P16861 (K6PF1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
6-phosphofructokinase subunit alpha
EC=2.7.1.11

Alternative name(s):
6PF-1-K subunit alpha
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)

Catalytic activity	ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate. HAMAP-Rule MF_00339
Enzyme regulation	Allosterically inhibited by ATP and activated by AMP and fructose 2,6-bisphosphate By similarity. HAMAP-Rule MF_00339
Pathway	Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4. HAMAP-Rule MF_00339
Subunit structure	Heterooctamer of 4 alpha and 4 beta chains.
Subcellular location	Cytoplasm HAMAP-Rule MF_00339.
Miscellaneous	Present with 89800 molecules/cell in log phase SD medium.
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	3D-structure Allosteric enzyme Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	carbohydrate phosphorylation Inferred from mutant phenotype PubMed 3007939. Source: GOC fructose 6-phosphate metabolic process Inferred from electronic annotation. Source: InterPro glycolysis Inferred from direct assay PubMed 3000145. 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 PubMed 3007939. Source: SGD mitochondrion Inferred from direct assay PubMed 16962558. Source: SGD
Molecular_function	6-phosphofructokinase activity Inferred from mutant phenotype PubMed 3007939. Source: SGD ATP binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
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

6-phosphofructokinase subunit alpha HAMAP-Rule MF_00339

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

166

1

Phosphoserine Ref.11

Modified residue

179

1

Phosphoserine Ref.9 Ref.11

Modified residue

185

1

Phosphoserine Ref.9 Ref.10 Ref.11

Modified residue

189

1

Phosphoserine Ref.11

Modified residue

192

1

Phosphoserine Ref.9 Ref.10 Ref.11

Modified residue

217

1

Phosphoserine Ref.11

Modified residue

450

1

Phosphothreonine Ref.11

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]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases 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]	"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].
[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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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-179; SER-185 AND SER-192, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Strain: ADR376.
[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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3; SER-185 AND SER-192, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]	"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].
[12]	"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].
[13]	"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].
+	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

Search...

MobiDB

Search...

Protein-protein interaction databases

BioGrid

33492. 222 interactions.

DIP

DIP-1505N.

IntAct

P16861. 44 interactions.

MINT

MINT-393741.

STRING

4932.YGR240C.

Proteomic databases

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

CEDWETE.

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_00339. Phosphofructokinase.

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

Search...

Other

NextBio

973249.

Entry information

Entry name

K6PF1_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:	April 16, 2014
This is version 133 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program