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O94201 (PFKA1_CANAX) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 79. 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 subunit alpha

EC=2.7.1.11
Alternative name(s):
ATP-dependent 6-phosphofructokinase 1
Short name=ATP-PFK 1
Short name=Phosphofructokinase 1
Phosphohexokinase 1
Gene names
Name:PFK1
OrganismCandida albicans (Yeast)
Taxonomic identifier5476 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida

Protein attributes

Sequence length987 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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. 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

Heterooctamer of 4 alpha and 4 beta chains By similarity.

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 – 987987ATP-dependent 6-phosphofructokinase subunit alpha HAMAP-Rule MF_03184
PRO_0000112038

Regions

Nucleotide binding300 – 3012ATP By similarity
Nucleotide binding330 – 3334ATP By similarity
Region1 – 602602N-terminal catalytic PFK domain 1 HAMAP-Rule MF_03184
Region376 – 3783Substrate binding By similarity
Region420 – 4223Substrate binding By similarity
Region510 – 5134Substrate binding By similarity
Region603 – 61614Interdomain linker HAMAP-Rule MF_03184
Region617 – 987371C-terminal regulatory PFK domain 2 HAMAP-Rule MF_03184
Region743 – 7475Allosteric activator fructose 2,6-bisphosphate binding By similarity
Region788 – 7903Allosteric activator fructose 2,6-bisphosphate binding By similarity
Region880 – 8834Allosteric activator fructose 2,6-bisphosphate binding By similarity

Sites

Active site3781Proton acceptor By similarity
Metal binding3311Magnesium; catalytic By similarity
Binding site2371ATP; via amide nitrogen By similarity
Binding site4131Substrate; shared with subunit beta By similarity
Binding site4771Substrate By similarity
Binding site5041Substrate; shared with subunit beta By similarity
Binding site6861Allosteric activator fructose 2,6-bisphosphate By similarity
Binding site7811Allosteric activator fructose 2,6-bisphosphate; shared with subunit beta By similarity
Binding site8481Allosteric activator fructose 2,6-bisphosphate By similarity
Binding site8741Allosteric activator fructose 2,6-bisphosphate; shared with subunit beta By similarity
Binding site9581Allosteric activator fructose 2,6-bisphosphate By similarity

Sequences

Sequence LengthMass (Da)Tools
O94201 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 4EE5BAB6D02349FA

FASTA987108,598
        10         20         30         40         50         60 
MPSSSDAINR ISYISLVTSD NDKFNQTFQF YSQLGFRLTK SFSKVSSYGS GLGANHPEFQ 

        70         80         90        100        110        120 
LGVSHDSLKE VWLESYPLQN VDSNGNLRPW QEMEVYDGDN CERLNESTVI KVRLLGETPL 

       130        140        150        160        170        180 
KSISQKQFVF FTTQLNKIEK ILTDANVKYG KVVDNVILAE DPLNNIISFS NTQNELCKTR 

       190        200        210        220        230        240 
FQSPEEYVEK TTAEILAKRK KSQLGSKFGS FEEISPSEVG GGNGLRKKKI GVMTSGGDAP 

       250        260        270        280        290        300 
GMNPAVRAVV RAGIYYGCDV YAVYEGYEGL VKGGDLLKKM EWSDVRSYMS LGGTSIGTAR 

       310        320        330        340        350        360 
CKEFRERAGR LQGAYNMIKN GIDALVVCGG DGSLTGADLF RSEWPSLVKE LVDTGKLTKE 

       370        380        390        400        410        420 
EVSPYEHLTI VGLVGSIDND MSGTDVTIGA FSALERITEM VDYIGATAAS HSRAFVVEVM 

       430        440        450        460        470        480 
GRHCGWLALL SGLATGADFV FIPERPPKAG LWKEQLKEVC LRHREYGRRK TTVIVAEGAI 

       490        500        510        520        530        540 
DDELNPITSE EVKQVLADLG LDTRNTILGH VQRGGTAVAF DRRLATLQGV EAVKAVLEMT 

       550        560        570        580        590        600 
PDTPSPMIGI LKHKIVRIPL VDAVKQTKAV AEAISNKDFD KAMSLRDNSF YDDYRYFRDI 

       610        620        630        640        650        660 
SIYDDGSKQL SEDKRLNIAI VHVGAASAGL NAATRAVALY SLSRGHKLYA VQDGFAGLVK 

       670        680        690        700        710        720 
GDLKNLTWMD VEGWHSLGGS EIGTNRSLPS QNIGKVAYNL QKFNIQGLLI VGGFEAFTSL 

       730        740        750        760        770        780 
HELSEQKANY PIFEIPMVVV PATVSNNVPG TEYSLGADTC LNQLVSYCDA VQQSASSTRR 

       790        800        810        820        830        840 
RVFVVEVQGG HSGYVASYCG LITGALATYT PESNINLREL QGDIDLLQKV FATDRGEDHN 

       850        860        870        880        890        900 
GTLIVRNEQA SAVYSTQLIA DILKENANKR FETRTAIPGH VQQGFTPSAN DRVMAVKFSL 

       910        920        930        940        950        960 
KAMEFIETRN GCYGKHDRKF SDEEISEHSQ VVIGIHGDVV KFTCIKHLYD NEANVALRKG 

       970        980 
KTVHWTDMID VANILNGKSL LKKQERY 

« Hide

References

[1]"Genetic and biochemical characterization of phosphofructokinase from the opportunistic pathogenic yeast Candida albicans."
Lorberg A., Kirchrath L., Ernst J.F., Heinisch J.J.
Eur. J. Biochem. 260:217-226(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
Strain: ATCC 10231 / CBS 6431 / DSM 1386 / NBRC 1594.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ007638 Genomic DNA. Translation: CAB38868.1.

3D structure databases

ProteinModelPortalO94201.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG0205.

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 namePFKA1_CANAX
AccessionPrimary (citable) accession number: O94201
Entry history
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: May 1, 1999
Last modified: July 9, 2014
This is version 79 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