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Protein

ATP-dependent 6-phosphofructokinase

Gene

PFK

Organism
Haemonchus contortus (Barber pole worm)
Status
Reviewed-Annotation score: Annotation score: 4 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 annotation1 Publication

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: glycolysis

This protein is involved in step 3 of the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose.UniRule annotation
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Glucose-6-phosphate isomerase (HCOI_00551200)
  3. ATP-dependent 6-phosphofructokinase (HCOI_00089800), ATP-dependent 6-phosphofructokinase (PFK)
  4. Fructose-bisphosphate aldolase (HCOI_00166200), Fructose-bisphosphate aldolase (HCOI_01281200), Fructose-bisphosphate aldolase (HCOI_01101200), Fructose-bisphosphate aldolase (HCOI_01101300), Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase (HCOI_01102100)
This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose, the pathway glycolysis and in Carbohydrate degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei41ATP; via amide nitrogenUniRule annotation1
Metal bindingi135Magnesium; catalyticUniRule annotation1
Active sitei182Proton acceptorUniRule annotation1
Binding sitei217Substrate; shared with dimeric partnerUniRule annotation1
Binding sitei280SubstrateUniRule annotation1
Binding sitei307Substrate; shared with dimeric partnerUniRule annotation1
Binding sitei489Allosteric activator fructose 2,6-bisphosphateUniRule annotation1
Binding sitei585Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partnerUniRule annotation1
Binding sitei647Allosteric activator fructose 2,6-bisphosphateUniRule annotation1
Binding sitei673Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partnerUniRule annotation1
Binding sitei753Allosteric activator fructose 2,6-bisphosphateUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi104 – 105ATPUniRule annotation2
Nucleotide bindingi134 – 137ATPUniRule annotation4

GO - Molecular functioni

GO - Biological processi

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

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
OrganismiHaemonchus contortus (Barber pole worm)
Taxonomic identifieri6289 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaStrongylidaTrichostrongyloideaHaemonchidaeHaemonchinaeHaemonchus

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001120321 – 789ATP-dependent 6-phosphofructokinaseAdd BLAST789

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ27665.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 404N-terminal catalytic PFK domain 1Add BLAST404
Regioni180 – 182Substrate bindingUniRule annotation3
Regioni224 – 226Substrate bindingUniRule annotation3
Regioni313 – 316Substrate bindingUniRule annotation4
Regioni405 – 419Interdomain linkerAdd BLAST15
Regioni420 – 789C-terminal regulatory PFK domain 2Add BLAST370
Regioni547 – 551Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation5
Regioni592 – 594Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation3
Regioni679 – 682Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation4

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

Family and domain databases

HAMAPiMF_03184. Phosphofructokinase_I_E. 1 hit.
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]

Sequencei

Sequence statusi: Complete.

Q27665-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLKRNIRRL DSIVPTAGRE GSDIQFNLYK GRGVAVFTSG GDSQGMNGAV
60 70 80 90 100
HSVVRMGIYL GCKVCFINEG YQGMVDGGDN IVEASWNSGS DIIQKGGTII
110 120 130 140 150
GSARCTDLRQ REGRMKAAYN LIEKGITNLV VIGGDGSLIG ANQFRKDWPG
160 170 180 190 200
LVKELVDTKK ITPEAAKSYP NIQIVGLVGS IDNDFCGTDM TIGTDSALQR
210 220 230 240 250
IIESIDAVVA TAQSHQRAFV VEVMGRHCGY LALVAALACE ADFCFIPEWP
260 270 280 290 300
PPVNWREILC KKLQEMRAEG QRLNIIVVAE DDDRDGTPIS SDLVKDVVAK
310 320 330 340 350
TLKYDTRVTV LGHVQRGGSP SAFDRLLGCR MGAEAVLALM EMNEESEPCV
360 370 380 390 400
ISIMVTRWYV PLMQCVERTK AVQKAMSEKD WELAVKLRGR SFQRNLETYK
410 420 430 440 450
LLTKLRTVEK DNLSGGQNFN VAVMNVGAPA GGMNAAVRSF VRMAIVPSLY
460 470 480 490 500
SLRYEDSFEG LANGAFKKFQ WGDVTNWVMH GGSFLGTQKQ LPNEKNVPLI
510 520 530 540 550
AEQLRKHNIQ ALLLVGGFEA YHSTLILSKN REKYPEFCIP LCVIPCTISN
560 570 580 590 600
NVPGTSISLG SDTAINEICT MIDKIKQSAT GTKRRVFIIE TMGGYCGYLA
610 620 630 640 650
TLSALASGAD NAYIFEEKFT VEISLRRGSH RCKMAQGVQR YLIVRNEYAN
660 670 680 690 700
KNFTTEFVKQ LFAEEGKGEF STRINILGHA QQGGSPTPFD RNMGTKLAAR
710 720 730 740 750
ALEYIITQIK ESMVNGVVST KSPERATLLG LTGRRVVFTP VEELAAETDF
760 770 780
DKRLPCDQWW LKLRPLLRIL AKHTSIYHTE AMEDTEDYD
Length:789
Mass (Da):87,184
Last modified:November 1, 1996 - v1
Checksum:i1245288AE2289DCF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M59805 mRNA. Translation: AAA29181.1.
PIRiA45617.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M59805 mRNA. Translation: AAA29181.1.
PIRiA45617.

3D structure databases

ProteinModelPortaliQ27665.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00109; UER00182.

Family and domain databases

HAMAPiMF_03184. Phosphofructokinase_I_E. 1 hit.
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...

Entry informationi

Entry nameiPFKA_HAECO
AccessioniPrimary (citable) accession number: Q27665
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: November 11, 2015
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

Allosteric enzyme

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.