Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

O42938

- PFKA_SCHPO

UniProt

O42938 - PFKA_SCHPO

Protein

ATP-dependent 6-phosphofructokinase

Gene

pfk1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 1 (01 Jun 1998)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis. May also have a role in cell cycle regulation.2 PublicationsUniRule annotation

    Catalytic activityi

    ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate.1 PublicationUniRule 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=0.025 mM for ATP (without effector)1 Publication
    2. KM=0.027 mM for ATP (with 2.6 µM fructose 2,6-bisphosphate)1 Publication
    3. KM=0.63 mM for fructose 6-phosphate (without effector)1 Publication
    4. KM=0.31 mM for fructose 6-phosphate (with 1 mM AMP)1 Publication
    5. KM=0.17 mM for fructose 6-phosphate (with 2.6 µM fructose 2,6-bisphosphate)1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei204 – 2041ATP; via amide nitrogenUniRule annotation
    Metal bindingi298 – 2981Magnesium; catalyticUniRule annotation
    Active sitei345 – 3451Proton acceptorUniRule annotation
    Binding sitei380 – 3801Substrate; shared with dimeric partnerUniRule annotation
    Binding sitei444 – 4441SubstrateUniRule annotation
    Binding sitei472 – 4721Substrate; shared with dimeric partnerUniRule annotation
    Binding sitei655 – 6551Allosteric activator fructose 2,6-bisphosphateUniRule annotation
    Binding sitei750 – 7501Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partnerUniRule annotation
    Binding sitei817 – 8171Allosteric activator fructose 2,6-bisphosphateUniRule annotation
    Binding sitei843 – 8431Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partnerUniRule annotation
    Binding sitei918 – 9181Allosteric activator fructose 2,6-bisphosphateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi267 – 2682ATPUniRule annotation
    Nucleotide bindingi297 – 3004ATPUniRule annotation

    GO - Molecular functioni

    1. 6-phosphofructokinase activity Source: PomBase
    2. ATP binding Source: PomBase
    3. fructose-6-phosphate binding Source: PomBase
    4. 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: PomBase

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Biological processi

    Glycolysis

    Keywords - Ligandi

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

    Enzyme and pathway databases

    ReactomeiREACT_227920. Glycolysis.
    SABIO-RKO42938.
    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:pfk1
    ORF Names:SPBC16H5.02
    OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
    Taxonomic identifieri284812 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
    ProteomesiUP000002485: Chromosome II

    Organism-specific databases

    PomBaseiSPBC16H5.02.

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. 6-phosphofructokinase complex Source: PomBase
    2. cytoplasm Source: PomBase
    3. cytosol Source: PomBase

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 942942ATP-dependent 6-phosphofructokinasePRO_0000112043Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei43 – 431Phosphoserine1 Publication
    Modified residuei45 – 451Phosphoserine1 Publication
    Modified residuei85 – 851Phosphoserine1 Publication
    Modified residuei160 – 1601Phosphoserine1 Publication
    Modified residuei163 – 1631Phosphoserine1 Publication
    Modified residuei167 – 1671Phosphoserine1 Publication
    Modified residuei171 – 1711Phosphoserine1 Publication
    Modified residuei175 – 1751Phosphothreonine1 Publication
    Modified residuei600 – 6001Phosphoserine1 Publication
    Modified residuei602 – 6021Phosphothreonine1 Publication

    Post-translational modificationi

    The N-terminus is blocked.

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiO42938.
    PaxDbiO42938.
    PRIDEiO42938.

    Interactioni

    Subunit structurei

    Homooctamer.1 Publication

    Protein-protein interaction databases

    BioGridi276516. 7 interactions.
    MINTiMINT-4674145.
    STRINGi4896.SPBC16H5.02-1.

    Structurei

    3D structure databases

    ProteinModelPortaliO42938.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 570570N-terminal catalytic PFK domain 1Add
    BLAST
    Regioni343 – 3453Substrate bindingUniRule annotation
    Regioni387 – 3893Substrate bindingUniRule annotation
    Regioni478 – 4814Substrate bindingUniRule annotation
    Regioni571 – 58414Interdomain linkerAdd
    BLAST
    Regioni585 – 942358C-terminal regulatory PFK domain 2Add
    BLAST
    Regioni712 – 7165Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation
    Regioni757 – 7593Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation
    Regioni849 – 8524Allosteric 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.
    HOGENOMiHOG000200154.
    KOiK00850.
    OMAiVYHMASK.
    OrthoDBiEOG7Q5HPV.
    PhylomeDBiO42938.

    Family and domain databases

    Gene3Di3.10.180.10. 1 hit.
    HAMAPiMF_03184. Phosphofructokinase_I_E.
    InterProiIPR009161. 6-phosphofructokinase_euk.
    IPR029068. Glyas_Bleomycin-R_OHBP_Dase.
    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.
    SSF54593. SSF54593. 1 hit.
    TIGRFAMsiTIGR02478. 6PF1K_euk. 1 hit.
    PROSITEiPS00433. PHOSPHOFRUCTOKINASE. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O42938-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSGETVHGIS CYSVVANTED TYNQTLDFYQ KLGFKKVASF GTSDSDNARV    50
    CNESLREDWM HVAGNNSAES VTIKFRLVPG ELSLSPAAED SEWRGQKSSL 100
    VFYYPNLLDL LKQLSADAIK YQAFPNEKKP DEVYVEDPLG NLIGFSDRYN 150
    PFAHANLKKS EESGAASNLE SGLATPVVET LKKATTSDKP AGVKKKIAVM 200
    TSGGDSPGMN AVVRAVARIA IHRGCDAFAI YEGYEGLVQG GDMIKQLQWG 250
    DVRGWLAEGG TLIGTARCMA FRERPGRLRA AKNLISAGID SIIVCGGDGS 300
    LTGADIFRSD WPGLVKELED TKAITPEQAK LYRHLTIVGL VGSIDNDMSS 350
    TDVTIGAFSS LHRICEAVDS ISSTAISHSR AFIVEVMGRH CGWLAVLAAL 400
    ATGADFVFIP ERPAEVGKWQ DELCNSLSSV RKLGKRKSIV IVAEGAIDSE 450
    LNHISPEDIK NLLVERLHLD TRVTTLGHVQ RGGIPCAYDR MLATLQGVDA 500
    VDAVLASTPD TPSPMIAING NKINRKPLME AVKLTHEVAD AIEKKQFAHA 550
    MELRDPEFAD YLHTWEGTTF IEDESHFVPK DERMRVAIIH VGAPAGGMNS 600
    ATRAAVRYCL NRGHTPLAID NGFSGFLRHD SIHELSWIDV DEWCIRGGSE 650
    IGTNRDTPDL DMGFTAFKFQ QHKIDALIII GGFEAFTALS QLESARVNYP 700
    SFRIPMAIIP ATISNNVPGT EFSLGCDTCL NAVMEYCDTI KQSASASRRR 750
    VFVCEVQGGR SGYIATVGGL ITGASAIYTP EDGISLDMLR KDIDHLKATF 800
    ALEAGRNRAG QLILRNECAS KVYTTEVIGN IISEEAHKRF SARTAVPGHV 850
    QQGGNPTPMD RARAARLAMR AIRFFETCRA NDLGNDPSSA VVIGIRGTGV 900
    SFSSVADVEN NETEIEMRRP KNAWWRDMHN LVNILAGKTF AD 942
    Length:942
    Mass (Da):102,555
    Last modified:June 1, 1998 - v1
    Checksum:iC6052AF7C1DB75B4
    GO

    Sequence cautioni

    The sequence BAA13773.1 differs from that shown. Reason: Frameshift at position 836.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CU329671 Genomic DNA. Translation: CAA17900.1.
    D89110 mRNA. Translation: BAA13773.1. Frameshift.
    PIRiT39624.
    T42087.
    RefSeqiNP_595946.1. NM_001021854.2.

    Genome annotation databases

    EnsemblFungiiSPBC16H5.02.1; SPBC16H5.02.1:pep; SPBC16H5.02.
    GeneIDi2539972.
    KEGGispo:SPBC16H5.02.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CU329671 Genomic DNA. Translation: CAA17900.1 .
    D89110 mRNA. Translation: BAA13773.1 . Frameshift.
    PIRi T39624.
    T42087.
    RefSeqi NP_595946.1. NM_001021854.2.

    3D structure databases

    ProteinModelPortali O42938.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 276516. 7 interactions.
    MINTi MINT-4674145.
    STRINGi 4896.SPBC16H5.02-1.

    Proteomic databases

    MaxQBi O42938.
    PaxDbi O42938.
    PRIDEi O42938.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii SPBC16H5.02.1 ; SPBC16H5.02.1:pep ; SPBC16H5.02 .
    GeneIDi 2539972.
    KEGGi spo:SPBC16H5.02.

    Organism-specific databases

    PomBasei SPBC16H5.02.

    Phylogenomic databases

    eggNOGi COG0205.
    HOGENOMi HOG000200154.
    KOi K00850.
    OMAi VYHMASK.
    OrthoDBi EOG7Q5HPV.
    PhylomeDBi O42938.

    Enzyme and pathway databases

    UniPathwayi UPA00109 ; UER00182 .
    Reactomei REACT_227920. Glycolysis.
    SABIO-RK O42938.

    Miscellaneous databases

    NextBioi 20801115.

    Family and domain databases

    Gene3Di 3.10.180.10. 1 hit.
    HAMAPi MF_03184. Phosphofructokinase_I_E.
    InterProi IPR009161. 6-phosphofructokinase_euk.
    IPR029068. Glyas_Bleomycin-R_OHBP_Dase.
    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.
    SSF54593. SSF54593. 1 hit.
    TIGRFAMsi TIGR02478. 6PF1K_euk. 1 hit.
    PROSITEi PS00433. PHOSPHOFRUCTOKINASE. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Analysis of 114 kb of DNA sequence from fission yeast chromosome 2 immediately centromere-distal to his5."
      Xiang Z., Moore K., Wood V., Rajandream M.A., Barrell B.G., Skelton J., Churcher C.M., Lyne M.H., Devlin K., Gwilliam R., Rutherford K.M., Aves S.J.
      Yeast 16:1405-1411(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "The genome sequence of Schizosaccharomyces pombe."
      Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
      , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
      Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 972 / ATCC 24843.
    3. "Identification of open reading frames in Schizosaccharomyces pombe cDNAs."
      Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.
      DNA Res. 4:363-369(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 583-942.
      Strain: PR745.
    4. "Purification, molecular and kinetic characterization of phosphofructokinase-1 from the yeast Schizosaccharomyces pombe: evidence for an unusual subunit composition."
      Reuter R., Naumann M., Baer J., Haferburg D., Kopperschlaeger G.
      Yeast 16:1273-1285(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 182-190 AND 552-558, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBUNIT.
      Strain: CBS 1057.
    5. "Genome-wide search of Schizosaccharomyces pombe genes causing overexpression-mediated cell cycle defects."
      Tallada V.A., Daga R.R., Palomeque C., Garzon A., Jimenez J.
      Yeast 19:1139-1151(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CELL CYCLE REGULATION.
    6. "Structures of S. pombe phosphofructokinase in the F6P-bound and ATP-bound states."
      Benjamin S., Radermacher M., Baer J., Edelmann A., Ruiz T.
      J. Struct. Biol. 159:498-506(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY ELECTRON MICROSCOPY.
    7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43; SER-45; SER-85; SER-160; SER-163; SER-167; SER-171; THR-175; SER-600 AND THR-602, IDENTIFICATION BY MASS SPECTROMETRY.

    Entry informationi

    Entry nameiPFKA_SCHPO
    AccessioniPrimary (citable) accession number: O42938
    Secondary accession number(s): P78762
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 16, 2003
    Last sequence update: June 1, 1998
    Last modified: October 1, 2014
    This is version 110 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. Schizosaccharomyces pombe
      Schizosaccharomyces pombe: entries and gene names
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3