ID   PFKA2_CLOPE             Reviewed;         366 AA.
AC   Q8XL57;
DT   16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   27-MAR-2024, entry version 114.
DE   RecName: Full=ATP-dependent 6-phosphofructokinase 2 {ECO:0000255|HAMAP-Rule:MF_01976};
DE            Short=ATP-PFK 2 {ECO:0000255|HAMAP-Rule:MF_01976};
DE            Short=Phosphofructokinase 2 {ECO:0000255|HAMAP-Rule:MF_01976};
DE            EC=2.7.1.11 {ECO:0000255|HAMAP-Rule:MF_01976};
DE   AltName: Full=Phosphohexokinase 2 {ECO:0000255|HAMAP-Rule:MF_01976};
GN   Name=pfkA2 {ECO:0000255|HAMAP-Rule:MF_01976}; Synonyms=pfk;
GN   OrderedLocusNames=CPE1185;
OS   Clostridium perfringens (strain 13 / Type A).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=195102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=13 / Type A;
RX   PubMed=11792842; DOI=10.1073/pnas.022493799;
RA   Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA   Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT   "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT   eater.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(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_01976}.
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_01976};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01976};
CC   -!- ACTIVITY REGULATION: Subject to allosteric activation by ADP and other
CC       diphosphonucleosides, and inhibition by phosphoenolpyruvate.
CC       {ECO:0000250}.
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_01976}.
CC   -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000255|HAMAP-Rule:MF_01976}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01976}.
CC   -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family.
CC       Mixed-substrate PFK group III subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_01976}.
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DR   EMBL; BA000016; BAB80891.1; -; Genomic_DNA.
DR   RefSeq; WP_003467367.1; NC_003366.1.
DR   AlphaFoldDB; Q8XL57; -.
DR   SMR; Q8XL57; -.
DR   STRING; 195102.gene:10490448; -.
DR   KEGG; cpe:CPE1185; -.
DR   HOGENOM; CLU_020655_0_0_9; -.
DR   UniPathway; UPA00109; UER00182.
DR   Proteomes; UP000000818; Chromosome.
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:UniProtKB-KW.
DR   GO; GO:0047334; F:diphosphate-fructose-6-phosphate 1-phosphotransferase activity; IEA:InterPro.
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   Gene3D; 3.40.50.460; Phosphofructokinase domain; 1.
DR   HAMAP; MF_01976; Phosphofructokinase_III; 1.
DR   InterPro; IPR022953; ATP_PFK.
DR   InterPro; IPR012003; ATP_PFK_prok-type.
DR   InterPro; IPR015912; Phosphofructokinase_CS.
DR   InterPro; IPR000023; Phosphofructokinase_dom.
DR   InterPro; IPR012829; Phosphofructokinase_III.
DR   InterPro; IPR035966; PKF_sf.
DR   NCBIfam; TIGR02483; PFK_mixed; 1.
DR   PANTHER; PTHR13697:SF52; ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE 3; 1.
DR   PANTHER; PTHR13697; PHOSPHOFRUCTOKINASE; 1.
DR   Pfam; PF00365; PFK; 1.
DR   PIRSF; PIRSF000532; ATP_PFK_prok; 1.
DR   PRINTS; PR00476; PHFRCTKINASE.
DR   SUPFAM; SSF53784; Phosphofructokinase; 1.
DR   PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Glycolysis; Kinase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Reference proteome; Transferase.
FT   CHAIN           1..366
FT                   /note="ATP-dependent 6-phosphofructokinase 2"
FT                   /id="PRO_0000111945"
FT   ACT_SITE        144
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
FT   BINDING         15
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
FT   BINDING         78..79
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
FT   BINDING         119..122
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
FT   BINDING         120
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
FT   BINDING         142..144
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
FT   BINDING         179
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
FT   BINDING         186..188
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
FT   BINDING         239
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
FT   BINDING         284
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
FT   BINDING         290..293
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
FT   SITE            121
FT                   /note="Important for substrate specificity; cannot use PPi
FT                   as phosphoryl donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
SQ   SEQUENCE   366 AA;  39514 MW;  C5614C41AE638C31 CRC64;
     MMQPIKKIAI LTGGGDCPGL NAVIRAVTRT AILKYGYEVI GYKFGYRGLY NNDFVKLDLD
     SVSGILHRGG TILHSSNKDN LFDYQVEDEN GKIVKKDVSD VGVENLKKEG VDALVVIGGD
     GTLTSARDFS RKGVNVIGVP KTIDNDLLAT DVTFGFNTAT EIATEALDRL HTTAESHHRI
     MLLEVMGRNA GWIALESGIA GSADVILLPE IPYDINKIVE KVKEREEAGK QFTIIVVAEG
     AKPKDGEVVV SKIVDDSPDP IRLGGIANKL AIDLEGLIKN HEIRSTVLGH IQRGGNTSTY
     DRILSTKYGV KAVELINSNL FGNMVALKGN KVSYESLENV IGHTKNVDPE GELVNTAKSI
     GISFAD
//