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P16861

- PFKA1_YEAST

UniProt

P16861 - PFKA1_YEAST

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Protein

ATP-dependent 6-phosphofructokinase subunit alpha

Gene

PFK1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.8 PublicationsUniRule annotation

Catalytic activityi

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

Cofactori

Magnesium.

Enzyme regulationi

Allosterically activated by ADP, AMP, or fructose 2,6-bisphosphate, and allosterically inhibited by ATP or citrate.3 PublicationsUniRule annotation

Kineticsi

  1. KM=0.24 mM for ATP (without effector)1 Publication
  2. KM=0.3 mM for ATP (with 1 mM AMP)1 Publication
  3. KM=0.31 mM for ATP (with 20 µM fructose 2,6-bisphosphate)1 Publication
  4. KM=1.65 mM for fructose 6-phosphate (without effector)1 Publication
  5. KM=0.51 mM for fructose 6-phosphate (with 1 mM AMP)1 Publication
  6. KM=0.11 mM for fructose 6-phosphate (with 20 µM fructose 2,6-bisphosphate)1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei215 – 2151ATP; via amide nitrogenUniRule annotation
Metal bindingi309 – 3091Magnesium; catalytic
Active sitei356 – 3561Proton acceptor
Binding sitei391 – 3911Substrate; shared with subunit beta
Binding sitei455 – 4551Substrate
Binding sitei482 – 4821Substrate; shared with subunit beta
Binding sitei665 – 6651Allosteric activator fructose 2,6-bisphosphate1 PublicationUniRule annotation
Binding sitei760 – 7601Allosteric activator fructose 2,6-bisphosphate; shared with subunit beta1 PublicationUniRule annotation
Binding sitei827 – 8271Allosteric activator fructose 2,6-bisphosphate1 PublicationUniRule annotation
Binding sitei853 – 8531Allosteric activator fructose 2,6-bisphosphate; shared with subunit beta1 PublicationUniRule annotation
Binding sitei952 – 9521Allosteric activator fructose 2,6-bisphosphate1 PublicationUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi278 – 2792ATPUniRule annotation
Nucleotide bindingi308 – 3114ATPUniRule annotation

GO - Molecular functioni

  1. 6-phosphofructokinase activity Source: SGD
  2. ATP binding Source: UniProtKB-KW
  3. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. carbohydrate phosphorylation Source: GOC
  2. fructose 6-phosphate metabolic process Source: InterPro
  3. glycolytic process Source: SGD
  4. hydrogen ion transmembrane transport Source: GOC
  5. proton transport Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:YGR240C-MONOMER.
SABIO-RKP16861.
UniPathwayiUPA00109; UER00182.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent 6-phosphofructokinase subunit alphaUniRule annotation (EC:2.7.1.11UniRule annotation)
Alternative name(s):
ATP-dependent 6-phosphofructokinaseUniRule annotation
Short name:
ATP-PFKUniRule annotation
Short name:
Phosphofructokinase 1UniRule annotation
PhosphohexokinaseUniRule annotation
Gene namesi
Name:PFK1
Ordered Locus Names:YGR240C
ORF Names:G8599
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome VII

Organism-specific databases

CYGDiYGR240c.
SGDiS000003472. PFK1.

Subcellular locationi

GO - Cellular componenti

  1. 6-phosphofructokinase complex Source: SGD
  2. mitochondrial outer membrane Source: UniProtKB-KW
  3. mitochondrion Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Mitochondrion, Mitochondrion outer membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi309 – 3091D → T: Reduces maximal activity of the holoenzyme by 50%. Completely abolishes catalytic activity; when associated with 'S-348' in subunit beta. 1 Publication
Mutagenesisi356 – 3561D → S: Reduces maximal activity of the holoenzyme by 50%. Completely abolishes catalytic activity; when associated with 'S-348' in subunit beta. 1 Publication
Mutagenesisi447 – 4471R → S: Reduces maximal activity of the holoenzyme by less than 25%. 1 Publication
Mutagenesisi488 – 4881H → S: Increases the KM for fructose 6-phosphate 20 fold. 1 Publication
Mutagenesisi724 – 7241S → D: Abolishes sensitivity of the holoenzyme to fructose 2,6-bisphosphate activation; when associated with 'D-718' in subunit beta. 1 Publication
Mutagenesisi728 – 7281P → L: Drastically reduces sensitivity of the holoenzyme to ATP inhibition. 1 Publication
Mutagenesisi859 – 8591H → S: Reduces sensitivity of the holoenzyme to fructose 2,6-bisphosphate activation; when associated with 'S-853' in subunit beta. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 987987ATP-dependent 6-phosphofructokinase subunit alphaPRO_0000112045Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei3 – 31Phosphoserine1 Publication
Modified residuei166 – 1661Phosphoserine1 Publication
Modified residuei179 – 1791Phosphoserine2 Publications
Modified residuei185 – 1851Phosphoserine3 Publications
Modified residuei189 – 1891Phosphoserine1 Publication
Modified residuei192 – 1921Phosphoserine3 Publications
Modified residuei217 – 2171Phosphoserine1 Publication
Modified residuei450 – 4501Phosphothreonine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP16861.
PaxDbiP16861.
PeptideAtlasiP16861.

Expressioni

Gene expression databases

GenevestigatoriP16861.

Interactioni

Subunit structurei

Heterooctamer of 4 alpha and 4 beta chains.3 PublicationsUniRule annotation

Binary interactionsi

WithEntry#Exp.IntActNotes
PFK2P168624EBI-9428,EBI-9435

Protein-protein interaction databases

BioGridi33492. 224 interactions.
DIPiDIP-1505N.
IntActiP16861. 44 interactions.
MINTiMINT-393741.
STRINGi4932.YGR240C.

Structurei

Secondary structure

1
987
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi207 – 2159
Helixi220 – 23314
Beta strandi237 – 2415
Helixi244 – 2507
Beta strandi254 – 2574
Helixi260 – 2634
Helixi266 – 2683
Helixi281 – 2833
Helixi285 – 29713
Beta strandi300 – 3078
Helixi309 – 31911
Helixi322 – 3309
Beta strandi331 – 3344
Turni337 – 3437
Beta strandi347 – 35610
Helixi368 – 38821
Beta strandi392 – 3976
Helixi404 – 4129
Beta strandi416 – 4194
Helixi421 – 4233
Turni427 – 4293
Helixi430 – 44314
Beta strandi449 – 4546
Helixi467 – 47711
Beta strandi481 – 4855
Helixi487 – 4904
Helixi497 – 51519
Beta strandi524 – 53714
Helixi538 – 55316
Helixi557 – 5626
Helixi568 – 57912
Beta strandi595 – 6039
Helixi608 – 62215
Beta strandi625 – 6295
Helixi632 – 6398
Beta strandi642 – 6443
Turni647 – 6526
Helixi653 – 6553
Helixi668 – 6703
Helixi672 – 68110
Beta strandi685 – 6928
Helixi693 – 70513
Turni706 – 7083
Helixi710 – 7134
Beta strandi716 – 7216
Helixi736 – 75722
Beta strandi758 – 7669
Helixi773 – 7808
Turni781 – 7833
Beta strandi785 – 7884
Beta strandi790 – 7923
Helixi796 – 81217
Beta strandi821 – 8266
Beta strandi831 – 8333
Helixi835 – 84612
Beta strandi849 – 8568
Helixi858 – 8625
Helixi868 – 89023
Helixi921 – 9233
Beta strandi924 – 9307
Beta strandi933 – 9386
Helixi939 – 9424
Turni948 – 9514
Beta strandi953 – 9553
Helixi960 – 96910
Helixi972 – 9787

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3O8OX-ray2.90A/C/E/G201-987[»]
ProteinModelPortaliP16861.
SMRiP16861. Positions 10-980.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 580580N-terminal catalytic PFK domain 1Add
BLAST
Regioni354 – 3563Substrate binding
Regioni398 – 4003Substrate binding
Regioni488 – 4914Substrate binding
Regioni581 – 59414Interdomain linkerAdd
BLAST
Regioni595 – 987393C-terminal regulatory PFK domain 2Add
BLAST
Regioni722 – 7265Allosteric activator fructose 2,6-bisphosphate binding
Regioni767 – 7693Allosteric activator fructose 2,6-bisphosphate binding
Regioni859 – 8624Allosteric activator fructose 2,6-bisphosphate binding

Sequence similaritiesi

Belongs to the phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Eukaryotic two domain clade "E" sub-subfamily.UniRule annotation

Phylogenomic databases

eggNOGiCOG0205.
GeneTreeiENSGT00390000013209.
HOGENOMiHOG000200154.
InParanoidiP16861.
KOiK00850.
OMAiSAKAMQW.
OrthoDBiEOG7Q5HPV.

Family and domain databases

HAMAPiMF_03184. Phosphofructokinase_I_E.
InterProiIPR009161. 6-phosphofructokinase_euk.
IPR022953. Phosphofructokinase.
IPR015912. Phosphofructokinase_CS.
IPR000023. Phosphofructokinase_dom.
[Graphical view]
PfamiPF00365. PFK. 2 hits.
[Graphical view]
PIRSFiPIRSF000533. ATP_PFK_euk. 1 hit.
PRINTSiPR00476. PHFRCTKINASE.
SUPFAMiSSF53784. SSF53784. 3 hits.
TIGRFAMsiTIGR02478. 6PF1K_euk. 1 hit.
PROSITEiPS00433. PHOSPHOFRUCTOKINASE. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P16861 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MQSQDSCYGV AFRSIITNDE ALFKKTIHFY HTLGFATVKD FNKFKHGENS
60 70 80 90 100
LLSSGTSQDS LREVWLESFK LSEVDASGFR IPQQEATNKA QSQGALLKIR
110 120 130 140 150
LVMSAPIDET FDTNETATIT YFSTDLNKIV EKFPKQAEKL SDTLVFLKDP
160 170 180 190 200
MGNNITFSGL ANATDSAPTS KDAFLEATSE DEIISRASSD ASDLLRQTLG
210 220 230 240 250
SSQKKKKIAV MTSGGDSPGM NAAVRAVVRT GIHFGCDVFA VYEGYEGLLR
260 270 280 290 300
GGKYLKKMAW EDVRGWLSEG GTLIGTARSM EFRKREGRRQ AAGNLISQGI
310 320 330 340 350
DALVVCGGDG SLTGADLFRH EWPSLVDELV AEGRFTKEEV APYKNLSIVG
360 370 380 390 400
LVGSIDNDMS GTDSTIGAYS ALERICEMVD YIDATAKSHS RAFVVEVMGR
410 420 430 440 450
HCGWLALMAG IATGADYIFI PERAVPHGKW QDELKEVCQR HRSKGRRNNT
460 470 480 490 500
IIVAEGALDD QLNPVTANDV KDALIELGLD TKVTILGHVQ RGGTAVAHDR
510 520 530 540 550
WLATLQGVDA VKAVLEFTPE TPSPLIGILE NKIIRMPLVE SVKLTKSVAT
560 570 580 590 600
AIENKDFDKA ISLRDTEFIE LYENFLSTTV KDDGSELLPV SDRLNIGIVH
610 620 630 640 650
VGAPSAALNA ATRAATLYCL SHGHKPYAIM NGFSGLIQTG EVKELSWIDV
660 670 680 690 700
ENWHNLGGSE IGTNRSVASE DLGTIAYYFQ KNKLDGLIIL GGFEGFRSLK
710 720 730 740 750
QLRDGRTQHP IFNIPMCLIP ATVSNNVPGT EYSLGVDTCL NALVNYTDDI
760 770 780 790 800
KQSASATRRR VFVCEVQGGH SGYIASFTGL ITGAVSVYTP EKKIDLASIR
810 820 830 840 850
EDITLLKENF RHDKGENRNG KLLVRNEQAS SVYSTQLLAD IISEASKGKF
860 870 880 890 900
GVRTAIPGHV QQGGVPSSKD RVTASRFAVK CIKFIEQWNK KNEASPNTDA
910 920 930 940 950
KVLRFKFDTH GEKVPTVEHE DDSAAVICVN GSHVSFKPIA NLWENETNVE
960 970 980
LRKGFEVHWA EYNKIGDILS GRLKLRAEVA ALAAENK
Length:987
Mass (Da):107,970
Last modified:August 1, 1990 - v1
Checksum:i995B3DF7C7781B29
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M26943 Genomic DNA. Translation: AAA34859.1.
Z73025 Genomic DNA. Translation: CAA97268.1.
X87941 Genomic DNA. Translation: CAA61193.1.
BK006941 Genomic DNA. Translation: DAA08331.1.
PIRiJQ0016.
RefSeqiNP_011756.1. NM_001181369.1.

Genome annotation databases

EnsemblFungiiYGR240C; YGR240C; YGR240C.
GeneIDi853155.
KEGGisce:YGR240C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M26943 Genomic DNA. Translation: AAA34859.1 .
Z73025 Genomic DNA. Translation: CAA97268.1 .
X87941 Genomic DNA. Translation: CAA61193.1 .
BK006941 Genomic DNA. Translation: DAA08331.1 .
PIRi JQ0016.
RefSeqi NP_011756.1. NM_001181369.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3O8O X-ray 2.90 A/C/E/G 201-987 [» ]
ProteinModelPortali P16861.
SMRi P16861. Positions 10-980.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 33492. 224 interactions.
DIPi DIP-1505N.
IntActi P16861. 44 interactions.
MINTi MINT-393741.
STRINGi 4932.YGR240C.

Proteomic databases

MaxQBi P16861.
PaxDbi P16861.
PeptideAtlasi P16861.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YGR240C ; YGR240C ; YGR240C .
GeneIDi 853155.
KEGGi sce:YGR240C.

Organism-specific databases

CYGDi YGR240c.
SGDi S000003472. PFK1.

Phylogenomic databases

eggNOGi COG0205.
GeneTreei ENSGT00390000013209.
HOGENOMi HOG000200154.
InParanoidi P16861.
KOi K00850.
OMAi SAKAMQW.
OrthoDBi EOG7Q5HPV.

Enzyme and pathway databases

UniPathwayi UPA00109 ; UER00182 .
BioCyci YEAST:YGR240C-MONOMER.
SABIO-RK P16861.

Miscellaneous databases

NextBioi 973249.

Gene expression databases

Genevestigatori P16861.

Family and domain databases

HAMAPi MF_03184. Phosphofructokinase_I_E.
InterProi IPR009161. 6-phosphofructokinase_euk.
IPR022953. Phosphofructokinase.
IPR015912. Phosphofructokinase_CS.
IPR000023. Phosphofructokinase_dom.
[Graphical view ]
Pfami PF00365. PFK. 2 hits.
[Graphical view ]
PIRSFi PIRSF000533. ATP_PFK_euk. 1 hit.
PRINTSi PR00476. PHFRCTKINASE.
SUPFAMi SSF53784. SSF53784. 3 hits.
TIGRFAMsi TIGR02478. 6PF1K_euk. 1 hit.
PROSITEi PS00433. PHOSPHOFRUCTOKINASE. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. 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. 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.

Entry informationi

Entry nameiPFKA1_YEAST
AccessioniPrimary (citable) accession number: P16861
Secondary accession number(s): D6VV20
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: October 29, 2014
This is version 138 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 89800 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

External Data

Dasty 3