PFP_ENTHI
ID PFP_ENTHI Reviewed; 546 AA.
AC C4LZC2; O15705;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Pyrophosphate--fructose 6-phosphate 1-phosphotransferase {ECO:0000255|HAMAP-Rule:MF_03185};
DE EC=2.7.1.90 {ECO:0000255|HAMAP-Rule:MF_03185};
DE AltName: Full=6-phosphofructokinase, pyrophosphate dependent {ECO:0000255|HAMAP-Rule:MF_03185};
DE AltName: Full=PPi-dependent phosphofructokinase {ECO:0000255|HAMAP-Rule:MF_03185};
DE Short=PPi-PFK {ECO:0000255|HAMAP-Rule:MF_03185};
DE AltName: Full=Pyrophosphate-dependent 6-phosphofructose-1-kinase {ECO:0000255|HAMAP-Rule:MF_03185};
GN ORFNames=EHI_000730;
OS Entamoeba histolytica.
OC Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC Entamoeba.
OX NCBI_TaxID=5759;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 9-14; 20-33; 105-109;
RP 133-144; 227-231; 372-383; 408-415 AND 494-546, FUNCTION, CATALYTIC
RP ACTIVITY, SUBUNIT, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 30459 / HM-1:IMSS;
RX PubMed=9445396; DOI=10.1042/bj3290659;
RA Deng Z., Huang M., Singh K., Albach R.A., Latshaw S.P., Chang K.P.,
RA Kemp R.G.;
RT "Cloning and expression of the gene for the active PPi-dependent
RT phosphofructokinase of entamoeba histolytica.";
RL Biochem. J. 329:659-664(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 30459 / HM-1:IMSS;
RX PubMed=15729342; DOI=10.1038/nature03291;
RA Loftus B.J., Anderson I., Davies R., Alsmark U.C., Samuelson J., Amedeo P.,
RA Roncaglia P., Berriman M., Hirt R.P., Mann B.J., Nozaki T., Suh B., Pop M.,
RA Duchene M., Ackers J., Tannich E., Leippe M., Hofer M., Bruchhaus I.,
RA Willhoeft U., Bhattacharya A., Chillingworth T., Churcher C.M., Hance Z.,
RA Harris B., Harris D., Jagels K., Moule S., Mungall K.L., Ormond D.,
RA Squares R., Whitehead S., Quail M.A., Rabbinowitsch E., Norbertczak H.,
RA Price C., Wang Z., Guillen N., Gilchrist C., Stroup S.E., Bhattacharya S.,
RA Lohia A., Foster P.G., Sicheritz-Ponten T., Weber C., Singh U.,
RA Mukherjee C., El-Sayed N.M.A., Petri W.A., Clark C.G., Embley T.M.,
RA Barrell B.G., Fraser C.M., Hall N.;
RT "The genome of the protist parasite Entamoeba histolytica.";
RL Nature 433:865-868(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 30459 / HM-1:IMSS;
RA Lorenzi H., Amedeo P., Inman J., Schobel S., Caler E.;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND COFACTOR.
RC STRAIN=H200;
RX PubMed=4372217; DOI=10.1016/s0021-9258(19)42029-2;
RA Reeves R.E., South D.J., Blytt H.J., Warren L.G.;
RT "Pyrophosphate:D-fructose 6-phosphate 1-phosphotransferase. A new enzyme
RT with the glycolytic function of 6-phosphofructokinase.";
RL J. Biol. Chem. 249:7737-7741(1974).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND
RP ACTIVITY REGULATION.
RC STRAIN=DKB;
RX PubMed=178659; DOI=10.1016/s0021-9258(17)33484-1;
RA Reeves R.E., Serrano R., South D.J.;
RT "6-phosphofructokinase (pyrophosphate). Properties of the enzyme from
RT Entamoeba histolytica and its reaction mechanism.";
RL J. Biol. Chem. 251:2958-2962(1976).
RN [6]
RP FUNCTION.
RX PubMed=11262402; DOI=10.1074/jbc.m011584200;
RA Chi A.S., Deng Z., Albach R.A., Kemp R.G.;
RT "The two phosphofructokinase gene products of Entamoeba histolytica.";
RL J. Biol. Chem. 276:19974-19981(2001).
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_03185, ECO:0000269|PubMed:11262402,
CC ECO:0000269|PubMed:178659, ECO:0000269|PubMed:4372217,
CC ECO:0000269|PubMed:9445396}.
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_03185, ECO:0000269|PubMed:178659,
CC ECO:0000269|PubMed:4372217, ECO:0000269|PubMed:9445396};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03185, ECO:0000269|PubMed:178659,
CC ECO:0000269|PubMed:4372217};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03185, ECO:0000269|PubMed:178659,
CC ECO:0000269|PubMed:4372217};
CC -!- ACTIVITY REGULATION: Non-allosteric. Competitively inhibited by PPi, Pi
CC and fructose 1,6-bisphosphate. {ECO:0000255|HAMAP-Rule:MF_03185,
CC ECO:0000269|PubMed:178659}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=14 uM for diphosphate {ECO:0000269|PubMed:178659,
CC ECO:0000269|PubMed:4372217, ECO:0000269|PubMed:9445396};
CC KM=800 uM for phosphate {ECO:0000269|PubMed:178659,
CC ECO:0000269|PubMed:4372217, ECO:0000269|PubMed:9445396};
CC KM=38 uM for fructose 6-phosphate {ECO:0000269|PubMed:178659,
CC ECO:0000269|PubMed:4372217, ECO:0000269|PubMed:9445396};
CC KM=18 uM for fructose 1,6-bisphosphate {ECO:0000269|PubMed:178659,
CC ECO:0000269|PubMed:4372217, ECO:0000269|PubMed:9445396};
CC pH dependence:
CC Optimum pH is 6.4-7.2. {ECO:0000269|PubMed:178659,
CC ECO:0000269|PubMed:4372217, ECO:0000269|PubMed:9445396};
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_03185}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:9445396}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03185}.
CC -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family.
CC PPi-dependent PFK group II subfamily. Clade 'Long' sub-subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03185}.
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DR EMBL; AF013986; AAC04465.1; -; mRNA.
DR EMBL; DS571186; EAL47787.1; -; Genomic_DNA.
DR RefSeq; XP_653173.1; XM_648081.2.
DR AlphaFoldDB; C4LZC2; -.
DR SMR; C4LZC2; -.
DR STRING; 5759.rna_EHI_000730-1; -.
DR EnsemblProtists; rna_EHI_000730-1; rna_EHI_000730-1; EHI_000730.
DR GeneID; 3407484; -.
DR KEGG; ehi:EHI_000730; -.
DR VEuPathDB; AmoebaDB:EHI5A_039260; -.
DR VEuPathDB; AmoebaDB:EHI7A_053070; -.
DR VEuPathDB; AmoebaDB:EHI8A_017480; -.
DR VEuPathDB; AmoebaDB:EHI_000730; -.
DR VEuPathDB; AmoebaDB:KM1_048590; -.
DR eggNOG; KOG2440; Eukaryota.
DR HOGENOM; CLU_022288_0_1_1; -.
DR InParanoid; C4LZC2; -.
DR OMA; SAKKYWH; -.
DR SABIO-RK; C4LZC2; -.
DR UniPathway; UPA00109; UER00182.
DR Proteomes; UP000001926; Partially assembled 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:InterPro.
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:0008443; F:phosphofructokinase activity; IBA:GO_Central.
DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:InterPro.
DR GO; GO:0009749; P:response to glucose; IBA:GO_Central.
DR Gene3D; 3.40.50.460; -; 1.
DR HAMAP; MF_01980; Phosphofructokinase_II_Long; 1.
DR InterPro; IPR022953; ATP_PFK.
DR InterPro; IPR011183; PfpB_PPi_PFK.
DR InterPro; IPR000023; Phosphofructokinase_dom.
DR InterPro; IPR035966; PKF_sf.
DR Pfam; PF00365; PFK; 1.
DR PIRSF; PIRSF005677; PPi_PFK_PfpB; 1.
DR PRINTS; PR00476; PHFRCTKINASE.
DR SUPFAM; SSF53784; SSF53784; 1.
DR TIGRFAMs; TIGR02477; PFKA_PPi; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Glycolysis; Kinase; Magnesium;
KW Metal-binding; Reference proteome; Transferase.
FT CHAIN 1..546
FT /note="Pyrophosphate--fructose 6-phosphate 1-
FT phosphotransferase"
FT /id="PRO_0000429719"
FT ACT_SITE 204
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03185"
FT BINDING 80
FT /ligand="diphosphate"
FT /ligand_id="ChEBI:CHEBI:33019"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03185"
FT BINDING 174
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03185"
FT BINDING 202..204
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03185"
FT BINDING 241..242
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03185"
FT BINDING 249..251
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03185"
FT BINDING 310
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03185"
FT BINDING 420..423
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03185"
FT SITE 175
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_03185"
FT SITE 201
FT /note="Important for catalytic activity; stabilizes the
FT transition state when the phosphoryl donor is PPi"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03185"
FT CONFLICT 320
FT /note="K -> I (in Ref. 1; AAC04465)"
FT /evidence="ECO:0000305"
FT CONFLICT 370
FT /note="A -> R (in Ref. 1; AAC04465)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 546 AA; 60161 MW; 557B52BDC00CC8F6 CRC64;
MSLSALHKYR LQYKPVLPKH IADIDNITIE EGAKTQSAVN QKELSELFKH TYGLPICNIV
AGKNADIHRV IRCGFILSGG PAAGGHNVVA GLFDGLMKGN KENKLYGFRC GAGGILSNDY
IEITAELVDK HRNTGGFDLV GSGRTKIETE EQFATAFKHI TALKLNAMVV VGGDDSNTNA
ALLAEYFAAH GSDCVFVGVP KTIDGDLKNQ YIETSFGFDT ACKTYSELIG NIQRDAISSR
KYWHFIKVMG RSASHIALEA ALETQPTYCI ISEEVEDKKM TVSQIASEIA DIVIERHKKG
LNFGVVLIPE GLVEFIPEVK ALIKELNNLL AHKKEEYSKI TEFSAQKAFV CENISESCAA
TFKNLPDNIA KQLLLDRDPH GNVNVSAIET ESFVSGIVKA EIVKRGIKVP FTPVHHFFGY
EGRCAFPSNF DSTYCYALGY TAFILLALKK TGQICCISGL QKPAEEWICG GVPLTIMMNM
EQRNGEMKPV IKKALVEIEG KPFKFYQSKR AQWASAEDFV FPGAIQYFGP SEVCDQPTKT
LLLEQN
