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Protein

ATP-dependent 6-phosphofructokinase

Gene

Pfk

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.UniRule annotation2 Publications

Catalytic activityi

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

Cofactori

Mg2+UniRule annotation

Enzyme regulationi

Allosterically activated by ADP, AMP, or fructose 2,6-bisphosphate, and allosterically inhibited by ATP or citrate.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei27 – 271ATP; via amide nitrogenUniRule annotation
Metal bindingi121 – 1211Magnesium; catalyticUniRule annotation
Active sitei168 – 1681Proton acceptorUniRule annotation
Binding sitei203 – 2031Substrate; shared with dimeric partnerUniRule annotation
Binding sitei266 – 2661SubstrateUniRule annotation
Binding sitei294 – 2941Substrate; shared with dimeric partnerUniRule annotation
Binding sitei480 – 4801Allosteric activator fructose 2,6-bisphosphateUniRule annotation
Binding sitei575 – 5751Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partnerUniRule annotation
Binding sitei638 – 6381Allosteric activator fructose 2,6-bisphosphateUniRule annotation
Binding sitei664 – 6641Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partnerUniRule annotation
Binding sitei745 – 7451Allosteric activator fructose 2,6-bisphosphateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi90 – 912ATPUniRule annotation
Nucleotide bindingi120 – 1234ATPUniRule annotation

GO - Molecular functioni

  • 6-phosphofructokinase activity Source: FlyBase
  • ATP binding Source: UniProtKB-KW
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • carbohydrate phosphorylation Source: GOC
  • fructose 6-phosphate metabolic process Source: InterPro
  • glycolytic process Source: FlyBase
  • myoblast fusion Source: FlyBase
  • somatic muscle development Source: FlyBase
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

ReactomeiREACT_319845. Glycolysis.
UniPathwayiUPA00109; UER00182.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent 6-phosphofructokinaseUniRule annotation (EC:2.7.1.11UniRule annotation)
Short name:
ATP-PFKUniRule annotation
Short name:
PhosphofructokinaseUniRule annotation
Alternative name(s):
PhosphohexokinaseUniRule annotation
Gene namesi
Name:Pfk
ORF Names:CG4001
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0003071. Pfk.

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

  • 6-phosphofructokinase complex Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 788788ATP-dependent 6-phosphofructokinasePRO_0000112031Add
BLAST

Proteomic databases

PaxDbiP52034.

Expressioni

Tissue specificityi

Nearly 90% of the PFK activity in adults is localized to the thorax.1 Publication

Gene expression databases

BgeeiP52034.
ExpressionAtlasiP52034. differential.

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

BioGridi61888. 2 interactions.
IntActiP52034. 2 interactions.
MINTiMINT-928619.

Structurei

3D structure databases

ProteinModelPortaliP52034.
SMRiP52034. Positions 18-765.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 392392N-terminal catalytic PFK domain 1Add
BLAST
Regioni166 – 1683Substrate bindingUniRule annotation
Regioni210 – 2123Substrate bindingUniRule annotation
Regioni300 – 3034Substrate bindingUniRule annotation
Regioni393 – 41018Interdomain linkerAdd
BLAST
Regioni411 – 788378C-terminal regulatory PFK domain 2Add
BLAST
Regioni537 – 5415Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation
Regioni582 – 5843Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation
Regioni670 – 6734Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation

Sequence similaritiesi

Belongs to the phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Eukaryotic two domain clade "E" sub-subfamily.UniRule annotation

Phylogenomic databases

eggNOGiCOG0205.
GeneTreeiENSGT00390000013209.
HOGENOMiHOG000148827.
InParanoidiP52034.
KOiK00850.
OMAiVYHMASK.
OrthoDBiEOG7ZSHV5.
PhylomeDBiP52034.

Family and domain databases

HAMAPiMF_03184. Phosphofructokinase_I_E.
InterProiIPR009161. 6-Pfructokinase_euk.
IPR022953. ATP_PFK.
IPR015912. Phosphofructokinase_CS.
IPR000023. Phosphofructokinase_dom.
[Graphical view]
PfamiPF00365. PFK. 2 hits.
[Graphical view]
PIRSFiPIRSF000533. ATP_PFK_euk. 1 hit.
PRINTSiPR00476. PHFRCTKINASE.
SUPFAMiSSF53784. SSF53784. 2 hits.
TIGRFAMsiTIGR02478. 6PF1K_euk. 1 hit.
PROSITEiPS00433. PHOSPHOFRUCTOKINASE. 2 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform B (identifier: P52034-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MNSEINQRFL ARGSQKDKGL AVFTSGGDSQ GMNAAVRACV RMAIYLGCKV
60 70 80 90 100
YFIREGYQGM VDGGDCIQEA NWASVSSIIH RGGTIIGSAR CQDFRERQGR
110 120 130 140 150
LKAANNLIQR GITNLVVIGG DGSLTGANLF RQEWSSLLDE LVKNKTITTE
160 170 180 190 200
QQEKFNVLHI VGLVGSIDND FCGTDMTIGT DTALHRIIEA IDAISSTAYS
210 220 230 240 250
HQRTFIMEVM GRHCGYLALV GGLACEADFI FIPEMPPKVD WPDRLCSQLA
260 270 280 290 300
QERSAGQRLN IVIVAEGAMD REGHPITAED VKKVIDERLK HDARITVLGH
310 320 330 340 350
VQRGGNPSAF DRILACRMGA EATLALMEAT KDSVPVVISL DGNQAVRVPL
360 370 380 390 400
MECVERTQAV AKAMAEKRWA DAVKLRGRSF ERNLETYKML TRLKPPKENF
410 420 430 440 450
DADGKGIEGY RLAVMHIGAP ACGMNAAVRS FVRNAIYRGD VVYGINDGVE
460 470 480 490 500
GLIAGNVREL GWSDVSGWVG QGGAYLGTKR TLPEGKFKEI AARLKEFKIQ
510 520 530 540 550
GLLIIGGFES YHAAGQIADQ RDNYPQFCIP IVVIPSTISN NVPGTEFSLG
560 570 580 590 600
CDTGLNEITE ICDRIRQSAQ GTKRRVFVIE TMGGYCGYLA TLAGLAGGAD
610 620 630 640 650
AAYIYEEKFS IKDLQQDVYH MASKMAEGVS RGLILRNEKA SENYSTDFIY
660 670 680 690 700
RLYSEEGKGL FTCRMNILGH MQQGGSPTPF DRNMGTKMAA KCVDWLAAQI
710 720 730 740 750
KANIDANGVV NCKSPDTATL LGIVSRQYRF SPLVDLIAET NFDQRIPKKQ
760 770 780
WWLRLRPLLR ILAKHDSAYE EEGMYITVEE ECDTDAVA
Length:788
Mass (Da):86,648
Last modified:August 16, 2005 - v2
Checksum:iBE45A03013299B75
GO
Isoform A (identifier: P52034-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-15: MNSEINQRFLARGSQ → MHSIKFRVFT...IDFVHPVKPF

Note: No experimental confirmation available.

Show »
Length:950
Mass (Da):105,187
Checksum:i28BD631321945759
GO
Isoform C (identifier: P52034-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     219-250: LVGGLACEADFIFIPEMPPKVDWPDRLCSQLA → ISAAIATEADFMFIPEEPVSVNWKDEICVKLH

Note: No experimental confirmation available.

Show »
Length:788
Mass (Da):86,720
Checksum:iD4E991EADAD0B084
GO

Sequence cautioni

The sequence AAN71109.1 differs from that shown. Reason: Frameshift at position 218. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti68 – 703QEA → RKS in AAA62385 (PubMed:7929140).Curated
Sequence conflicti80 – 9213HRGGT…SARCQ → PFVGWHHPLLRPLP (PubMed:7929140).CuratedAdd
BLAST
Sequence conflicti130 – 1312FR → LP in AAA62385 (PubMed:7929140).Curated
Sequence conflicti160 – 1612IV → ML in AAA62385 (PubMed:7929140).Curated
Sequence conflicti190 – 19910AIDAISSTAY → QSKAKVQSPVQPN in AAA62385 (PubMed:7929140).Curated
Sequence conflicti209 – 2124VMGR → GQVS in AAA62385 (PubMed:7929140).Curated
Sequence conflicti228 – 25225DFIFI…QLAQE → IHIHPNAPGRLGQTGSALSW TQ in AAA62385 (PubMed:7929140).CuratedAdd
BLAST
Sequence conflicti313 – 3131I → F in AAA62385 (PubMed:7929140).Curated
Sequence conflicti322 – 3254ATLA → PLWP in AAA62385 (PubMed:7929140).Curated
Sequence conflicti360 – 3612VA → G in AAA62385 (PubMed:7929140).Curated
Sequence conflicti374 – 3752KL → NV in AAA62385 (PubMed:7929140).Curated
Sequence conflicti455 – 4551G → R in AAA62385 (PubMed:7929140).Curated
Sequence conflicti478 – 4781T → S in AAA62385 (PubMed:7929140).Curated
Sequence conflicti522 – 5265DNYPQ → TTTHS in AAA62385 (PubMed:7929140).Curated
Sequence conflicti590 – 5912AT → PP in AAA62385 (PubMed:7929140).Curated
Sequence conflicti613 – 6131D → E in AAA62385 (PubMed:7929140).Curated
Sequence conflicti622 – 63615ASKMA…GLILR → PPRWPRRLPRSNPA in AAA62385 (PubMed:7929140).CuratedAdd
BLAST
Sequence conflicti695 – 70511WLAAQIKANID → CWPPRSRRTST in AAA62385 (PubMed:7929140).CuratedAdd
BLAST

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1515MNSEI…ARGSQ → MHSIKFRVFTKLKPIFLEIN GRIPICRHFHGPTTFRLEIS NKTPPIRQKLTFPNIGIQCT RSHHLCCPRDISGNTLLSVK FNCKRHCIKLRSDSGDQKND SPGEKNIQKDKSAQRCGKPI NNLHNGFLNAVNYSEKNAVK KKKSAPKRKCGKSVDELRKC LRTMQDVIDFVHPVKPF in isoform A. 1 PublicationVSP_014950Add
BLAST
Alternative sequencei219 – 25032LVGGL…CSQLA → ISAAIATEADFMFIPEEPVS VNWKDEICVKLH in isoform C. 1 PublicationVSP_014951Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L27653 Genomic DNA. Translation: AAA62385.1.
AE013599 Genomic DNA. Translation: AAF58840.1.
AE013599 Genomic DNA. Translation: AAF58841.1.
AE013599 Genomic DNA. Translation: AAM71065.2.
AF145673 mRNA. Translation: AAD38648.1.
BT001354 mRNA. Translation: AAN71109.1. Frameshift.
PIRiA55034.
RefSeqiNP_523676.1. NM_078952.3. [P52034-2]
NP_724890.1. NM_165746.3. [P52034-1]
NP_724891.2. NM_165747.4. [P52034-3]
UniGeneiDm.7095.

Genome annotation databases

EnsemblMetazoaiFBtr0088422; FBpp0087508; FBgn0003071. [P52034-1]
GeneIDi36060.
KEGGidme:Dmel_CG4001.
UCSCiCG4001-RA. d. melanogaster. [P52034-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L27653 Genomic DNA. Translation: AAA62385.1.
AE013599 Genomic DNA. Translation: AAF58840.1.
AE013599 Genomic DNA. Translation: AAF58841.1.
AE013599 Genomic DNA. Translation: AAM71065.2.
AF145673 mRNA. Translation: AAD38648.1.
BT001354 mRNA. Translation: AAN71109.1. Frameshift.
PIRiA55034.
RefSeqiNP_523676.1. NM_078952.3. [P52034-2]
NP_724890.1. NM_165746.3. [P52034-1]
NP_724891.2. NM_165747.4. [P52034-3]
UniGeneiDm.7095.

3D structure databases

ProteinModelPortaliP52034.
SMRiP52034. Positions 18-765.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi61888. 2 interactions.
IntActiP52034. 2 interactions.
MINTiMINT-928619.

Proteomic databases

PaxDbiP52034.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0088422; FBpp0087508; FBgn0003071. [P52034-1]
GeneIDi36060.
KEGGidme:Dmel_CG4001.
UCSCiCG4001-RA. d. melanogaster. [P52034-1]

Organism-specific databases

CTDi36060.
FlyBaseiFBgn0003071. Pfk.

Phylogenomic databases

eggNOGiCOG0205.
GeneTreeiENSGT00390000013209.
HOGENOMiHOG000148827.
InParanoidiP52034.
KOiK00850.
OMAiVYHMASK.
OrthoDBiEOG7ZSHV5.
PhylomeDBiP52034.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00182.
ReactomeiREACT_319845. Glycolysis.

Miscellaneous databases

GenomeRNAii36060.
NextBioi796655.
PROiP52034.

Gene expression databases

BgeeiP52034.
ExpressionAtlasiP52034. differential.

Family and domain databases

HAMAPiMF_03184. Phosphofructokinase_I_E.
InterProiIPR009161. 6-Pfructokinase_euk.
IPR022953. ATP_PFK.
IPR015912. Phosphofructokinase_CS.
IPR000023. Phosphofructokinase_dom.
[Graphical view]
PfamiPF00365. PFK. 2 hits.
[Graphical view]
PIRSFiPIRSF000533. ATP_PFK_euk. 1 hit.
PRINTSiPR00476. PHFRCTKINASE.
SUPFAMiSSF53784. SSF53784. 2 hits.
TIGRFAMsiTIGR02478. 6PF1K_euk. 1 hit.
PROSITEiPS00433. PHOSPHOFRUCTOKINASE. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Structure and expression of the gene encoding phosphofructokinase (PFK) in Drosophila melanogaster."
    Currie P.D., Sullivan D.T.
    J. Biol. Chem. 269:24679-24687(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM B), FUNCTION.
    Strain: Oregon-R.
  2. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
    Strain: Berkeley.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
    Strain: Berkeley.
    Tissue: Head.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 101-788 (ISOFORM C).
    Strain: Berkeley.
    Tissue: Testis.
  6. "Genetic and biochemical characterization of phosphofructokinase from Drosophila melanogaster."
    Munneke L.R., Collier G.E.
    Biochem. Genet. 23:847-857(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiPFKA_DROME
AccessioniPrimary (citable) accession number: P52034
Secondary accession number(s): Q8IH94
, Q8MKV4, Q9V5G7, Q9Y100
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: August 16, 2005
Last modified: April 29, 2015
This is version 113 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Allosteric enzyme, Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.