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Q9M0F9 (K6PF1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
6-phosphofructokinase 1

EC=2.7.1.11
Alternative name(s):
Phosphofructokinase 1
Phosphohexokinase 1
Gene names
Name:PFK1
Ordered Locus Names:At4g29220
ORF Names:F17A13.40
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length473 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate. Ref.5

Pathway

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

Subcellular location

Cytoplasm. Note: May be associated with the plasma membrane. Ref.5

Tissue specificity

Expressed in roots, leaves, stems and flowers. Ref.5

Sequence similarities

Belongs to the phosphofructokinase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 4734726-phosphofructokinase 1
PRO_0000330768

Regions

Nucleotide binding112 – 1165ATP By similarity
Nucleotide binding248 – 2525ATP By similarity
Nucleotide binding266 – 28318ATP By similarity

Sites

Active site2211Proton acceptor By similarity

Amino acid modifications

Modified residue711Phosphoserine Ref.6

Experimental info

Sequence conflict4031M → V in AAM91591. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9M0F9 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: E1B31E547259FF4B

FASTA47351,991
        10         20         30         40         50         60 
MSSSVPNSDR KIVTGPAGYI LEDVPHFSDD FPDHPTYPNP LQDNAAYSVV KQYFVDEDDT 

        70         80         90        100        110        120 
VPQKIVVHPD SPRGTHFRRA GPRQRVYFES DDVLACIVTC GGLCPGLNTV IREIVCGLSY 

       130        140        150        160        170        180 
MYGVKRILGI DGGYRGFYAR NTIHLDLKTV NDIHRSGGTI LGTSRGGHNT TKIVDSIQDR 

       190        200        210        220        230        240 
GINQVYIIGG DGSQKGAAAI FEEIRKRKLK VAVAGIPKTI DNDIPIIDRS FGFDTAVEEA 

       250        260        270        280        290        300 
QRAINAAHVE ATSFENGIGL VKLMGRYSGF IAMHATLASR DVDCCLIPES PFFLEGSGGL 

       310        320        330        340        350        360 
FEFIDKRLKE SGHMVIVIAE GAGQDLLSES MKESTTLKDA SGNKLLQDIG LWISQRIKDH 

       370        380        390        400        410        420 
FAKKMTLTLK YIDPTYMIRA VPSNASDNVC CTLLAQSAVH GVMAGYNGFT VGLVNGRHTY 

       430        440        450        460        470 
IPFNRITEKQ NKVVITDRMW ARLLSSTNQP SFMKQADKIH SNQLVGEPGT MKW 

« 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]"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].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL161574 Genomic DNA. Translation: CAB79680.1.
CP002687 Genomic DNA. Translation: AEE85604.1.
AY128388 mRNA. Translation: AAM91591.1.
BT015793 mRNA. Translation: AAU90083.1.
PIRT13433.
RefSeqNP_194651.1. NM_119066.3.
UniGeneAt.48917.
At.71085.

3D structure databases

ProteinModelPortalQ9M0F9.
SMRQ9M0F9. Positions 37-443.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid14330. 4 interactions.
IntActQ9M0F9. 3 interactions.

Proteomic databases

PaxDbQ9M0F9.
PRIDEQ9M0F9.

Protocols and materials databases

DNASU829043.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G29220.1; AT4G29220.1; AT4G29220.
GeneID829043.
KEGGath:AT4G29220.

Organism-specific databases

TAIRAT4G29220.

Phylogenomic databases

eggNOGCOG0205.
HOGENOMHOG000016186.
InParanoidQ9M0F9.
KOK00850.
OMARRGYQGM.
PhylomeDBQ9M0F9.
ProtClustDBPLN02564.

Enzyme and pathway databases

BioCycARA:AT4G29220-MONOMER.
UniPathwayUPA00109; UER00182.

Gene expression databases

GenevestigatorQ9M0F9.

Family and domain databases

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 nameK6PF1_ARATH
AccessionPrimary (citable) accession number: Q9M0F9
Secondary accession number(s): Q8L7L4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: October 1, 2000
Last modified: April 16, 2014
This is version 85 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