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

Gene

pfk

Organism
Trypanosoma brucei brucei
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 annotation1 Publication

Cofactori

Mg2+UniRule annotation

Enzyme 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. Glucose-6-phosphate isomerase (Gpi), Glucose-6-phosphate isomerase, glycosomal (PGI)
  3. ATP-dependent 6-phosphofructokinase (pfk)
  4. Fructose-bisphosphate aldolase, glycosomal (ALD)
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 sitei107ATP; via amide nitrogenUniRule annotation1 Publication1
Metal bindingi199Magnesium; catalyticUniRule annotation1
Sitei200Important for substrate specificity; cannot use PPi as phosphoryl donorUniRule annotation1
Binding sitei226ATP1 Publication1
Active sitei229Proton acceptorUniRule annotation1
Binding sitei325SubstrateUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi173 – 174ATPUniRule annotation1 Publication2
Nucleotide bindingi198 – 201ATPUniRule annotation1 Publication4
Nucleotide bindingi341 – 343ATPUniRule annotation1 Publication3

GO - Molecular functioni

  • 6-phosphofructokinase activity Source: GeneDB
  • ATP binding Source: GeneDB
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • fructose 6-phosphate metabolic process Source: InterPro
  • glycolytic process Source: GeneDB
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-RKO15648.
UniPathwayiUPA00109; 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
OrganismiTrypanosoma brucei brucei
Taxonomic identifieri5702 [NCBI]
Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeTrypanosoma

Subcellular locationi

  • Glycosome UniRule annotation1 Publication

GO - Cellular componenti

  • glycosome Source: GeneDB
Complete GO annotation...

Keywords - Cellular componenti

Glycosome, Peroxisome

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL5686.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004297231 – 487ATP-dependent 6-phosphofructokinaseAdd BLAST487

Interactioni

Subunit structurei

Homotetramer.UniRule annotation2 Publications

Chemistry databases

BindingDBiO15648.

Structurei

Secondary structure

1487
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi11 – 15Combined sources5
Turni26 – 29Combined sources4
Helixi42 – 44Combined sources3
Helixi46 – 51Combined sources6
Beta strandi52 – 55Combined sources4
Beta strandi58 – 61Combined sources4
Beta strandi75 – 77Combined sources3
Beta strandi81 – 84Combined sources4
Beta strandi88 – 93Combined sources6
Helixi95 – 97Combined sources3
Beta strandi99 – 104Combined sources6
Helixi112 – 127Combined sources16
Beta strandi130 – 134Combined sources5
Helixi138 – 142Combined sources5
Helixi144 – 147Combined sources4
Beta strandi151 – 153Combined sources3
Helixi155 – 158Combined sources4
Helixi161 – 163Combined sources3
Beta strandi164 – 166Combined sources3
Helixi178 – 188Combined sources11
Beta strandi191 – 197Combined sources7
Helixi199 – 215Combined sources17
Beta strandi220 – 225Combined sources6
Helixi241 – 260Combined sources20
Beta strandi265 – 271Combined sources7
Helixi278 – 287Combined sources10
Beta strandi291 – 294Combined sources4
Helixi302 – 312Combined sources11
Beta strandi317 – 324Combined sources8
Turni325 – 328Combined sources4
Helixi329 – 331Combined sources3
Helixi349 – 362Combined sources14
Turni363 – 367Combined sources5
Beta strandi368 – 370Combined sources3
Beta strandi372 – 376Combined sources5
Helixi379 – 383Combined sources5
Helixi389 – 407Combined sources19
Beta strandi410 – 418Combined sources9
Beta strandi421 – 426Combined sources6
Helixi427 – 430Combined sources4
Beta strandi433 – 437Combined sources5
Helixi442 – 450Combined sources9
Beta strandi454 – 456Combined sources3
Helixi458 – 481Combined sources24

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2HIGX-ray2.40A/B1-487[»]
3CVLX-ray2.15B481-487[»]
3F5MX-ray2.70A/B/C/D1-487[»]
ProteinModelPortaliO15648.
SMRiO15648.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO15648.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni227 – 229Substrate bindingUniRule annotation3
Regioni272 – 274Substrate bindingUniRule annotation3
Regioni380 – 383Substrate bindingUniRule annotation4

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi485 – 487Peroxisomal targeting signalUniRule annotation3

Sequence similaritiesi

Belongs to the phosphofructokinase type A (PFKA) family. PPi-dependent PFK group II subfamily. Atypical ATP-dependent clade "X" sub-subfamily.UniRule annotation

Family and domain databases

HAMAPiMF_01981. Phosphofructokinase_II_X. 1 hit.
InterProiIPR022953. ATP_PFK.
IPR000023. Phosphofructokinase_dom.
IPR012004. PyroP-dep_PFK_TP0108.
[Graphical view]
PfamiPF00365. PFK. 1 hit.
[Graphical view]
PIRSFiPIRSF000534. PPi_PFK_TP0108. 1 hit.
PRINTSiPR00476. PHFRCTKINASE.
SUPFAMiSSF53784. SSF53784. 1 hit.

Sequencei

Sequence statusi: Complete.

O15648-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVESRSRVT SKLVKAHRAM LNSVTQEDLK VDRLPGADYP NPSKKYSSRT
60 70 80 90 100
EFRDKTDYIM YNPRPRDEPS SENPVSVSPL LCELAAARSR IHFNPTETTI
110 120 130 140 150
GIVTCGGICP GLNDVIRSIT LTGINVYNVK RVIGFRFGYW GLSKKGSQTA
160 170 180 190 200
IELHRGRVTN IHHYGGTILG SSRGPQDPKE MVDTLERLGV NILFTVGGDG
210 220 230 240 250
TQRGALVISQ EAKRRGVDIS VFGVPKTIDN DLSFSHRTFG FQTAVEKAVQ
260 270 280 290 300
AIRAAYAEAV SANYGVGVVK LMGRDSGFIA AQAAVASAQA NICLVPENPI
310 320 330 340 350
SEQEVMSLLE RRFCHSRSCV IIVAEGFGQD WGRGSGGYDA SGNKKLIDIG
360 370 380 390 400
VILTEKVKAF LKANKSRYPD STVKYIDPSY MIRACPPSAN DALFCATLAT
410 420 430 440 450
LAVHEAMAGA TGCIIAMRHN NYILVPIKVA TSVRRVLDLR GQLWRQVREI
460 470 480
TVDLGSDVRL ARKLEIRREL EAINRNRDRL HEELAKL
Length:487
Mass (Da):53,517
Last modified:January 1, 1998 - v1
Checksum:i59357FF92ADA1FA9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF008186 Genomic DNA. Translation: AAC47836.1.

Genome annotation databases

GeneDBiTb927.3.3270:pep.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF008186 Genomic DNA. Translation: AAC47836.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2HIGX-ray2.40A/B1-487[»]
3CVLX-ray2.15B481-487[»]
3F5MX-ray2.70A/B/C/D1-487[»]
ProteinModelPortaliO15648.
SMRiO15648.
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

BindingDBiO15648.
ChEMBLiCHEMBL5686.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneDBiTb927.3.3270:pep.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00182.
SABIO-RKO15648.

Miscellaneous databases

EvolutionaryTraceiO15648.

Family and domain databases

HAMAPiMF_01981. Phosphofructokinase_II_X. 1 hit.
InterProiIPR022953. ATP_PFK.
IPR000023. Phosphofructokinase_dom.
IPR012004. PyroP-dep_PFK_TP0108.
[Graphical view]
PfamiPF00365. PFK. 1 hit.
[Graphical view]
PIRSFiPIRSF000534. PPi_PFK_TP0108. 1 hit.
PRINTSiPR00476. PHFRCTKINASE.
SUPFAMiSSF53784. SSF53784. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiPFKA_TRYBB
AccessioniPrimary (citable) accession number: O15648
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 9, 2014
Last sequence update: January 1, 1998
Last modified: November 2, 2016
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

3D-structure, Allosteric enzyme, Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.