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Protein

ATP-dependent 6-phosphofructokinase

Gene

pfkA

Organism
Aspergillus niger
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-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

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 (pgiA), Glucose-6-phosphate isomerase (ABL_05991)
  3. ATP-dependent 6-phosphofructokinase (pfkA), ATP-dependent 6-phosphofructokinase (ABL_08899)
  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 sitei23ATP; via amide nitrogenUniRule annotation1
Metal bindingi117Magnesium; catalyticUniRule annotation1
Active sitei164Proton acceptorUniRule annotation1
Binding sitei199Substrate; shared with dimeric partnerUniRule annotation1
Binding sitei263SubstrateUniRule annotation1
Binding sitei291Substrate; shared with dimeric partnerUniRule annotation1
Binding sitei480Allosteric activator fructose 2,6-bisphosphateUniRule annotation1
Binding sitei575Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partnerUniRule annotation1
Binding sitei642Allosteric activator fructose 2,6-bisphosphateUniRule annotation1
Binding sitei668Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partnerUniRule annotation1
Binding sitei749Allosteric activator fructose 2,6-bisphosphateUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi86 – 87ATPUniRule annotation2
Nucleotide bindingi116 – 119ATPUniRule annotation4

GO - Molecular functioni

GO - Biological processi

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

BRENDAi2.7.1.11. 518.
SABIO-RKP78985.
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:pfkA
OrganismiAspergillus niger
Taxonomic identifieri5061 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001120351 – 783ATP-dependent 6-phosphofructokinaseAdd BLAST783

Proteomic databases

PaxDbiP78985.
PRIDEiP78985.

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi5061.CADANGAP00013544.

Structurei

3D structure databases

ProteinModelPortaliP78985.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 389N-terminal catalytic PFK domain 1Add BLAST389
Regioni162 – 164Substrate bindingUniRule annotation3
Regioni206 – 208Substrate bindingUniRule annotation3
Regioni297 – 300Substrate bindingUniRule annotation4
Regioni390 – 403Interdomain linkerAdd BLAST14
Regioni404 – 783C-terminal regulatory PFK domain 2Add BLAST380
Regioni537 – 541Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation5
Regioni582 – 584Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation3
Regioni674 – 677Allosteric 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.

Family and domain databases

HAMAPiMF_03184. Phosphofructokinase_I_E. 1 hit.
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.

P78985-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPPQAPVQP PKRRRIGVLT SGGDAPGMNG VVRAVVRMAI HSDCEAFAVY
60 70 80 90 100
EGYEGLVNGG DMIRQLHWED VRGWLSRGGT LIGSARCMTF RERPGRLRAA
110 120 130 140 150
KNMVLRGIDA LVVCGGDGSL TGADVFRSEW PGLLKELVET GELTEEQVKP
160 170 180 190 200
YQILNIVGLV GSIDNDMSGT DATIGCYSSL TRICDAVDDV FDTAFSHQRG
210 220 230 240 250
FVIEVMGRHC GWLALMSAIS TGADWLFVPE MPPKDGWEDD MCAIITKNRK
260 270 280 290 300
ERGKRRTIVI VAEGAQDRHL NKISSSKIKD ILTERLNLDT RVTVLGHTQR
310 320 330 340 350
GGAACAYDRW LSTLQGVEAV RAVLDMKPEA PSPVITIREN KILRMPLMDA
360 370 380 390 400
VQHTKTVTKH IQNKEFAEAM ALRDSEFKEY HFSYINTSTP DHPKLLLPEN
410 420 430 440 450
KRMRIGIIHV GAPAGGMNQA TRAAVAYCLT RGHTPLAIHN GFPGLCRHYD
460 470 480 490 500
DTPICSVREV AWQESDAWVN EGGSDIGTNR GLPGDDLATT AKSFKKFGFD
510 520 530 540 550
ALFVVGGFEA FTAVSQLRQA REKYPEFKIP MTVLPATISN NVPGTEYSLG
560 570 580 590 600
SDTCLNTLID FCDAIRQSAS SSRRRVFVIE TQGGKSGYIA TTAGLSVGAV
610 620 630 640 650
AVYIPEEGID IKMLARDIDF LRDNFARDKG ANRAGKIILR NECASSTYTT
660 670 680 690 700
QVVADMIKEE AKGRFESRAA VPGHFQQGGK PSPMDRIRAL RMATKCMLHL
710 720 730 740 750
ESYAGKSADE IAADELSASV IGIKGSQVLF SPMGGETGLE ATETDWARRR
760 770 780
PKTEFWLELQ DTVNILSGRA SVNNATWSCY ENA
Length:783
Mass (Da):85,760
Last modified:May 1, 1997 - v1
Checksum:i7BE3F6B553F06304
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z79690 Genomic DNA. Translation: CAB01923.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z79690 Genomic DNA. Translation: CAB01923.1.

3D structure databases

ProteinModelPortaliP78985.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi5061.CADANGAP00013544.

Proteomic databases

PaxDbiP78985.
PRIDEiP78985.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG2440. Eukaryota.
COG0205. LUCA.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00182.
BRENDAi2.7.1.11. 518.
SABIO-RKP78985.

Family and domain databases

HAMAPiMF_03184. Phosphofructokinase_I_E. 1 hit.
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...

Entry informationi

Entry nameiPFKA_ASPNG
AccessioniPrimary (citable) accession number: P78985
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: May 1, 1997
Last modified: November 30, 2016
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Allosteric enzyme

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.