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P59680 (PFKA_YARLI) 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
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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:PFK1
Ordered Locus Names:YALI0D16357g
OrganismYarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica) [Reference proteome]
Taxonomic identifier284591 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDipodascaceaeYarrowia

Protein attributes

Sequence length953 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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 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

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 953953ATP-dependent 6-phosphofructokinase HAMAP-Rule MF_03184
PRO_0000112044

Regions

Nucleotide binding256 – 2572ATP By similarity
Nucleotide binding286 – 2894ATP By similarity
Region1 – 558558N-terminal catalytic PFK domain 1 HAMAP-Rule MF_03184
Region332 – 3343Substrate binding By similarity
Region376 – 3783Substrate binding By similarity
Region466 – 4694Substrate binding By similarity
Region559 – 57214Interdomain linker HAMAP-Rule MF_03184
Region573 – 953381C-terminal regulatory PFK domain 2 HAMAP-Rule MF_03184
Region702 – 7065Allosteric activator fructose 2,6-bisphosphate binding By similarity
Region747 – 7493Allosteric activator fructose 2,6-bisphosphate binding By similarity
Region839 – 8424Allosteric activator fructose 2,6-bisphosphate binding By similarity

Sites

Active site3341Proton acceptor By similarity
Metal binding2871Magnesium; catalytic By similarity
Binding site1931ATP; via amide nitrogen By similarity
Binding site3691Substrate; shared with dimeric partner By similarity
Binding site4331Substrate By similarity
Binding site4601Substrate; shared with dimeric partner By similarity
Binding site6451Allosteric activator fructose 2,6-bisphosphate By similarity
Binding site7401Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partner By similarity
Binding site8071Allosteric activator fructose 2,6-bisphosphate By similarity
Binding site8331Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partner By similarity
Binding site9061Allosteric activator fructose 2,6-bisphosphate By similarity

Sequences

Sequence LengthMass (Da)Tools
P59680 [UniParc].

Last modified July 19, 2004. Version 2.
Checksum: 50DA57F8D774F74B

FASTA953103,753
        10         20         30         40         50         60 
MIEGISFASF VTHEKPKFVR ALDFYKALGF LPTKEYKHGT DHHATDEEGA GSIQEVWLTS 

        70         80         90        100        110        120 
SRAGVPSVTV KLRLSRHGNE HVSLPNLKHD WRSLVPSLVY YAPDLDAVRA AITPFLHEDH 

       130        140        150        160        170        180 
STLLERPSHT NFIELYAIDP MGNLVGFSRR ENPYSSAMQK PFSADDIGPQ NFSKPNETKI 

       190        200        210        220        230        240 
KGKKRIGVMT SGGDAPGMCA AVRAVVRAGI ARGCEVYAVR EGYEGLVKGG DLIEPLSWED 

       250        260        270        280        290        300 
VRGWLSLGGT LIGTARCKEF REREGRLAGA LNMVKNGIDA LIVIGGDGSL TGADLFREEW 

       310        320        330        340        350        360 
PSLIEELVTN GSITAEQAER HRHLDICGMV GSIDNDMATT DVTIGAYSSL DRICELVDFI 

       370        380        390        400        410        420 
DATAQSHSRA FVVEVMGRHC GWLALMAGTA TGADYIFIPE AAPDATQWAE KMTRVVKRHR 

       430        440        450        460        470        480 
SQGKRKTVVI VAEGAIDSDL NPITAKMVKD VLDGIGLDTR ISTLGHVQRG GPPVAADRVL 

       490        500        510        520        530        540 
ASLQGVEAID AILSLTPETP SPMIALNENK ITRKPLVESV ALTKKVADAI GNKDFAEAMR 

       550        560        570        580        590        600 
LRNPEFVEQL QGFLLTNSAD KDRPQEPAKD PLRVAIVCTG APAGGMNAAI RSAVLYGLAR 

       610        620        630        640        650        660 
GHQMFAIHNG WSGLVKNGDD AVRELTWLEV EPLCQKGGCE IGTNRSLPEC DLGMIAYHFQ 

       670        680        690        700        710        720 
RQRFDGLIVI GGFEAFRALN QLDDARHAYP ALRIPMVGIP ATISNNVPGT DYSLGADTCL 

       730        740        750        760        770        780 
NSLVQYCDVL KTSASATRLR LFVVEVQGGN SGYIATVAGL ITGAYVVYTP ESGINLRLLQ 

       790        800        810        820        830        840 
HDISYLKDTF AHQADVNRTG KLLLRNERSS NVFTTDVITG IINEEAKGSF DARTAIPGHV 

       850        860        870        880        890        900 
QQGGHPSPTD RVRAQRFAIK AVQFIEEHHG SKNNADHCVI LGVRGSKFKY TSVSHLYAHK 

       910        920        930        940        950 
TEHGARRPKH SYWHAIGDIA NMLVGRKAPP LPETLNDEIE KNIAKEQGII DPC 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY142710 mRNA. Translation: AAN34943.2.
CR382130 Genomic DNA. Translation: CAG81088.1.
RefSeqXP_502897.1. XM_502897.1.

3D structure databases

ProteinModelPortalP59680.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING4952.P59680.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCAG81088; CAG81088; YALI0_D16357g.
GeneID2910306.
KEGGyli:YALI0D16357g.

Phylogenomic databases

eggNOGCOG0205.
HOGENOMHOG000200154.
KOK00850.
OMAMIALNEN.
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_YARLI
AccessionPrimary (citable) accession number: P59680
Entry history
Integrated into UniProtKB/Swiss-Prot: May 16, 2003
Last sequence update: July 19, 2004
Last modified: July 9, 2014
This is version 80 of the entry and version 2 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