Reviewed, UniProtKB/Swiss-Prot Q9M0F9 (K6PF1_ARATH)

Names and origin

Protein names

Recommended 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

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	473 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate. Ref.4
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.4
Tissue specificity	Expressed in roots, leaves, stems and flowers. Ref.4
Sequence similarities	Belongs to the phosphofructokinase family.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	glycolysis Ref.4 Inferred from direct assay. Source: TAIR
Cellular component	6-phosphofructokinase complex Inferred from electronic annotation. Source: InterPro plasma membrane Ref.4 Inferred from direct assay. Source: TAIR
Molecular function	6-phosphofructokinase activity Ref.4 Inferred from direct assay. Source: TAIR ATP binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 473	473	6-phosphofructokinase 1		PRO_0000330768
Regions
	Nucleotide binding	112 – 116	5	ATP By similarity
	Nucleotide binding	248 – 252	5	ATP By similarity
	Nucleotide binding	266 – 283	18	ATP By similarity
Sites
	Active site	221	1	Proton acceptor By similarity
Amino acid modifications
	Modified residue	71	1	Phosphoserine Ref.5
Experimental info
	Sequence conflict	403	1	M → V in AAM91591. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9M0F9-1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: E1B31E547259FF4B	FASTA	473	51,991
	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

References

	« Hide 'large scale' referencesShow '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. , 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: 10617198] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[2]	"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: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[3]	"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.
[4]	"Characterisation of the ATP-dependent phosphofructokinase gene family from Arabidopsis thaliana." Mustroph A., Sonnewald U., Biemelt S. FEBS Lett. 581:2401-2410(2007) [PubMed: 17485088] [Abstract] Cited for: CATALYTIC ACTIVITY, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, GENE FAMILY, NOMENCLATURE.
[5]	"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: 19376835] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71, MASS SPECTROMETRY. Tissue: Seedling.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL161574 Genomic DNA. Translation: CAB79680.1. AY128388 mRNA. Translation: AAM91591.1. BT015793 mRNA. Translation: AAU90083.1.
IPI	IPI00541393.
PIR	T13433.
RefSeq	NP_194651.1.
UniGene	At.48917 At.71085 Rsa.16529 Rsa.4778
3D structure databases
HSSP	HSSP built from PDB template 3PFK based on UniProtKB P00512.
SMR	Q9M0F9. Positions 34-448.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9M0F9.
Proteomic databases
PRIDE	Q9M0F9.
Genome annotation databases
GeneID	829043.
GenomeReviews	Gene locus AT4G29220 in contig CT486007_GR.
KEGG	ath:AT4G29220.
NMPDR	fig|3702.1.peg.20891.
Organism-specific databases
TAIR	At4g29220.
Phylogenomic databases
eggNOG	KOG2440.
HOGENOM	HBG316947.
InParanoid	Q9M0F9.
Gene expression databases
Genevestigator	Q9M0F9.
Family and domain databases
InterPro	IPR000023. Phosphofructokinase. IPR012004. PyroP-dep_PFruKinase_TP0108. [Graphical view]
Pfam	PF00365. PFK. 1 hit. [Graphical view]
PIRSF	PIRSF000534. PPi_PFK_TP0108. 1 hit.
PRINTS	PR00476. PHFRCTKINASE.
ProtoNet	Search...

Entry information

Entry name

K6PF1_ARATH

Accession

Primary (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:	February 9, 2010
This is version 54 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)