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Q27778 (PFKA_SCHMA) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

Short name=ATP-PFK
Short name=Phosphofructokinase
EC=2.7.1.11
Alternative name(s):
Phosphohexokinase
Gene names
Name:PFK
OrganismSchistosoma mansoni (Blood fluke)
Taxonomic identifier6183 [NCBI]
Taxonomic lineageEukaryotaMetazoaPlatyhelminthesTrematodaDigeneaStrigeididaSchistosomatoideaSchistosomatidaeSchistosoma

Protein attributes

Sequence length781 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. Ref.2

Catalytic activity

ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate. Ref.1 Ref.2

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. Ref.2

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.

Sequence similarities

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

Biophysicochemical properties

Kinetic parameters:

KM=3.5 mM for ATP Ref.2

KM=0.8 mM for fructose 6-phosphate

pH dependence:

Optimum pH is 7.5-9.0.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentCytoplasm
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   Technical termAllosteric enzyme
Gene Ontology (GO)
   Biological_processfructose 6-phosphate metabolic process

Inferred from electronic annotation. Source: InterPro

glycolytic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_component6-phosphofructokinase complex

Inferred from electronic annotation. Source: InterPro

   Molecular_function6-phosphofructokinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

ATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 781781ATP-dependent 6-phosphofructokinase HAMAP-Rule MF_03184
PRO_0000112033

Regions

Nucleotide binding90 – 912ATP By similarity
Nucleotide binding120 – 1234ATP By similarity
Region1 – 394394N-terminal catalytic PFK domain 1 HAMAP-Rule MF_03184
Region166 – 1683Substrate binding By similarity
Region210 – 2123Substrate binding By similarity
Region300 – 3034Substrate binding By similarity
Region395 – 40915Interdomain linker HAMAP-Rule MF_03184
Region410 – 781372C-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 site4791Allosteric 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

Sequences

Sequence LengthMass (Da)Tools
Q27778 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: B2CDF20CAE926C38

FASTA78186,060
        10         20         30         40         50         60 
MATWMEGKYV ARGQFTGECI AVLTSGGDAQ GMNAAVRAVV RMGIYCGCRV FFIREGYQGL 

        70         80         90        100        110        120 
VDGGQNIQEA SWADVSGILQ LGGTKIGSAR CMDFRERYGR LKAAENLVKN QITNLVVIGG 

       130        140        150        160        170        180 
DGSLTGANLF RAEWSSLLEE LVTSNKISAE SAKQFHRLNI VGLVGSIDND FCGTDMTIGA 

       190        200        210        220        230        240 
DSALHRIIEA TDAISTTAHS HQRCFILEVM GRHCGYLALV ASMACEADWV FIPEMPPTDD 

       250        260        270        280        290        300 
WREKLCHKLR MNREHGQRVN IIMVAEGAID RACKPITCEI VKNLIVSELQ LDTRITVLGH 

       310        320        330        340        350        360 
VQRGGSPSAF DRILGSRMGA EAVLALMDAD RDPNLPSCVI SLDGNQAVRV PLVKCVDRTR 

       370        380        390        400        410        420 
QVAEAMKACD FDHAVELRGT SFMNNLATYI KLSKIEQPRQ SVMSSENNLR IGIVNVGAPA 

       430        440        450        460        470        480 
CGINAVIRGF TRLGITKGYK VIGIHEGFSG LVKGDASEIQ WADVRGWVGM GGSMLGTRRD 

       490        500        510        520        530        540 
TPNGLGIDKV AAKFKELKLS GLLIIGGFEA YECMIELVEG REKYPELCIP MAMVPATISN 

       550        560        570        580        590        600 
NVPGTDFSLG CDTALNEITS VLDKIKQSAL GTKRRVFVVE TMGGYCGYLA TMSALAGGAD 

       610        620        630        640        650        660 
AAYIFEEPFT IDDLREDVVH LRAKIDDNVK RGLVLRADML INTITSEFIH QLYAQEGQGI 

       670        680        690        700        710        720 
FDCRCNVLGH MQQGDRPSPF DRSLGTKFAS KAIDWLDEQI NANIVQILQS IHQTFMLYIN 

       730        740        750        760        770        780 
WYCTSSDNLF KYSLELREHT DFVHRLPKEE WWLSLRPLMR IMAKHDSLYE SESIMAGTDR 


K 

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References

[1]"Cloning and characterization of a cDNA encoding phosphofructokinase from Schistosoma mansoni."
Ding J., Su J.G.J., Mansour T.E.
Mol. Biochem. Parasitol. 66:105-110(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY.
[2]"Purification, kinetics and inhibition by antimonials of recombinant phosphofructokinase from Schistosoma mansoni."
Su J.G., Mansour J.M., Mansour T.E.
Mol. Biochem. Parasitol. 81:171-178(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L31531 mRNA. Translation: AAA29911.1.

3D structure databases

ProteinModelPortalQ27778.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKQ27778.
UniPathwayUPA00109; UER00182.

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. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePFKA_SCHMA
AccessionPrimary (citable) accession number: Q27778
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways