ID S0AWD4_ENTHI Unreviewed; 546 AA. AC S0AWD4; DT 18-SEP-2013, integrated into UniProtKB/TrEMBL. DT 18-SEP-2013, sequence version 1. DT 22-APR-2020, entry version 32. DE RecName: Full=Pyrophosphate--fructose 6-phosphate 1-phosphotransferase {ECO:0000256|HAMAP-Rule:MF_03185}; DE EC=2.7.1.90 {ECO:0000256|HAMAP-Rule:MF_03185}; DE AltName: Full=6-phosphofructokinase, pyrophosphate dependent {ECO:0000256|HAMAP-Rule:MF_03185}; DE AltName: Full=PPi-dependent phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_03185}; DE Short=PPi-PFK {ECO:0000256|HAMAP-Rule:MF_03185}; DE AltName: Full=Pyrophosphate-dependent 6-phosphofructose-1-kinase {ECO:0000256|HAMAP-Rule:MF_03185}; OS Entamoeba histolytica. OC Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae; OC Entamoeba. OX NCBI_TaxID=5759 {ECO:0000313|EMBL:BAN39695.1}; RN [1] {ECO:0000313|EMBL:BAN39695.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HM-1:IMSS {ECO:0000313|EMBL:BAN39695.1}; RA Hiranuka K., Kumagai M., Wakaguri H., Suzuki Y., Sugano S., Watanabe J., RA Makioka A.; RT "Short 5' UTR of Entamoeba genes."; RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases. 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:0000256|HAMAP-Rule:MF_03185}. 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:0000256|HAMAP-Rule:MF_03185}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_03185}; CC -!- ACTIVITY REGULATION: Non-allosteric. {ECO:0000256|HAMAP-Rule:MF_03185}. CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- CC phosphate and glycerone phosphate from D-glucose: step 3/4. CC {ECO:0000256|HAMAP-Rule:MF_03185}. CC -!- SUBUNIT: Homodimer or monomer. {ECO:0000256|HAMAP-Rule:MF_03185}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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:0000256|HAMAP-Rule:MF_03185}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_03185}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK421127; BAN39695.1; -; mRNA. DR eggNOG; KOG2440; Eukaryota. DR eggNOG; COG0205; LUCA. 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: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:0006002; P:fructose 6-phosphate metabolic process; IEA:InterPro. 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 2: Evidence at transcript level; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03185}; KW Glycolysis {ECO:0000256|HAMAP-Rule:MF_03185}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_03185, ECO:0000313|EMBL:BAN39695.1}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_03185}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_03185}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_03185}. FT DOMAIN 74..330 FT /note="PFK" FT /evidence="ECO:0000259|Pfam:PF00365" FT REGION 202..204 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03185" FT REGION 241..242 FT /note="Substrate binding; shared with dimeric partner" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03185" FT REGION 249..251 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03185" FT REGION 420..423 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03185" FT COILED 316..336 FT /evidence="ECO:0000256|SAM:Coils" FT ACT_SITE 204 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03185" FT METAL 174 FT /note="Magnesium; catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03185" FT BINDING 80 FT /note="Diphosphate; via amide nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03185" FT BINDING 310 FT /note="Substrate" FT /evidence="ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_03185" SQ SEQUENCE 546 AA; 60162 MW; 562DB85D8F7A8360 CRC64; MSLSALHKYR LQYKPVLPKH IADIDNITIE EGAKTQSAVN QKELSELFKH TYGLPICNIV AGKNADIHRV IRCGFILSGG PAAGGHNVVA GLFDGLMKGN KENKLYGFRC GAGGILSNDY IEITAELVDK HRNTGGFDLV GSGRTKIETE EQFATAFEHI 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 //