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Q27778

- PFKA_SCHMA

UniProt

Q27778 - PFKA_SCHMA

Protein

ATP-dependent 6-phosphofructokinase

Gene

PFK

Organism
Schistosoma mansoni (Blood fluke)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 70 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      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.1 PublicationUniRule annotation

    Catalytic activityi

    ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate.2 PublicationsUniRule annotation

    Cofactori

    Magnesium.UniRule annotation

    Enzyme regulationi

    Allosterically activated by ADP, AMP, or fructose 2,6-bisphosphate, and allosterically inhibited by ATP or citrate.1 PublicationUniRule annotation

    Kineticsi

    1. KM=3.5 mM for ATP1 Publication
    2. KM=0.8 mM for fructose 6-phosphate1 Publication

    pH dependencei

    Optimum pH is 7.5-9.0.1 Publication

    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 sitei479 – 4791Allosteric 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: UniProtKB-EC
    2. ATP binding Source: UniProtKB-KW
    3. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. fructose 6-phosphate metabolic process Source: InterPro
    2. glycolytic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Biological processi

    Glycolysis

    Keywords - Ligandi

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

    Enzyme and pathway databases

    SABIO-RKQ27778.
    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
    OrganismiSchistosoma mansoni (Blood fluke)
    Taxonomic identifieri6183 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaPlatyhelminthesTrematodaDigeneaStrigeididaSchistosomatoideaSchistosomatidaeSchistosoma

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. 6-phosphofructokinase complex Source: InterPro

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 781781ATP-dependent 6-phosphofructokinasePRO_0000112033Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation

    Structurei

    3D structure databases

    ProteinModelPortaliQ27778.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 394394N-terminal catalytic PFK domain 1Add
    BLAST
    Regioni166 – 1683Substrate bindingUniRule annotation
    Regioni210 – 2123Substrate bindingUniRule annotation
    Regioni300 – 3034Substrate bindingUniRule annotation
    Regioni395 – 40915Interdomain linkerAdd
    BLAST
    Regioni410 – 781372C-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

    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. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q27778-1 [UniParc]FASTAAdd to Basket

    « Hide

    MATWMEGKYV ARGQFTGECI AVLTSGGDAQ GMNAAVRAVV RMGIYCGCRV    50
    FFIREGYQGL VDGGQNIQEA SWADVSGILQ LGGTKIGSAR CMDFRERYGR 100
    LKAAENLVKN QITNLVVIGG DGSLTGANLF RAEWSSLLEE LVTSNKISAE 150
    SAKQFHRLNI VGLVGSIDND FCGTDMTIGA DSALHRIIEA TDAISTTAHS 200
    HQRCFILEVM GRHCGYLALV ASMACEADWV FIPEMPPTDD WREKLCHKLR 250
    MNREHGQRVN IIMVAEGAID RACKPITCEI VKNLIVSELQ LDTRITVLGH 300
    VQRGGSPSAF DRILGSRMGA EAVLALMDAD RDPNLPSCVI SLDGNQAVRV 350
    PLVKCVDRTR QVAEAMKACD FDHAVELRGT SFMNNLATYI KLSKIEQPRQ 400
    SVMSSENNLR IGIVNVGAPA CGINAVIRGF TRLGITKGYK VIGIHEGFSG 450
    LVKGDASEIQ WADVRGWVGM GGSMLGTRRD TPNGLGIDKV AAKFKELKLS 500
    GLLIIGGFEA YECMIELVEG REKYPELCIP MAMVPATISN NVPGTDFSLG 550
    CDTALNEITS VLDKIKQSAL GTKRRVFVVE TMGGYCGYLA TMSALAGGAD 600
    AAYIFEEPFT IDDLREDVVH LRAKIDDNVK RGLVLRADML INTITSEFIH 650
    QLYAQEGQGI FDCRCNVLGH MQQGDRPSPF DRSLGTKFAS KAIDWLDEQI 700
    NANIVQILQS IHQTFMLYIN WYCTSSDNLF KYSLELREHT DFVHRLPKEE 750
    WWLSLRPLMR IMAKHDSLYE SESIMAGTDR K 781
    Length:781
    Mass (Da):86,060
    Last modified:November 1, 1996 - v1
    Checksum:iB2CDF20CAE926C38
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L31531 mRNA. Translation: AAA29911.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L31531 mRNA. Translation: AAA29911.1 .

    3D structure databases

    ProteinModelPortali Q27778.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00109 ; UER00182 .
    SABIO-RK Q27778.

    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. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterization of a cDNA encoding phosphofructokinase from Schistosoma mansoni."
      Ding J., Su J.G.J., Mansour T.E.
      Mol. Biochem. Parasitol. 66:105-110(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY.
    2. "Purification, kinetics and inhibition by antimonials of recombinant phosphofructokinase from Schistosoma mansoni."
      Su J.G., Mansour J.M., Mansour T.E.
      Mol. Biochem. Parasitol. 81:171-178(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.

    Entry informationi

    Entry nameiPFKA_SCHMA
    AccessioniPrimary (citable) accession number: Q27778
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 70 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Keywords - Technical termi

    Allosteric enzyme

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3