – 6131D → E in AAA62385. (PubMed:7929140)Curated
    Sequence conflicti622 – 63615ASKMA…GLILR → PPRWPRRLPRSNPA in AAA62385. (PubMed:7929140)CuratedAdd
    BLAST
    Sequence conflicti695 – 70511WLAAQIKANID → CWPPRSRRTST in AAA62385. (PubMed:7929140)CuratedAdd
    BLAST

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 1515MNSEI…ARGSQ → MHSIKFRVFTKLKPIFLEIN GRIPICRHFHGPTTFRLEIS NKTPPIRQKLTFPNIGIQCT RSHHLCCPRDISGNTLLSVK FNCKRHCIKLRSDSGDQKND SPGEKNIQKDKSAQRCGKPI NNLHNGFLNAVNYSEKNAVK KKKSAPKRKCGKSVDELRKC LRTMQDVIDFVHPVKPF in isoform A. 1 PublicationVSP_014950Add
    BLAST
    Alternative sequencei219 – 25032LVGGL…CSQLA → ISAAIATEADFMFIPEEPVS VNWKDEICVKLH in isoform C. 1 PublicationVSP_014951Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L27653 Genomic DNA. Translation: AAA62385.1.
    AE013599 Genomic DNA. Translation: AAF58840.1.
    AE013599 Genomic DNA. Translation: AAF58841.1.
    AE013599 Genomic DNA. Translation: AAM71065.2.
    AF145673 mRNA. Translation: AAD38648.1.
    BT001354 mRNA. Translation: AAN71109.1. Frameshift.
    PIRiA55034.
    RefSeqiNP_523676.1. NM_078952.3. [P52034-2]
    NP_724890.1. NM_165746.3. [P52034-1]
    NP_724891.2. NM_165747.4. [P52034-3]
    UniGeneiDm.7095.

    Genome annotation databases

    EnsemblMetazoaiFBtr0088422; FBpp0087508; FBgn0003071. [P52034-1]
    GeneIDi36060.
    KEGGidme:Dmel_CG4001.
    UCSCiCG4001-RA. d. melanogaster. [P52034-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L27653 Genomic DNA. Translation: AAA62385.1 .
    AE013599 Genomic DNA. Translation: AAF58840.1 .
    AE013599 Genomic DNA. Translation: AAF58841.1 .
    AE013599 Genomic DNA. Translation: AAM71065.2 .
    AF145673 mRNA. Translation: AAD38648.1 .
    BT001354 mRNA. Translation: AAN71109.1 . Frameshift.
    PIRi A55034.
    RefSeqi NP_523676.1. NM_078952.3. [P52034-2 ]
    NP_724890.1. NM_165746.3. [P52034-1 ]
    NP_724891.2. NM_165747.4. [P52034-3 ]
    UniGenei Dm.7095.

    3D structure databases

    ProteinModelPortali P52034.
    SMRi P52034. Positions 18-766.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 61888. 2 interactions.
    MINTi MINT-928619.

    Proteomic databases

    PaxDbi P52034.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0088422 ; FBpp0087508 ; FBgn0003071 . [P52034-1 ]
    GeneIDi 36060.
    KEGGi dme:Dmel_CG4001.
    UCSCi CG4001-RA. d. melanogaster. [P52034-1 ]

    Organism-specific databases

    CTDi 36060.
    FlyBasei FBgn0003071. Pfk.

    Phylogenomic databases

    eggNOGi COG0205.
    GeneTreei ENSGT00390000013209.
    HOGENOMi HOG000148827.
    InParanoidi P52034.
    KOi K00850.
    OMAi VYHMASK.
    OrthoDBi EOG7ZSHV5.
    PhylomeDBi P52034.

    Enzyme and pathway databases

    UniPathwayi UPA00109 ; UER00182 .
    Reactomei REACT_206319. Glycolysis.

    Miscellaneous databases

    GenomeRNAii 36060.
    NextBioi 796655.

    Gene expression databases

    Bgeei P52034.

    Family and domain databases

    HAMAPi MF_03184. Phosphofructokinase_I_E.
    InterProi IPR009161. 6-phosphofructokinase_euk.
    IPR022953. Phosphofructokinase.
    IPR015912. Phosphofructokinase_CS.
    IPR000023. Phosphofructokinase_dom.
    [Graphical view ]
    Pfami PF00365. PFK. 2 hits.
    [Graphical view ]
    PIRSFi PIRSF000533. ATP_PFK_euk. 1 hit.
    PRINTSi PR00476. PHFRCTKINASE.
    SUPFAMi SSF53784. SSF53784. 2 hits.
    TIGRFAMsi TIGR02478. 6PF1K_euk. 1 hit.
    PROSITEi PS00433. PHOSPHOFRUCTOKINASE. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Structure and expression of the gene encoding phosphofructokinase (PFK) in Drosophila melanogaster."
      Currie P.D., Sullivan D.T.
      J. Biol. Chem. 269:24679-24687(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM B), FUNCTION.
      Strain: Oregon-R.
    2. "The genome sequence of Drosophila melanogaster."
      Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
      , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
      Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Berkeley.
    3. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
      Strain: Berkeley.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
      Strain: Berkeley.
      Tissue: Head.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 101-788 (ISOFORM C).
      Strain: Berkeley.
      Tissue: Testis.
    6. "Genetic and biochemical characterization of phosphofructokinase from Drosophila melanogaster."
      Munneke L.R., Collier G.E.
      Biochem. Genet. 23:847-857(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiPFKA_DROME
    AccessioniPrimary (citable) accession number: P52034
    Secondary accession number(s): Q8IH94
    , Q8MKV4, Q9V5G7, Q9Y100
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: August 16, 2005
    Last modified: October 1, 2014
    This is version 108 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Keywords - Technical termi

    Allosteric enzyme, Complete proteome, Reference proteome

    Documents

    1. Drosophila
      Drosophila: entries, gene names and cross-references to FlyBase
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3