ID   PFKA_SCHMA              Reviewed;         781 AA.
AC   Q27778;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 105.
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=PFK;
OS   Schistosoma mansoni (Blood fluke).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX   NCBI_TaxID=6183;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND CATALYTIC ACTIVITY.
RX   PubMed=7984171; DOI=10.1016/0166-6851(94)90040-x;
RA   Ding J., Su J.G.J., Mansour T.E.;
RT   "Cloning and characterization of a cDNA encoding phosphofructokinase from
RT   Schistosoma mansoni.";
RL   Mol. Biochem. Parasitol. 66:105-110(1994).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY
RP   REGULATION.
RX   PubMed=8898332; DOI=10.1016/0166-6851(96)02702-8;
RA   Su J.G., Mansour J.M., Mansour T.E.;
RT   "Purification, kinetics and inhibition by antimonials of recombinant
RT   phosphofructokinase from Schistosoma mansoni.";
RL   Mol. Biochem. Parasitol. 81:171-178(1996).
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. {ECO:0000255|HAMAP-Rule:MF_03184,
CC       ECO:0000269|PubMed:8898332}.
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:7984171,
CC         ECO:0000269|PubMed:8898332};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-
CC         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:8898332}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=3.5 mM for ATP {ECO:0000269|PubMed:8898332};
CC         KM=0.8 mM for fructose 6-phosphate {ECO:0000269|PubMed:8898332};
CC       pH dependence:
CC         Optimum pH is 7.5-9.0. {ECO:0000269|PubMed:8898332};
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: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_03184}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03184}.
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}.
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DR   EMBL; L31531; AAA29911.1; -; mRNA.
DR   AlphaFoldDB; Q27778; -.
DR   SMR; Q27778; -.
DR   STRING; 6183.Q27778; -.
DR   eggNOG; KOG2440; Eukaryota.
DR   InParanoid; Q27778; -.
DR   SABIO-RK; Q27778; -.
DR   UniPathway; UPA00109; UER00182.
DR   Proteomes; UP000008854; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003872; F:6-phosphofructokinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.450; -; 2.
DR   Gene3D; 3.40.50.460; Phosphofructokinase domain; 2.
DR   HAMAP; MF_03184; Phosphofructokinase_I_E; 1.
DR   InterPro; IPR009161; 6-Pfructokinase_euk.
DR   InterPro; IPR022953; ATP_PFK.
DR   InterPro; IPR015912; Phosphofructokinase_CS.
DR   InterPro; IPR000023; Phosphofructokinase_dom.
DR   InterPro; IPR035966; PKF_sf.
DR   NCBIfam; TIGR02478; 6PF1K_euk; 1.
DR   PANTHER; PTHR13697:SF4; ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE; 1.
DR   PANTHER; PTHR13697; PHOSPHOFRUCTOKINASE; 1.
DR   Pfam; PF00365; PFK; 2.
DR   PIRSF; PIRSF000533; ATP_PFK_euk; 1.
DR   PRINTS; PR00476; PHFRCTKINASE.
DR   SUPFAM; SSF53784; Phosphofructokinase; 2.
DR   PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 1.
PE   1: Evidence at protein level;
KW   Allosteric enzyme; ATP-binding; Cytoplasm; Glycolysis; Kinase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Reference proteome; Transferase.
FT   CHAIN           1..781
FT                   /note="ATP-dependent 6-phosphofructokinase"
FT                   /id="PRO_0000112033"
FT   REGION          1..394
FT                   /note="N-terminal catalytic PFK domain 1"
FT   REGION          395..409
FT                   /note="Interdomain linker"
FT   REGION          410..781
FT                   /note="C-terminal regulatory PFK domain 2"
FT   ACT_SITE        168
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         27
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         90..91
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         120..123
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         121
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         166..168
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         203
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         210..212
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         266
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         294
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         300..303
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         479
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         537..541
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         575
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         582..584
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         638
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         664
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         670..673
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         745
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"
SQ   SEQUENCE   781 AA;  86060 MW;  B2CDF20CAE926C38 CRC64;
     MATWMEGKYV ARGQFTGECI AVLTSGGDAQ GMNAAVRAVV RMGIYCGCRV FFIREGYQGL
     VDGGQNIQEA SWADVSGILQ LGGTKIGSAR CMDFRERYGR LKAAENLVKN QITNLVVIGG
     DGSLTGANLF RAEWSSLLEE LVTSNKISAE SAKQFHRLNI VGLVGSIDND FCGTDMTIGA
     DSALHRIIEA TDAISTTAHS HQRCFILEVM GRHCGYLALV ASMACEADWV FIPEMPPTDD
     WREKLCHKLR MNREHGQRVN IIMVAEGAID RACKPITCEI VKNLIVSELQ LDTRITVLGH
     VQRGGSPSAF DRILGSRMGA EAVLALMDAD RDPNLPSCVI SLDGNQAVRV PLVKCVDRTR
     QVAEAMKACD FDHAVELRGT SFMNNLATYI KLSKIEQPRQ SVMSSENNLR IGIVNVGAPA
     CGINAVIRGF TRLGITKGYK VIGIHEGFSG LVKGDASEIQ WADVRGWVGM GGSMLGTRRD
     TPNGLGIDKV AAKFKELKLS GLLIIGGFEA YECMIELVEG REKYPELCIP MAMVPATISN
     NVPGTDFSLG CDTALNEITS VLDKIKQSAL GTKRRVFVVE TMGGYCGYLA TMSALAGGAD
     AAYIFEEPFT IDDLREDVVH LRAKIDDNVK RGLVLRADML INTITSEFIH QLYAQEGQGI
     FDCRCNVLGH MQQGDRPSPF DRSLGTKFAS KAIDWLDEQI NANIVQILQS IHQTFMLYIN
     WYCTSSDNLF KYSLELREHT DFVHRLPKEE WWLSLRPLMR IMAKHDSLYE SESIMAGTDR
     K
//