ID S0AWD4_ENTHI Unreviewed; 546 AA. AC S0AWD4; DT 18-SEP-2013, integrated into UniProtKB/TrEMBL. DT 18-SEP-2013, sequence version 1. DT 13-NOV-2019, entry version 30. 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; Entamoebidae; 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., RA Watanabe J., 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, CC the first committing step of glycolysis. Uses inorganic phosphate CC (PPi) as phosphoryl donor instead of ATP like common ATP-dependent CC phosphofructokinases (ATP-PFKs), which renders the reaction CC reversible, and can thus function both in glycolysis and CC gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of CC both the forward (ATP-PFK) and reverse (fructose-bisphosphatase CC (FBPase)) reactions. {ECO:0000256|HAMAP-Rule:MF_03185}. CC -!- CATALYTIC ACTIVITY: CC Reaction=beta-D-fructose 6-phosphate + diphosphate = beta-D- CC fructose 1,6-bisphosphate + H(+) + phosphate; CC Xref=Rhea:RHEA:13613, ChEBI:CHEBI:15378, ChEBI:CHEBI:32966, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:43474, ChEBI:CHEBI:57634; CC EC=2.7.1.90; Evidence={ECO:0000256|HAMAP-Rule:MF_03185}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_03185}; CC -!- ACTIVITY REGULATION: Non-allosteric. {ECO:0000256|HAMAP- CC 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) CC family. PPi-dependent PFK group II subfamily. Clade 'Long' sub- CC subfamily. {ECO:0000256|HAMAP-Rule:MF_03185}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of 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 PFK. {ECO:0000259|Pfam:PF00365}. FT REGION 202 204 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_03185}. FT REGION 241 242 Substrate binding; shared with dimeric FT partner. {ECO:0000256|HAMAP-Rule: FT MF_03185}. FT REGION 249 251 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_03185}. FT REGION 420 423 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_03185}. FT COILED 316 336 {ECO:0000256|SAM:Coils}. FT ACT_SITE 204 204 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_03185}. FT METAL 174 174 Magnesium; catalytic. {ECO:0000256|HAMAP- FT Rule:MF_03185}. FT BINDING 80 80 Diphosphate; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_03185}. FT BINDING 310 310 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_03185}. FT SITE 175 175 Important for catalytic activity and FT substrate specificity; stabilizes the FT transition state when the phosphoryl FT donor is PPi; prevents ATP from binding FT by mimicking the alpha-phosphate group of FT ATP. {ECO:0000256|HAMAP-Rule:MF_03185}. FT SITE 201 201 Important for catalytic activity; FT stabilizes the transition state when the FT phosphoryl donor is PPi. FT {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 //