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Protein

ATP-dependent 6-phosphofructokinase, platelet type

Gene

PFKP

Organism
Oryctolagus cuniculus (Rabbit)
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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei34 – 341ATP; via amide nitrogenUniRule annotation
Active sitei175 – 1751Proton acceptorUniRule annotation
Binding sitei210 – 2101Substrate; shared with dimeric partnerUniRule annotation
Binding sitei273 – 2731SubstrateUniRule annotation
Binding sitei301 – 3011Substrate; shared with dimeric partnerUniRule annotation
Binding sitei481 – 4811Allosteric activator fructose 2,6-bisphosphateUniRule annotation
Binding sitei576 – 5761Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partnerUniRule annotation
Binding sitei639 – 6391Allosteric activator fructose 2,6-bisphosphateUniRule annotation
Binding sitei665 – 6651Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partnerUniRule annotation
Binding sitei744 – 7441Allosteric activator fructose 2,6-bisphosphateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi97 – 982ATPUniRule annotation
Nucleotide bindingi127 – 1304ATPUniRule annotation

GO - Molecular functioni

  1. 6-phosphofructokinase activity Source: UniProtKB
  2. ATP binding Source: UniProtKB-KW
  3. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. carbohydrate phosphorylation Source: GOC
  2. fructose 6-phosphate metabolic process Source: InterPro
  3. glycolytic process Source: UniProtKB-UniPathway
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-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
ProteomesiUP000001811 Componenti: Unplaced

Subcellular locationi

  1. Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 791791ATP-dependent 6-phosphofructokinase, platelet typePRO_0000112026Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei12 – 121Phosphoserine; by PKA1 Publication
Modified residuei386 – 3861PhosphoserineBy similarity
Modified residuei395 – 3951N6-acetyllysineBy similarity
Modified residuei486 – 4861N6-acetyllysineBy similarity
Glycosylationi540 – 5401O-linked (GlcNAc)By similarity
Modified residuei651 – 6511PhosphotyrosineBy similarity
Modified residuei688 – 6881N6-acetyllysineBy similarity

Post-translational modificationi

GlcNAcylation decreases enzyme activity.By similarity

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

PRIDEiP47859.

Interactioni

Subunit structurei

Homo- and heterotetramers.UniRule annotation

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000009500.

Structurei

3D structure databases

ProteinModelPortaliP47859.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 399399N-terminal catalytic PFK domain 1Add
BLAST
Regioni173 – 1753Substrate bindingUniRule annotation
Regioni217 – 2193Substrate bindingUniRule annotation
Regioni307 – 3104Substrate bindingUniRule annotation
Regioni400 – 41112Interdomain linkerAdd
BLAST
Regioni412 – 791380C-terminal regulatory PFK domain 2Add
BLAST
Regioni538 – 5425Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation
Regioni583 – 5853Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation
Regioni671 – 6744Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation

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

eggNOGiCOG0205.
HOGENOMiHOG000200154.
HOVERGENiHBG000976.
InParanoidiP47859.
KOiK00850.

Family and domain databases

HAMAPiMF_03184. Phosphofructokinase_I_E.
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.

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.

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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000009500.

Proteomic databases

PRIDEiP47859.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100009526.
KEGGiocu:100009526.

Organism-specific databases

CTDi5214.

Phylogenomic databases

eggNOGiCOG0205.
HOGENOMiHOG000200154.
HOVERGENiHBG000976.
InParanoidiP47859.
KOiK00850.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00182.

Family and domain databases

HAMAPiMF_03184. Phosphofructokinase_I_E.
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...

Publicationsi

  1. "Structure and expression of the cDNA for the C isozyme of phosphofructo-1-kinase from rabbit brain."
    Li Y., Valaitis A.P., Latshaw S.P., Kwiatkowska D., Tripathi R.L., Campbell M.C., Kemp R.G.
    J. Biol. Chem. 269:5781-5787(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    Tissue: Brain.
  2. "The sites of phosphorylation of rabbit brain phosphofructo-1-kinase by cyclic AMP-dependent protein kinase."
    Valaitis A.P., Foe L.G., Kwiatkowska D., Latshaw S.P., Kemp R.G.
    Biochim. Biophys. Acta 995:187-194(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 5-17, PHOSPHORYLATION AT SER-12.

Entry informationi

Entry nameiPFKAP_RABIT
AccessioniPrimary (citable) accession number: P47859
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: April 29, 2015
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

Documents

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

External Data

Dasty 3

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 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.