Reviewed, UniProtKB/Swiss-Prot Q94AA4 (K6PF3_ARATH)

Names and origin

Protein names

Recommended name:
    6-phosphofructokinase 3
    EC=2.7.1.11
Alternative name(s):
    Phosphofructokinase 3
    Phosphohexokinase 3

Gene names

Name:	PFK3
Ordered Locus Names:	At4g26270
ORF Names:	T25K17.80

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 › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	489 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate. Ref.3
Pathway	Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4.
Subcellular location	Cytoplasm. Ref.3
Tissue specificity	Mostly expressed in roots and flowers. Ref.3
Sequence similarities	Belongs to the phosphofructokinase family.
Sequence caution	The sequence CAB38956.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAB79482.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	glycolysis Ref.3 Inferred from direct assay. Source: TAIR
Cellular component	6-phosphofructokinase complex Inferred from electronic annotation. Source: InterPro
Molecular function	6-phosphofructokinase activity Ref.3 Inferred from direct assay. Source: TAIR ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CAM1	P25854	1	EBI-1238600,EBI-1235664
CAM6	Q03509	1	EBI-1238600,EBI-1236097
CML9	Q9S744	1	EBI-1238600,EBI-1236048

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 489	489	6-phosphofructokinase 3		PRO_0000330770
Regions
	Nucleotide binding	111 – 115	5	ATP By similarity
	Nucleotide binding	247 – 251	5	ATP By similarity
	Nucleotide binding	265 – 282	18	ATP By similarity
Sites
	Active site	220	1	Proton acceptor By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q94AA4-1 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: AE2C1EA15B64F7E0	FASTA	489	53,666
	10 20 30 40 50 60 MSTVESSKPK IINGSCGYVL EDVPHLSDYL PGLPTYPNPL QDNPAYSVVK QYFVDADDSV 70 80 90 100 110 120 PQKIVVHKDG PRGIHFRRAG PRQKVYFESD EVHACIVTCG GLCPGLNTVI REIVSSLSYM 130 140 150 160 170 180 YGVKRILGID GGYRGFYAKN TVSLDSKVVN DIHKRGGTIL GTSRGGHDTT KIVDSIQDRG 190 200 210 220 230 240 INQVYIIGGD GTQRGASVIF EEIRRRGLKV AVIGIPKTID NDIPVIDKSF GFDTAVEEAQ 250 260 270 280 290 300 RAINAAHVEA ESIENGIGVV KLMGRYSGFI AMYATLASRD VDCCLIPESP FYLEGEGGLF 310 320 330 340 350 360 EYIEKRLKES GHMVLVIAEG AGQDLMSKSM ESMTLKDASG NKLLKDVGLW LSQSIKDHFN 370 380 390 400 410 420 QKKMVMNLKY IDPTYMIRAV PSNASDNVYC TLLAQSAVHG AMAGYTGYIS GLVNGRQTYI 430 440 450 460 470 480 PFYRITEKQN HVVITDRMWA RLLSSTNQPS FLGPKDVFDN KEKPMSALLD DGNCNGVVDV PPVTKEITK

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]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AL049171 Genomic DNA. Translation: CAB38956.1. Sequence problems. AL161564 Genomic DNA. Translation: CAB79482.1. Sequence problems. AY049245 mRNA. Translation: AAK83587.1. AY090267 mRNA. Translation: AAL90928.1.
IPI	IPI00545493.
PIR	T06011.
RefSeq	NP_567742.1.
UniGene	At.2887
3D structure databases
HSSP	HSSP built from PDB template 1MTO based on UniProtKB P00512.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q94AA4. 3 interactions.
STRING	Q94AA4.
Proteomic databases
PRIDE	Q94AA4.
Genome annotation databases
GeneID	828733.
GenomeReviews	Gene locus AT4G26270 in contig CT486007_GR.
KEGG	ath:AT4G26270.
NMPDR	fig|3702.1.peg.20549.
Organism-specific databases
TAIR	At4g26270.
Phylogenomic databases
OMA	ERMNISA.
Gene expression databases
Genevestigator	Q94AA4.
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.
ProDom	PD000707. Ppfruckinase. 1 hit. [Graphical view] [Entries sharing at least one domain]
ProtoNet	Search...

Entry information

Entry name

K6PF3_ARATH

Accession

Primary (citable) accession number: Q94AA4
Secondary accession number(s): Q9STQ7

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 29, 2008
Last sequence update:	December 1, 2001
Last modified:	November 3, 2009
This is version 43 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)