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Q9M076 (PFKA6_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
ATP-dependent 6-phosphofructokinase 6

Short name=ATP-PFK 6
Short name=Phosphofructokinase 6
EC=2.7.1.11
Alternative name(s):
Phosphohexokinase 6
Gene names
Name:PFK6
Ordered Locus Names:At4g32840
ORF Names:T16I18.50
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length462 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis By similarity. HAMAP-Rule MF_03186

Catalytic activity

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

Cofactor

Magnesium By similarity. HAMAP-Rule MF_03186

Enzyme regulation

Allosterically activated by AMP By similarity. HAMAP-Rule MF_03186

Pathway

Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4. HAMAP-Rule MF_03186

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_03186

Subcellular location

Cytoplasm. Note: May be associated with the outer membrane of mitochondria. Ref.6

Tissue specificity

Expressed in roots, leaves, stems and flowers. Ref.6

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 462461ATP-dependent 6-phosphofructokinase 6 HAMAP-Rule MF_03186
PRO_0000330773

Regions

Nucleotide binding165 – 1662ATP By similarity
Nucleotide binding190 – 1934ATP By similarity
Region219 – 2213Substrate binding By similarity
Region264 – 2663Substrate binding By similarity
Region374 – 3774Substrate binding By similarity

Sites

Active site2211Proton acceptor By similarity
Metal binding1911Magnesium; catalytic By similarity
Binding site1021ATP; via amide nitrogen By similarity
Binding site3201Substrate By similarity
Site1921Important for substrate specificity; cannot use PPi as phosphoryl donor By similarity

Amino acid modifications

Modified residue21N-acetylalanine Ref.7
Modified residue711Phosphoserine By similarity

Experimental info

Sequence conflict2821V → A in AAM65566. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q9M076 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 283E7758C5DB8C24

FASTA46250,788
        10         20         30         40         50         60 
MASNGVDEQI KLVEGPAGYV LEDVPHLSDY ILDLPTYPNP LQSNAAYSVV RQYFVDEDDT 

        70         80         90        100        110        120 
VQEKIVVHKD SPRGTHFRRA GPRQKVYFKP SDVRACIVTC GGLCPGLNTV IREIVCGLHF 

       130        140        150        160        170        180 
MYGVTEVIGV DCGFRGFYSK NTVALTPKTV SDIHKRGGTI LGTSRGGHDT SKIVDNIQDR 

       190        200        210        220        230        240 
EINQVYIIGG DGTQKGANAI YKEIRRRGLK VAVAGIPKTI DNDIPVIDKS FGFDTAVEEA 

       250        260        270        280        290        300 
QRAINAAHVE ATSVENGIGI VKLMGRYSGF IAMYATLASR DVDCCLIPES PFYLEGKGGL 

       310        320        330        340        350        360 
YEFIAKRLRE NGHMVIVIAE GAGQDLVAES IEQQDASGNK LLKDVGLWMS LKIKEYFAKH 

       370        380        390        400        410        420 
NVMDITLKYI DPTYMIRAIP ANASDNVYST LLAQSAVHGA MAGYTGFVSG LVNGRHTYIP 

       430        440        450        460 
FNRITERQNK VVITDRMWAR MLSSTNQPSF MNPPKGTTEF TD 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]"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. expand/collapse author list , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
Submitted (JUL-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 (MAR-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(2007) [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(2012) [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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRT10691.
RefSeqNP_195010.1. NM_119437.2.
UniGeneAt.31631.

3D structure databases

ProteinModelPortalQ9M076.
SMRQ9M076. Positions 37-441.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PaxDbQ9M076.
PRIDEQ9M076.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G32840.1; AT4G32840.1; AT4G32840.
GeneID829420.
KEGGath:AT4G32840.

Organism-specific databases

TAIRAT4G32840.

Phylogenomic databases

eggNOGCOG0205.
HOGENOMHOG000016186.
InParanoidQ9M076.
KOK00850.
OMADYCKSKK.
PhylomeDBQ9M076.

Enzyme and pathway databases

BioCycARA:AT4G32840-MONOMER.
UniPathwayUPA00109; UER00182.

Gene expression databases

GenevestigatorQ9M076.

Family and domain databases

HAMAPMF_01981. Phosphofructokinase_II_X.
InterProIPR022953. Phosphofructokinase.
IPR000023. Phosphofructokinase_dom.
IPR012004. PyroP-dep_PFruKinase_TP0108.
[Graphical view]
PfamPF00365. PFK. 1 hit.
[Graphical view]
PIRSFPIRSF000534. PPi_PFK_TP0108. 1 hit.
PRINTSPR00476. PHFRCTKINASE.
SUPFAMSSF53784. SSF53784. 1 hit.
ProtoNetSearch...

Entry information

Entry namePFKA6_ARATH
AccessionPrimary (citable) accession number: Q9M076
Secondary accession number(s): Q8LA55
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: October 1, 2000
Last modified: July 9, 2014
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names