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Protein

ATP-dependent 6-phosphofructokinase, platelet type

Gene

Pfkp

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -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 (Pfkl), ATP-dependent 6-phosphofructokinase (Pfkp), 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: RGD
  • ATP binding Source: RGD
  • cadherin binding Source: RGD
  • fructose-6-phosphate binding Source: RGD
  • identical protein binding Source: RGD
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • cellular response to leukemia inhibitory factor Source: RGD
  • fructose 1,6-bisphosphate metabolic process Source: RGD
  • fructose 6-phosphate metabolic process Source: RGD
  • glycolytic process Source: RGD
  • protein homotetramerization Source: RGD

Keywordsi

Molecular functionAllosteric enzyme, Kinase, Transferase
Biological processGlycolysis
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

SABIO-RKiP47860
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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi61893 Pfkp

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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) serineBy 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-2DPAGEi0004:P47860

PTM databases

iPTMnetiP47860
PhosphoSitePlusiP47860

Expressioni

Tissue specificityi

Expressed at high level in neuroendocrine tissues.

Interactioni

Subunit structurei

Homo- and heterotetramers (By similarity). Phosphofructokinase (PFK) enzyme functions as a tetramer composed of different combinations of 3 types of subunits, called PFKM (M), PFKL (L) and PFKP (P). The composition of the PFK tetramer differs according to the tissue type it is present in. The kinetic and regulatory properties of the tetrameric enzyme are dependent on the subunit composition, hence can vary across tissues (Probable).UniRule annotationCurated

GO - Molecular functioni

Protein-protein interaction databases

BioGridi248822, 2 interactors
IntActiP47860, 2 interactors
STRINGi10116.ENSRNOP00000023252

Structurei

3D structure databases

ProteinModelPortaliP47860
SMRiP47860
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
InterProiView protein in InterPro
IPR009161 6-Pfructokinase_euk
IPR022953 ATP_PFK
IPR015912 Phosphofructokinase_CS
IPR000023 Phosphofructokinase_dom
IPR035966 PKF_sf
PfamiView protein in Pfam
PF00365 PFK, 2 hits
PIRSFiPIRSF000533 ATP_PFK_euk, 1 hit
PRINTSiPR00476 PHFRCTKINASE
SUPFAMiSSF53784 SSF53784, 2 hits
TIGRFAMsiTIGR02478 6PF1K_euk, 1 hit
PROSITEiView protein in PROSITE
PS00433 PHOSPHOFRUCTOKINASE, 2 hits

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

Similar proteinsi

Entry informationi

Entry nameiPFKAP_RAT
AccessioniPrimary (citable) accession number: P47860
Secondary accession number(s): Q5HZX8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: December 20, 2005
Last modified: April 25, 2018
This is version 136 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health