PFKA_SCHPO
ID PFKA_SCHPO Reviewed; 942 AA.
AC O42938; P78762;
DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=ATP-dependent 6-phosphofructokinase {ECO:0000255|HAMAP-Rule:MF_03184};
DE Short=ATP-PFK {ECO:0000255|HAMAP-Rule:MF_03184};
DE Short=Phosphofructokinase {ECO:0000255|HAMAP-Rule:MF_03184};
DE EC=2.7.1.11 {ECO:0000255|HAMAP-Rule:MF_03184};
DE AltName: Full=Phosphohexokinase {ECO:0000255|HAMAP-Rule:MF_03184};
GN Name=pfk1; ORFNames=SPBC16H5.02;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11054821;
RX DOI=10.1002/1097-0061(200011)16:15<1405::aid-yea625>3.0.co;2-h;
RA Xiang Z., Moore K., Wood V., Rajandream M.A., Barrell B.G., Skelton J.,
RA Churcher C.M., Lyne M.H., Devlin K., Gwilliam R., Rutherford K.M.,
RA Aves S.J.;
RT "Analysis of 114 kb of DNA sequence from fission yeast chromosome 2
RT immediately centromere-distal to his5.";
RL Yeast 16:1405-1411(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 583-942.
RC STRAIN=PR745;
RX PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT "Identification of open reading frames in Schizosaccharomyces pombe
RT cDNAs.";
RL DNA Res. 4:363-369(1997).
RN [4]
RP PROTEIN SEQUENCE OF 182-190 AND 552-558, FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, AND SUBUNIT.
RC STRAIN=CBS 1057;
RX PubMed=11015725;
RX DOI=10.1002/1097-0061(200010)16:14<1273::aid-yea621>3.0.co;2-#;
RA Reuter R., Naumann M., Baer J., Haferburg D., Kopperschlaeger G.;
RT "Purification, molecular and kinetic characterization of
RT phosphofructokinase-1 from the yeast Schizosaccharomyces pombe: evidence
RT for an unusual subunit composition.";
RL Yeast 16:1273-1285(2000).
RN [5]
RP FUNCTION IN CELL CYCLE REGULATION.
RX PubMed=12237855; DOI=10.1002/yea.902;
RA Tallada V.A., Daga R.R., Palomeque C., Garzon A., Jimenez J.;
RT "Genome-wide search of Schizosaccharomyces pombe genes causing
RT overexpression-mediated cell cycle defects.";
RL Yeast 19:1139-1151(2002).
RN [6]
RP STRUCTURE BY ELECTRON MICROSCOPY.
RX PubMed=17643314; DOI=10.1016/j.jsb.2007.06.001;
RA Benjamin S., Radermacher M., Baer J., Edelmann A., Ruiz T.;
RT "Structures of S. pombe phosphofructokinase in the F6P-bound and ATP-bound
RT states.";
RL J. Struct. Biol. 159:498-506(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43; SER-45; SER-85; SER-160;
RP SER-163; SER-167; SER-171; THR-175; SER-600 AND THR-602, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate to
CC fructose 1,6-bisphosphate by ATP, the first committing step of
CC glycolysis. May also have a role in cell cycle regulation.
CC {ECO:0000255|HAMAP-Rule:MF_03184, ECO:0000269|PubMed:11015725,
CC ECO:0000269|PubMed:12237855}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-
CC bisphosphate + H(+); Xref=Rhea:RHEA:16109, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:32966, ChEBI:CHEBI:57634,
CC ChEBI:CHEBI:456216; EC=2.7.1.11; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03184, ECO:0000269|PubMed:11015725};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03184};
CC -!- ACTIVITY REGULATION: Allosterically activated by ADP, AMP, or fructose
CC 2,6-bisphosphate, and allosterically inhibited by ATP or citrate.
CC {ECO:0000255|HAMAP-Rule:MF_03184, ECO:0000269|PubMed:11015725}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.025 mM for ATP (without effector) {ECO:0000269|PubMed:11015725};
CC KM=0.027 mM for ATP (with 2.6 uM fructose 2,6-bisphosphate)
CC {ECO:0000269|PubMed:11015725};
CC KM=0.63 mM for fructose 6-phosphate (without effector)
CC {ECO:0000269|PubMed:11015725};
CC KM=0.31 mM for fructose 6-phosphate (with 1 mM AMP)
CC {ECO:0000269|PubMed:11015725};
CC KM=0.17 mM for fructose 6-phosphate (with 2.6 uM fructose 2,6-
CC bisphosphate) {ECO:0000269|PubMed:11015725};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 3/4.
CC {ECO:0000255|HAMAP-Rule:MF_03184}.
CC -!- SUBUNIT: Homooctamer. {ECO:0000269|PubMed:11015725}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03184}.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family.
CC ATP-dependent PFK group I subfamily. Eukaryotic two domain clade 'E'
CC sub-subfamily. {ECO:0000255|HAMAP-Rule:MF_03184}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA13773.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; CU329671; CAA17900.1; -; Genomic_DNA.
DR EMBL; D89110; BAA13773.1; ALT_FRAME; mRNA.
DR PIR; T39624; T39624.
DR PIR; T42087; T42087.
DR RefSeq; NP_595946.1; NM_001021854.2.
DR AlphaFoldDB; O42938; -.
DR SMR; O42938; -.
DR BioGRID; 276516; 9.
DR ComplexPortal; CPX-555; 6-phosphofructokinase complex.
DR STRING; 4896.SPBC16H5.02.1; -.
DR iPTMnet; O42938; -.
DR MaxQB; O42938; -.
DR PaxDb; O42938; -.
DR PRIDE; O42938; -.
DR EnsemblFungi; SPBC16H5.02.1; SPBC16H5.02.1:pep; SPBC16H5.02.
DR GeneID; 2539972; -.
DR KEGG; spo:SPBC16H5.02; -.
DR PomBase; SPBC16H5.02; pfk1.
DR VEuPathDB; FungiDB:SPBC16H5.02; -.
DR eggNOG; KOG2440; Eukaryota.
DR HOGENOM; CLU_011053_0_0_1; -.
DR InParanoid; O42938; -.
DR OMA; SRYAVKC; -.
DR PhylomeDB; O42938; -.
DR Reactome; R-SPO-6798695; Neutrophil degranulation.
DR Reactome; R-SPO-70171; Glycolysis.
DR SABIO-RK; O42938; -.
DR UniPathway; UPA00109; UER00182.
DR PRO; PR:O42938; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005945; C:6-phosphofructokinase complex; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0003872; F:6-phosphofructokinase activity; IDA:PomBase.
DR GO; GO:0016208; F:AMP binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IDA:PomBase.
DR GO; GO:0070095; F:fructose-6-phosphate binding; IDA:PomBase.
DR GO; GO:0042802; F:identical protein binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0048029; F:monosaccharide binding; IBA:GO_Central.
DR GO; GO:0061621; P:canonical glycolysis; IBA:GO_Central.
DR GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IDA:PomBase.
DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IDA:PomBase.
DR GO; GO:0006096; P:glycolytic process; IDA:ComplexPortal.
DR Gene3D; 3.10.180.10; -; 1.
DR Gene3D; 3.40.50.460; -; 2.
DR HAMAP; MF_03184; Phosphofructokinase_I_E; 1.
DR InterPro; IPR009161; 6-Pfructokinase_euk.
DR InterPro; IPR022953; ATP_PFK.
DR InterPro; IPR029068; Glyas_Bleomycin-R_OHBP_Dase.
DR InterPro; IPR040712; Pfk_N.
DR InterPro; IPR015912; Phosphofructokinase_CS.
DR InterPro; IPR000023; Phosphofructokinase_dom.
DR InterPro; IPR035966; PKF_sf.
DR Pfam; PF00365; PFK; 2.
DR Pfam; PF18468; Pfk_N; 1.
DR PIRSF; PIRSF000533; ATP_PFK_euk; 1.
DR PRINTS; PR00476; PHFRCTKINASE.
DR SUPFAM; SSF53784; SSF53784; 2.
DR SUPFAM; SSF54593; SSF54593; 1.
DR TIGRFAMs; TIGR02478; 6PF1K_euk; 1.
DR PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 2.
PE 1: Evidence at protein level;
KW Allosteric enzyme; ATP-binding; Cytoplasm; Direct protein sequencing;
KW Glycolysis; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..942
FT /note="ATP-dependent 6-phosphofructokinase"
FT /id="PRO_0000112043"
FT REGION 1..570
FT /note="N-terminal catalytic PFK domain 1"
FT REGION 571..584
FT /note="Interdomain linker"
FT REGION 585..942
FT /note="C-terminal regulatory PFK domain 2"
FT ACT_SITE 345
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 204
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 267..268
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 297..300
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 298
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 343..345
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 380
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 387..389
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 444
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 472
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 478..481
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 655
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /ligand_note="allosteric activator; ligand shared between
FT dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 712..716
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /ligand_note="allosteric activator; ligand shared between
FT dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 750
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /ligand_note="allosteric activator; ligand shared between
FT dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 757..759
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /ligand_note="allosteric activator; ligand shared between
FT dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 817
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /ligand_note="allosteric activator; ligand shared between
FT dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 843
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /ligand_note="allosteric activator; ligand shared between
FT dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 849..852
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /ligand_note="allosteric activator; ligand shared between
FT dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 918
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /ligand_note="allosteric activator; ligand shared between
FT dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT MOD_RES 43
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 163
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 167
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 171
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 175
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 600
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 602
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 942 AA; 102555 MW; C6052AF7C1DB75B4 CRC64;
MSGETVHGIS CYSVVANTED TYNQTLDFYQ KLGFKKVASF GTSDSDNARV CNESLREDWM
HVAGNNSAES VTIKFRLVPG ELSLSPAAED SEWRGQKSSL VFYYPNLLDL LKQLSADAIK
YQAFPNEKKP DEVYVEDPLG NLIGFSDRYN PFAHANLKKS EESGAASNLE SGLATPVVET
LKKATTSDKP AGVKKKIAVM TSGGDSPGMN AVVRAVARIA IHRGCDAFAI YEGYEGLVQG
GDMIKQLQWG DVRGWLAEGG TLIGTARCMA FRERPGRLRA AKNLISAGID SIIVCGGDGS
LTGADIFRSD WPGLVKELED TKAITPEQAK LYRHLTIVGL VGSIDNDMSS TDVTIGAFSS
LHRICEAVDS ISSTAISHSR AFIVEVMGRH CGWLAVLAAL ATGADFVFIP ERPAEVGKWQ
DELCNSLSSV RKLGKRKSIV IVAEGAIDSE LNHISPEDIK NLLVERLHLD TRVTTLGHVQ
RGGIPCAYDR MLATLQGVDA VDAVLASTPD TPSPMIAING NKINRKPLME AVKLTHEVAD
AIEKKQFAHA MELRDPEFAD YLHTWEGTTF IEDESHFVPK DERMRVAIIH VGAPAGGMNS
ATRAAVRYCL NRGHTPLAID NGFSGFLRHD SIHELSWIDV DEWCIRGGSE IGTNRDTPDL
DMGFTAFKFQ QHKIDALIII GGFEAFTALS QLESARVNYP SFRIPMAIIP ATISNNVPGT
EFSLGCDTCL NAVMEYCDTI KQSASASRRR VFVCEVQGGR SGYIATVGGL ITGASAIYTP
EDGISLDMLR KDIDHLKATF ALEAGRNRAG QLILRNECAS KVYTTEVIGN IISEEAHKRF
SARTAVPGHV QQGGNPTPMD RARAARLAMR AIRFFETCRA NDLGNDPSSA VVIGIRGTGV
SFSSVADVEN NETEIEMRRP KNAWWRDMHN LVNILAGKTF AD
