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Protein

ATP-dependent 6-phosphofructokinase 6

Gene

PFK6

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.UniRule annotation1 Publication

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:AT4G32840-MONOMER.
BRENDAi2.7.1.11. 399.
ReactomeiREACT_293115. Glycolysis.
UniPathwayiUPA00109; UER00182.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent 6-phosphofructokinase 6UniRule annotation (EC:2.7.1.11UniRule annotation)
Short name:
ATP-PFK 6UniRule annotation
Short name:
Phosphofructokinase 6UniRule annotation
Alternative name(s):
Phosphohexokinase 6UniRule annotation
Gene namesi
Name:PFK6UniRule annotation
Ordered Locus Names:At4g32840
ORF Names:T16I18.50
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G32840.

Subcellular locationi

Cytoplasm UniRule annotation1 Publication
Note: May be associated with the outer membrane of mitochondria.

GO - Cellular componenti

  1. cytosol Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 462461ATP-dependent 6-phosphofructokinase 6PRO_0000330773Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei71 – 711PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ9M076.
PRIDEiQ9M076.

Expressioni

Tissue specificityi

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

Gene expression databases

GenevestigatoriQ9M076.

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ9M076.
SMRiQ9M076. Positions 37-441.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni219 – 2213Substrate bindingUniRule annotation
Regioni264 – 2663Substrate bindingUniRule annotation
Regioni374 – 3774Substrate 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.
InParanoidiQ9M076.
KOiK00850.
OMAiITERQNK.
PhylomeDBiQ9M076.

Family and domain databases

HAMAPiMF_01981. Phosphofructokinase_II_X.
InterProiIPR022953. Phosphofructokinase.
IPR000023. Phosphofructokinase_dom.
IPR012004. PyroP-dep_PFK_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.

Q9M076-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASNGVDEQI KLVEGPAGYV LEDVPHLSDY ILDLPTYPNP LQSNAAYSVV
60 70 80 90 100
RQYFVDEDDT VQEKIVVHKD SPRGTHFRRA GPRQKVYFKP SDVRACIVTC
110 120 130 140 150
GGLCPGLNTV IREIVCGLHF MYGVTEVIGV DCGFRGFYSK NTVALTPKTV
160 170 180 190 200
SDIHKRGGTI LGTSRGGHDT SKIVDNIQDR EINQVYIIGG DGTQKGANAI
210 220 230 240 250
YKEIRRRGLK VAVAGIPKTI DNDIPVIDKS FGFDTAVEEA QRAINAAHVE
260 270 280 290 300
ATSVENGIGI VKLMGRYSGF IAMYATLASR DVDCCLIPES PFYLEGKGGL
310 320 330 340 350
YEFIAKRLRE NGHMVIVIAE GAGQDLVAES IEQQDASGNK LLKDVGLWMS
360 370 380 390 400
LKIKEYFAKH NVMDITLKYI DPTYMIRAIP ANASDNVYST LLAQSAVHGA
410 420 430 440 450
MAGYTGFVSG LVNGRHTYIP FNRITERQNK VVITDRMWAR MLSSTNQPSF
460
MNPPKGTTEF TD
Length:462
Mass (Da):50,788
Last modified:October 1, 2000 - v1
Checksum:i283E7758C5DB8C24
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti282 – 2821V → A in AAM65566 (Ref. 5) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL161582 Genomic DNA. Translation: CAB80001.1.
CP002687 Genomic DNA. Translation: AEE86125.1.
BT006001 mRNA. Translation: AAO64936.1.
AK227471 mRNA. Translation: BAE99473.1.
AY088020 mRNA. Translation: AAM65566.1.
PIRiT10691.
RefSeqiNP_195010.1. NM_119437.2.
UniGeneiAt.31631.

Genome annotation databases

EnsemblPlantsiAT4G32840.1; AT4G32840.1; AT4G32840.
GeneIDi829420.
KEGGiath:AT4G32840.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL161582 Genomic DNA. Translation: CAB80001.1.
CP002687 Genomic DNA. Translation: AEE86125.1.
BT006001 mRNA. Translation: AAO64936.1.
AK227471 mRNA. Translation: BAE99473.1.
AY088020 mRNA. Translation: AAM65566.1.
PIRiT10691.
RefSeqiNP_195010.1. NM_119437.2.
UniGeneiAt.31631.

3D structure databases

ProteinModelPortaliQ9M076.
SMRiQ9M076. Positions 37-441.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PaxDbiQ9M076.
PRIDEiQ9M076.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G32840.1; AT4G32840.1; AT4G32840.
GeneIDi829420.
KEGGiath:AT4G32840.

Organism-specific databases

TAIRiAT4G32840.

Phylogenomic databases

eggNOGiCOG0205.
HOGENOMiHOG000016186.
InParanoidiQ9M076.
KOiK00850.
OMAiITERQNK.
PhylomeDBiQ9M076.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00182.
BioCyciARA:AT4G32840-MONOMER.
BRENDAi2.7.1.11. 399.
ReactomeiREACT_293115. Glycolysis.

Gene expression databases

GenevestigatoriQ9M076.

Family and domain databases

HAMAPiMF_01981. Phosphofructokinase_II_X.
InterProiIPR022953. Phosphofructokinase.
IPR000023. Phosphofructokinase_dom.
IPR012004. PyroP-dep_PFK_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(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (MAR-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(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  4. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
    Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
    , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
    Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "Full-length cDNA from Arabidopsis thaliana."
    Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
    Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  6. "Characterisation of the ATP-dependent phosphofructokinase gene family from Arabidopsis thaliana."
    Mustroph A., Sonnewald U., Biemelt S.
    FEBS Lett. 581:2401-2410(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, GENE FAMILY, NOMENCLATURE.
  7. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPFKA6_ARATH
AccessioniPrimary (citable) accession number: Q9M076
Secondary accession number(s): Q8LA55
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: October 1, 2000
Last modified: April 1, 2015
This is version 95 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.