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P16862 (PFKA2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 148. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ATP-dependent 6-phosphofructokinase subunit beta

EC=2.7.1.11
Alternative name(s):
ATP-dependent 6-phosphofructokinase
Short name=ATP-PFK
Short name=Phosphofructokinase 2
Phosphohexokinase
Gene names
Name:PFK2
Ordered Locus Names:YMR205C
ORF Names:YM8325.06C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length959 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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. Ref.7 Ref.9 Ref.10 Ref.11 Ref.13 Ref.14 Ref.15 Ref.16

Catalytic activity

ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate. Ref.10

Cofactor

Magnesium.

Enzyme regulation

Allosterically activated by ADP, AMP, or fructose 2,6-bisphosphate, and allosterically inhibited by ATP or citrate. Ref.6 Ref.8 Ref.10

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. Ref.5 Ref.12

Subcellular location

Cytoplasm. Mitochondrion outer membrane; Peripheral membrane protein; Cytoplasmic side Ref.19 Ref.22.

Miscellaneous

Present with 90200 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Eukaryotic two domain clade "E" sub-subfamily.

Biophysicochemical properties

Kinetic parameters:

KM=0.24 mM for ATP (without effector) Ref.10

KM=0.3 mM for ATP (with 1 mM AMP)

KM=0.31 mM for ATP (with 20 µM fructose 2,6-bisphosphate)

KM=1.65 mM for fructose 6-phosphate (without effector)

KM=0.51 mM for fructose 6-phosphate (with 1 mM AMP)

KM=0.11 mM for fructose 6-phosphate (with 20 µM fructose 2,6-bisphosphate)

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PFK1P168614EBI-9435,EBI-9428
RSP5P399403EBI-9435,EBI-16219

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4
Chain2 – 959958ATP-dependent 6-phosphofructokinase subunit beta HAMAP-Rule MF_03184
PRO_0000112046

Regions

Nucleotide binding270 – 2712ATP By similarity
Nucleotide binding300 – 3034ATP By similarity
Region2 – 573572N-terminal catalytic PFK domain 1 HAMAP-Rule MF_03184
Region346 – 3483Substrate binding HAMAP-Rule MF_03184
Region390 – 3923Substrate binding HAMAP-Rule MF_03184
Region481 – 4844Substrate binding HAMAP-Rule MF_03184
Region574 – 58714Interdomain linker HAMAP-Rule MF_03184
Region588 – 959372C-terminal regulatory PFK domain 2 HAMAP-Rule MF_03184
Region716 – 7205Allosteric activator fructose 2,6-bisphosphate binding By similarity
Region716 – 7183Allosteric activator fructose 2,6-bisphosphate binding HAMAP-Rule MF_03184
Region761 – 7633Allosteric activator fructose 2,6-bisphosphate binding HAMAP-Rule MF_03184
Region853 – 8564Allosteric activator fructose 2,6-bisphosphate binding HAMAP-Rule MF_03184

Sites

Active site3481Proton acceptor
Metal binding3011Magnesium; catalytic
Binding site2061ATP; via amide nitrogen By similarity
Binding site3831Substrate; shared with subunit alpha
Binding site4471Substrate
Binding site4751Substrate; shared with subunit alpha
Binding site6581Allosteric activator fructose 2,6-bisphosphate
Binding site7541Allosteric activator fructose 2,6-bisphosphate; shared with subunit alpha By similarity
Binding site8471Allosteric activator fructose 2,6-bisphosphate; shared with subunit alpha By similarity
Binding site9351Allosteric activator fructose 2,6-bisphosphate

Amino acid modifications

Modified residue1521Phosphothreonine Ref.24
Modified residue1631Phosphoserine Ref.20 Ref.24
Modified residue1711Phosphoserine Ref.20 Ref.24
Modified residue8031Phosphoserine Ref.23

Experimental info

Mutagenesis3011D → T: Reduces maximal activity of the holoenzyme by 30%. Ref.14
Mutagenesis3481D → S: Reduces maximal activity of the holoenzyme by 50%. Completely abolishes catalytic activity; when associated with 'T-309' or 'S-356' in subunit alpha. Ref.14
Mutagenesis4391R → V: Reduces maximal activity of the holoenzyme by less than 25%. Ref.14
Mutagenesis4811H → S: Increases the KM for fructose 6-phosphate 50 fold. Ref.14
Mutagenesis7181S → D: Abolishes sensitivity of the holoenzyme to fructose 2,6-bisphosphate activation; when associated with 'D-724' in subunit alpha. Ref.15
Mutagenesis7221P → L: Drastically reduces sensitivity of the holoenzyme to ATP inhibition. Ref.16
Mutagenesis8531H → S: Reduces sensitivity of the holoenzyme to fructose 2,6-bisphosphate activation; when associated with 'S-859' in subunit alpha. Ref.15
Sequence conflict1371V → G in AAA34860. Ref.1
Sequence conflict8801K → E in AAA34860. Ref.1

Secondary structure

.............................................................................................................................. 959
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P16862 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 82CE6402CEDBBCB2

FASTA959104,618
        10         20         30         40         50         60 
MTVTTPFVNG TSYCTVTAYS VQSYKAAIDF YTKFLSLENR SSPDENSTLL SNDSISLKIL 

        70         80         90        100        110        120 
LRPDEKINKN VEAHLKELNS ITKTQDWRSH ATQSLVFNTS DILAVKDTLN AMNAPLQGYP 

       130        140        150        160        170        180 
TELFPMQLYT LDPLGNVVGV TSTKNAVSTK PTPPPAPEAS AESGLSSKVH SYTDLAYRMK 

       190        200        210        220        230        240 
TTDTYPSLPK PLNRPQKAIA VMTSGGDAPG MNSNVRAIVR SAIFKGCRAF VVMEGYEGLV 

       250        260        270        280        290        300 
RGGPEYIKEF HWEDVRGWSA EGGTNIGTAR CMEFKKREGR LLGAQHLIEA GVDALIVCGG 

       310        320        330        340        350        360 
DGSLTGADLF RSEWPSLIEE LLKTNRISNE QYERMKHLNI CGTVGSIDND MSTTDATIGA 

       370        380        390        400        410        420 
YSALDRICKA IDYVEATANS HSRAFVVEVM GRNCGWLALL AGIATSADYI FIPEKPATSS 

       430        440        450        460        470        480 
EWQDQMCDIV SKHRSRGKRT TIVVVAEGAI AADLTPISPS DVHKVLVDRL GLDTRITTLG 

       490        500        510        520        530        540 
HVQRGGTAVA YDRILATLQG LEAVNAVLES TPDTPSPLIA VNENKIVRKP LMESVKLTKA 

       550        560        570        580        590        600 
VAEAIQAKDF KRAMSLRDTE FIEHLNNFMA INSADHNEPK LPKDKRLKIA IVNVGAPAGG 

       610        620        630        640        650        660 
INSAVYSMAT YCMSQGHRPY AIYNGWSGLA RHESVRSLNW KDMLGWQSRG GSEIGTNRVT 

       670        680        690        700        710        720 
PEEADLGMIA YYFQKYEFDG LIIVGGFEAF ESLHQLERAR ESYPAFRIPM VLIPATLSNN 

       730        740        750        760        770        780 
VPGTEYSLGS DTALNALMEY CDVVKQSASS TRGRAFVVDC QGGNSGYLAT YASLAVGAQV 

       790        800        810        820        830        840 
SYVPEEGISL EQLSEDIEYL AQSFEKAEGR GRFGKLILKS TNASKALSAT KLAEVITAEA 

       850        860        870        880        890        900 
DGRFDAKPAY PGHVQQGGLP SPIDRTRATR MAIKAVGFIK DNQAAIAEAR AAEENFNADD 

       910        920        930        940        950 
KTISDTAAVV GVKGSHVVYN SIRQLYDYET EVSMRMPKVI HWQATRLIAD HLVGRKRVD 

« Hide

References

« Hide 'large scale' references
[1]"The phosphofructokinase genes of yeast evolved from two duplication events."
Heinisch J.J., Ritzel R.G., von Borstel R.C., Aguilera A., Rodicio R., Zimmermann F.K.
Gene 78:309-321(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII."
Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P. expand/collapse author list , Skelton J., Walsh S.V., Whitehead S., Barrell B.G.
Nature 387:90-93(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Limited proteolysis of yeast phosphofructokinase. Sequence locations of cleavage sites created by the actions of different proteinases."
Kopperschlaeger G., Baer J., Stellwagen E.
Eur. J. Biochem. 217:527-533(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-12; 181-185 AND 193-197.
[5]"Physicochemical parameters and subunit composition of yeast phosphofructokinase."
Kopperschlaeger G., Baer J., Nissler K., Hofmann E.
Eur. J. Biochem. 81:317-325(1977) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT.
[6]"Activation by phosphate of yeast phosphofructokinase."
Banuelos M., Gancedo C., Gancedo J.M.
J. Biol. Chem. 252:6394-6398(1977) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION.
[7]"Phosphorus-31 nuclear magnetic resonance studies of wild-type and glycolytic pathway mutants of Saccharomyces cerevisiae."
Navon G., Shulman R.G., Yamane T., Eccleshall T.R., Lam K.B., Baronofsky J.J., Marmur J.
Biochemistry 18:4487-4499(1979) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"Stimulation of yeast phosphofructokinase activity by fructose 2,6-bisphosphate."
Avigad G.
Biochem. Biophys. Res. Commun. 102:985-991(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION.
[9]"Mutant studies of yeast phosphofructokinase."
Clifton D., Fraenkel D.G.
Biochemistry 21:1935-1942(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[10]"Similarity of activation of yeast phosphofructokinase by AMP and fructose-2,6-bisphosphate."
Nissler K., Otto A., Schellenberger W., Hofmann E.
Biochem. Biophys. Res. Commun. 111:294-300(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
[11]"Temporal organization of the phosphofructokinase/fructose-1,6-biphosphatase cycle."
Hofmann E., Eschrich K., Schellenberger W.
Adv. Enzyme Regul. 23:331-362(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[12]"An electron microscopy study of the quarternary structure of yeast phosphofructokinase."
Nissler K., Hofmann E., Stel'maschchuk V., Orlova E., Kiselev N.
Biomed. Biochim. Acta 44:251-259(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT.
[13]"Isolation and characterization of the two structural genes coding for phosphofructokinase in yeast."
Heinisch J.
Mol. Gen. Genet. 202:75-82(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[14]"Studies on the function of yeast phosphofructokinase subunits by in vitro mutagenesis."
Arvanitidis A., Heinisch J.J.
J. Biol. Chem. 269:8911-8918(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF ASP-301; ASP-348; ARG-439 AND HIS-481.
[15]"A yeast phosphofructokinase insensitive to the allosteric activator fructose 2,6-bisphosphate. Glycolysis/metabolic regulation/allosteric control."
Heinisch J.J., Boles E., Timpel C.
J. Biol. Chem. 271:15928-15933(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF SER-718 AND HIS-853.
[16]"Single point mutations in either gene encoding the subunits of the heterooctameric yeast phosphofructokinase abolish allosteric inhibition by ATP."
Rodicio R., Strauss A., Heinisch J.J.
J. Biol. Chem. 275:40952-40960(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF PRO-722.
[17]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[18]"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: YAL6B.
[19]"Enolase takes part in a macromolecular complex associated to mitochondria in yeast."
Brandina I., Graham J., Lemaitre-Guillier C., Entelis N., Krasheninnikov I., Sweetlove L., Tarassov I., Martin R.P.
Biochim. Biophys. Acta 1757:1217-1228(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[20]"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-163 AND SER-171, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[21]"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"Detection and localisation of protein-protein interactions in Saccharomyces cerevisiae using a split-GFP method."
Barnard E., McFerran N.V., Trudgett A., Nelson J., Timson D.J.
Fungal Genet. Biol. 45:597-604(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[23]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-803, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[24]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-152; SER-163 AND SER-171, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[25]"The crystal structures of eukaryotic phosphofructokinases from baker's yeast and rabbit skeletal muscle."
Banaszak K., Mechin I., Obmolova G., Oldham M., Chang S.H., Ruiz T., Radermacher M., Kopperschlager G., Rypniewski W.
J. Mol. Biol. 407:284-297(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 194-959 IN COMPLEX WITH SUBSTRATE FRUCTOSE 6-PHOSPHATE AND ALLOSTERIC ACTIVATOR FRUCTOSE 2,6-BISPHOSPHATE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M26944 Genomic DNA. Translation: AAA34860.1.
Z48755 Genomic DNA. Translation: CAA88646.1.
BK006946 Genomic DNA. Translation: DAA10104.1.
PIRJQ0017. S59446.
RefSeqNP_013932.1. NM_001182712.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3O8OX-ray2.90B/D/F/H194-959[»]
ProteinModelPortalP16862.
SMRP16862. Positions 9-957.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid35383. 169 interactions.
DIPDIP-2619N.
IntActP16862. 42 interactions.
MINTMINT-424355.
STRING4932.YMR205C.

Proteomic databases

MaxQBP16862.
PaxDbP16862.
PeptideAtlasP16862.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYMR205C; YMR205C; YMR205C.
GeneID855245.
KEGGsce:YMR205C.

Organism-specific databases

SGDS000004818. PFK2.

Phylogenomic databases

eggNOGCOG0205.
GeneTreeENSGT00390000013209.
HOGENOMHOG000200154.
KOK00850.
OMAMEYCDVV.
OrthoDBEOG7Q5HPV.

Enzyme and pathway databases

BioCycYEAST:YMR205C-MONOMER.
SABIO-RKP16862.
UniPathwayUPA00109; UER00182.

Gene expression databases

GenevestigatorP16862.

Family and domain databases

Gene3D3.10.180.10. 1 hit.
HAMAPMF_03184. Phosphofructokinase_I_E.
InterProIPR009161. 6-phosphofructokinase_euk.
IPR029068. Glyas_Bleomycin-R_OHBP_Dase.
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.
SSF54593. SSF54593. 1 hit.
TIGRFAMsTIGR02478. 6PF1K_euk. 1 hit.
PROSITEPS00433. PHOSPHOFRUCTOKINASE. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio978807.

Entry information

Entry namePFKA2_YEAST
AccessionPrimary (citable) accession number: P16862
Secondary accession number(s): D6W030
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 148 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XIII

Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways