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Q27665 (PFKA_HAECO) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 72. 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
OrganismHaemonchus contortus (Barber pole worm)
Taxonomic identifier6289 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaStrongylidaTrichostrongyloideaHaemonchidaeHaemonchinaeHaemonchus

Protein attributes

Sequence length789 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

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.

Sequence similarities

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

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 – 789789ATP-dependent 6-phosphofructokinase HAMAP-Rule MF_03184
PRO_0000112032

Regions

Nucleotide binding104 – 1052ATP By similarity
Nucleotide binding134 – 1374ATP By similarity
Region1 – 404404N-terminal catalytic PFK domain 1 HAMAP-Rule MF_03184
Region180 – 1823Substrate binding By similarity
Region224 – 2263Substrate binding By similarity
Region313 – 3164Substrate binding By similarity
Region405 – 41915Interdomain linker HAMAP-Rule MF_03184
Region420 – 789370C-terminal regulatory PFK domain 2 HAMAP-Rule MF_03184
Region547 – 5515Allosteric activator fructose 2,6-bisphosphate binding By similarity
Region592 – 5943Allosteric activator fructose 2,6-bisphosphate binding By similarity
Region679 – 6824Allosteric activator fructose 2,6-bisphosphate binding By similarity

Sites

Active site1821Proton acceptor By similarity
Metal binding1351Magnesium; catalytic By similarity
Binding site411ATP; via amide nitrogen By similarity
Binding site2171Substrate; shared with dimeric partner By similarity
Binding site2801Substrate By similarity
Binding site3071Substrate; shared with dimeric partner By similarity
Binding site4891Allosteric activator fructose 2,6-bisphosphate By similarity
Binding site5851Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partner By similarity
Binding site6471Allosteric activator fructose 2,6-bisphosphate By similarity
Binding site6731Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partner By similarity
Binding site7531Allosteric activator fructose 2,6-bisphosphate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q27665 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 1245288AE2289DCF

FASTA78987,184
        10         20         30         40         50         60 
MSLKRNIRRL DSIVPTAGRE GSDIQFNLYK GRGVAVFTSG GDSQGMNGAV HSVVRMGIYL 

        70         80         90        100        110        120 
GCKVCFINEG YQGMVDGGDN IVEASWNSGS DIIQKGGTII GSARCTDLRQ REGRMKAAYN 

       130        140        150        160        170        180 
LIEKGITNLV VIGGDGSLIG ANQFRKDWPG LVKELVDTKK ITPEAAKSYP NIQIVGLVGS 

       190        200        210        220        230        240 
IDNDFCGTDM TIGTDSALQR IIESIDAVVA TAQSHQRAFV VEVMGRHCGY LALVAALACE 

       250        260        270        280        290        300 
ADFCFIPEWP PPVNWREILC KKLQEMRAEG QRLNIIVVAE DDDRDGTPIS SDLVKDVVAK 

       310        320        330        340        350        360 
TLKYDTRVTV LGHVQRGGSP SAFDRLLGCR MGAEAVLALM EMNEESEPCV ISIMVTRWYV 

       370        380        390        400        410        420 
PLMQCVERTK AVQKAMSEKD WELAVKLRGR SFQRNLETYK LLTKLRTVEK DNLSGGQNFN 

       430        440        450        460        470        480 
VAVMNVGAPA GGMNAAVRSF VRMAIVPSLY SLRYEDSFEG LANGAFKKFQ WGDVTNWVMH 

       490        500        510        520        530        540 
GGSFLGTQKQ LPNEKNVPLI AEQLRKHNIQ ALLLVGGFEA YHSTLILSKN REKYPEFCIP 

       550        560        570        580        590        600 
LCVIPCTISN NVPGTSISLG SDTAINEICT MIDKIKQSAT GTKRRVFIIE TMGGYCGYLA 

       610        620        630        640        650        660 
TLSALASGAD NAYIFEEKFT VEISLRRGSH RCKMAQGVQR YLIVRNEYAN KNFTTEFVKQ 

       670        680        690        700        710        720 
LFAEEGKGEF STRINILGHA QQGGSPTPFD RNMGTKLAAR ALEYIITQIK ESMVNGVVST 

       730        740        750        760        770        780 
KSPERATLLG LTGRRVVFTP VEELAAETDF DKRLPCDQWW LKLRPLLRIL AKHTSIYHTE 


AMEDTEDYD 

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References

[1]"Cloning of a cDNA encoding phosphofructokinase from Haemonchus contortus."
Klein R.D., Faureau M.A., Winterrowd C.A., Hatzenbuhler N.T., Shea M.H., Nulf S.C., Geary T.G., Olson E.R.
Mol. Biochem. Parasitol. 48:17-26(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M59805 mRNA. Translation: AAA29181.1.
PIRA45617.

3D structure databases

ProteinModelPortalQ27665.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

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. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePFKA_HAECO
AccessionPrimary (citable) accession number: Q27665
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 72 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