Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P78985 (PFKA_ASPNG) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ATP-dependent 6-phosphofructokinase

Short name=ATP-PFK
Short name=Phosphofructokinase
EC=2.7.1.11
Alternative name(s):
Phosphohexokinase
Gene names
Name:pfkA
OrganismAspergillus niger
Taxonomic identifier5061 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length783 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis By similarity. HAMAP-Rule MF_03184

Catalytic activity

ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate. HAMAP-Rule MF_03184

Cofactor

Magnesium By similarity. HAMAP-Rule MF_03184

Enzyme regulation

Allosterically activated by ADP, AMP, or fructose 2,6-bisphosphate, and allosterically inhibited by ATP or citrate By similarity. HAMAP-Rule MF_03184

Pathway

Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4. HAMAP-Rule MF_03184

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_03184

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_03184.

Sequence similarities

Belongs to the phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Eukaryotic two domain clade "E" sub-subfamily.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentCytoplasm
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   Technical termAllosteric enzyme
Gene Ontology (GO)
   Biological_processfructose 6-phosphate metabolic process

Inferred from electronic annotation. Source: InterPro

glycolytic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_component6-phosphofructokinase complex

Inferred from electronic annotation. Source: InterPro

   Molecular_function6-phosphofructokinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

ATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 783783ATP-dependent 6-phosphofructokinase HAMAP-Rule MF_03184
PRO_0000112035

Regions

Nucleotide binding86 – 872ATP By similarity
Nucleotide binding116 – 1194ATP By similarity
Region1 – 389389N-terminal catalytic PFK domain 1 HAMAP-Rule MF_03184
Region162 – 1643Substrate binding By similarity
Region206 – 2083Substrate binding By similarity
Region297 – 3004Substrate binding By similarity
Region390 – 40314Interdomain linker HAMAP-Rule MF_03184
Region404 – 783380C-terminal regulatory PFK domain 2 HAMAP-Rule MF_03184
Region537 – 5415Allosteric activator fructose 2,6-bisphosphate binding By similarity
Region582 – 5843Allosteric activator fructose 2,6-bisphosphate binding By similarity
Region674 – 6774Allosteric activator fructose 2,6-bisphosphate binding By similarity

Sites

Active site1641Proton acceptor By similarity
Metal binding1171Magnesium; catalytic By similarity
Binding site231ATP; via amide nitrogen By similarity
Binding site1991Substrate; shared with dimeric partner By similarity
Binding site2631Substrate By similarity
Binding site2911Substrate; shared with dimeric partner By similarity
Binding site4801Allosteric activator fructose 2,6-bisphosphate By similarity
Binding site5751Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partner By similarity
Binding site6421Allosteric activator fructose 2,6-bisphosphate By similarity
Binding site6681Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partner By similarity
Binding site7491Allosteric activator fructose 2,6-bisphosphate By similarity

Sequences

Sequence LengthMass (Da)Tools
P78985 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: 7BE3F6B553F06304

FASTA78385,760
        10         20         30         40         50         60 
MAPPQAPVQP PKRRRIGVLT SGGDAPGMNG VVRAVVRMAI HSDCEAFAVY EGYEGLVNGG 

        70         80         90        100        110        120 
DMIRQLHWED VRGWLSRGGT LIGSARCMTF RERPGRLRAA KNMVLRGIDA LVVCGGDGSL 

       130        140        150        160        170        180 
TGADVFRSEW PGLLKELVET GELTEEQVKP YQILNIVGLV GSIDNDMSGT DATIGCYSSL 

       190        200        210        220        230        240 
TRICDAVDDV FDTAFSHQRG FVIEVMGRHC GWLALMSAIS TGADWLFVPE MPPKDGWEDD 

       250        260        270        280        290        300 
MCAIITKNRK ERGKRRTIVI VAEGAQDRHL NKISSSKIKD ILTERLNLDT RVTVLGHTQR 

       310        320        330        340        350        360 
GGAACAYDRW LSTLQGVEAV RAVLDMKPEA PSPVITIREN KILRMPLMDA VQHTKTVTKH 

       370        380        390        400        410        420 
IQNKEFAEAM ALRDSEFKEY HFSYINTSTP DHPKLLLPEN KRMRIGIIHV GAPAGGMNQA 

       430        440        450        460        470        480 
TRAAVAYCLT RGHTPLAIHN GFPGLCRHYD DTPICSVREV AWQESDAWVN EGGSDIGTNR 

       490        500        510        520        530        540 
GLPGDDLATT AKSFKKFGFD ALFVVGGFEA FTAVSQLRQA REKYPEFKIP MTVLPATISN 

       550        560        570        580        590        600 
NVPGTEYSLG SDTCLNTLID FCDAIRQSAS SSRRRVFVIE TQGGKSGYIA TTAGLSVGAV 

       610        620        630        640        650        660 
AVYIPEEGID IKMLARDIDF LRDNFARDKG ANRAGKIILR NECASSTYTT QVVADMIKEE 

       670        680        690        700        710        720 
AKGRFESRAA VPGHFQQGGK PSPMDRIRAL RMATKCMLHL ESYAGKSADE IAADELSASV 

       730        740        750        760        770        780 
IGIKGSQVLF SPMGGETGLE ATETDWARRR PKTEFWLELQ DTVNILSGRA SVNNATWSCY 


ENA 

« Hide

References

[1]de Graaff L.H., Everse S.J., van den Broeck H.C., Bussink R., Visser J.
Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z79690 Genomic DNA. Translation: CAB01923.1.

3D structure databases

ProteinModelPortalP78985.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5061.CADANGAP00013544.

Proteomic databases

PRIDEP78985.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG0205.

Enzyme and pathway databases

SABIO-RKP78985.
UniPathwayUPA00109; UER00182.

Family and domain databases

HAMAPMF_03184. Phosphofructokinase_I_E.
InterProIPR009161. 6-phosphofructokinase_euk.
IPR022953. Phosphofructokinase.
IPR015912. Phosphofructokinase_CS.
IPR000023. Phosphofructokinase_dom.
[Graphical view]
PfamPF00365. PFK. 2 hits.
[Graphical view]
PIRSFPIRSF000533. ATP_PFK_euk. 1 hit.
PRINTSPR00476. PHFRCTKINASE.
SUPFAMSSF53784. SSF53784. 2 hits.
TIGRFAMsTIGR02478. 6PF1K_euk. 1 hit.
PROSITEPS00433. PHOSPHOFRUCTOKINASE. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePFKA_ASPNG
AccessionPrimary (citable) accession number: P78985
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: May 1, 1997
Last modified: July 9, 2014
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways