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Q03215 (PFKA1_KLULA) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 102. 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

Short name=ATP-PFK 1
Short name=Phosphofructokinase 1
EC=2.7.1.11
Alternative name(s):
Phosphohexokinase 1
Gene names
Name:PFK1
Ordered Locus Names:KLLA0A05544g
OrganismKluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica) [Complete proteome]
Taxonomic identifier284590 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeKluyveromyces

Protein attributes

Sequence length992 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 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.

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
Complete proteome
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 – 992992ATP-dependent 6-phosphofructokinase subunit alpha HAMAP-Rule MF_03184
PRO_0000112040

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 – 992420C-terminal regulatory PFK domain 2 HAMAP-Rule MF_03184
Region700 – 7045Allosteric activator fructose 2,6-bisphosphate binding By similarity
Region745 – 7473Allosteric activator fructose 2,6-bisphosphate binding By similarity
Region837 – 8404Allosteric 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 subunit beta By similarity
Binding site4331Substrate By similarity
Binding site4601Substrate; shared with subunit beta By similarity
Binding site6431Allosteric activator fructose 2,6-bisphosphate By similarity
Binding site7381Allosteric activator fructose 2,6-bisphosphate; shared with subunit beta By similarity
Binding site8051Allosteric activator fructose 2,6-bisphosphate By similarity
Binding site8311Allosteric activator fructose 2,6-bisphosphate; shared with subunit beta By similarity
Binding site9291Allosteric activator fructose 2,6-bisphosphate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q03215 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: 724687F850F27F79

FASTA992109,336
        10         20         30         40         50         60 
MNNSVYGVAF RSLSTGDEKL YKEATRFYHS LGFQTVKLYD NFKNHDDSNL IVGTSKNSVK 

        70         80         90        100        110        120 
ECWLESFKLS ELDSQGFRVP QQEASNQLQT DGVMIKLRLV DTEPLNQTAD TVVYYTVSLD 

       130        140        150        160        170        180 
EVSKIGERVD DHNVKLVDPL GNVVLVTDSH DGKELNASEF IAPKDSSVEQ KITVELVDKD 

       190        200        210        220        230        240 
SKKKKIAVMT SGGDSQGMNA AVRAVVRSSI YYGCDVYAVY EGYEGLVKGG DYLRKMEWKD 

       250        260        270        280        290        300 
VRGWLSEGGT LIGTARSKEF RERWGRKQAC SNLIDQGIDA LVVIGGDGSL TGADLFRSEW 

       310        320        330        340        350        360 
PSLVEELVKD GKFTEDEVAL YQNLTIVGMV GSIDNDMSGT DSTIGAYSAL ERICEMVDYI 

       370        380        390        400        410        420 
DATAKSHSRA FVVEVMGRHC GWLGLMSGIA TAADYIFIPE RAAPHGKWQD ELKRVCQRHR 

       430        440        450        460        470        480 
EKGRRNNTVI VAEGALDDQL NPITAEQVKD VLVELGLDTK ITTLGHVQRG GTAVAHDRWL 

       490        500        510        520        530        540 
ATLQGVDAVK AILNMTPETP SPLIGILENK VIRMPLVESV KLTKQVAAAI EAKDFDKAIS 

       550        560        570        580        590        600 
LRDTEFIELY SNFMSTTVND DGSQLLPEAD RLNIAIVHVG APSAALNAAT RAATLYCLAH 

       610        620        630        640        650        660 
GHRPYAITNG FSGLIQTGQV KELSWIDVED WHNLGGSEIG TNRSVAAEDM GTIAYHFQKN 

       670        680        690        700        710        720 
KFDGVIILGG FEGFKSLKQL RDGRDQYPIF NIPMCLIPAT VSNNVPGTEY SLGSDTCLNA 

       730        740        750        760        770        780 
LVKYTDAIKQ SASSTRRRVF VVEVQGGHSG YVASFTGLVT GAVSVYTPEN AINLKTIQED 

       790        800        810        820        830        840 
LALLKESFKH EQGETRNGKL VIRNEMASDV YTTELLADII TEQSNDRFGV RTAIPGHVQQ 

       850        860        870        880        890        900 
GGVPSSKDRV IASRFAVKCV KFIEQWNKKN TAADNEDFKI LRFNYVNGVK QYTVLDEDLS 

       910        920        930        940        950        960 
AAVICVNGSK ISFKPIAHIW ENETNIELRK GQEIHWEEYN EIGDILSGRS MLRRKIQKEQ 

       970        980        990 
QEESSLPSVA DTPLSSVTVS TSAAKEDSAL YV 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z17315 Genomic DNA. Translation: CAA78963.1.
CR382121 Genomic DNA. Translation: CAH02833.1.
PIRS32902.
RefSeqXP_451245.1. XM_451245.1.

3D structure databases

ProteinModelPortalQ03215.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING28985.Q03215.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2896656.
KEGGkla:KLLA0A05544g.

Phylogenomic databases

eggNOGCOG0205.
HOGENOMHOG000200154.
KOK00850.
OMASAKAMQW.
OrthoDBEOG7Q5HPV.

Enzyme and pathway databases

SABIO-RKQ03215.
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. 3 hits.
TIGRFAMsTIGR02478. 6PF1K_euk. 1 hit.
PROSITEPS00433. PHOSPHOFRUCTOKINASE. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePFKA1_KLULA
AccessionPrimary (citable) accession number: Q03215
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: July 9, 2014
This is version 102 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