ID   PFKA2_THET8             Reviewed;          25 AA.
AC   P21778;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   12-APR-2005, sequence version 3.
DT   28-JUN-2023, entry version 99.
DE   RecName: Full=ATP-dependent 6-phosphofructokinase 2;
DE            Short=ATP-PFK 2;
DE            Short=Phosphofructokinase 2;
DE            EC=2.7.1.11 {ECO:0000269|PubMed:1830879};
DE   AltName: Full=Phosphohexokinase 2;
DE   Flags: Fragment;
GN   Name=pfkA2;
OS   Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC   Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=300852;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND
RP   SUBUNIT.
RX   PubMed=1830879;
RA   Xu J., Oshima T., Yoshida M.;
RT   "Phosphoenolpyruvate-insensitive phosphofructokinase isozyme from Thermus
RT   thermophilus HB8.";
RL   J. Biochem. 109:199-203(1991).
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:0000269|PubMed:1830879}.
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:0000269|PubMed:1830879};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P0A796};
CC   -!- ACTIVITY REGULATION: In contrast with PFK1 this enzyme is not affected
CC       by phosphoenolpyruvate. {ECO:0000269|PubMed:1830879}.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 3/4.
CC       {ECO:0000250|UniProtKB:P0A796}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:1830879}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0A796}.
CC   -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family.
CC       ATP-dependent PFK group I subfamily. Prokaryotic clade 'B1' sub-
CC       subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P21778; -.
DR   SMR; P21778; -.
DR   UniPathway; UPA00109; UER00182.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003872; F:6-phosphofructokinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.450; -; 1.
DR   InterPro; IPR000023; Phosphofructokinase_dom.
DR   InterPro; IPR035966; PKF_sf.
DR   Pfam; PF00365; PFK; 1.
DR   SUPFAM; SSF53784; Phosphofructokinase; 1.
PE   1: Evidence at protein level;
KW   Allosteric enzyme; ATP-binding; Cytoplasm; Direct protein sequencing;
KW   Glycolysis; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Transferase.
FT   CHAIN           1..>25
FT                   /note="ATP-dependent 6-phosphofructokinase 2"
FT                   /id="PRO_0000112002"
FT   BINDING         11
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P0A796"
FT   NON_TER         25
SQ   SEQUENCE   25 AA;  2557 MW;  E7AEC8D6110EBA46 CRC64;
     MKRIGVLTSG GDSPGMNAAI RAVVR
//