6-phosphofructokinase subunit beta - Saccharomyces cerevisiae (Baker's yeast)

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Reviewed, UniProtKB/Swiss-Prot P16862 (K6PF2_YEAST)

Last modified November 3, 2009. Version 103. History...

Clusters with 100%, 90%, 50% identity |

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    6-phosphofructokinase subunit beta
    EC=2.7.1.11
Alternative name(s):
    Phosphofructokinase 2
    Phosphohexokinase
    6PF-1-K subunit beta

Gene names

Name:	PFK2
Ordered Locus Names:	YMR205C
ORF Names:	YM8325.06C

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

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Protein attributes

Sequence length	959 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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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. Ref.5
Sequence similarities	Belongs to the phosphofructokinase family. Two domains subfamily.

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Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Cytoplasm
Domain	Repeat
Ligand	ATP-binding Magnesium Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Methylation Phosphoprotein
Technical term	Allosteric enzyme Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	glycolysis Inferred from direct assay. Source: SGD proton transport Inferred from genetic interaction. Source: UniProtKB
Cellular component	6-phosphofructokinase complex Inferred from mutant phenotype. Source: SGD mitochondrion Inferred from direct assay. Source: SGD
Molecular function	6-phosphofructokinase activity Inferred from mutant phenotype. Source: SGD ATP binding Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct
GIS4	Q04233	1	EBI-9435,EBI-27721
PFK1	P16861	1	EBI-9435,EBI-9428
PRP40	P33203	1	EBI-9435,EBI-701
RSP5	P39940	1	EBI-9435,EBI-16219
SSM4	P40318	1	EBI-9435,EBI-18208

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.3

Chain

2 – 959

958

6-phosphofructokinase subunit beta

PRO_0000112046

Regions

Nucleotide binding

216 – 220

ATP By similarity

Nucleotide binding

375 – 379

ATP By similarity

Nucleotide binding

392 – 408

ATP By similarity

Sites

Active site

348

Proton acceptor By similarity

Binding site

383

Substrate By similarity

Binding site

481

Substrate By similarity

Binding site

484

Substrate By similarity

Amino acid modifications

Modified residue

Phosphoserine Ref.11

Modified residue

Phosphoserine Ref.11 Ref.7

Modified residue

152

Phosphothreonine Ref.11

Modified residue

160

Phosphoserine Ref.11 Ref.7 Ref.6

Modified residue

163

Phosphoserine Ref.11 Ref.8 Ref.10

Modified residue

166

Phosphoserine Ref.11 Ref.10

Modified residue

167

Phosphoserine Ref.11 Ref.10

Modified residue

171

Phosphoserine Ref.11 Ref.7 Ref.6 Ref.8 Ref.10 Ref.4 Ref.9

Modified residue

172

Phosphotyrosine Ref.11

Modified residue

173

Phosphothreonine Ref.11 Ref.10 Ref.9

Modified residue

177

Phosphotyrosine Ref.11

Modified residue

180

N6-methyllysine Ref.9

Modified residue

184

Phosphothreonine Ref.11

Modified residue

514

Phosphothreonine Ref.11

Modified residue

803

Phosphoserine Ref.11

Experimental info

Sequence conflict

137

V → G in AAA34860. Ref.1

Sequence conflict

880

K → E in AAA34860. Ref.1

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Sequences

Sequence

Length

Mass (Da)

Tools

P16862-1 [UniParc].

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

959

104,618

        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

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References

	« Hide 'large scale' referencesShow '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: 2528496] [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. Barrell B.G. Nature 387:90-93(1997) [PubMed: 9169872] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	"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: 8223596] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-12; 181-185 AND 193-197.
[4]	"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: 11875433] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-171, MASS SPECTROMETRY.
[5]	"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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[6]	"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: 12872131] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160 AND SER-171, MASS SPECTROMETRY.
[7]	"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: 15665377] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42; SER-160 AND SER-171, MASS SPECTROMETRY.
[8]	"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: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-163 AND SER-171, MASS SPECTROMETRY.
[9]	"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: 17287358] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-171 AND THR-173, METHYLATION AT LYS-180, MASS SPECTROMETRY.
[10]	"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: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-163; SER-166; SER-167; SER-171 AND THR-173, MASS SPECTROMETRY.
[11]	"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: 18407956] [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.

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Cross-references

Sequence databases
	M26944 Genomic DNA. Translation: AAA34860.1. Z48755 Genomic DNA. Translation: CAA88646.1.
PIR	JQ0017. S59446.
RefSeq	NP_013932.1.
3D structure databases
HSSP	HSSP built from PDB template 3PFK based on UniProtKB P00512.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:2619N.
IntAct	P16862. 39 interactions.
STRING	P16862.
Proteomic databases
PeptideAtlas	P16862.
PRIDE	P16862.
Genome annotation databases
Ensembl	YMR205C; YMR205C; YMR205C; Saccharomyces cerevisiae. [Genome view]
GeneID	855245.
GenomeReviews	Gene locus YMR205C in contig Z71257_GR.
KEGG	sce:YMR205C.
NMPDR	fig\|4932.3.peg.4985.
Organism-specific databases
CYGD	YMR205c.
SGD	S000004818. PFK2.
Phylogenomic databases
HOGENOM	P16862.
OMA	ANSHSRA.
Enzyme and pathway databases
BRENDA	2.7.1.11. 250.
Gene expression databases
ArrayExpress	P16862.
Genevestigator	P16862.
GermOnline	YMR205C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR009161. 6-phosphofructokinase_euk. IPR000023. Phosphofructokinase. IPR015912. Phosphofructokinase_CS. [Graphical view]
Pfam	PF00365. PFK. 2 hits. [Graphical view]
PIRSF	PIRSF000533. ATP_PFK_euk. 1 hit.
PRINTS	PR00476. PHFRCTKINASE.
ProDom	PD000707. Ppfruckinase. 2 hits. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR02478. 6PF1K_euk. 1 hit.
PROSITE	PS00433. PHOSPHOFRUCTOKINASE. 2 hits. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	978807.

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Entry information

Entry name

K6PF2_YEAST

Accession

Primary (citable) accession number: P16862

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	January 23, 2007
Last modified:	November 3, 2009
This is version 103 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Yeast

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

Yeast chromosome XIII

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

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents