Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q94AA4 (PFKA3_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 80. 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:
ATP-dependent 6-phosphofructokinase 3

Short name=ATP-PFK 3
Short name=Phosphofructokinase 3
EC=2.7.1.11
Alternative name(s):
Phosphohexokinase 3
Gene names
Name:PFK3
Ordered Locus Names:At4g26270
ORF Names:T25K17.80
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length489 AA.
Sequence statusComplete.
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.4

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 Ref.4.

Tissue specificity

Mostly expressed in roots and flowers. Ref.4

Sequence similarities

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

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 489489ATP-dependent 6-phosphofructokinase 3 HAMAP-Rule MF_03186
PRO_0000330770

Regions

Nucleotide binding164 – 1652ATP By similarity
Nucleotide binding189 – 1924ATP By similarity
Region218 – 2203Substrate binding By similarity
Region263 – 2653Substrate binding By similarity
Region375 – 3784Substrate binding By similarity

Sites

Active site2201Proton acceptor By similarity
Metal binding1901Magnesium; catalytic By similarity
Binding site1011ATP; via amide nitrogen By similarity
Binding site3191Substrate By similarity
Site1911Important for substrate specificity; cannot use PPi as phosphoryl donor By similarity

Sequences

Sequence LengthMass (Da)Tools
Q94AA4 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: AE2C1EA15B64F7E0

FASTA48953,666
        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 

« 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]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL049171 Genomic DNA. Translation: CAB38956.1. Sequence problems.
AL161564 Genomic DNA. Translation: CAB79482.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE85178.1.
AY049245 mRNA. Translation: AAK83587.1.
AY090267 mRNA. Translation: AAL90928.1.
PIRT06011.
RefSeqNP_567742.1. NM_118760.2.
UniGeneAt.2887.

3D structure databases

ProteinModelPortalQ94AA4.
SMRQ94AA4. Positions 28-442.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid14020. 2 interactions.
IntActQ94AA4. 5 interactions.
STRING3702.AT4G26270.1-P.

Proteomic databases

PaxDbQ94AA4.
PRIDEQ94AA4.

Protocols and materials databases

DNASU828733.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G26270.1; AT4G26270.1; AT4G26270.
GeneID828733.
KEGGath:AT4G26270.

Organism-specific databases

TAIRAT4G26270.

Phylogenomic databases

eggNOGCOG0205.
HOGENOMHOG000016186.
InParanoidQ94AA4.
KOK00850.
OMALRLIQGM.
PhylomeDBQ94AA4.

Enzyme and pathway databases

BioCycARA:AT4G26270-MONOMER.
UniPathwayUPA00109; UER00182.

Gene expression databases

GenevestigatorQ94AA4.

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 namePFKA3_ARATH
AccessionPrimary (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: July 9, 2014
This is version 80 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