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P59680 (K6PF1_YARLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 77. 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 subunit alpha

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

Catalytic activity

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

Enzyme regulation

Allosterically inhibited by ATP and activated by AMP and fructose 2,6-bisphosphate By similarity. 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

Subunit structure

Heterooctamer of 4 alpha and 4 beta chains By similarity.

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 – 9539536-phosphofructokinase subunit alpha HAMAP-Rule MF_00339
PRO_0000112044

Regions

Nucleotide binding203 – 2075ATP By similarity
Nucleotide binding361 – 3655ATP By similarity
Nucleotide binding378 – 39417ATP By similarity

Sites

Active site3341Proton acceptor By similarity
Metal binding3921Magnesium; via carbonyl oxygen By similarity
Binding site3691Substrate By similarity
Binding site4601Substrate By similarity
Binding site4661Substrate By similarity
Binding site4691Substrate 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.
OMAWLFIPER.
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 nameK6PF1_YARLI
AccessionPrimary (citable) accession number: P59680
Entry history
Integrated into UniProtKB/Swiss-Prot: May 16, 2003
Last sequence update: July 19, 2004
Last modified: April 16, 2014
This is version 77 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