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Q9M0F9

- PFKA1_ARATH

UniProt

Q9M0F9 - PFKA1_ARATH

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Protein

ATP-dependent 6-phosphofructokinase 1

Gene
PFK1, At4g29220, F17A13.40
Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - 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 By similarity.UniRule annotation

Catalytic activityi

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

Cofactori

Magnesium By similarity.UniRule annotation

Enzyme regulationi

Allosterically activated by AMP By similarity.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei102 – 1021ATP; via amide nitrogen By similarity
Metal bindingi191 – 1911Magnesium; catalytic By similarity
Sitei192 – 1921Important for substrate specificity; cannot use PPi as phosphoryl donor By similarity
Active sitei221 – 2211Proton acceptor By similarity
Binding sitei320 – 3201Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi165 – 1662ATP By similarity
Nucleotide bindingi190 – 1934ATP By similarity

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.
UniPathwayiUPA00109; UER00182.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent 6-phosphofructokinase 1 (EC:2.7.1.11)
Short name:
ATP-PFK 1
Short name:
Phosphofructokinase 1
Alternative name(s):
Phosphohexokinase 1
Gene namesi
Name:PFK1
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
Note: May be associated with the plasma membrane.1 Publication

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 473472ATP-dependent 6-phosphofructokinase 1UniRule annotationPRO_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 By similarity.UniRule annotation

Protein-protein interaction databases

BioGridi14330. 4 interactions.
IntActiQ9M0F9. 3 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ9M0F9.
SMRiQ9M0F9. Positions 37-443.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni219 – 2213Substrate binding By similarity
Regioni264 – 2663Substrate binding By similarity
Regioni376 – 3794Substrate binding By similarity

Sequence similaritiesi

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

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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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti403 – 4031M → V in AAM91591. 1 Publication

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

« 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: July 9, 2014
This is version 88 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

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