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Protein

ATP-dependent 6-phosphofructokinase, platelet type

Gene

PFKP

Organism
Oryctolagus cuniculus (Rabbit)
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

Activity 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), Glucose-6-phosphate isomerase (GPI)
  3. ATP-dependent 6-phosphofructokinase, muscle type (PFKM), ATP-dependent 6-phosphofructokinase, platelet type (PFKP), ATP-dependent 6-phosphofructokinase (PFKP), ATP-dependent 6-phosphofructokinase (PFKM), ATP-dependent 6-phosphofructokinase (PFKP)
  4. Fructose-bisphosphate aldolase B (ALDOB), Fructose-bisphosphate aldolase A (ALDOA), Fructose-bisphosphate aldolase (ALDOC)
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
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: UniProtKB-KW
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

Keywordsi

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

Enzyme and pathway databases

UniPathwayi
UPA00109;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
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
Proteomesi
  • UP000001811 Componenti: Unplaced

Subcellular locationi

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001120261 – 791ATP-dependent 6-phosphofructokinase, platelet typeAdd BLAST791

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei6PhosphoserineBy similarity1
Modified residuei12Phosphoserine; by PKA1 Publication1
Modified residuei21PhosphoserineBy similarity1
Modified residuei142PhosphoserineBy similarity1
Modified residuei386PhosphoserineBy similarity1
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

PRIDEiP47859

PTM databases

iPTMnetiP47859

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

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000009500

Structurei

3D structure databases

ProteinModelPortaliP47859
SMRiP47859
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 – 791C-terminal regulatory PFK domain 2Add BLAST380
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

Phylogenomic databases

eggNOGiKOG2440 Eukaryota
COG0205 LUCA
HOGENOMiHOG000200154
HOVERGENiHBG000976
InParanoidiP47859
KOiK00850

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.

P47859-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MDNKVSASPR GSYRKFLEHL SGAGKAIGVL TSGGDAQGMN AAVRAVVRMG
60 70 80 90 100
IYVGAKVYFI YEGYQGMVDG GSNIVEANWE SVSSILQVGG TIIGSARSKA
110 120 130 140 150
FRTREGRLKA ACNLIHRGIT NLCVIGGSGS LTGANIFRME WSGLLEELAQ
160 170 180 190 200
DGKIDNEAVQ KYAYLNVVGM VGSIDNDFCG TDMTIGTDSA CHRIIEVIDA
210 220 230 240 250
IMTTAQSHQR TFVLEVMGRH CGYLALVSAL ACGADWVFLP ESPPEEGWEE
260 270 280 290 300
QMCVKLSENR AQKKRLNIII VAEGAIDTLN RPITSEKIKE LVVTQLGYDT
310 320 330 340 350
RVTILGHVQR GGTPSAFDRI LASRMGVEAV LALLEATPET PACVVSLSGN
360 370 380 390 400
HAVRLPLVEC VQMTQEVQKA MDERRFKDAV QLRGRSFENN LNTYKRLAIK
410 420 430 440 450
LPDDKIQKSN CNVAVINVGA PAAGMNAAVR SAVRVGIADG HKMFAVYDGF
460 470 480 490 500
DGFAKGQIKE IRWGDVGGWT GQGGSILGTK RILPGKYLEE IATQIRTHNI
510 520 530 540 550
NAILIIGGFE AYLGLLELSA AREKHEEFCV PMVMVPATVS NNVPGSDFSI
560 570 580 590 600
GADTALNTIT DTCDRIKQSA SGTKRRVFII ETMGGYCGYL ANMGGLAAGA
610 620 630 640 650
DAAYIFEEPF DIRDLQSNVE HLTEKMKTTI QRGLVLRNES CSENYTTDFI
660 670 680 690 700
YQLYSEEGRG VFDCRKNVLG HMQQGGAPSP FDRNFGTKIS ARAMQWITTK
710 720 730 740 750
LKESPGKGKR FVSDDSICVL GISKRNVLFQ PVAELKNETD FEHRIPKEQW
760 770 780 790
WLKLRPLMKI LAKYKTSYDV SDSGQLVPVR HRGGPEEPAA I
Length:791
Mass (Da):86,350
Last modified:February 1, 1996 - v1
Checksum:i3C10A36F229FD8E8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U01154 mRNA Translation: AAA17707.1
PIRiA53206
RefSeqiNP_001076217.1, NM_001082748.1
UniGeneiOcu.6209

Genome annotation databases

GeneIDi100009526
KEGGiocu:100009526

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U01154 mRNA Translation: AAA17707.1
PIRiA53206
RefSeqiNP_001076217.1, NM_001082748.1
UniGeneiOcu.6209

3D structure databases

ProteinModelPortaliP47859
SMRiP47859
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000009500

PTM databases

iPTMnetiP47859

Proteomic databases

PRIDEiP47859

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100009526
KEGGiocu:100009526

Organism-specific databases

CTDi5214

Phylogenomic databases

eggNOGiKOG2440 Eukaryota
COG0205 LUCA
HOGENOMiHOG000200154
HOVERGENiHBG000976
InParanoidiP47859
KOiK00850

Enzyme and pathway databases

UniPathwayi
UPA00109;UER00182

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
ProtoNetiSearch...

Entry informationi

Entry nameiPFKAP_RABIT
AccessioniPrimary (citable) accession number: P47859
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: September 12, 2018
This is version 113 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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