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Q4W9B8 (K6PF_ASPFU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 68. 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:
6-phosphofructokinase

Short name=Phosphofructokinase
EC=2.7.1.11
Alternative name(s):
6PF-1-K
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)

Catalytic activity

ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate. HAMAP-Rule MF_00339

Pathway

Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4. HAMAP-Rule MF_00339

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00339.

Sequence similarities

Belongs to the phosphofructokinase family. Two domains subfamily.

Ontologies

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

Inferred from electronic annotation. Source: InterPro

glycolysis

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 – 8088086-phosphofructokinase HAMAP-Rule MF_00339
PRO_0000112034

Regions

Nucleotide binding33 – 375ATP By similarity
Nucleotide binding191 – 1955ATP By similarity
Nucleotide binding208 – 22417ATP By similarity

Sites

Active site1641Proton acceptor By similarity
Metal binding2221Magnesium; via carbonyl oxygen By similarity
Binding site1991Substrate By similarity
Binding site2911Substrate By similarity
Binding site2971Substrate By similarity
Binding site3001Substrate 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.
OMAYFEKYQF.
OrthoDBEOG7Q5HPV.

Enzyme and pathway databases

UniPathwayUPA00109; UER00182.

Family and domain databases

HAMAPMF_00339. Phosphofructokinase.
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 nameK6PF_ASPFU
AccessionPrimary (citable) accession number: Q4W9B8
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: July 5, 2005
Last modified: April 16, 2014
This is version 68 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