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Protein

ATP-dependent 6-phosphofructokinase 1

Gene

PFK1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

Mg2+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
Complete GO annotation...

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.
ReactomeiREACT_248260. Glycolysis.
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. cytosol Source: TAIR
  2. plasma membrane Source: TAIR
Complete GO annotation...

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.
OMAiVKCIGIL.
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

        10         20         30         40         50
MSSSVPNSDR KIVTGPAGYI LEDVPHFSDD FPDHPTYPNP LQDNAAYSVV
60 70 80 90 100
KQYFVDEDDT VPQKIVVHPD SPRGTHFRRA GPRQRVYFES DDVLACIVTC
110 120 130 140 150
GGLCPGLNTV IREIVCGLSY MYGVKRILGI DGGYRGFYAR NTIHLDLKTV
160 170 180 190 200
NDIHRSGGTI LGTSRGGHNT TKIVDSIQDR GINQVYIIGG DGSQKGAAAI
210 220 230 240 250
FEEIRKRKLK VAVAGIPKTI DNDIPIIDRS FGFDTAVEEA QRAINAAHVE
260 270 280 290 300
ATSFENGIGL VKLMGRYSGF IAMHATLASR DVDCCLIPES PFFLEGSGGL
310 320 330 340 350
FEFIDKRLKE SGHMVIVIAE GAGQDLLSES MKESTTLKDA SGNKLLQDIG
360 370 380 390 400
LWISQRIKDH FAKKMTLTLK YIDPTYMIRA VPSNASDNVC CTLLAQSAVH
410 420 430 440 450
GVMAGYNGFT VGLVNGRHTY IPFNRITEKQ NKVVITDRMW ARLLSSTNQP
460 470
SFMKQADKIH SNQLVGEPGT MKW
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi14330. 4 interactions.
IntActiQ9M0F9. 3 interactions.

Proteomic databases

PaxDbiQ9M0F9.
PRIDEiQ9M0F9.

Protocols and materials databases

DNASUi829043.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

TAIRiAT4G29220.

Phylogenomic databases

eggNOGiCOG0205.
HOGENOMiHOG000016186.
InParanoidiQ9M0F9.
KOiK00850.
OMAiVKCIGIL.
PhylomeDBiQ9M0F9.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00182.
BioCyciARA:AT4G29220-MONOMER.
ReactomeiREACT_248260. Glycolysis.

Gene expression databases

GenevestigatoriQ9M0F9.

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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: January 7, 2015
This is version 92 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.