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P52034 (PFKA_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 106. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ATP-dependent 6-phosphofructokinase

Short name=ATP-PFK
Short name=Phosphofructokinase
EC=2.7.1.11
Alternative name(s):
Phosphohexokinase
Gene names
Name:Pfk
ORF Names:CG4001
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length788 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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. Ref.1 Ref.6

Catalytic activity

ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate. HAMAP-Rule MF_03184

Cofactor

Magnesium By similarity. HAMAP-Rule MF_03184

Enzyme regulation

Allosterically activated by ADP, AMP, or fructose 2,6-bisphosphate, and allosterically inhibited by ATP or citrate By similarity. HAMAP-Rule MF_03184

Pathway

Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4. HAMAP-Rule MF_03184

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_03184

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_03184.

Tissue specificity

Nearly 90% of the PFK activity in adults is localized to the thorax. Ref.6

Sequence similarities

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

Sequence caution

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

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform B (identifier: P52034-1)

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.
Isoform A (identifier: P52034-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-15: MNSEINQRFLARGSQ → MHSIKFRVFT...IDFVHPVKPF
Note: No experimental confirmation available.
Isoform C (identifier: P52034-3)

The sequence of this isoform differs from the canonical sequence as follows:
     219-250: LVGGLACEADFIFIPEMPPKVDWPDRLCSQLA → ISAAIATEADFMFIPEEPVSVNWKDEICVKLH
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 788788ATP-dependent 6-phosphofructokinase HAMAP-Rule MF_03184
PRO_0000112031

Regions

Nucleotide binding90 – 912ATP By similarity
Nucleotide binding120 – 1234ATP By similarity
Region1 – 392392N-terminal catalytic PFK domain 1 HAMAP-Rule MF_03184
Region166 – 1683Substrate binding By similarity
Region210 – 2123Substrate binding By similarity
Region300 – 3034Substrate binding By similarity
Region393 – 41018Interdomain linker HAMAP-Rule MF_03184
Region411 – 788378C-terminal regulatory PFK domain 2 HAMAP-Rule MF_03184
Region537 – 5415Allosteric activator fructose 2,6-bisphosphate binding By similarity
Region582 – 5843Allosteric activator fructose 2,6-bisphosphate binding By similarity
Region670 – 6734Allosteric activator fructose 2,6-bisphosphate binding By similarity

Sites

Active site1681Proton acceptor By similarity
Metal binding1211Magnesium; catalytic By similarity
Binding site271ATP; via amide nitrogen By similarity
Binding site2031Substrate; shared with dimeric partner By similarity
Binding site2661Substrate By similarity
Binding site2941Substrate; shared with dimeric partner By similarity
Binding site4801Allosteric activator fructose 2,6-bisphosphate By similarity
Binding site5751Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partner By similarity
Binding site6381Allosteric activator fructose 2,6-bisphosphate By similarity
Binding site6641Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partner By similarity
Binding site7451Allosteric activator fructose 2,6-bisphosphate By similarity

Natural variations

Alternative sequence1 – 1515MNSEI…ARGSQ → MHSIKFRVFTKLKPIFLEIN GRIPICRHFHGPTTFRLEIS NKTPPIRQKLTFPNIGIQCT RSHHLCCPRDISGNTLLSVK FNCKRHCIKLRSDSGDQKND SPGEKNIQKDKSAQRCGKPI NNLHNGFLNAVNYSEKNAVK KKKSAPKRKCGKSVDELRKC LRTMQDVIDFVHPVKPF in isoform A.
VSP_014950
Alternative sequence219 – 25032LVGGL…CSQLA → ISAAIATEADFMFIPEEPVS VNWKDEICVKLH in isoform C.
VSP_014951

Experimental info

Sequence conflict68 – 703QEA → RKS in AAA62385. Ref.1
Sequence conflict80 – 9213HRGGT…SARCQ → PFVGWHHPLLRPLP Ref.1
Sequence conflict130 – 1312FR → LP in AAA62385. Ref.1
Sequence conflict160 – 1612IV → ML in AAA62385. Ref.1
Sequence conflict190 – 19910AIDAISSTAY → QSKAKVQSPVQPN in AAA62385. Ref.1
Sequence conflict209 – 2124VMGR → GQVS in AAA62385. Ref.1
Sequence conflict228 – 25225DFIFI…QLAQE → IHIHPNAPGRLGQTGSALSW TQ in AAA62385. Ref.1
Sequence conflict3131I → F in AAA62385. Ref.1
Sequence conflict322 – 3254ATLA → PLWP in AAA62385. Ref.1
Sequence conflict360 – 3612VA → G in AAA62385. Ref.1
Sequence conflict374 – 3752KL → NV in AAA62385. Ref.1
Sequence conflict4551G → R in AAA62385. Ref.1
Sequence conflict4781T → S in AAA62385. Ref.1
Sequence conflict522 – 5265DNYPQ → TTTHS in AAA62385. Ref.1
Sequence conflict590 – 5912AT → PP in AAA62385. Ref.1
Sequence conflict6131D → E in AAA62385. Ref.1
Sequence conflict622 – 63615ASKMA…GLILR → PPRWPRRLPRSNPA in AAA62385. Ref.1
Sequence conflict695 – 70511WLAAQIKANID → CWPPRSRRTST in AAA62385. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform B [UniParc].

Last modified August 16, 2005. Version 2.
Checksum: BE45A03013299B75

FASTA78886,648
        10         20         30         40         50         60 
MNSEINQRFL ARGSQKDKGL AVFTSGGDSQ GMNAAVRACV RMAIYLGCKV YFIREGYQGM 

        70         80         90        100        110        120 
VDGGDCIQEA NWASVSSIIH RGGTIIGSAR CQDFRERQGR LKAANNLIQR GITNLVVIGG 

       130        140        150        160        170        180 
DGSLTGANLF RQEWSSLLDE LVKNKTITTE QQEKFNVLHI VGLVGSIDND FCGTDMTIGT 

       190        200        210        220        230        240 
DTALHRIIEA IDAISSTAYS HQRTFIMEVM GRHCGYLALV GGLACEADFI FIPEMPPKVD 

       250        260        270        280        290        300 
WPDRLCSQLA QERSAGQRLN IVIVAEGAMD REGHPITAED VKKVIDERLK HDARITVLGH 

       310        320        330        340        350        360 
VQRGGNPSAF DRILACRMGA EATLALMEAT KDSVPVVISL DGNQAVRVPL MECVERTQAV 

       370        380        390        400        410        420 
AKAMAEKRWA DAVKLRGRSF ERNLETYKML TRLKPPKENF DADGKGIEGY RLAVMHIGAP 

       430        440        450        460        470        480 
ACGMNAAVRS FVRNAIYRGD VVYGINDGVE GLIAGNVREL GWSDVSGWVG QGGAYLGTKR 

       490        500        510        520        530        540 
TLPEGKFKEI AARLKEFKIQ GLLIIGGFES YHAAGQIADQ RDNYPQFCIP IVVIPSTISN 

       550        560        570        580        590        600 
NVPGTEFSLG CDTGLNEITE ICDRIRQSAQ GTKRRVFVIE TMGGYCGYLA TLAGLAGGAD 

       610        620        630        640        650        660 
AAYIYEEKFS IKDLQQDVYH MASKMAEGVS RGLILRNEKA SENYSTDFIY RLYSEEGKGL 

       670        680        690        700        710        720 
FTCRMNILGH MQQGGSPTPF DRNMGTKMAA KCVDWLAAQI KANIDANGVV NCKSPDTATL 

       730        740        750        760        770        780 
LGIVSRQYRF SPLVDLIAET NFDQRIPKKQ WWLRLRPLLR ILAKHDSAYE EEGMYITVEE 


ECDTDAVA 

« Hide

Isoform A [UniParc].

Checksum: 28BD631321945759
Show »

FASTA950105,187
Isoform C [UniParc].

Checksum: D4E991EADAD0B084
Show »

FASTA78886,720

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
Strain: Berkeley.
[4]"A Drosophila complementary DNA resource."
Rubin G.M., Hong L., Brokstein P., Evans-Holm M., Frise E., Stapleton M., Harvey D.A.
Science 287:2222-2224(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
Strain: Berkeley.
Tissue: Head.
[5]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRA55034.
RefSeqNP_523676.1. NM_078952.3. [P52034-2]
NP_724890.1. NM_165746.3. [P52034-1]
NP_724891.2. NM_165747.4. [P52034-3]
UniGeneDm.7095.

3D structure databases

ProteinModelPortalP52034.
SMRP52034. Positions 18-766.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid61888. 2 interactions.
MINTMINT-928619.

Proteomic databases

PaxDbP52034.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0088422; FBpp0087508; FBgn0003071. [P52034-1]
GeneID36060.
KEGGdme:Dmel_CG4001.
UCSCCG4001-RA. d. melanogaster. [P52034-1]

Organism-specific databases

CTD36060.
FlyBaseFBgn0003071. Pfk.

Phylogenomic databases

eggNOGCOG0205.
GeneTreeENSGT00390000013209.
HOGENOMHOG000148827.
InParanoidP52034.
KOK00850.
OMAVYHMASK.
OrthoDBEOG7ZSHV5.
PhylomeDBP52034.

Enzyme and pathway databases

UniPathwayUPA00109; UER00182.

Gene expression databases

BgeeP52034.

Family and domain databases

HAMAPMF_03184. Phosphofructokinase_I_E.
InterProIPR009161. 6-phosphofructokinase_euk.
IPR022953. Phosphofructokinase.
IPR015912. Phosphofructokinase_CS.
IPR000023. Phosphofructokinase_dom.
[Graphical view]
PfamPF00365. PFK. 2 hits.
[Graphical view]
PIRSFPIRSF000533. ATP_PFK_euk. 1 hit.
PRINTSPR00476. PHFRCTKINASE.
SUPFAMSSF53784. SSF53784. 2 hits.
TIGRFAMsTIGR02478. 6PF1K_euk. 1 hit.
PROSITEPS00433. PHOSPHOFRUCTOKINASE. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi36060.
NextBio796655.

Entry information

Entry namePFKA_DROME
AccessionPrimary (citable) accession number: P52034
Secondary accession number(s): Q8IH94 expand/collapse secondary AC list , Q8MKV4, Q9V5G7, Q9Y100
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: August 16, 2005
Last modified: July 9, 2014
This is version 106 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase