PFP1_TRIVA
ID PFP1_TRIVA Reviewed; 426 AA.
AC O61068; A2E3A6;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Pyrophosphate--fructose 6-phosphate 1-phosphotransferase 1 {ECO:0000255|HAMAP-Rule:MF_01979};
DE EC=2.7.1.90 {ECO:0000255|HAMAP-Rule:MF_01979};
DE AltName: Full=6-phosphofructokinase, pyrophosphate dependent 1 {ECO:0000255|HAMAP-Rule:MF_01979};
DE AltName: Full=PPi-dependent phosphofructokinase 1 {ECO:0000255|HAMAP-Rule:MF_01979};
DE Short=PPi-PFK 1 {ECO:0000255|HAMAP-Rule:MF_01979};
DE AltName: Full=Pyrophosphate-dependent 6-phosphofructose-1-kinase 1 {ECO:0000255|HAMAP-Rule:MF_01979};
GN Name=Pfk1; ORFNames=TVAG_430830;
OS Trichomonas vaginalis.
OC Eukaryota; Metamonada; Parabasalia; Trichomonadida; Trichomonadidae;
OC Trichomonas.
OX NCBI_TaxID=5722;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 88-97; 140-175;
RP 180-204; 261-279; 301-310; 312-335 AND 383-387, AND SUBUNIT.
RC STRAIN=ATCC 30001 / NIH C1;
RX PubMed=9847416; DOI=10.1007/pl00006433;
RA Mertens E., Ladror U.S., Lee J.A., Miretsky A., Morris A., Rozario C.,
RA Kemp R.G., Muller M.;
RT "The pyrophosphate-dependent phosphofructokinase of the protist,
RT Trichomonas vaginalis, and the evolutionary relationships of protist
RT phosphofructokinases.";
RL J. Mol. Evol. 47:739-750(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC PRA-98 / G3;
RX PubMed=17218520; DOI=10.1126/science.1132894;
RA Carlton J.M., Hirt R.P., Silva J.C., Delcher A.L., Schatz M., Zhao Q.,
RA Wortman J.R., Bidwell S.L., Alsmark U.C.M., Besteiro S.,
RA Sicheritz-Ponten T., Noel C.J., Dacks J.B., Foster P.G., Simillion C.,
RA Van de Peer Y., Miranda-Saavedra D., Barton G.J., Westrop G.D., Mueller S.,
RA Dessi D., Fiori P.L., Ren Q., Paulsen I., Zhang H., Bastida-Corcuera F.D.,
RA Simoes-Barbosa A., Brown M.T., Hayes R.D., Mukherjee M., Okumura C.Y.,
RA Schneider R., Smith A.J., Vanacova S., Villalvazo M., Haas B.J., Pertea M.,
RA Feldblyum T.V., Utterback T.R., Shu C.L., Osoegawa K., de Jong P.J.,
RA Hrdy I., Horvathova L., Zubacova Z., Dolezal P., Malik S.B.,
RA Logsdon J.M. Jr., Henze K., Gupta A., Wang C.C., Dunne R.L., Upcroft J.A.,
RA Upcroft P., White O., Salzberg S.L., Tang P., Chiu C.-H., Lee Y.-S.,
RA Embley T.M., Coombs G.H., Mottram J.C., Tachezy J., Fraser-Liggett C.M.,
RA Johnson P.J.;
RT "Draft genome sequence of the sexually transmitted pathogen Trichomonas
RT vaginalis.";
RL Science 315:207-212(2007).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 30001 / NIH C1;
RX PubMed=2558319; DOI=10.1016/0166-6851(89)90150-3;
RA Mertens E., Van Schaftingen E., Muller M.;
RT "Presence of a fructose-2,6-bisphosphate-insensitive pyrophosphate:
RT fructose-6-phosphate phosphotransferase in the anaerobic protozoa
RT Tritrichomonas foetus, Trichomonas vaginalis and Isotricha prostoma.";
RL Mol. Biochem. Parasitol. 37:183-190(1989).
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_01979, ECO:0000269|PubMed:2558319}.
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_01979,
CC ECO:0000269|PubMed:2558319};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01979};
CC -!- ACTIVITY REGULATION: Non-allosteric. {ECO:0000255|HAMAP-Rule:MF_01979}.
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_01979}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01979,
CC ECO:0000269|PubMed:9847416}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01979}.
CC -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family.
CC PPi-dependent PFK group II subfamily. Clade 'Short' sub-subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01979}.
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DR EMBL; AF044973; AAD13344.1; -; Genomic_DNA.
DR EMBL; DS113294; EAY12916.1; -; Genomic_DNA.
DR RefSeq; XP_001325139.1; XM_001325104.1.
DR AlphaFoldDB; O61068; -.
DR SMR; O61068; -.
DR STRING; 5722.XP_001325139.1; -.
DR GeneID; 4770885; -.
DR KEGG; tva:TVAG_430830; -.
DR VEuPathDB; TrichDB:TVAG_364620; -.
DR eggNOG; KOG2440; Eukaryota.
DR InParanoid; O61068; -.
DR OMA; YDSEDAF; -.
DR UniPathway; UPA00109; UER00182.
DR Proteomes; UP000001542; Unassembled 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: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_01979; Phosphofructokinase_II_Short; 1.
DR InterPro; IPR022953; ATP_PFK.
DR InterPro; IPR000023; Phosphofructokinase_dom.
DR InterPro; IPR035966; PKF_sf.
DR InterPro; IPR011403; PPi-PFK_TM0289.
DR Pfam; PF00365; PFK; 1.
DR PIRSF; PIRSF036482; PPi_PFK_TM0289; 1.
DR PRINTS; PR00476; PHFRCTKINASE.
DR SUPFAM; SSF53784; SSF53784; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Glycolysis; Kinase; Magnesium;
KW Metal-binding; Reference proteome; Transferase.
FT CHAIN 1..426
FT /note="Pyrophosphate--fructose 6-phosphate 1-
FT phosphotransferase 1"
FT /id="PRO_0000429702"
FT ACT_SITE 142
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01979"
FT BINDING 15
FT /ligand="diphosphate"
FT /ligand_id="ChEBI:CHEBI:33019"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01979"
FT BINDING 114
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01979"
FT BINDING 140..142
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01979"
FT BINDING 186..188
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01979"
FT BINDING 247
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01979"
FT BINDING 308..311
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01979"
FT SITE 115
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_01979"
FT SITE 139
FT /note="Important for catalytic activity; stabilizes the
FT transition state when the phosphoryl donor is PPi"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01979"
FT CONFLICT 335
FT /note="L -> KL (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 426 AA; 46535 MW; ADDEFE53E507B8D2 CRC64;
MSTEAPVLGI LCGGGPAPGL NGVIAGATLY ALRLGWKVIG FMEGFKYLCT GDVDVVKAHT
IDLTYDIVSR IHFQGGTIIQ TSRANPRKSP ELQENVRKCL RALKVRYFLT IGGDDTASSA
VSVASGMNGN EISVISCPKT IDNDLPLPAD QSTFGFHTAR SLGMEIIRNL MVDSKSAPRW
FLVEAMGRSA GHLALGMAEA SGAHLCLIPE EFKQDEIEFE DVVELVEATI LKRLAYGKNY
GVCVLAEGLV SKMSKKALYK LFGNREPPTD PHGHILLDDA ELARSLSEEL LKRLGNLGIR
ITPKKIGYEL RCADPVAFDA VYTRELGYGA IDAFLNGHSA ALIVRENGQV KPVQFKDLLD
PATGRVRTRL VDVTSQSFKV ARVYMWRMSK KDYENKDLVA RVAAAGKMTP EAFTEKFAHL
TDVVVE
