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O42938 (PFKA_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ATP-dependent 6-phosphofructokinase

Short name=ATP-PFK
Short name=Phosphofructokinase
EC=2.7.1.11
Alternative name(s):
Phosphohexokinase
Gene names
Name:pfk1
ORF Names:SPBC16H5.02
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length942 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. May also have a role in cell cycle regulation. Ref.4 Ref.5

Catalytic activity

ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate. Ref.4

Cofactor

Magnesium By similarity. HAMAP-Rule MF_03184

Enzyme regulation

Allosterically activated by ADP, AMP, or fructose 2,6-bisphosphate, and allosterically inhibited by ATP or citrate. Ref.4

Pathway

Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4. HAMAP-Rule MF_03184

Subunit structure

Homooctamer. Ref.4

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_03184.

Post-translational modification

The N-terminus is blocked. HAMAP-Rule MF_03184

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=0.025 mM for ATP (without effector) Ref.4

KM=0.027 mM for ATP (with 2.6 µM fructose 2,6-bisphosphate)

KM=0.63 mM for fructose 6-phosphate (without effector)

KM=0.31 mM for fructose 6-phosphate (with 1 mM AMP)

KM=0.17 mM for fructose 6-phosphate (with 2.6 µM fructose 2,6-bisphosphate)

Sequence caution

The sequence BAA13773.1 differs from that shown. Reason: Frameshift at position 836.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 942942ATP-dependent 6-phosphofructokinase HAMAP-Rule MF_03184
PRO_0000112043

Regions

Nucleotide binding267 – 2682ATP By similarity
Nucleotide binding297 – 3004ATP By similarity
Region1 – 570570N-terminal catalytic PFK domain 1 HAMAP-Rule MF_03184
Region343 – 3453Substrate binding By similarity
Region387 – 3893Substrate binding By similarity
Region478 – 4814Substrate binding By similarity
Region571 – 58414Interdomain linker HAMAP-Rule MF_03184
Region585 – 942358C-terminal regulatory PFK domain 2 HAMAP-Rule MF_03184
Region712 – 7165Allosteric activator fructose 2,6-bisphosphate binding By similarity
Region757 – 7593Allosteric activator fructose 2,6-bisphosphate binding By similarity
Region849 – 8524Allosteric activator fructose 2,6-bisphosphate binding By similarity

Sites

Active site3451Proton acceptor By similarity
Metal binding2981Magnesium; catalytic By similarity
Binding site2041ATP; via amide nitrogen By similarity
Binding site3801Substrate; shared with dimeric partner By similarity
Binding site4441Substrate By similarity
Binding site4721Substrate; shared with dimeric partner By similarity
Binding site6551Allosteric activator fructose 2,6-bisphosphate By similarity
Binding site7501Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partner By similarity
Binding site8171Allosteric activator fructose 2,6-bisphosphate By similarity
Binding site8431Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partner By similarity
Binding site9181Allosteric activator fructose 2,6-bisphosphate By similarity

Amino acid modifications

Modified residue431Phosphoserine Ref.7
Modified residue451Phosphoserine Ref.7
Modified residue851Phosphoserine Ref.7
Modified residue1601Phosphoserine Ref.7
Modified residue1631Phosphoserine Ref.7
Modified residue1671Phosphoserine Ref.7
Modified residue1711Phosphoserine Ref.7
Modified residue1751Phosphothreonine Ref.7
Modified residue6001Phosphoserine Ref.7
Modified residue6021Phosphothreonine Ref.7

Sequences

Sequence LengthMass (Da)Tools
O42938 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: C6052AF7C1DB75B4

FASTA942102,555
        10         20         30         40         50         60 
MSGETVHGIS CYSVVANTED TYNQTLDFYQ KLGFKKVASF GTSDSDNARV CNESLREDWM 

        70         80         90        100        110        120 
HVAGNNSAES VTIKFRLVPG ELSLSPAAED SEWRGQKSSL VFYYPNLLDL LKQLSADAIK 

       130        140        150        160        170        180 
YQAFPNEKKP DEVYVEDPLG NLIGFSDRYN PFAHANLKKS EESGAASNLE SGLATPVVET 

       190        200        210        220        230        240 
LKKATTSDKP AGVKKKIAVM TSGGDSPGMN AVVRAVARIA IHRGCDAFAI YEGYEGLVQG 

       250        260        270        280        290        300 
GDMIKQLQWG DVRGWLAEGG TLIGTARCMA FRERPGRLRA AKNLISAGID SIIVCGGDGS 

       310        320        330        340        350        360 
LTGADIFRSD WPGLVKELED TKAITPEQAK LYRHLTIVGL VGSIDNDMSS TDVTIGAFSS 

       370        380        390        400        410        420 
LHRICEAVDS ISSTAISHSR AFIVEVMGRH CGWLAVLAAL ATGADFVFIP ERPAEVGKWQ 

       430        440        450        460        470        480 
DELCNSLSSV RKLGKRKSIV IVAEGAIDSE LNHISPEDIK NLLVERLHLD TRVTTLGHVQ 

       490        500        510        520        530        540 
RGGIPCAYDR MLATLQGVDA VDAVLASTPD TPSPMIAING NKINRKPLME AVKLTHEVAD 

       550        560        570        580        590        600 
AIEKKQFAHA MELRDPEFAD YLHTWEGTTF IEDESHFVPK DERMRVAIIH VGAPAGGMNS 

       610        620        630        640        650        660 
ATRAAVRYCL NRGHTPLAID NGFSGFLRHD SIHELSWIDV DEWCIRGGSE IGTNRDTPDL 

       670        680        690        700        710        720 
DMGFTAFKFQ QHKIDALIII GGFEAFTALS QLESARVNYP SFRIPMAIIP ATISNNVPGT 

       730        740        750        760        770        780 
EFSLGCDTCL NAVMEYCDTI KQSASASRRR VFVCEVQGGR SGYIATVGGL ITGASAIYTP 

       790        800        810        820        830        840 
EDGISLDMLR KDIDHLKATF ALEAGRNRAG QLILRNECAS KVYTTEVIGN IISEEAHKRF 

       850        860        870        880        890        900 
SARTAVPGHV QQGGNPTPMD RARAARLAMR AIRFFETCRA NDLGNDPSSA VVIGIRGTGV 

       910        920        930        940 
SFSSVADVEN NETEIEMRRP KNAWWRDMHN LVNILAGKTF AD 

« Hide

References

« Hide 'large scale' references
[1]"Analysis of 114 kb of DNA sequence from fission yeast chromosome 2 immediately centromere-distal to his5."
Xiang Z., Moore K., Wood V., Rajandream M.A., Barrell B.G., Skelton J., Churcher C.M., Lyne M.H., Devlin K., Gwilliam R., Rutherford K.M., Aves S.J.
Yeast 16:1405-1411(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
[3]"Identification of open reading frames in Schizosaccharomyces pombe cDNAs."
Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.
DNA Res. 4:363-369(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 583-942.
Strain: PR745.
[4]"Purification, molecular and kinetic characterization of phosphofructokinase-1 from the yeast Schizosaccharomyces pombe: evidence for an unusual subunit composition."
Reuter R., Naumann M., Baer J., Haferburg D., Kopperschlaeger G.
Yeast 16:1273-1285(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 182-190 AND 552-558, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBUNIT.
Strain: CBS 1057.
[5]"Genome-wide search of Schizosaccharomyces pombe genes causing overexpression-mediated cell cycle defects."
Tallada V.A., Daga R.R., Palomeque C., Garzon A., Jimenez J.
Yeast 19:1139-1151(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CELL CYCLE REGULATION.
[6]"Structures of S. pombe phosphofructokinase in the F6P-bound and ATP-bound states."
Benjamin S., Radermacher M., Baer J., Edelmann A., Ruiz T.
J. Struct. Biol. 159:498-506(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY ELECTRON MICROSCOPY.
[7]"Phosphoproteome analysis of fission yeast."
Wilson-Grady J.T., Villen J., Gygi S.P.
J. Proteome Res. 7:1088-1097(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43; SER-45; SER-85; SER-160; SER-163; SER-167; SER-171; THR-175; SER-600 AND THR-602, IDENTIFICATION BY MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU329671 Genomic DNA. Translation: CAA17900.1.
D89110 mRNA. Translation: BAA13773.1. Frameshift.
PIRT39624.
T42087.
RefSeqNP_595946.1. NM_001021854.2.

3D structure databases

ProteinModelPortalO42938.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid276516. 6 interactions.
MINTMINT-4674145.
STRING4896.SPBC16H5.02-1.

Proteomic databases

MaxQBO42938.
PaxDbO42938.
PRIDEO42938.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPBC16H5.02.1; SPBC16H5.02.1:pep; SPBC16H5.02.
GeneID2539972.
KEGGspo:SPBC16H5.02.

Organism-specific databases

PomBaseSPBC16H5.02.

Phylogenomic databases

eggNOGCOG0205.
HOGENOMHOG000200154.
KOK00850.
OMAVYHMASK.
OrthoDBEOG7Q5HPV.
PhylomeDBO42938.

Enzyme and pathway databases

SABIO-RKO42938.
UniPathwayUPA00109; UER00182.

Family and domain databases

Gene3D3.10.180.10. 1 hit.
HAMAPMF_03184. Phosphofructokinase_I_E.
InterProIPR009161. 6-phosphofructokinase_euk.
IPR029068. Glyas_Bleomycin-R_OHBP_Dase.
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. 2 hits.
SSF54593. SSF54593. 1 hit.
TIGRFAMsTIGR02478. 6PF1K_euk. 1 hit.
PROSITEPS00433. PHOSPHOFRUCTOKINASE. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio20801115.

Entry information

Entry namePFKA_SCHPO
AccessionPrimary (citable) accession number: O42938
Secondary accession number(s): P78762
Entry history
Integrated into UniProtKB/Swiss-Prot: May 16, 2003
Last sequence update: June 1, 1998
Last modified: July 9, 2014
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways