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P16862 (K6PF2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 137. 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
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:
6-phosphofructokinase subunit beta
EC=2.7.1.11
Alternative name(s):
6PF-1-K subunit beta
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 lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

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)

Catalytic activity

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

Enzyme regulation

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

Pathway

Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4.

Subunit structure

Heterooctamer of 4 alpha and 4 beta chains.

Subcellular location

Cytoplasm.

Miscellaneous

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

Sequence similarities

Belongs to the phosphofructokinase family. Two domains subfamily.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PFK1P168616EBI-9435,EBI-9428
RSP5P399403EBI-9435,EBI-16219

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4
Chain2 – 9599586-phosphofructokinase subunit beta
PRO_0000112046

Regions

Nucleotide binding216 – 2205ATP By similarity
Nucleotide binding375 – 3795ATP By similarity
Nucleotide binding392 – 40817ATP By similarity

Sites

Active site3481Proton acceptor By similarity
Binding site3831Substrate By similarity
Binding site4811Substrate By similarity
Binding site4841Substrate By similarity

Amino acid modifications

Modified residue411Phosphoserine Ref.12
Modified residue421Phosphoserine Ref.8 Ref.12
Modified residue1521Phosphothreonine Ref.12
Modified residue1601Phosphoserine Ref.7 Ref.8 Ref.12
Modified residue1631Phosphoserine Ref.9 Ref.11 Ref.12
Modified residue1661Phosphoserine Ref.11 Ref.12
Modified residue1671Phosphoserine Ref.11 Ref.12
Modified residue1711Phosphoserine Ref.5 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12
Modified residue1721Phosphotyrosine Ref.12
Modified residue1731Phosphothreonine Ref.10 Ref.11 Ref.12
Modified residue1771Phosphotyrosine Ref.12
Modified residue1801N6-methyllysine Ref.10
Modified residue1841Phosphothreonine Ref.12
Modified residue5141Phosphothreonine Ref.12
Modified residue8031Phosphoserine Ref.12

Experimental info

Sequence conflict1371V → G in AAA34860. Ref.1
Sequence conflict8801K → E in AAA34860. Ref.1

Secondary structure

1 .............................................................................................................................. 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 204511 / S288c / AB972.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
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]"Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae."
Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M., Shabanowitz J., Hunt D.F., White F.M.
Nat. Biotechnol. 20:301-305(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-171, MASS SPECTROMETRY.
Strain: 2124.
[6]"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].
[7]"A proteomics approach to understanding protein ubiquitination."
Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G., Roelofs J., Finley D., Gygi S.P.
Nat. Biotechnol. 21:921-926(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160 AND SER-171, MASS SPECTROMETRY.
Strain: SUB592.
[8]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42; SER-160 AND SER-171, MASS SPECTROMETRY.
Strain: YAL6B.
[9]"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, MASS SPECTROMETRY.
Strain: ADR376.
[10]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-171 AND THR-173, METHYLATION AT LYS-180, MASS SPECTROMETRY.
[11]"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases."
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-163; SER-166; SER-167; SER-171 AND THR-173, MASS SPECTROMETRY.
[12]"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-41; SER-42; THR-152; SER-160; SER-163; SER-166; SER-167; SER-171; TYR-172; THR-173; TYR-177; THR-184; THR-514 AND SER-803, MASS SPECTROMETRY.
+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...

Protein-protein interaction databases

DIPDIP-2619N.
IntActP16862. 43 interactions.
MINTMINT-424355.
STRING4932.YMR205C.

Proteomic databases

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.
OMAQQGGLPS.
OrthoDBEOG418FWH.

Enzyme and pathway databases

SABIO-RKP16862.
UniPathwayUPA00109; UER00182.

Gene expression databases

GenevestigatorP16862.
GermOnlineYMR205C. Saccharomyces cerevisiae.

Family and domain databases

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. Ppfruckinase. 2 hits.
TIGRFAMsTIGR02478. 6PF1K_euk. 1 hit.
PROSITEPS00433. PHOSPHOFRUCTOKINASE. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio978807.

Entry information

Entry nameK6PF2_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: May 1, 2013
This is version 137 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome XIII

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents