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Protein

ATP-dependent 6-phosphofructokinase

Gene

pfk

Organism
Trypanoplasma borreli
Status
Reviewed-Annotation score: -Protein inferred from homologyi

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

Mg2+UniRule annotation

Activity regulationi

Allosterically activated by AMP.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. no protein annotated in this organism
  3. ATP-dependent 6-phosphofructokinase (pfk)
  4. no protein annotated in this organism
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 sitei109ATP; via amide nitrogenUniRule annotation1
Metal bindingi201Magnesium; catalyticUniRule annotation1
Sitei202Important for substrate specificity; cannot use PPi as phosphoryl donorUniRule annotation1
Active sitei231Proton acceptorUniRule annotation1
Binding sitei327SubstrateUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi175 – 176ATPUniRule annotation2
Nucleotide bindingi200 – 203ATPUniRule annotation4

GO - Molecular functioni

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-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:pfkUniRule annotation
OrganismiTrypanoplasma borreli
Taxonomic identifieri5710 [NCBI]
Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaBodonidaeTrypanoplasma

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Glycosome, Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004297221 – 490ATP-dependent 6-phosphofructokinaseAdd BLAST490

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ8WPP2
SMRiQ8WPP2
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni229 – 231Substrate bindingUniRule annotation3
Regioni274 – 276Substrate bindingUniRule annotation3
Regioni383 – 386Substrate bindingUniRule annotation4

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi488 – 490Peroxisomal targeting signalUniRule annotation3

Sequence similaritiesi

Family and domain databases

HAMAPiMF_01981 Phosphofructokinase_II_X, 1 hit
InterProiView protein in InterPro
IPR022953 ATP_PFK
IPR000023 Phosphofructokinase_dom
IPR035966 PKF_sf
IPR012004 PyroP-dep_PFK_TP0108
PfamiView protein in Pfam
PF00365 PFK, 1 hit
PRINTSiPR00476 PHFRCTKINASE
SUPFAMiSSF53784 SSF53784, 1 hit

Sequencei

Sequence statusi: Complete.

Q8WPP2-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MDEPSNMSTT SSKIPQYDFY SDVDNLHPDQ FRIQCLPGRN FISPLVEQKK
60 70 80 90 100
DFVKAHVIHD KDLDIMYDPM PKGKCNISQS CLTLPLACPR VSLHFDPSKT
110 120 130 140 150
TVAMVTCGGV CPGLNDVIRG ITLAAVCSYH VKKVIGFKYG YWGLSKAGRH
160 170 180 190 200
TAIELTSNIV RGLRHLGGTF LGTSRGGQNI SDMVDTLVEY GVNILFTIGG
210 220 230 240 250
DGTQKGAVAI SEEVNRRGLD IAVFGIPKTI DNDLSFSQRT FGYETAVSEA
260 270 280 290 300
VIAIRAAHAE AISHEYGVGI VKLMGRNSGF IAASATVASA LSHICLIPEK
310 320 330 340 350
NVSKKVLLSL IEARFMMAKD IVIVVAEGFG QDWPDCNEDL GSDASGNKRL
360 370 380 390 400
TDIGLVIKKI VQDHLSKNPK YHQSTVKYID PSYMIRACPA STSDAAFCSN
410 420 430 440 450
LSTLAVHEAM AGRTACLITL WYSNFVLVPI KTAVSHRKIV STGGALWRQV
460 470 480 490
REVTVDGSGD IAMVHQQELS RELKAINAHR NSIMEQLSKL
Length:490
Mass (Da):53,376
Last modified:March 1, 2002 - v1
Checksum:i62360A4071A700DF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ310928 Genomic DNA Translation: CAC84571.1

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ310928 Genomic DNA Translation: CAC84571.1

3D structure databases

ProteinModelPortaliQ8WPP2
SMRiQ8WPP2
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayi
UPA00109;UER00182

Family and domain databases

HAMAPiMF_01981 Phosphofructokinase_II_X, 1 hit
InterProiView protein in InterPro
IPR022953 ATP_PFK
IPR000023 Phosphofructokinase_dom
IPR035966 PKF_sf
IPR012004 PyroP-dep_PFK_TP0108
PfamiView protein in Pfam
PF00365 PFK, 1 hit
PRINTSiPR00476 PHFRCTKINASE
SUPFAMiSSF53784 SSF53784, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiPFKA_TRYBO
AccessioniPrimary (citable) accession number: Q8WPP2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 9, 2014
Last sequence update: March 1, 2002
Last modified: October 10, 2018
This is version 61 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

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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