Reviewed, UniProtKB/Swiss-Prot P16861 (K6PF1_YEAST)

Names and origin

Protein names

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

Gene names

Name:	PFK1
Ordered Locus Names:	YGR240C
ORF Names:	G8599

Organism

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

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	987 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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 89800 molecules/cell in log phase SD medium. Ref.6
Sequence similarities	Belongs to the phosphofructokinase family. Two domains subfamily.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Cytoplasm
Domain	Repeat
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	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...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
FMP31	Q08742	1	EBI-9428,EBI-33610
PFK2	P16862	1	EBI-9428,EBI-9435
RSA1	Q08932	1	EBI-9428,EBI-16186

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 987	987	6-phosphofructokinase subunit alpha		PRO_0000112045
Regions
	Nucleotide binding	225 – 229	5	ATP By similarity
	Nucleotide binding	383 – 387	5	ATP By similarity
	Nucleotide binding	400 – 416	17	ATP By similarity
Sites
	Active site	356	1	Proton acceptor By similarity
	Metal binding	414	1	Magnesium; via carbonyl oxygen By similarity
	Binding site	391	1	Substrate By similarity
	Binding site	488	1	Substrate By similarity
	Binding site	491	1	Substrate By similarity
Amino acid modifications
	Modified residue	3	1	Phosphoserine Ref.10
	Modified residue	57	1	Phosphoserine Ref.10
	Modified residue	166	1	Phosphoserine Ref.10
	Modified residue	178	1	Phosphothreonine Ref.10
	Modified residue	179	1	Phosphoserine Ref.10 Ref.7 Ref.8
	Modified residue	185	1	Phosphoserine Ref.10 Ref.8
	Modified residue	188	1	Phosphoserine Ref.10
	Modified residue	189	1	Phosphoserine Ref.10
	Modified residue	192	1	Phosphoserine Ref.10 Ref.8
	Modified residue	895	1	Phosphoserine Ref.10 Ref.9

Sequences

	Sequence		Length	Mass (Da)
	P16861-1 [UniParc]. Last modified August 1, 1990. Version 1. Checksum: 995B3DF7C7781B29	FASTA	987	107,970
	10 20 30 40 50 60 MQSQDSCYGV AFRSIITNDE ALFKKTIHFY HTLGFATVKD FNKFKHGENS LLSSGTSQDS 70 80 90 100 110 120 LREVWLESFK LSEVDASGFR IPQQEATNKA QSQGALLKIR LVMSAPIDET FDTNETATIT 130 140 150 160 170 180 YFSTDLNKIV EKFPKQAEKL SDTLVFLKDP MGNNITFSGL ANATDSAPTS KDAFLEATSE 190 200 210 220 230 240 DEIISRASSD ASDLLRQTLG SSQKKKKIAV MTSGGDSPGM NAAVRAVVRT GIHFGCDVFA 250 260 270 280 290 300 VYEGYEGLLR GGKYLKKMAW EDVRGWLSEG GTLIGTARSM EFRKREGRRQ AAGNLISQGI 310 320 330 340 350 360 DALVVCGGDG SLTGADLFRH EWPSLVDELV AEGRFTKEEV APYKNLSIVG LVGSIDNDMS 370 380 390 400 410 420 GTDSTIGAYS ALERICEMVD YIDATAKSHS RAFVVEVMGR HCGWLALMAG IATGADYIFI 430 440 450 460 470 480 PERAVPHGKW QDELKEVCQR HRSKGRRNNT IIVAEGALDD QLNPVTANDV KDALIELGLD 490 500 510 520 530 540 TKVTILGHVQ RGGTAVAHDR WLATLQGVDA VKAVLEFTPE TPSPLIGILE NKIIRMPLVE 550 560 570 580 590 600 SVKLTKSVAT AIENKDFDKA ISLRDTEFIE LYENFLSTTV KDDGSELLPV SDRLNIGIVH 610 620 630 640 650 660 VGAPSAALNA ATRAATLYCL SHGHKPYAIM NGFSGLIQTG EVKELSWIDV ENWHNLGGSE 670 680 690 700 710 720 IGTNRSVASE DLGTIAYYFQ KNKLDGLIIL GGFEGFRSLK QLRDGRTQHP IFNIPMCLIP 730 740 750 760 770 780 ATVSNNVPGT EYSLGVDTCL NALVNYTDDI KQSASATRRR VFVCEVQGGH SGYIASFTGL 790 800 810 820 830 840 ITGAVSVYTP EKKIDLASIR EDITLLKENF RHDKGENRNG KLLVRNEQAS SVYSTQLLAD 850 860 870 880 890 900 IISEASKGKF GVRTAIPGHV QQGGVPSSKD RVTASRFAVK CIKFIEQWNK KNEASPNTDA 910 920 930 940 950 960 KVLRFKFDTH GEKVPTVEHE DDSAAVICVN GSHVSFKPIA NLWENETNVE LRKGFEVHWA 970 980 EYNKIGDILS GRLKLRAEVA ALAAENK

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]	"Sequencing of a 9.9 kb segment on the right arm of yeast chromosome VII reveals four open reading frames, including PFK1, the gene coding for succinyl-CoA synthetase (beta-chain) and two ORFs sharing homology with ORFs of the yeast chromosome VIII." Guerreiro P., Azevedo D., Barreiros T., Rodrigues-Pousada C. Yeast 13:275-280(1997) [PubMed: 9090057] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII." Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E. , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K. Nature 387:81-84(1997) [PubMed: 9169869] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[4]	"Sequence analysis of the 43 kb CRM1-YLM9-PET54-DIE2-SMI1-PHO81-YHB4-PFK1 region from the right arm of Saccharomyces cerevisiae chromosome VII." van der Aart Q.J.M., Kleine K., Steensma H.Y. Yeast 12:385-390(1996) [PubMed: 8701610] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 794-987. Strain: ATCC 204508 / S288c.
[5]	"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 1-6; 90-97; 197-205 AND 914-921.
[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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[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-179, 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-179; SER-185 AND SER-192, MASS SPECTROMETRY.
[9]	"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-895, MASS SPECTROMETRY.
[10]	"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-3; SER-57; SER-166; THR-178; SER-179; SER-185; SER-188; SER-189; SER-192 AND SER-895, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M26943 Genomic DNA. Translation: AAA34859.1. Z73025 Genomic DNA. Translation: CAA97268.1. X87941 Genomic DNA. Translation: CAA61193.1.
PIR	JQ0016.
RefSeq	NP_011756.1.
3D structure databases
HSSP	HSSP built from PDB template 3PFK based on UniProtKB P00512.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:1505N.
IntAct	P16861. 56 interactions.
STRING	P16861.
Proteomic databases
PeptideAtlas	P16861.
PRIDE	P16861.
Genome annotation databases
Ensembl	YGR240C; YGR240C; YGR240C; Saccharomyces cerevisiae. [Genome view]
GeneID	853155.
GenomeReviews	Gene locus YGR240C in contig Y13135_GR.
KEGG	sce:YGR240C.
NMPDR	fig|4932.3.peg.2884.
Organism-specific databases
CYGD	YGR240c.
SGD	S000003472. PFK1.
Phylogenomic databases
HOGENOM	P16861.
OMA	DSTIGAY.
Enzyme and pathway databases
BRENDA	2.7.1.11. 250.
Gene expression databases
ArrayExpress	P16861.
Genevestigator	P16861.
GermOnline	YGR240C. 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	973249.

Entry information

Entry name

K6PF1_YEAST

Accession

Primary (citable) accession number: P16861

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	August 1, 1990
Last modified:	November 3, 2009
This is version 93 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)