PFP_NAEFO
ID PFP_NAEFO Reviewed; 437 AA.
AC Q27705;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Pyrophosphate--fructose 6-phosphate 1-phosphotransferase {ECO:0000255|HAMAP-Rule:MF_01979};
DE EC=2.7.1.90 {ECO:0000255|HAMAP-Rule:MF_01979};
DE AltName: Full=6-phosphofructokinase, pyrophosphate dependent {ECO:0000255|HAMAP-Rule:MF_01979};
DE AltName: Full=PPi-dependent phosphofructokinase {ECO:0000255|HAMAP-Rule:MF_01979};
DE Short=PPi-PFK {ECO:0000255|HAMAP-Rule:MF_01979};
DE AltName: Full=Pyrophosphate-dependent 6-phosphofructose-1-kinase {ECO:0000255|HAMAP-Rule:MF_01979};
OS Naegleria fowleri (Brain eating amoeba).
OC Eukaryota; Discoba; Heterolobosea; Tetramitia; Eutetramitia;
OC Vahlkampfiidae; Naegleria.
OX NCBI_TaxID=5763;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=LEE / ATCC 30894;
RX PubMed=7717968; DOI=10.1042/bj3070143;
RA Wessberg K.L., Skolnick S., Xu J., Marciano-Cabral F., Kemp R.G.;
RT "Cloning, sequencing and expression of the pyrophosphate-dependent
RT phosphofructo-1-kinase from Naegleria fowleri.";
RL Biochem. J. 307:143-149(1995).
RN [2]
RP FUNCTION, SUBUNIT, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP COFACTOR, AND ACTIVITY REGULATION.
RC STRAIN=KUL;
RX PubMed=8391256; DOI=10.1042/bj2920797;
RA Mertens E., De Jonckheere J., Van Schaftingen E.;
RT "Pyrophosphate-dependent phosphofructokinase from the amoeba Naegleria
RT fowleri, an AMP-sensitive enzyme.";
RL Biochem. J. 292:797-803(1993).
CC -!- FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate, the
CC first committing step of glycolysis. Uses inorganic phosphate (PPi) as
CC phosphoryl donor instead of ATP like common ATP-dependent
CC phosphofructokinases (ATP-PFKs), which renders the reaction reversible,
CC and can thus function both in glycolysis and gluconeogenesis.
CC Consistently, PPi-PFK can replace the enzymes of both the forward (ATP-
CC PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions.
CC {ECO:0000255|HAMAP-Rule:MF_01979, ECO:0000269|PubMed:8391256}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-fructose 6-phosphate + diphosphate = beta-D-fructose
CC 1,6-bisphosphate + H(+) + phosphate; Xref=Rhea:RHEA:13613,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:32966, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57634; EC=2.7.1.90;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01979,
CC ECO:0000269|PubMed:8391256};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01979,
CC ECO:0000269|PubMed:8391256};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01979,
CC ECO:0000269|PubMed:8391256};
CC -!- ACTIVITY REGULATION: Activated by AMP. Probably promotes
CC oligomerization of the enzyme. {ECO:0000269|PubMed:8391256}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=590 uM for phosphate {ECO:0000269|PubMed:8391256};
CC KM=15 uM for diphosphate {ECO:0000269|PubMed:8391256};
CC KM=10 uM for fructose 6-phosphate {ECO:0000269|PubMed:8391256};
CC KM=35 uM for fructose 1,6-bisphosphate {ECO:0000269|PubMed:8391256};
CC pH dependence:
CC Optimum pH is 6 for the forward reaction and 7.5 for the reverse
CC reaction. {ECO:0000269|PubMed:8391256};
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_01979}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01979,
CC ECO:0000269|PubMed:8391256}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01979}.
CC -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family.
CC PPi-dependent PFK group II subfamily. Clade 'Short' sub-subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01979}.
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DR EMBL; U11733; AAA85791.1; -; mRNA.
DR PIR; S54978; S54978.
DR AlphaFoldDB; Q27705; -.
DR SMR; Q27705; -.
DR VEuPathDB; AmoebaDB:NF0074270; -.
DR VEuPathDB; AmoebaDB:NfTy_073640; -.
DR SABIO-RK; Q27705; -.
DR UniPathway; UPA00109; UER00182.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003872; F:6-phosphofructokinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0047334; F:diphosphate-fructose-6-phosphate 1-phosphotransferase activity; IEA:UniProtKB-EC.
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; 3.40.50.460; -; 1.
DR HAMAP; MF_01979; Phosphofructokinase_II_Short; 1.
DR InterPro; IPR022953; ATP_PFK.
DR InterPro; IPR000023; Phosphofructokinase_dom.
DR InterPro; IPR035966; PKF_sf.
DR InterPro; IPR011403; PPi-PFK_TM0289.
DR Pfam; PF00365; PFK; 1.
DR PIRSF; PIRSF036482; PPi_PFK_TM0289; 1.
DR PRINTS; PR00476; PHFRCTKINASE.
DR SUPFAM; SSF53784; SSF53784; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Glycolysis; Kinase; Magnesium; Metal-binding; Transferase.
FT CHAIN 1..437
FT /note="Pyrophosphate--fructose 6-phosphate 1-
FT phosphotransferase"
FT /id="PRO_0000429701"
FT ACT_SITE 149
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01979"
FT BINDING 27
FT /ligand="diphosphate"
FT /ligand_id="ChEBI:CHEBI:33019"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01979"
FT BINDING 122
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01979"
FT BINDING 147..149
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01979"
FT BINDING 193..195
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01979"
FT BINDING 261
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01979"
FT BINDING 323..326
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01979"
FT SITE 123
FT /note="Important for catalytic activity and substrate
FT specificity; stabilizes the transition state when the
FT phosphoryl donor is PPi; prevents ATP from binding by
FT mimicking the alpha-phosphate group of ATP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01979"
FT SITE 146
FT /note="Important for catalytic activity; stabilizes the
FT transition state when the phosphoryl donor is PPi"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01979"
SQ SEQUENCE 437 AA; 48098 MW; 20863E055F18A284 CRC64;
MLSSSHLPTT IVTPKNVPTL GVLVGGGPAP GINGVIGAVT IEAINNGYRV LGFLEGFQNL
ILQDDSKIVE LTIDSVSRIH FEGGSILKTS RANPTKKQED LQKVVKQLQK FNVSLLVTIG
GDDTAFSSMS VAKAANNEIH VVTLPKTIDN DLPLPYGIPT FGYETAREFG ANVVRNLMTD
ASTASRYFIV VAMGRQAGHL ALGIGKSAGS HLTLIPEEFL PTTDSTEPEV TFSRICDMIE
ASIIKRLYTS KKDHGVIVLA EGLLEYMSTD ELKQAFGSSL KYDAHDHIML AELDFGRLVR
DEMRERMNRR GLKIAFTEKN LGYELRCAPP NAFDREYTRD LGNGAVRYLL NGGNGALITV
QGVKMVPLSF DDLKDPRTGK TRTRQVDVSS EGFQVAKRYM IRLEKKDFEK EETLKGLAAT
AKCSVEDFIK QFKYLVQ
