Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

ATP-dependent 6-phosphofructokinase, platelet type

Gene

Pfkp

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Cofactori

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 (Gpi)
  3. ATP-dependent 6-phosphofructokinase (Pfkm), ATP-dependent 6-phosphofructokinase, liver type (Pfkl), ATP-dependent 6-phosphofructokinase, platelet type (Pfkp), ATP-dependent 6-phosphofructokinase (Pfkm), ATP-dependent 6-phosphofructokinase (Pfkp), ATP-dependent 6-phosphofructokinase (Pfkl), ATP-dependent 6-phosphofructokinase, muscle type (Pfkm), ATP-dependent 6-phosphofructokinase (Pfkp)
  4. Fructose-bisphosphate aldolase (Aldoc), Fructose-bisphosphate aldolase (Aldoart2), Fructose-bisphosphate aldolase A (Aldoa), Fructose-bisphosphate aldolase B (Aldob), Fructose-bisphosphate aldolase C (Aldoc), Fructose-bisphosphate aldolase (Aldob)
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 sitei34ATP; via amide nitrogenUniRule annotation1
Metal bindingi128Magnesium; catalyticUniRule annotation1
Active sitei175Proton acceptorUniRule annotation1
Binding sitei210Substrate; shared with dimeric partnerUniRule annotation1
Binding sitei273SubstrateUniRule annotation1
Binding sitei301Substrate; shared with dimeric partnerUniRule annotation1
Binding sitei481Allosteric activator fructose 2,6-bisphosphateUniRule annotation1
Binding sitei576Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partnerUniRule annotation1
Binding sitei639Allosteric activator fructose 2,6-bisphosphateUniRule annotation1
Binding sitei665Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partnerUniRule annotation1
Binding sitei744Allosteric activator fructose 2,6-bisphosphateUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi97 – 98ATPUniRule annotation2
Nucleotide bindingi127 – 130ATPUniRule annotation4

GO - Molecular functioni

  • 6-phosphofructokinase activity Source: UniProtKB
  • ATP binding Source: RGD
  • fructose-6-phosphate binding Source: RGD
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • fructose 1,6-bisphosphate metabolic process Source: RGD
  • fructose 6-phosphate metabolic process Source: RGD
  • glycolytic process Source: RGD
  • protein homotetramerization Source: RGD
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

SABIO-RKP47860.
UniPathwayiUPA00109; UER00182.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent 6-phosphofructokinase, platelet typeUniRule annotation (EC:2.7.1.11UniRule annotation)
Short name:
ATP-PFKUniRule annotation
Short name:
PFK-P
Alternative name(s):
6-phosphofructokinase type C
Phosphofructo-1-kinase isozyme C
Short name:
PFK-C
PhosphohexokinaseUniRule annotation
Gene namesi
Name:Pfkp
Synonyms:Pfkc
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi61893. Pfkp.

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_00001120271 – 788ATP-dependent 6-phosphofructokinase, platelet typeAdd BLAST788

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei2PhosphoserineCombined sources1
Modified residuei6PhosphoserineBy similarity1
Modified residuei12PhosphoserineBy similarity1
Modified residuei21PhosphoserineBy similarity1
Modified residuei142PhosphoserineCombined sources1
Modified residuei386PhosphoserineCombined sources1
Modified residuei395N6-acetyllysineBy similarity1
Modified residuei486N6-acetyllysineBy similarity1
Glycosylationi540O-linked (GlcNAc)By similarity1
Modified residuei651PhosphotyrosineBy similarity1
Modified residuei688N6-acetyllysineBy similarity1

Post-translational modificationi

GlcNAcylation decreases enzyme activity.By similarity

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP47860.
PRIDEiP47860.

2D gel databases

World-2DPAGE0004:P47860.

PTM databases

iPTMnetiP47860.
PhosphoSitePlusiP47860.

Expressioni

Tissue specificityi

Expressed at high level in neuroendocrine tissues.

Interactioni

Subunit structurei

Homo- and heterotetramers.UniRule annotation

Protein-protein interaction databases

BioGridi248822. 2 interactors.
IntActiP47860. 2 interactors.
STRINGi10116.ENSRNOP00000023252.

Structurei

3D structure databases

ProteinModelPortaliP47860.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 399N-terminal catalytic PFK domain 1Add BLAST399
Regioni173 – 175Substrate bindingUniRule annotation3
Regioni217 – 219Substrate bindingUniRule annotation3
Regioni307 – 310Substrate bindingUniRule annotation4
Regioni400 – 411Interdomain linkerAdd BLAST12
Regioni412 – 788C-terminal regulatory PFK domain 2Add BLAST377
Regioni538 – 542Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation5
Regioni583 – 585Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation3
Regioni671 – 674Allosteric 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

Phylogenomic databases

eggNOGiKOG2440. Eukaryota.
COG0205. LUCA.
HOGENOMiHOG000200154.
HOVERGENiHBG000976.
InParanoidiP47860.
KOiK00850.
PhylomeDBiP47860.

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.

P47860-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDQDSSTSS TSFPKYLEHL SGDGKAIGVL TSGGDAQGMN AAVRAVVRMG
60 70 80 90 100
IYTGAKVYFI YEGYQGMVDG GSNIVEAKWE CVSSILQVGG TIIGSARCQA
110 120 130 140 150
FRSREGRLKA ACNLVRLGIT NLCVIGGDGS LTGANLFRKE WSGLLEELAK
160 170 180 190 200
NGEIDSDTVK KHAYLNVVGM VGSIDNDFCG TDMTIGTDSA LHRIIEVVDA
210 220 230 240 250
IMTTAQSHQR TFVLEVMGRH CGYLALVSAL ACGADWVFLP ESPPEEGWEE
260 270 280 290 300
EMCLKLSENR ARKKRLNIII VSEGAIDTQN KPITSEKIKE LVVTNLGFDT
310 320 330 340 350
RVTILGHVQR GGTPSAFDRI LASRMGVEAV LALLEATPET PACVVSLRGN
360 370 380 390 400
QAVRLPLMEC VQMTQDVQKA MDERRFDEAV KLRGRSFEGN LNTYKRLAIK
410 420 430 440 450
EPDDKIPKSN CNVAIINVGA PAAGMNAAVR SAVRVGIAEG HKMFAIYDGF
460 470 480 490 500
DGLANGQIKE IGWGDVGGWT GQGGSILGTK RTLPGKYLEK IAEQMHSKNI
510 520 530 540 550
NALLIIGGFE AYLGLLELAA ARNKHEAFCV PMVMVPATVS NNVPGSDFSI
560 570 580 590 600
GADTALNTIT DTCDRIKQSA SGTKRRVFII ETMGGYCGYL ANMGGLAAGA
610 620 630 640 650
DAAYIFEEQF DIRDLQSNVM HLTEKMKTSI QRGLVLRNEN CSVNYTTDFI
660 670 680 690 700
YQLYSEEGKG VFDCRKNVLG HMQQGGAPSP FDRNFGTKIS AKAMEWISAK
710 720 730 740 750
LKGSHGTGKK FVSDDSICVL GIQKRDLLFK PVAELRKATD FEHRIPKQQW
760 770 780
WLKLRPIMKI LAKYEASYDM SDVGKLEPVH NHGELSAI
Length:788
Mass (Da):85,720
Last modified:December 20, 2005 - v2
Checksum:i16FEB963C3297CA6
GO

Sequence cautioni

The sequence AAA17757 differs from that shown. Reason: Frameshift at position 27.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti35 – 36DA → ES in AAA17757 (PubMed:8106374).Curated2
Sequence conflicti51I → M in AAA17757 (PubMed:8106374).Curated1
Sequence conflicti56K → Q in AAA17757 (PubMed:8106374).Curated1
Sequence conflicti111A → T in AAA17757 (PubMed:8106374).Curated1
Sequence conflicti220H → Y in AAA17757 (PubMed:8106374).Curated1
Sequence conflicti600A → R in AAA17757 (PubMed:8106374).Curated1
Sequence conflicti755R → L in AAA17757 (PubMed:8106374).Curated1
Sequence conflicti758M → S in AAA17757 (PubMed:8106374).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC088847 mRNA. Translation: AAH88847.1.
L25387 mRNA. Translation: AAA17757.1. Frameshift.
PIRiA53047.
RefSeqiNP_996729.1. NM_206847.1.
UniGeneiRn.2278.

Genome annotation databases

GeneIDi60416.
KEGGirno:60416.
UCSCiRGD:61893. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC088847 mRNA. Translation: AAH88847.1.
L25387 mRNA. Translation: AAA17757.1. Frameshift.
PIRiA53047.
RefSeqiNP_996729.1. NM_206847.1.
UniGeneiRn.2278.

3D structure databases

ProteinModelPortaliP47860.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi248822. 2 interactors.
IntActiP47860. 2 interactors.
STRINGi10116.ENSRNOP00000023252.

PTM databases

iPTMnetiP47860.
PhosphoSitePlusiP47860.

2D gel databases

World-2DPAGE0004:P47860.

Proteomic databases

PaxDbiP47860.
PRIDEiP47860.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi60416.
KEGGirno:60416.
UCSCiRGD:61893. rat.

Organism-specific databases

CTDi5214.
RGDi61893. Pfkp.

Phylogenomic databases

eggNOGiKOG2440. Eukaryota.
COG0205. LUCA.
HOGENOMiHOG000200154.
HOVERGENiHBG000976.
InParanoidiP47860.
KOiK00850.
PhylomeDBiP47860.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00182.
SABIO-RKP47860.

Miscellaneous databases

PROiP47860.

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 nameiPFKAP_RAT
AccessioniPrimary (citable) accession number: P47860
Secondary accession number(s): Q5HZX8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: December 20, 2005
Last modified: November 2, 2016
This is version 129 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Allosteric enzyme, Complete proteome, Reference proteome

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.