ID PFKA_TRYBO Reviewed; 490 AA.
AC Q8WPP2;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 22-FEB-2023, entry version 70.
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=pfk {ECO:0000255|HAMAP-Rule:MF_03186};
OS Trypanoplasma borreli.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Parabodonida; Trypanoplasma.
OX NCBI_TaxID=5710;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12180974; DOI=10.1046/j.1432-1033.2002.03086.x;
RA Lopez C., Chevalier N., Hannaert V., Rigden D.J., Michels P.A.,
RA Ramirez J.L.;
RT "Leishmania donovani phosphofructokinase. Gene characterization,
RT biochemical properties and structure-modeling studies.";
RL Eur. J. Biochem. 269:3978-3989(2002).
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 -!- 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 -!- ACTIVITY REGULATION: Allosterically activated by AMP.
CC {ECO:0000255|HAMAP-Rule:MF_03186}.
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: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_03186}.
CC -!- SUBCELLULAR LOCATION: Glycosome {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}.
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DR EMBL; AJ310928; CAC84571.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8WPP2; -.
DR SMR; Q8WPP2; -.
DR UniPathway; UPA00109; UER00182.
DR GO; GO:0020015; C:glycosome; IEA:UniProtKB-SubCell.
DR GO; GO:0003872; F:6-phosphofructokinase activity; IEA:UniProtKB-UniRule.
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 Gene3D; 3.40.50.450; -; 1.
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 PANTHER; PTHR45770; ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE 1; 1.
DR PANTHER; PTHR45770:SF11; ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE 1; 1.
DR Pfam; PF00365; PFK; 1.
DR PRINTS; PR00476; PHFRCTKINASE.
DR SUPFAM; SSF53784; Phosphofructokinase; 1.
PE 3: Inferred from homology;
KW Allosteric enzyme; ATP-binding; Glycolysis; Glycosome; Kinase; Magnesium;
KW Metal-binding; Nucleotide-binding; Peroxisome; Transferase.
FT CHAIN 1..490
FT /note="ATP-dependent 6-phosphofructokinase"
FT /id="PRO_0000429722"
FT MOTIF 488..490
FT /note="Peroxisomal targeting signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT ACT_SITE 231
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT BINDING 109
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT BINDING 175..176
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT BINDING 200..203
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT BINDING 201
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT BINDING 229..231
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT BINDING 274..276
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT BINDING 327
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT BINDING 383..386
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT SITE 202
FT /note="Important for substrate specificity; cannot use PPi
FT as phosphoryl donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
SQ SEQUENCE 490 AA; 53376 MW; 62360A4071A700DF CRC64;
MDEPSNMSTT SSKIPQYDFY SDVDNLHPDQ FRIQCLPGRN FISPLVEQKK DFVKAHVIHD
KDLDIMYDPM PKGKCNISQS CLTLPLACPR VSLHFDPSKT TVAMVTCGGV CPGLNDVIRG
ITLAAVCSYH VKKVIGFKYG YWGLSKAGRH TAIELTSNIV RGLRHLGGTF LGTSRGGQNI
SDMVDTLVEY GVNILFTIGG DGTQKGAVAI SEEVNRRGLD IAVFGIPKTI DNDLSFSQRT
FGYETAVSEA VIAIRAAHAE AISHEYGVGI VKLMGRNSGF IAASATVASA LSHICLIPEK
NVSKKVLLSL IEARFMMAKD IVIVVAEGFG QDWPDCNEDL GSDASGNKRL TDIGLVIKKI
VQDHLSKNPK YHQSTVKYID PSYMIRACPA STSDAAFCSN LSTLAVHEAM AGRTACLITL
WYSNFVLVPI KTAVSHRKIV STGGALWRQV REVTVDGSGD IAMVHQQELS RELKAINAHR
NSIMEQLSKL
//
