P16861 (PFKA1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
ATP-dependent 6-phosphofructokinase subunit alpha
EC=2.7.1.11

Alternative name(s):
ATP-dependent 6-phosphofructokinase
Short name=ATP-PFK
Short name=Phosphofructokinase 1
Phosphohexokinase

Gene names

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

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	987 AA.
Sequence status	Complete.
Protein existence	Evidence 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.9 Ref.11 Ref.12 Ref.13 Ref.15 Ref.16 Ref.17 Ref.18
Catalytic activity	ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate. Ref.12
Cofactor	Magnesium.
Enzyme regulation	Allosterically activated by ADP, AMP, or fructose 2,6-bisphosphate, and allosterically inhibited by ATP or citrate. Ref.8 Ref.10 Ref.12
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.7 Ref.14
Subcellular location	Cytoplasm. Mitochondrion outer membrane; Peripheral membrane protein; Cytoplasmic side Ref.21 Ref.23.
Miscellaneous	Present with 89800 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.12 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)

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Cytoplasm Membrane Mitochondrion Mitochondrion outer membrane
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Allosteric enzyme Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	carbohydrate phosphorylation Inferred from mutant phenotype Ref.15. Source: GOC fructose 6-phosphate metabolic process Inferred from electronic annotation. Source: InterPro glycolytic process Inferred from direct assay Ref.13. Source: SGD hydrogen ion transmembrane transport Inferred from genetic interaction PubMed 18632794. Source: GOC proton transport Inferred from genetic interaction PubMed 18632794. Source: UniProtKB
Cellular_component	6-phosphofructokinase complex Inferred from mutant phenotype Ref.15. Source: SGD mitochondrion Inferred from direct assay Ref.21. Source: SGD
Molecular_function	6-phosphofructokinase activity Inferred from mutant phenotype Ref.15. Source: SGD ATP binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction PubMed 11805826PubMed 12051897PubMed 16429126PubMed 18719252. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PFK2	P16862	4	EBI-9428,EBI-9435

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 987

987

ATP-dependent 6-phosphofructokinase subunit alpha HAMAP-Rule MF_03184

PRO_0000112045

Regions

Nucleotide binding

278 – 279

2

ATP By similarity

Nucleotide binding

308 – 311

4

ATP By similarity

Region

1 – 580

580

N-terminal catalytic PFK domain 1 HAMAP-Rule MF_03184

Region

354 – 356

3

Substrate binding HAMAP-Rule MF_03184

Region

398 – 400

3

Substrate binding HAMAP-Rule MF_03184

Region

488 – 491

4

Substrate binding HAMAP-Rule MF_03184

Region

581 – 594

14

Interdomain linker HAMAP-Rule MF_03184

Region

595 – 987

393

C-terminal regulatory PFK domain 2 HAMAP-Rule MF_03184

Region

722 – 726

5

Allosteric activator fructose 2,6-bisphosphate binding HAMAP-Rule MF_03184

Region

767 – 769

3

Allosteric activator fructose 2,6-bisphosphate binding HAMAP-Rule MF_03184

Region

859 – 862

4

Allosteric activator fructose 2,6-bisphosphate binding HAMAP-Rule MF_03184

Sites

Active site

356

1

Proton acceptor

Metal binding

309

1

Magnesium; catalytic

Binding site

215

1

ATP; via amide nitrogen By similarity

Binding site

391

1

Substrate; shared with subunit beta

Binding site

455

1

Substrate

Binding site

482

1

Substrate; shared with subunit beta

Binding site

665

1

Allosteric activator fructose 2,6-bisphosphate

Binding site

760

1

Allosteric activator fructose 2,6-bisphosphate; shared with subunit beta

Binding site

827

1

Allosteric activator fructose 2,6-bisphosphate

Binding site

853

1

Allosteric activator fructose 2,6-bisphosphate; shared with subunit beta

Binding site

952

1

Allosteric activator fructose 2,6-bisphosphate

Amino acid modifications

Modified residue

3

1

Phosphoserine Ref.24

Modified residue

166

1

Phosphoserine Ref.25

Modified residue

179

1

Phosphoserine Ref.22 Ref.25

Modified residue

185

1

Phosphoserine Ref.22 Ref.24 Ref.25

Modified residue

189

1

Phosphoserine Ref.25

Modified residue

192

1

Phosphoserine Ref.22 Ref.24 Ref.25

Modified residue

217

1

Phosphoserine Ref.25

Modified residue

450

1

Phosphothreonine Ref.25

Experimental info

Mutagenesis

309

1

D → T: Reduces maximal activity of the holoenzyme by 50%. Completely abolishes catalytic activity; when associated with 'S-348' in subunit beta. Ref.16

Mutagenesis

356

1

D → S: Reduces maximal activity of the holoenzyme by 50%. Completely abolishes catalytic activity; when associated with 'S-348' in subunit beta. Ref.16

Mutagenesis

447

1

R → S: Reduces maximal activity of the holoenzyme by less than 25%. Ref.16

Mutagenesis

488

1

H → S: Increases the KM for fructose 6-phosphate 20 fold. Ref.16

Mutagenesis

724

1

S → D: Abolishes sensitivity of the holoenzyme to fructose 2,6-bisphosphate activation; when associated with 'D-718' in subunit beta. Ref.17

Mutagenesis

728

1

P → L: Drastically reduces sensitivity of the holoenzyme to ATP inhibition. Ref.18

Mutagenesis

859

1

H → S: Reduces sensitivity of the holoenzyme to fructose 2,6-bisphosphate activation; when associated with 'S-853' in subunit beta. Ref.17

Secondary structure

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987

Helix Strand Turn

Details...

Beta strand

207 – 215

9

Helix

220 – 233

14

Beta strand

237 – 241

5

Helix

244 – 250

7

Beta strand

254 – 257

4

Helix

260 – 263

4

Helix

266 – 268

3

Helix

281 – 283

3

Helix

285 – 297

13

Beta strand

300 – 307

8

Helix

309 – 319

11

Helix

322 – 330

9

Beta strand

331 – 334

4

Turn

337 – 343

7

Beta strand

347 – 356

10

Helix

368 – 388

21

Beta strand

392 – 397

6

Helix

404 – 412

9

Beta strand

416 – 419

4

Helix

421 – 423

3

Turn

427 – 429

3

Helix

430 – 443

14

Beta strand

449 – 454

6

Helix

467 – 477

11

Beta strand

481 – 485

5

Helix

487 – 490

4

Helix

497 – 515

19

Beta strand

524 – 537

14

Helix

538 – 553

16

Helix

557 – 562

6

Helix

568 – 579

12

Beta strand

595 – 603

9

Helix

608 – 622

15

Beta strand

625 – 629

5

Helix

632 – 639

8

Beta strand

642 – 644

3

Turn

647 – 652

6

Helix

653 – 655

3

Helix

668 – 670

3

Helix

672 – 681

10

Beta strand

685 – 692

8

Helix

693 – 705

13

Turn

706 – 708

3

Helix

710 – 713

4

Beta strand

716 – 721

6

Helix

736 – 757

22

Beta strand

758 – 766

9

Helix

773 – 780

8

Turn

781 – 783

3

Beta strand

785 – 788

4

Beta strand

790 – 792

3

Helix

796 – 812

17

Beta strand

821 – 826

6

Beta strand

831 – 833

3

Helix

835 – 846

12

Beta strand

849 – 856

8

Helix

858 – 862

5

Helix

868 – 890

23

Helix

921 – 923

3

Beta strand

924 – 930

7

Beta strand

933 – 938

6

Helix

939 – 942

4

Turn

948 – 951

4

Beta strand

953 – 955

3

Helix

960 – 969

10

Helix

972 – 978

7

Sequences

	Sequence		Length	Mass (Da)
	P16861 [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[4]	"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.
[5]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 794-987. Strain: ATCC 204508 / S288c.
[6]	"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 1-6; 90-97; 197-205 AND 914-921.
[7]	"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.
[8]	"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.
[9]	"Glycolysis mutants in Saccharomyces cerevisiae." Clifton D., Weinstock S.B., Fraenkel D.G. Genetics 88:1-11(1978) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[10]	"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.
[11]	"Mutant studies of yeast phosphofructokinase." Clifton D., Fraenkel D.G. Biochemistry 21:1935-1942(1982) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[12]	"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.
[13]	"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.
[14]	"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.
[15]	"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.
[16]	"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-309; ASP-356; ARG-447 AND HIS-488.
[17]	"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-724 AND HIS-859.
[18]	"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-728.
[19]	"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].
[20]	"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.
[21]	"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.
[22]	"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-179; SER-185 AND SER-192, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Strain: ADR376.
[23]	"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.
[24]	"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-3; SER-185 AND SER-192, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[25]	"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 SER-166; SER-179; SER-185; SER-189; SER-192; SER-217 AND THR-450, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[26]	"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB." Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R. Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[27]	"Sites of ubiquitin attachment in Saccharomyces cerevisiae." Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S. Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[28]	"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 201-987 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

M26943 Genomic DNA. Translation: AAA34859.1.
Z73025 Genomic DNA. Translation: CAA97268.1.
X87941 Genomic DNA. Translation: CAA61193.1.
BK006941 Genomic DNA. Translation: DAA08331.1.

PIR

JQ0016.

RefSeq

NP_011756.1. NM_001181369.1.

3D structure databases

PDBe
RCSB-PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3O8O	X-ray	2.90	A/C/E/G	201-987	[»]

ProteinModelPortal

P16861.

SMR

P16861. Positions 10-980.

ModBase

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MobiDB

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Protein-protein interaction databases

BioGrid

33492. 223 interactions.

DIP

DIP-1505N.

IntAct

P16861. 44 interactions.

MINT

MINT-393741.

STRING

4932.YGR240C.

Proteomic databases

MaxQB

P16861.

PaxDb

P16861.

PeptideAtlas

P16861.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YGR240C; YGR240C; YGR240C.

GeneID

853155.

KEGG

sce:YGR240C.

Organism-specific databases

CYGD

YGR240c.

SGD

S000003472. PFK1.

Phylogenomic databases

eggNOG

COG0205.

GeneTree

ENSGT00390000013209.

HOGENOM

HOG000200154.

KO

K00850.

OMA

SAKAMQW.

OrthoDB

EOG7Q5HPV.

Enzyme and pathway databases

BioCyc

YEAST:YGR240C-MONOMER.

SABIO-RK

P16861.

UniPathway

UPA00109; UER00182.

Gene expression databases

Genevestigator

P16861.

Family and domain databases

HAMAP

MF_03184. Phosphofructokinase_I_E.

InterPro

IPR009161. 6-phosphofructokinase_euk.
IPR022953. Phosphofructokinase.
IPR015912. Phosphofructokinase_CS.
IPR000023. Phosphofructokinase_dom.
[Graphical view]

Pfam

PF00365. PFK. 2 hits.
[Graphical view]

PIRSF

PIRSF000533. ATP_PFK_euk. 1 hit.

PRINTS

PR00476. PHFRCTKINASE.

SUPFAM

SSF53784. SSF53784. 3 hits.

TIGRFAMs

TIGR02478. 6PF1K_euk. 1 hit.

PROSITE

PS00433. PHOSPHOFRUCTOKINASE. 2 hits.
[Graphical view]

ProtoNet

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Other

NextBio

973249.

Entry information

Entry name

PFKA1_YEAST

Accession

Primary (citable) accession number: P16861
Secondary accession number(s): D6VV20

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	August 1, 1990
Last modified:	July 9, 2014
This is version 136 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program