PFKA_ENTHI
ID PFKA_ENTHI Reviewed; 436 AA.
AC Q27651; C4LVK3; Q24812;
DT 24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT 09-JUL-2014, sequence version 2.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=ATP-dependent 6-phosphofructokinase {ECO:0000255|HAMAP-Rule:MF_03186};
DE Short=ATP-PFK {ECO:0000255|HAMAP-Rule:MF_03186};
DE Short=Phosphofructokinase {ECO:0000255|HAMAP-Rule:MF_03186};
DE EC=2.7.1.11 {ECO:0000255|HAMAP-Rule:MF_03186};
DE AltName: Full=Phosphohexokinase {ECO:0000255|HAMAP-Rule:MF_03186};
GN Name=PPi-PFK; ORFNames=EHI_103590;
OS Entamoeba histolytica.
OC Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC Entamoeba.
OX NCBI_TaxID=5759;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND ACTIVITY REGULATION.
RC STRAIN=ATCC 30459 / HM-1:IMSS;
RX PubMed=8645233; DOI=10.1042/bj3160057;
RA Bruchhaus I., Jacobs T., Denart M., Tannich E.;
RT "Pyrophosphate-dependent phosphofructokinase of Entamoeba histolytica:
RT molecular cloning, recombinant expression and inhibition by pyrophosphate
RT analogues.";
RL Biochem. J. 316:57-63(1996).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 19-436.
RC STRAIN=ATCC 30459 / HM-1:IMSS;
RX PubMed=7841199; DOI=10.1016/0167-4781(94)00216-p;
RA Huang M., Albach R.A., Chang K.P., Tripathi R.L., Kemp R.G.;
RT "Cloning and sequencing a putative pyrophosphate-dependent
RT phosphofructokinase gene from Entamoeba histolytica.";
RL Biochim. Biophys. Acta 1260:215-217(1995).
RN [5]
RP FUNCTION, SUBUNIT, AND COFACTOR.
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 to
CC fructose 1,6-bisphosphate by ATP, the first committing step of
CC glycolysis. {ECO:0000255|HAMAP-Rule:MF_03186,
CC ECO:0000269|PubMed:11262402}.
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_03186};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03186,
CC ECO:0000269|PubMed:11262402};
CC -!- ACTIVITY REGULATION: Activated by nucleoside triphosphates. Inhibited
CC by phosphoenolpyruvate. EDTA and biphosphonates play the role of
CC inhibitors of kinase activity. {ECO:0000269|PubMed:8645233}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.12 mM for ATP;
CC KM=0.067 mM for GTP;
CC KM=0.136 mM for ITP;
CC KM=1.93 mM for UTP;
CC KM=3.6 mM for CTP;
CC KM=3.8 mM for fructose 6-phosphate;
CC pH dependence:
CC Optimum pH is 6-7.;
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_03186}.
CC -!- SUBUNIT: Homodimer. Aggregates to a homotetramer after activation by
CC ATP. {ECO:0000269|PubMed:11262402}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03186}.
CC -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family.
CC PPi-dependent PFK group II subfamily. Atypical ATP-dependent clade 'X'
CC sub-subfamily. {ECO:0000255|HAMAP-Rule:MF_03186}.
CC -!- CAUTION: Was originally thought to be a PPi-dependent
CC phosphofructokinase (PubMed:8645233), but it has later been shown that
CC the enzyme does not possess PPi-dependent activity and instead is an
CC ATP-dependent phosphofructokinase (PubMed:11262402).
CC {ECO:0000305|PubMed:11262402, ECO:0000305|PubMed:8645233}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA92671.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAA92671.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X82173; CAA57659.1; -; mRNA.
DR EMBL; DS571158; EAL47987.1; -; Genomic_DNA.
DR EMBL; U12513; AAA92671.1; ALT_SEQ; Genomic_DNA.
DR PIR; S49458; S49458.
DR RefSeq; XP_653373.1; XM_648281.1.
DR AlphaFoldDB; Q27651; -.
DR SMR; Q27651; -.
DR STRING; 5759.rna_EHI_103590-1; -.
DR EnsemblProtists; rna_EHI_103590-1; rna_EHI_103590-1; EHI_103590.
DR GeneID; 3407680; -.
DR KEGG; ehi:EHI_103590; -.
DR VEuPathDB; AmoebaDB:EHI5A_077230; -.
DR VEuPathDB; AmoebaDB:EHI7A_062050; -.
DR VEuPathDB; AmoebaDB:EHI8A_049590; -.
DR VEuPathDB; AmoebaDB:EHI_103590; -.
DR VEuPathDB; AmoebaDB:KM1_109080; -.
DR eggNOG; KOG2440; Eukaryota.
DR HOGENOM; CLU_020655_7_4_1; -.
DR OMA; YGHERFA; -.
DR BRENDA; 2.7.1.90; 2080.
DR UniPathway; UPA00109; UER00182.
DR Proteomes; UP000001926; Partially assembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0003872; F:6-phosphofructokinase activity; IBA:GO_Central.
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 HAMAP; MF_01981; Phosphofructokinase_II_X; 1.
DR InterPro; IPR022953; ATP_PFK.
DR InterPro; IPR000023; Phosphofructokinase_dom.
DR InterPro; IPR035966; PKF_sf.
DR InterPro; IPR012004; PyroP-dep_PFK_TP0108.
DR Pfam; PF00365; PFK; 1.
DR PIRSF; PIRSF000534; PPi_PFK_TP0108; 1.
DR PRINTS; PR00476; PHFRCTKINASE.
DR SUPFAM; SSF53784; SSF53784; 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..436
FT /note="ATP-dependent 6-phosphofructokinase"
FT /id="PRO_0000423021"
FT ACT_SITE 211
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT BINDING 90
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT BINDING 155..156
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT BINDING 180..183
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT BINDING 181
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT BINDING 209..211
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT BINDING 254..256
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT BINDING 307
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT BINDING 362..365
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT SITE 182
FT /note="Important for substrate specificity; cannot use PPi
FT as phosphoryl donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT CONFLICT 109
FT /note="R -> A (in Ref. 1; CAA57659)"
FT /evidence="ECO:0000305"
FT CONFLICT 430
FT /note="T -> S (in Ref. 1; CAA57659)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 436 AA; 47670 MW; BFD2E9639DAA1138 CRC64;
MSVKRRDHIL IPKNPDAPLP SLKIEEVGEC TIDNIYASPE PFVNGMTMKL SAVKNHGIER
DSGEVELAGP MEKIFYNPET TKVAIVTCGG LCPGLNNVIR GLVLNLYNRY HVNNIFGLRW
GYEGLVPELS EVQRLTPEIV SDIHQKGGSI LGTSRGAQSP EVMAQFLIDN NFNILFTLGG
DGTLRGANAI NKELRRRKVP ITVVGIPKTI DNDICYTDST FGFQTAVGLS QEAINAVHSE
AKSAKNGIGI VRLMGRDAGF IALYASLANG DANLVLIPEI DIPITQICEF VGKRIMSKGH
VVIVVAEGAL QNQKPKDLDL GTDKSGNILH WDSINYLRDS ITKYLKSIGI EEHTIKFVDP
SYMIRSAPCS AADAHFCMCL ANAAVHVAMA GKTGLVICHH HNNFVSVPID RTSYYIKRVN
TDGPLYTMMT AIEKPK
