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Q4W9B8 (PFKA_ASPFU) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 71. 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
ORF Names:AFUA_4G00960
OrganismNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) [Reference proteome]
Taxonomic identifier330879 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length808 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 808808ATP-dependent 6-phosphofructokinase HAMAP-Rule MF_03184
PRO_0000112034

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 – 808405C-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
Q4W9B8 [UniParc].

Last modified July 5, 2005. Version 1.
Checksum: 3F4A02B1B87C6DF0

FASTA80888,713
        10         20         30         40         50         60 
MSSTQAPVEP PKRRRIGVLT SGGDAPGMNG AVRAVVRMAI YSDCEAYAVF EGYEGLVHGG 

        70         80         90        100        110        120 
HMIRQLHWED VRGWLSKGGT LIGSARSMAF RERAGRLKAA KNMVLRGIDA LVVCGGDGSL 

       130        140        150        160        170        180 
TGADVFRSEW PGLLEELVKN GELTEEQIEP YKVLNIVGLV GSIDNDMSGT DATIGCYSSL 

       190        200        210        220        230        240 
TRICDAVDDV FDTAFSHQRG FVIEVMGRHC GWLALMSAIS TGADWLFIPE MPPRDGWEDD 

       250        260        270        280        290        300 
MCSIITKNRK ERGKRRTIVI VAEGAQDRSL NKISSSTVKD ILTQRLGLDT RVTVLGHTQR 

       310        320        330        340        350        360 
GGPACAYDRW LSTLQGVEAV RAVLDMKPDS PSPVITIREN KIMRTPLVDA VQETKHVAKL 

       370        380        390        400        410        420 
IHDKDFEAAM RLRDAEFKEY HFAYRNTATP DHPKMILPQD KRMRIAIIHV GAPAGGMNQA 

       430        440        450        460        470        480 
TRAAVGYCLT RGHTPLAIHN GFPGLCRHHD DQPVGSVREV KWLESDAWVN EGGSDIGTNR 

       490        500        510        520        530        540 
SLPSEDFETT AMCFEKYKFD ALFVVGGFEA FTAVSQLRQA RDKYPAFKIP MVVLPATISN 

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

       610        620        630        640        650        660 
AVYIPEEGID IKMLSNDIDF LRENFARDKG ANRAGKLILR NECASSTYTT QVIADIFKEE 

       670        680        690        700        710        720 
AKGRFESRSA VPGHFQQGGK PSPMDRIRAL RMAVKCMLHL ENYAGKSRDE IAADPMSAAV 

       730        740        750        760        770        780 
IGIKGSQVLF SAMGGEDGLE ATETDWARRR PKTEFWLELQ NYVNVLSGRA SAGKPLWSCY 

       790        800 
ESKHFPSCCR LYNTDLSIDI DPSALTSS 

« Hide

References

[1]"Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus."
Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L. expand/collapse author list , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W.
Nature 438:1151-1156(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AAHF01000017 Genomic DNA. Translation: EAL84323.1.
RefSeqXP_746361.1. XM_741268.1.

3D structure databases

ProteinModelPortalQ4W9B8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5085.CADAFUAP00002374.

Proteomic databases

PRIDEQ4W9B8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAFUAT00002374; CADAFUAP00002374; CADAFUAG00002374.
GeneID3503711.
KEGGafm:AFUA_4G00960.

Phylogenomic databases

eggNOGCOG0205.
HOGENOMHOG000200154.
KOK00850.
OMAMEYCDVV.
OrthoDBEOG7Q5HPV.

Enzyme and pathway databases

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_ASPFU
AccessionPrimary (citable) accession number: Q4W9B8
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: July 5, 2005
Last modified: July 9, 2014
This is version 71 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