ID   PFKA_ANOFW              Reviewed;         319 AA.
AC   B7GGT1;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   27-MAR-2024, entry version 81.
DE   RecName: Full=ATP-dependent 6-phosphofructokinase {ECO:0000255|HAMAP-Rule:MF_00339};
DE            Short=ATP-PFK {ECO:0000255|HAMAP-Rule:MF_00339};
DE            Short=Phosphofructokinase {ECO:0000255|HAMAP-Rule:MF_00339};
DE            EC=2.7.1.11 {ECO:0000255|HAMAP-Rule:MF_00339};
DE   AltName: Full=Phosphohexokinase {ECO:0000255|HAMAP-Rule:MF_00339};
GN   Name=pfkA {ECO:0000255|HAMAP-Rule:MF_00339};
GN   OrderedLocusNames=Aflv_0499;
OS   Anoxybacillus flavithermus (strain DSM 21510 / WK1).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Anoxybacillus.
OX   NCBI_TaxID=491915;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21510 / WK1;
RX   PubMed=19014707; DOI=10.1186/gb-2008-9-11-r161;
RA   Saw J.H., Mountain B.W., Feng L., Omelchenko M.V., Hou S., Saito J.A.,
RA   Stott M.B., Li D., Zhao G., Wu J., Galperin M.Y., Koonin E.V.,
RA   Makarova K.S., Wolf Y.I., Rigden D.J., Dunfield P.F., Wang L., Alam M.;
RT   "Encapsulated in silica: genome, proteome and physiology of the
RT   thermophilic bacterium Anoxybacillus flavithermus WK1.";
RL   Genome Biol. 9:R161.1-R161.16(2008).
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_00339}.
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_00339};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00339};
CC   -!- ACTIVITY REGULATION: Allosterically activated by ADP and other
CC       diphosphonucleosides, and allosterically inhibited by
CC       phosphoenolpyruvate. {ECO:0000255|HAMAP-Rule:MF_00339}.
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_00339}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00339}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00339}.
CC   -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family.
CC       ATP-dependent PFK group I subfamily. Prokaryotic clade 'B1' sub-
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00339}.
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DR   EMBL; CP000922; ACJ32883.1; -; Genomic_DNA.
DR   RefSeq; WP_012574203.1; NC_011567.1.
DR   AlphaFoldDB; B7GGT1; -.
DR   SMR; B7GGT1; -.
DR   STRING; 491915.Aflv_0499; -.
DR   GeneID; 7036756; -.
DR   KEGG; afl:Aflv_0499; -.
DR   PATRIC; fig|491915.6.peg.511; -.
DR   eggNOG; COG0205; Bacteria.
DR   HOGENOM; CLU_020655_0_1_9; -.
DR   UniPathway; UPA00109; UER00182.
DR   Proteomes; UP000000742; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:InterPro.
DR   CDD; cd00763; Bacterial_PFK; 1.
DR   Gene3D; 3.40.50.450; -; 1.
DR   Gene3D; 3.40.50.460; Phosphofructokinase domain; 1.
DR   HAMAP; MF_00339; Phosphofructokinase_I_B1; 1.
DR   InterPro; IPR022953; ATP_PFK.
DR   InterPro; IPR012003; ATP_PFK_prok-type.
DR   InterPro; IPR012828; PFKA_ATP_prok.
DR   InterPro; IPR015912; Phosphofructokinase_CS.
DR   InterPro; IPR000023; Phosphofructokinase_dom.
DR   InterPro; IPR035966; PKF_sf.
DR   NCBIfam; TIGR02482; PFKA_ATP; 1.
DR   PANTHER; PTHR13697:SF4; ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE; 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   Allosteric enzyme; ATP-binding; Cytoplasm; Glycolysis; Kinase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Reference proteome; Transferase.
FT   CHAIN           1..319
FT                   /note="ATP-dependent 6-phosphofructokinase"
FT                   /id="PRO_1000120026"
FT   ACT_SITE        127
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00339"
FT   BINDING         11
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00339"
FT   BINDING         21..25
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /ligand_note="allosteric activator; ligand shared between
FT                   dimeric partners"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00339"
FT   BINDING         72..73
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00339"
FT   BINDING         102..105
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00339"
FT   BINDING         103
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00339"
FT   BINDING         125..127
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00339"
FT   BINDING         154
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /ligand_note="allosteric activator; ligand shared between
FT                   dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00339"
FT   BINDING         162
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00339"
FT   BINDING         169..171
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00339"
FT   BINDING         185..187
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /ligand_note="allosteric activator; ligand shared between
FT                   dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00339"
FT   BINDING         211
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /ligand_note="allosteric activator; ligand shared between
FT                   dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00339"
FT   BINDING         213..215
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /ligand_note="allosteric activator; ligand shared between
FT                   dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00339"
FT   BINDING         222
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00339"
FT   BINDING         243
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00339"
FT   BINDING         249..252
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00339"
SQ   SEQUENCE   319 AA;  34174 MW;  B87117BB2F29CE7D CRC64;
     MKRIGVLTSG GDSPGMNAAI RAVVRKAIYH GLEVYGIYHG YAGLIAGQIK KLEIGDVGDI
     IHRGGTMLYT ARCPEFKTLE GQLKGIEQLK KHGIEGLVVI GGDGSYQGAK KLTEHGYPCV
     GVPGTIDNDI PGTDFTIGFD TALNTVIDAI DKIRDTATSH ERTYVIEVMG RHAGDIALWA
     GLAGGAESIL IPEADYDMDE IVSRLKRGHE RGKKHSIIIV AEGVGSGVDF GKRIEEATGL
     ETRVTVLGHV QRGGSPTAFD RVLASRLGAR AVELLIEGKG GRCVGIQNNQ LVDHDIIEAL
     AQTHTVDQKM YQLSKELSI
//