PFKA_WHEAT
ID PFKA_WHEAT Reviewed; 68 AA.
AC Q8H215;
DT 24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=ATP-dependent 6-phosphofructokinase;
DE Short=ATP-PFK;
DE Short=Phosphofructokinase;
DE EC=2.7.1.11;
DE AltName: Full=Phosphohexokinase;
DE Flags: Fragment;
GN Name=PFK;
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Li Y., Tong Y., Liu J., Li B., Li J., Li Z.;
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:Q9M0F9}.
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;
CC Evidence={ECO:0000250|UniProtKB:Q9M0F9};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9M0F9};
CC -!- ACTIVITY REGULATION: Allosterically activated by AMP.
CC {ECO:0000250|UniProtKB:Q9M0F9}.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 3/4.
CC {ECO:0000250|UniProtKB:Q9M0F9}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:Q9M0F9}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9M0F9}.
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:0000305}.
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DR EMBL; AY130765; AAN08156.1; -; mRNA.
DR AlphaFoldDB; Q8H215; -.
DR SMR; Q8H215; -.
DR STRING; 4565.Traes_5BL_E13C98A72.2; -.
DR PRIDE; Q8H215; -.
DR eggNOG; KOG2440; Eukaryota.
DR SABIO-RK; Q8H215; -.
DR UniPathway; UPA00109; UER00182.
DR Proteomes; UP000019116; Unplaced.
DR ExpressionAtlas; Q8H215; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0003872; F:6-phosphofructokinase activity; IBA:GO_Central.
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 InterPro; IPR022953; ATP_PFK.
DR InterPro; IPR000023; Phosphofructokinase_dom.
DR InterPro; IPR035966; PKF_sf.
DR Pfam; PF00365; PFK; 1.
DR PRINTS; PR00476; PHFRCTKINASE.
DR SUPFAM; SSF53784; SSF53784; 1.
PE 2: Evidence at transcript level;
KW Allosteric enzyme; ATP-binding; Cytoplasm; Glycolysis; Kinase; Magnesium;
KW Metal-binding; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN <1..>68
FT /note="ATP-dependent 6-phosphofructokinase"
FT /id="PRO_0000423046"
FT ACT_SITE 48
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:O15648"
FT BINDING 17..20
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O15648"
FT BINDING 18
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O15648"
FT SITE 19
FT /note="Important for substrate specificity; cannot use PPi
FT as phosphoryl donor"
FT /evidence="ECO:0000250|UniProtKB:O15648"
FT NON_TER 1
FT NON_TER 68
SQ SEQUENCE 68 AA; 7767 MW; 15223D0F41F79B56 CRC64;
FSRKTWRIFL QVYVIGGDGT MRGAVVIFEE FKRCRLRISI TGIPKNLDND IEIIDKAFGF
QTAVESAQ
