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)

Q9M0F9

- PFKA1_ARATH

UniProt

Q9M0F9 - PFKA1_ARATH

Protein

ATP-dependent 6-phosphofructokinase 1

Gene

PFK1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 89 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      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.UniRule 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 AMP.UniRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei102 – 1021ATP; via amide nitrogenUniRule annotation
    Metal bindingi191 – 1911Magnesium; catalyticUniRule annotation
    Sitei192 – 1921Important for substrate specificity; cannot use PPi as phosphoryl donorUniRule annotation
    Active sitei221 – 2211Proton acceptorUniRule annotation
    Binding sitei320 – 3201SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi165 – 1662ATPUniRule annotation
    Nucleotide bindingi190 – 1934ATPUniRule annotation

    GO - Molecular functioni

    1. 6-phosphofructokinase activity Source: TAIR
    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: TAIR

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Biological processi

    Glycolysis

    Keywords - Ligandi

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

    Enzyme and pathway databases

    BioCyciARA:AT4G29220-MONOMER.
    UniPathwayiUPA00109; UER00182.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    ATP-dependent 6-phosphofructokinase 1UniRule annotation (EC:2.7.1.11UniRule annotation)
    Short name:
    ATP-PFK 1UniRule annotation
    Short name:
    Phosphofructokinase 1UniRule annotation
    Alternative name(s):
    Phosphohexokinase 1UniRule annotation
    Gene namesi
    Name:PFK1UniRule annotation
    Ordered Locus Names:At4g29220
    ORF Names:F17A13.40
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 4

    Organism-specific databases

    TAIRiAT4G29220.

    Subcellular locationi

    Cytoplasm 1 PublicationUniRule annotation
    Note: May be associated with the plasma membrane.

    GO - Cellular componenti

    1. 6-phosphofructokinase complex Source: InterPro
    2. cytosol Source: TAIR
    3. plasma membrane Source: TAIR

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 473472ATP-dependent 6-phosphofructokinase 1PRO_0000330768Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei71 – 711Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ9M0F9.
    PRIDEiQ9M0F9.

    Expressioni

    Tissue specificityi

    Expressed in roots, leaves, stems and flowers.1 Publication

    Gene expression databases

    GenevestigatoriQ9M0F9.

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation

    Protein-protein interaction databases

    BioGridi14330. 4 interactions.
    IntActiQ9M0F9. 3 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9M0F9.
    SMRiQ9M0F9. Positions 37-443.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni219 – 2213Substrate bindingUniRule annotation
    Regioni264 – 2663Substrate bindingUniRule annotation
    Regioni376 – 3794Substrate bindingUniRule annotation

    Sequence similaritiesi

    Belongs to the phosphofructokinase type A (PFKA) family. PPi-dependent PFK group II subfamily. Atypical ATP-dependent clade "X" sub-subfamily.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0205.
    HOGENOMiHOG000016186.
    InParanoidiQ9M0F9.
    KOiK00850.
    OMAiGIYRGYK.
    PhylomeDBiQ9M0F9.

    Family and domain databases

    HAMAPiMF_01981. Phosphofructokinase_II_X.
    InterProiIPR022953. Phosphofructokinase.
    IPR000023. Phosphofructokinase_dom.
    IPR012004. PyroP-dep_PFruKinase_TP0108.
    [Graphical view]
    PfamiPF00365. PFK. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000534. PPi_PFK_TP0108. 1 hit.
    PRINTSiPR00476. PHFRCTKINASE.
    SUPFAMiSSF53784. SSF53784. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    Q9M0F9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSSSVPNSDR KIVTGPAGYI LEDVPHFSDD FPDHPTYPNP LQDNAAYSVV    50
    KQYFVDEDDT VPQKIVVHPD SPRGTHFRRA GPRQRVYFES DDVLACIVTC 100
    GGLCPGLNTV IREIVCGLSY MYGVKRILGI DGGYRGFYAR NTIHLDLKTV 150
    NDIHRSGGTI LGTSRGGHNT TKIVDSIQDR GINQVYIIGG DGSQKGAAAI 200
    FEEIRKRKLK VAVAGIPKTI DNDIPIIDRS FGFDTAVEEA QRAINAAHVE 250
    ATSFENGIGL VKLMGRYSGF IAMHATLASR DVDCCLIPES PFFLEGSGGL 300
    FEFIDKRLKE SGHMVIVIAE GAGQDLLSES MKESTTLKDA SGNKLLQDIG 350
    LWISQRIKDH FAKKMTLTLK YIDPTYMIRA VPSNASDNVC CTLLAQSAVH 400
    GVMAGYNGFT VGLVNGRHTY IPFNRITEKQ NKVVITDRMW ARLLSSTNQP 450
    SFMKQADKIH SNQLVGEPGT MKW 473
    Length:473
    Mass (Da):51,991
    Last modified:October 1, 2000 - v1
    Checksum:iE1B31E547259FF4B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti403 – 4031M → V in AAM91591. (PubMed:14593172)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL161574 Genomic DNA. Translation: CAB79680.1.
    CP002687 Genomic DNA. Translation: AEE85604.1.
    AY128388 mRNA. Translation: AAM91591.1.
    BT015793 mRNA. Translation: AAU90083.1.
    PIRiT13433.
    RefSeqiNP_194651.1. NM_119066.3.
    UniGeneiAt.48917.
    At.71085.

    Genome annotation databases

    EnsemblPlantsiAT4G29220.1; AT4G29220.1; AT4G29220.
    GeneIDi829043.
    KEGGiath:AT4G29220.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL161574 Genomic DNA. Translation: CAB79680.1 .
    CP002687 Genomic DNA. Translation: AEE85604.1 .
    AY128388 mRNA. Translation: AAM91591.1 .
    BT015793 mRNA. Translation: AAU90083.1 .
    PIRi T13433.
    RefSeqi NP_194651.1. NM_119066.3.
    UniGenei At.48917.
    At.71085.

    3D structure databases

    ProteinModelPortali Q9M0F9.
    SMRi Q9M0F9. Positions 37-443.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 14330. 4 interactions.
    IntActi Q9M0F9. 3 interactions.

    Proteomic databases

    PaxDbi Q9M0F9.
    PRIDEi Q9M0F9.

    Protocols and materials databases

    DNASUi 829043.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT4G29220.1 ; AT4G29220.1 ; AT4G29220 .
    GeneIDi 829043.
    KEGGi ath:AT4G29220.

    Organism-specific databases

    TAIRi AT4G29220.

    Phylogenomic databases

    eggNOGi COG0205.
    HOGENOMi HOG000016186.
    InParanoidi Q9M0F9.
    KOi K00850.
    OMAi GIYRGYK.
    PhylomeDBi Q9M0F9.

    Enzyme and pathway databases

    UniPathwayi UPA00109 ; UER00182 .
    BioCyci ARA:AT4G29220-MONOMER.

    Gene expression databases

    Genevestigatori Q9M0F9.

    Family and domain databases

    HAMAPi MF_01981. Phosphofructokinase_II_X.
    InterProi IPR022953. Phosphofructokinase.
    IPR000023. Phosphofructokinase_dom.
    IPR012004. PyroP-dep_PFruKinase_TP0108.
    [Graphical view ]
    Pfami PF00365. PFK. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000534. PPi_PFK_TP0108. 1 hit.
    PRINTSi PR00476. PHFRCTKINASE.
    SUPFAMi SSF53784. SSF53784. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
      Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
      , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
      Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    2. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    3. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
      Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
      , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
      Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.
    4. "Arabidopsis ORF clones."
      Shinn P., Chen H., Cheuk R.F., Kim C.J., Ecker J.R.
      Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.
    5. "Characterisation of the ATP-dependent phosphofructokinase gene family from Arabidopsis thaliana."
      Mustroph A., Sonnewald U., Biemelt S.
      FEBS Lett. 581:2401-2410(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, GENE FAMILY, NOMENCLATURE.
    6. "Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks."
      Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S.
      Plant Physiol. 150:889-903(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiPFKA1_ARATH
    AccessioniPrimary (citable) accession number: Q9M0F9
    Secondary accession number(s): Q8L7L4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 29, 2008
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 89 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Allosteric enzyme, Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3