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P16861 (PFKA1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length987 AA.
Sequence statusComplete.
Protein existenceEvidence 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)

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PFK2P168624EBI-9428,EBI-9435

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 987987ATP-dependent 6-phosphofructokinase subunit alpha HAMAP-Rule MF_03184
PRO_0000112045

Regions

Nucleotide binding278 – 2792ATP By similarity
Nucleotide binding308 – 3114ATP By similarity
Region1 – 580580N-terminal catalytic PFK domain 1 HAMAP-Rule MF_03184
Region354 – 3563Substrate binding HAMAP-Rule MF_03184
Region398 – 4003Substrate binding HAMAP-Rule MF_03184
Region488 – 4914Substrate binding HAMAP-Rule MF_03184
Region581 – 59414Interdomain linker HAMAP-Rule MF_03184
Region595 – 987393C-terminal regulatory PFK domain 2 HAMAP-Rule MF_03184
Region722 – 7265Allosteric activator fructose 2,6-bisphosphate binding HAMAP-Rule MF_03184
Region767 – 7693Allosteric activator fructose 2,6-bisphosphate binding HAMAP-Rule MF_03184
Region859 – 8624Allosteric activator fructose 2,6-bisphosphate binding HAMAP-Rule MF_03184

Sites

Active site3561Proton acceptor
Metal binding3091Magnesium; catalytic
Binding site2151ATP; via amide nitrogen By similarity
Binding site3911Substrate; shared with subunit beta
Binding site4551Substrate
Binding site4821Substrate; shared with subunit beta
Binding site6651Allosteric activator fructose 2,6-bisphosphate
Binding site7601Allosteric activator fructose 2,6-bisphosphate; shared with subunit beta
Binding site8271Allosteric activator fructose 2,6-bisphosphate
Binding site8531Allosteric activator fructose 2,6-bisphosphate; shared with subunit beta
Binding site9521Allosteric activator fructose 2,6-bisphosphate

Amino acid modifications

Modified residue31Phosphoserine Ref.24
Modified residue1661Phosphoserine Ref.25
Modified residue1791Phosphoserine Ref.22 Ref.25
Modified residue1851Phosphoserine Ref.22 Ref.24 Ref.25
Modified residue1891Phosphoserine Ref.25
Modified residue1921Phosphoserine Ref.22 Ref.24 Ref.25
Modified residue2171Phosphoserine Ref.25
Modified residue4501Phosphothreonine Ref.25

Experimental info

Mutagenesis3091D → T: Reduces maximal activity of the holoenzyme by 50%. Completely abolishes catalytic activity; when associated with 'S-348' in subunit beta. Ref.16
Mutagenesis3561D → S: Reduces maximal activity of the holoenzyme by 50%. Completely abolishes catalytic activity; when associated with 'S-348' in subunit beta. Ref.16
Mutagenesis4471R → S: Reduces maximal activity of the holoenzyme by less than 25%. Ref.16
Mutagenesis4881H → S: Increases the KM for fructose 6-phosphate 20 fold. Ref.16
Mutagenesis7241S → D: Abolishes sensitivity of the holoenzyme to fructose 2,6-bisphosphate activation; when associated with 'D-718' in subunit beta. Ref.17
Mutagenesis7281P → L: Drastically reduces sensitivity of the holoenzyme to ATP inhibition. Ref.18
Mutagenesis8591H → S: Reduces sensitivity of the holoenzyme to fructose 2,6-bisphosphate activation; when associated with 'S-853' in subunit beta. Ref.17

Secondary structure

........................................................................................................................... 987
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P16861 [UniParc].

Last modified August 1, 1990. Version 1.
Checksum: 995B3DF7C7781B29

FASTA987107,970
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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.
PIRJQ0016.
RefSeqNP_011756.1. NM_001181369.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3O8OX-ray2.90A/C/E/G201-987[»]
ProteinModelPortalP16861.
SMRP16861. Positions 10-980.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid33492. 223 interactions.
DIPDIP-1505N.
IntActP16861. 44 interactions.
MINTMINT-393741.
STRING4932.YGR240C.

Proteomic databases

MaxQBP16861.
PaxDbP16861.
PeptideAtlasP16861.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYGR240C; YGR240C; YGR240C.
GeneID853155.
KEGGsce:YGR240C.

Organism-specific databases

CYGDYGR240c.
SGDS000003472. PFK1.

Phylogenomic databases

eggNOGCOG0205.
GeneTreeENSGT00390000013209.
HOGENOMHOG000200154.
KOK00850.
OMASAKAMQW.
OrthoDBEOG7Q5HPV.

Enzyme and pathway databases

BioCycYEAST:YGR240C-MONOMER.
SABIO-RKP16861.
UniPathwayUPA00109; UER00182.

Gene expression databases

GenevestigatorP16861.

Family and domain databases

HAMAPMF_03184. Phosphofructokinase_I_E.
InterProIPR009161. 6-phosphofructokinase_euk.
IPR022953. Phosphofructokinase.
IPR015912. Phosphofructokinase_CS.
IPR000023. Phosphofructokinase_dom.
[Graphical view]
PfamPF00365. PFK. 2 hits.
[Graphical view]
PIRSFPIRSF000533. ATP_PFK_euk. 1 hit.
PRINTSPR00476. PHFRCTKINASE.
SUPFAMSSF53784. SSF53784. 3 hits.
TIGRFAMsTIGR02478. 6PF1K_euk. 1 hit.
PROSITEPS00433. PHOSPHOFRUCTOKINASE. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio973249.

Entry information

Entry namePFKA1_YEAST
AccessionPrimary (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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome VII

Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways