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Protein

ATP-dependent 6-phosphofructokinase

Gene

pfk1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission 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. May also have a role in cell cycle regulation.UniRule annotation2 Publications

Catalytic activityi

ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate.UniRule annotation1 Publication

Cofactori

Mg2+UniRule annotation

Enzyme regulationi

Allosterically activated by ADP, AMP, or fructose 2,6-bisphosphate, and allosterically inhibited by ATP or citrate.UniRule annotation1 Publication

Kineticsi

  1. KM=0.025 mM for ATP (without effector)1 Publication
  2. KM=0.027 mM for ATP (with 2.6 µM fructose 2,6-bisphosphate)1 Publication
  3. KM=0.63 mM for fructose 6-phosphate (without effector)1 Publication
  4. KM=0.31 mM for fructose 6-phosphate (with 1 mM AMP)1 Publication
  5. KM=0.17 mM for fructose 6-phosphate (with 2.6 µM fructose 2,6-bisphosphate)1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei204 – 2041ATP; via amide nitrogenUniRule annotation
Metal bindingi298 – 2981Magnesium; catalyticUniRule annotation
Active sitei345 – 3451Proton acceptorUniRule annotation
Binding sitei380 – 3801Substrate; shared with dimeric partnerUniRule annotation
Binding sitei444 – 4441SubstrateUniRule annotation
Binding sitei472 – 4721Substrate; shared with dimeric partnerUniRule annotation
Binding sitei655 – 6551Allosteric activator fructose 2,6-bisphosphateUniRule annotation
Binding sitei750 – 7501Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partnerUniRule annotation
Binding sitei817 – 8171Allosteric activator fructose 2,6-bisphosphateUniRule annotation
Binding sitei843 – 8431Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partnerUniRule annotation
Binding sitei918 – 9181Allosteric activator fructose 2,6-bisphosphateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi267 – 2682ATPUniRule annotation
Nucleotide bindingi297 – 3004ATPUniRule annotation

GO - Molecular functioni

  1. 6-phosphofructokinase activity Source: PomBase
  2. ATP binding Source: PomBase
  3. fructose-6-phosphate binding Source: PomBase
  4. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. canonical glycolysis Source: PomBase
  2. carbohydrate phosphorylation Source: GOC
  3. fructose 1,6-bisphosphate metabolic process Source: PomBase
  4. fructose 6-phosphate metabolic process Source: PomBase
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

ReactomeiREACT_304275. Glycolysis.
SABIO-RKO42938.
UniPathwayiUPA00109; UER00182.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent 6-phosphofructokinaseUniRule annotation (EC:2.7.1.11UniRule annotation)
Short name:
ATP-PFKUniRule annotation
Short name:
PhosphofructokinaseUniRule annotation
Alternative name(s):
PhosphohexokinaseUniRule annotation
Gene namesi
Name:pfk1
ORF Names:SPBC16H5.02
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC16H5.02.
PomBaseiSPBC16H5.02.

Subcellular locationi

  1. Cytoplasm UniRule annotation

GO - Cellular componenti

  1. 6-phosphofructokinase complex Source: PomBase
  2. cytoplasm Source: PomBase
  3. cytosol Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 942942ATP-dependent 6-phosphofructokinasePRO_0000112043Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei43 – 431Phosphoserine1 Publication
Modified residuei45 – 451Phosphoserine1 Publication
Modified residuei85 – 851Phosphoserine1 Publication
Modified residuei160 – 1601Phosphoserine1 Publication
Modified residuei163 – 1631Phosphoserine1 Publication
Modified residuei167 – 1671Phosphoserine1 Publication
Modified residuei171 – 1711Phosphoserine1 Publication
Modified residuei175 – 1751Phosphothreonine1 Publication
Modified residuei600 – 6001Phosphoserine1 Publication
Modified residuei602 – 6021Phosphothreonine1 Publication

Post-translational modificationi

The N-terminus is blocked.

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO42938.
PaxDbiO42938.
PRIDEiO42938.

Interactioni

Subunit structurei

Homooctamer.1 Publication

Protein-protein interaction databases

BioGridi276516. 5 interactions.
MINTiMINT-4674145.
STRINGi4896.SPBC16H5.02-1.

Structurei

3D structure databases

ProteinModelPortaliO42938.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 570570N-terminal catalytic PFK domain 1Add
BLAST
Regioni343 – 3453Substrate bindingUniRule annotation
Regioni387 – 3893Substrate bindingUniRule annotation
Regioni478 – 4814Substrate bindingUniRule annotation
Regioni571 – 58414Interdomain linkerAdd
BLAST
Regioni585 – 942358C-terminal regulatory PFK domain 2Add
BLAST
Regioni712 – 7165Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation
Regioni757 – 7593Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation
Regioni849 – 8524Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation

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.
HOGENOMiHOG000200154.
InParanoidiO42938.
KOiK00850.
OMAiVYHMASK.
OrthoDBiEOG7Q5HPV.
PhylomeDBiO42938.

Family and domain databases

Gene3Di3.10.180.10. 1 hit.
HAMAPiMF_03184. Phosphofructokinase_I_E.
InterProiIPR009161. 6-Pfructokinase_euk.
IPR022953. ATP_PFK.
IPR029068. Glyas_Bleomycin-R_OHBP_Dase.
IPR015912. Phosphofructokinase_CS.
IPR000023. Phosphofructokinase_dom.
[Graphical view]
PfamiPF00365. PFK. 2 hits.
[Graphical view]
PIRSFiPIRSF000533. ATP_PFK_euk. 1 hit.
PRINTSiPR00476. PHFRCTKINASE.
SUPFAMiSSF53784. SSF53784. 2 hits.
SSF54593. SSF54593. 1 hit.
TIGRFAMsiTIGR02478. 6PF1K_euk. 1 hit.
PROSITEiPS00433. PHOSPHOFRUCTOKINASE. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O42938-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGETVHGIS CYSVVANTED TYNQTLDFYQ KLGFKKVASF GTSDSDNARV
60 70 80 90 100
CNESLREDWM HVAGNNSAES VTIKFRLVPG ELSLSPAAED SEWRGQKSSL
110 120 130 140 150
VFYYPNLLDL LKQLSADAIK YQAFPNEKKP DEVYVEDPLG NLIGFSDRYN
160 170 180 190 200
PFAHANLKKS EESGAASNLE SGLATPVVET LKKATTSDKP AGVKKKIAVM
210 220 230 240 250
TSGGDSPGMN AVVRAVARIA IHRGCDAFAI YEGYEGLVQG GDMIKQLQWG
260 270 280 290 300
DVRGWLAEGG TLIGTARCMA FRERPGRLRA AKNLISAGID SIIVCGGDGS
310 320 330 340 350
LTGADIFRSD WPGLVKELED TKAITPEQAK LYRHLTIVGL VGSIDNDMSS
360 370 380 390 400
TDVTIGAFSS LHRICEAVDS ISSTAISHSR AFIVEVMGRH CGWLAVLAAL
410 420 430 440 450
ATGADFVFIP ERPAEVGKWQ DELCNSLSSV RKLGKRKSIV IVAEGAIDSE
460 470 480 490 500
LNHISPEDIK NLLVERLHLD TRVTTLGHVQ RGGIPCAYDR MLATLQGVDA
510 520 530 540 550
VDAVLASTPD TPSPMIAING NKINRKPLME AVKLTHEVAD AIEKKQFAHA
560 570 580 590 600
MELRDPEFAD YLHTWEGTTF IEDESHFVPK DERMRVAIIH VGAPAGGMNS
610 620 630 640 650
ATRAAVRYCL NRGHTPLAID NGFSGFLRHD SIHELSWIDV DEWCIRGGSE
660 670 680 690 700
IGTNRDTPDL DMGFTAFKFQ QHKIDALIII GGFEAFTALS QLESARVNYP
710 720 730 740 750
SFRIPMAIIP ATISNNVPGT EFSLGCDTCL NAVMEYCDTI KQSASASRRR
760 770 780 790 800
VFVCEVQGGR SGYIATVGGL ITGASAIYTP EDGISLDMLR KDIDHLKATF
810 820 830 840 850
ALEAGRNRAG QLILRNECAS KVYTTEVIGN IISEEAHKRF SARTAVPGHV
860 870 880 890 900
QQGGNPTPMD RARAARLAMR AIRFFETCRA NDLGNDPSSA VVIGIRGTGV
910 920 930 940
SFSSVADVEN NETEIEMRRP KNAWWRDMHN LVNILAGKTF AD
Length:942
Mass (Da):102,555
Last modified:June 1, 1998 - v1
Checksum:iC6052AF7C1DB75B4
GO

Sequence cautioni

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAA17900.1.
D89110 mRNA. Translation: BAA13773.1. Frameshift.
PIRiT39624.
T42087.
RefSeqiNP_595946.1. NM_001021854.2.

Genome annotation databases

EnsemblFungiiSPBC16H5.02.1; SPBC16H5.02.1:pep; SPBC16H5.02.
GeneIDi2539972.
KEGGispo:SPBC16H5.02.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAA17900.1.
D89110 mRNA. Translation: BAA13773.1. Frameshift.
PIRiT39624.
T42087.
RefSeqiNP_595946.1. NM_001021854.2.

3D structure databases

ProteinModelPortaliO42938.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi276516. 5 interactions.
MINTiMINT-4674145.
STRINGi4896.SPBC16H5.02-1.

Proteomic databases

MaxQBiO42938.
PaxDbiO42938.
PRIDEiO42938.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC16H5.02.1; SPBC16H5.02.1:pep; SPBC16H5.02.
GeneIDi2539972.
KEGGispo:SPBC16H5.02.

Organism-specific databases

EuPathDBiFungiDB:SPBC16H5.02.
PomBaseiSPBC16H5.02.

Phylogenomic databases

eggNOGiCOG0205.
HOGENOMiHOG000200154.
InParanoidiO42938.
KOiK00850.
OMAiVYHMASK.
OrthoDBiEOG7Q5HPV.
PhylomeDBiO42938.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00182.
ReactomeiREACT_304275. Glycolysis.
SABIO-RKO42938.

Miscellaneous databases

NextBioi20801115.
PROiO42938.

Family and domain databases

Gene3Di3.10.180.10. 1 hit.
HAMAPiMF_03184. Phosphofructokinase_I_E.
InterProiIPR009161. 6-Pfructokinase_euk.
IPR022953. ATP_PFK.
IPR029068. Glyas_Bleomycin-R_OHBP_Dase.
IPR015912. Phosphofructokinase_CS.
IPR000023. Phosphofructokinase_dom.
[Graphical view]
PfamiPF00365. PFK. 2 hits.
[Graphical view]
PIRSFiPIRSF000533. ATP_PFK_euk. 1 hit.
PRINTSiPR00476. PHFRCTKINASE.
SUPFAMiSSF53784. SSF53784. 2 hits.
SSF54593. SSF54593. 1 hit.
TIGRFAMsiTIGR02478. 6PF1K_euk. 1 hit.
PROSITEiPS00433. PHOSPHOFRUCTOKINASE. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.

Entry informationi

Entry nameiPFKA_SCHPO
AccessioniPrimary (citable) accession number: O42938
Secondary accession number(s): P78762
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2003
Last sequence update: June 1, 1998
Last modified: April 29, 2015
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

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.