PFP_GIAIC
ID PFP_GIAIC Reviewed; 544 AA.
AC E2RU81; A8BDR0; Q27659;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 60.
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=GL50803_14993;
OS Giardia intestinalis (strain ATCC 50803 / WB clone C6) (Giardia lamblia).
OC Eukaryota; Metamonada; Diplomonadida; Hexamitidae; Giardiinae; Giardia.
OX NCBI_TaxID=184922;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=WB;
RX PubMed=7841200; DOI=10.1016/0167-4781(94)00217-q;
RA Rozario C., Smith M.W., Muller M.;
RT "Primary sequence of a putative pyrophosphate-linked phosphofructokinase
RT gene of Giardia lamblia.";
RL Biochim. Biophys. Acta 1260:218-222(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50803 / WB clone C6;
RX PubMed=17901334; DOI=10.1126/science.1143837;
RA Morrison H.G., McArthur A.G., Gillin F.D., Aley S.B., Adam R.D.,
RA Olsen G.J., Best A.A., Cande W.Z., Chen F., Cipriano M.J., Davids B.J.,
RA Dawson S.C., Elmendorf H.G., Hehl A.B., Holder M.E., Huse S.M., Kim U.U.,
RA Lasek-Nesselquist E., Manning G., Nigam A., Nixon J.E.J., Palm D.,
RA Passamaneck N.E., Prabhu A., Reich C.I., Reiner D.S., Samuelson J.,
RA Svard S.G., Sogin M.L.;
RT "Genomic minimalism in the early diverging intestinal parasite Giardia
RT lamblia.";
RL Science 317:1921-1926(2007).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=8577346; DOI=10.1016/0166-6851(95)00087-h;
RA Phillips N.F., Li Z.;
RT "Kinetic mechanism of pyrophosphate-dependent phosphofructokinase from
RT Giardia lamblia.";
RL Mol. Biochem. Parasitol. 73:43-51(1995).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP ACTIVITY REGULATION.
RC STRAIN=ATCC 30888 / Portland-1;
RX PubMed=7663168; DOI=10.1006/prep.1995.1042;
RA Li Z., Phillips N.F.;
RT "Pyrophosphate-dependent phosphofructokinase from Giardia lamblia:
RT purification and characterization.";
RL Protein Expr. Purif. 6:319-328(1995).
RN [5]
RP FUNCTION.
RX PubMed=9242987; DOI=10.1016/s0300-9084(97)83509-2;
RA Li Z., Phillips N.F.;
RT "Involvement and identification of a lysine in the PPi-site of
RT pyrophosphate-dependent phosphofructokinase from Giardia lamblia.";
RL Biochimie 79:221-227(1997).
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:7663168,
CC ECO:0000269|PubMed:8577346, ECO:0000269|PubMed:9242987}.
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,
CC ECO:0000269|PubMed:7663168, ECO:0000269|PubMed:8577346};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03185};
CC -!- ACTIVITY REGULATION: Non-allosteric. Competitively inhibited by
CC fructose 2,6-bisphosphate. {ECO:0000255|HAMAP-Rule:MF_03185,
CC ECO:0000269|PubMed:7663168}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.09 mM for phosphate {ECO:0000269|PubMed:7663168,
CC ECO:0000269|PubMed:8577346};
CC KM=0.039 mM for diphosphate {ECO:0000269|PubMed:7663168,
CC ECO:0000269|PubMed:8577346};
CC KM=0.25 mM for fructose 6-phosphate {ECO:0000269|PubMed:7663168,
CC ECO:0000269|PubMed:8577346};
CC KM=0.072 mM for fructose 1,6-bisphosphate
CC {ECO:0000269|PubMed:7663168, ECO:0000269|PubMed:8577346};
CC Vmax=4.62 umol/min/mg enzyme for the forward reaction
CC {ECO:0000269|PubMed:7663168, ECO:0000269|PubMed:8577346};
CC Vmax=0.15 umol/min/mg enzyme for the reverse reaction
CC {ECO:0000269|PubMed:7663168, ECO:0000269|PubMed:8577346};
CC pH dependence:
CC Optimum pH is 7.2 for the forward reaction and 7.0 for the reverse
CC reaction. {ECO:0000269|PubMed:7663168, ECO:0000269|PubMed:8577346};
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: Monomer. {ECO:0000269|PubMed:7663168}.
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; U12337; AAC46511.1; -; Genomic_DNA.
DR EMBL; AACB02000013; EDO79833.1; -; Genomic_DNA.
DR PIR; S52081; S52081.
DR RefSeq; XP_001707507.1; XM_001707455.1.
DR AlphaFoldDB; E2RU81; -.
DR SMR; E2RU81; -.
DR STRING; 5741.EDO79833; -.
DR EnsemblProtists; EDO79833; EDO79833; GL50803_14993.
DR GeneID; 5700403; -.
DR KEGG; gla:GL50803_0014993; -.
DR VEuPathDB; GiardiaDB:GL50803_14993; -.
DR HOGENOM; CLU_022288_0_1_1; -.
DR InParanoid; E2RU81; -.
DR OMA; SAKKYWH; -.
DR OrthoDB; 347054at2759; -.
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: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; Glycolysis; Kinase; Magnesium; Metal-binding; Transferase.
FT CHAIN 1..544
FT /note="Pyrophosphate--fructose 6-phosphate 1-
FT phosphotransferase"
FT /id="PRO_0000429720"
FT ACT_SITE 202
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03185"
FT BINDING 78
FT /ligand="diphosphate"
FT /ligand_id="ChEBI:CHEBI:33019"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03185"
FT BINDING 172
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03185"
FT BINDING 200..202
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 240..241
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03185"
FT BINDING 248..250
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 309
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 412..415
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 173
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 199
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"
SQ SEQUENCE 544 AA; 59964 MW; 73C045A90B6D4D54 CRC64;
MSAFEVYRRK FKPALPRAIQ GASYHLHTEE KTHPVADEQD IAALFPKTTH LPLLDIQPDT
GAPKLLEPKR VGVIFSGGQA PGGHNVLCGL YDKLQQIAPK SVLLGFQNGP KGLMTNKYVE
LTEKFLEPFR NMGGFHAIGS GRDKIAKPED FDAAAKTAKD NNLDIICIIG GDDSNTNACL
LAEDFLKRGL KTAVIGVPKT IDRDLYSTKG IECSFGFDSS TKVYAELIGN ICYDCLSAKK
YWHFIRLMGR SASHITLECG LQTHANICLV GEEILSKKMT SRQLFEYLAD CVTKRADSGK
NYGVCLVPEG LIEFIPENNE LFAYLNNTLL PHWTGELTAD AVAAKLPDPL RTTFMAIPAS
IRTQLLLDRD PHGNIAISQI ETEKFLGAGV QQVLRERGSK TKFTPLYHFF GYEGRCAAPS
DFDCSLCYSL GAVAAILGCN GKTGYMASLR NLVRPPADWS PIGLPLTCLM NMEMRHGHKT
PVIMKQMTDL NGNPYKLLAR NRDTWLMNDD YQNPGPIQQI ATESAEGTAV CARPTITLIE
EARK
