Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P16861 - PFKA1_YEAST

UniProt

P16861 - PFKA1_YEAST

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

ATP-dependent 6-phosphofructokinase subunit alpha

Gene

PFK1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: 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

Mg2+

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

Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4.

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.
ReactomeiREACT_229625. Glycolysis.
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 lineageiEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›
ProteomesiUP000002311: Chromosome VII

Organism-specific databases

CYGDiYGR240c.
SGDiS000003472. PFK1.

Subcellular locationi

Cytoplasm. Mitochondrion outer membrane; Peripheral membrane protein; Cytoplasmic side

GO - Cellular componenti

  1. 6-phosphofructokinase complex Source: SGD
  2. mitochondrial outer membrane Source: UniProtKB-SubCell
  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 – 2159Combined sources
Helixi220 – 23314Combined sources
Beta strandi237 – 2415Combined sources
Helixi244 – 2507Combined sources
Beta strandi254 – 2574Combined sources
Helixi260 – 2634Combined sources
Helixi266 – 2683Combined sources
Helixi281 – 2833Combined sources
Helixi285 – 29713Combined sources
Beta strandi300 – 3078Combined sources
Helixi309 – 31911Combined sources
Helixi322 – 3309Combined sources
Beta strandi331 – 3344Combined sources
Turni337 – 3437Combined sources
Beta strandi347 – 35610Combined sources
Helixi368 – 38821Combined sources
Beta strandi392 – 3976Combined sources
Helixi404 – 4129Combined sources
Beta strandi416 – 4194Combined sources
Helixi421 – 4233Combined sources
Turni427 – 4293Combined sources
Helixi430 – 44314Combined sources
Beta strandi449 – 4546Combined sources
Helixi467 – 47711Combined sources
Beta strandi481 – 4855Combined sources
Helixi487 – 4904Combined sources
Helixi497 – 51519Combined sources
Beta strandi524 – 53714Combined sources
Helixi538 – 55316Combined sources
Helixi557 – 5626Combined sources
Helixi568 – 57912Combined sources
Beta strandi595 – 6039Combined sources
Helixi608 – 62215Combined sources
Beta strandi625 – 6295Combined sources
Helixi632 – 6398Combined sources
Beta strandi642 – 6443Combined sources
Turni647 – 6526Combined sources
Helixi653 – 6553Combined sources
Helixi668 – 6703Combined sources
Helixi672 – 68110Combined sources
Beta strandi685 – 6928Combined sources
Helixi693 – 70513Combined sources
Turni706 – 7083Combined sources
Helixi710 – 7134Combined sources
Beta strandi716 – 7216Combined sources
Helixi736 – 75722Combined sources
Beta strandi758 – 7669Combined sources
Helixi773 – 7808Combined sources
Turni781 – 7833Combined sources
Beta strandi785 – 7884Combined sources
Beta strandi790 – 7923Combined sources
Helixi796 – 81217Combined sources
Beta strandi821 – 8266Combined sources
Beta strandi831 – 8333Combined sources
Helixi835 – 84612Combined sources
Beta strandi849 – 8568Combined sources
Helixi858 – 8625Combined sources
Helixi868 – 89023Combined sources
Helixi921 – 9233Combined sources
Beta strandi924 – 9307Combined sources
Beta strandi933 – 9386Combined sources
Helixi939 – 9424Combined sources
Turni948 – 9514Combined sources
Beta strandi953 – 9553Combined sources
Helixi960 – 96910Combined sources
Helixi972 – 9787Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
OMAiKMCQKLS.
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.

P16861-1 [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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

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

Proteomic databases

MaxQBiP16861.
PaxDbiP16861.
PeptideAtlasiP16861.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CYGDiYGR240c.
SGDiS000003472. PFK1.

Phylogenomic databases

eggNOGiCOG0205.
GeneTreeiENSGT00390000013209.
HOGENOMiHOG000200154.
InParanoidiP16861.
KOiK00850.
OMAiKMCQKLS.
OrthoDBiEOG7Q5HPV.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00182.
BioCyciYEAST:YGR240C-MONOMER.
ReactomeiREACT_229625. Glycolysis.
SABIO-RKP16861.

Miscellaneous databases

NextBioi973249.

Gene expression databases

GenevestigatoriP16861.

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]
ProtoNetiSearch...

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.
+Additional computationally mapped references.

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: January 7, 2015
This is version 140 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.