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Q94AA4

- PFKA3_ARATH

UniProt

Q94AA4 - PFKA3_ARATH

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Protein

ATP-dependent 6-phosphofructokinase 3

Gene

PFK3

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.UniRule annotation

Catalytic activityi

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

Cofactori

Mg2+UniRule annotation

Enzyme regulationi

Allosterically activated by AMP.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei101 – 1011ATP; via amide nitrogenUniRule annotation
Metal bindingi190 – 1901Magnesium; catalyticUniRule annotation
Sitei191 – 1911Important for substrate specificity; cannot use PPi as phosphoryl donorUniRule annotation
Active sitei220 – 2201Proton acceptorUniRule annotation
Binding sitei319 – 3191SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi164 – 1652ATPUniRule annotation
Nucleotide bindingi189 – 1924ATPUniRule annotation

GO - Molecular functioni

  1. 6-phosphofructokinase activity Source: TAIR
  2. ATP binding Source: UniProtKB-KW
  3. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. carbohydrate phosphorylation Source: GOC
  2. fructose 6-phosphate metabolic process Source: InterPro
  3. glycolytic process Source: TAIR
  4. root epidermal cell differentiation Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciARA:AT4G26270-MONOMER.
ReactomeiREACT_248260. Glycolysis.
UniPathwayiUPA00109; UER00182.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent 6-phosphofructokinase 3UniRule annotation (EC:2.7.1.11UniRule annotation)
Short name:
ATP-PFK 3UniRule annotation
Short name:
Phosphofructokinase 3UniRule annotation
Alternative name(s):
Phosphohexokinase 3UniRule annotation
Gene namesi
Name:PFK3UniRule annotation
Ordered Locus Names:At4g26270
ORF Names:T25K17.80
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 4

Organism-specific databases

TAIRiAT4G26270.

Subcellular locationi

Cytoplasm 1 PublicationUniRule annotation

GO - Cellular componenti

  1. cytosol Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 489489ATP-dependent 6-phosphofructokinase 3PRO_0000330770Add
BLAST

Proteomic databases

PaxDbiQ94AA4.
PRIDEiQ94AA4.

Expressioni

Tissue specificityi

Mostly expressed in roots and flowers.1 Publication

Gene expression databases

GenevestigatoriQ94AA4.

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

BioGridi14020. 2 interactions.
IntActiQ94AA4. 5 interactions.
STRINGi3702.AT4G26270.1-P.

Structurei

3D structure databases

ProteinModelPortaliQ94AA4.
SMRiQ94AA4. Positions 28-442.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni218 – 2203Substrate bindingUniRule annotation
Regioni263 – 2653Substrate bindingUniRule annotation
Regioni375 – 3784Substrate bindingUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0205.
HOGENOMiHOG000016186.
InParanoidiQ94AA4.
KOiK00850.
OMAiLRLIQGM.
PhylomeDBiQ94AA4.

Family and domain databases

HAMAPiMF_01981. Phosphofructokinase_II_X.
InterProiIPR022953. Phosphofructokinase.
IPR000023. Phosphofructokinase_dom.
IPR012004. PyroP-dep_PFruKinase_TP0108.
[Graphical view]
PfamiPF00365. PFK. 1 hit.
[Graphical view]
PIRSFiPIRSF000534. PPi_PFK_TP0108. 1 hit.
PRINTSiPR00476. PHFRCTKINASE.
SUPFAMiSSF53784. SSF53784. 1 hit.

Sequencei

Sequence statusi: Complete.

Q94AA4-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSTVESSKPK IINGSCGYVL EDVPHLSDYL PGLPTYPNPL QDNPAYSVVK
60 70 80 90 100
QYFVDADDSV PQKIVVHKDG PRGIHFRRAG PRQKVYFESD EVHACIVTCG
110 120 130 140 150
GLCPGLNTVI REIVSSLSYM YGVKRILGID GGYRGFYAKN TVSLDSKVVN
160 170 180 190 200
DIHKRGGTIL GTSRGGHDTT KIVDSIQDRG INQVYIIGGD GTQRGASVIF
210 220 230 240 250
EEIRRRGLKV AVIGIPKTID NDIPVIDKSF GFDTAVEEAQ RAINAAHVEA
260 270 280 290 300
ESIENGIGVV KLMGRYSGFI AMYATLASRD VDCCLIPESP FYLEGEGGLF
310 320 330 340 350
EYIEKRLKES GHMVLVIAEG AGQDLMSKSM ESMTLKDASG NKLLKDVGLW
360 370 380 390 400
LSQSIKDHFN QKKMVMNLKY IDPTYMIRAV PSNASDNVYC TLLAQSAVHG
410 420 430 440 450
AMAGYTGYIS GLVNGRQTYI PFYRITEKQN HVVITDRMWA RLLSSTNQPS
460 470 480
FLGPKDVFDN KEKPMSALLD DGNCNGVVDV PPVTKEITK
Length:489
Mass (Da):53,666
Last modified:December 1, 2001 - v1
Checksum:iAE2C1EA15B64F7E0
GO

Sequence cautioni

The sequence CAB38956.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAB79482.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiT06011.
RefSeqiNP_567742.1. NM_118760.2.
UniGeneiAt.2887.

Genome annotation databases

EnsemblPlantsiAT4G26270.1; AT4G26270.1; AT4G26270.
GeneIDi828733.
KEGGiath:AT4G26270.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
PIRi T06011.
RefSeqi NP_567742.1. NM_118760.2.
UniGenei At.2887.

3D structure databases

ProteinModelPortali Q94AA4.
SMRi Q94AA4. Positions 28-442.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 14020. 2 interactions.
IntActi Q94AA4. 5 interactions.
STRINGi 3702.AT4G26270.1-P.

Proteomic databases

PaxDbi Q94AA4.
PRIDEi Q94AA4.

Protocols and materials databases

DNASUi 828733.
Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT4G26270.1 ; AT4G26270.1 ; AT4G26270 .
GeneIDi 828733.
KEGGi ath:AT4G26270.

Organism-specific databases

TAIRi AT4G26270.

Phylogenomic databases

eggNOGi COG0205.
HOGENOMi HOG000016186.
InParanoidi Q94AA4.
KOi K00850.
OMAi LRLIQGM.
PhylomeDBi Q94AA4.

Enzyme and pathway databases

UniPathwayi UPA00109 ; UER00182 .
BioCyci ARA:AT4G26270-MONOMER.
Reactomei REACT_248260. Glycolysis.

Gene expression databases

Genevestigatori Q94AA4.

Family and domain databases

HAMAPi MF_01981. Phosphofructokinase_II_X.
InterProi IPR022953. Phosphofructokinase.
IPR000023. Phosphofructokinase_dom.
IPR012004. PyroP-dep_PFruKinase_TP0108.
[Graphical view ]
Pfami PF00365. PFK. 1 hit.
[Graphical view ]
PIRSFi PIRSF000534. PPi_PFK_TP0108. 1 hit.
PRINTSi PR00476. PHFRCTKINASE.
SUPFAMi SSF53784. SSF53784. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [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.
    , 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.

Entry informationi

Entry nameiPFKA3_ARATH
AccessioniPrimary (citable) accession number: Q94AA4
Secondary accession number(s): Q9STQ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: December 1, 2001
Last modified: November 26, 2014
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Allosteric enzyme, Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3