PFKA_STACT
ID PFKA_STACT Reviewed; 322 AA.
AC B9DN94;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 80.
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}; OrderedLocusNames=Sca_1304;
OS Staphylococcus carnosus (strain TM300).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=396513;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TM300;
RX PubMed=19060169; DOI=10.1128/aem.01982-08;
RA Rosenstein R., Nerz C., Biswas L., Resch A., Raddatz G., Schuster S.C.,
RA Goetz F.;
RT "Genome analysis of the meat starter culture bacterium Staphylococcus
RT carnosus TM300.";
RL Appl. Environ. Microbiol. 75:811-822(2009).
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;
CC Evidence={ECO:0000255|HAMAP-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; AM295250; CAL28209.1; -; Genomic_DNA.
DR RefSeq; WP_015900549.1; NC_012121.1.
DR AlphaFoldDB; B9DN94; -.
DR SMR; B9DN94; -.
DR STRING; 396513.SCA_1304; -.
DR GeneID; 60545013; -.
DR KEGG; sca:SCA_1304; -.
DR eggNOG; COG0205; Bacteria.
DR HOGENOM; CLU_020655_0_1_9; -.
DR OMA; KFAVICV; -.
DR OrthoDB; 1421302at2; -.
DR BioCyc; SCAR396513:SCA_RS06495-MON; -.
DR UniPathway; UPA00109; UER00182.
DR Proteomes; UP000000444; 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 Gene3D; 3.40.50.460; -; 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 Pfam; PF00365; PFK; 1.
DR PIRSF; PIRSF000532; ATP_PFK_prok; 1.
DR PRINTS; PR00476; PHFRCTKINASE.
DR SUPFAM; SSF53784; SSF53784; 1.
DR TIGRFAMs; TIGR02482; PFKA_ATP; 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; Transferase.
FT CHAIN 1..322
FT /note="ATP-dependent 6-phosphofructokinase"
FT /id="PRO_1000192379"
FT ACT_SITE 129
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 127..129
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 156
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 164
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00339"
FT BINDING 171..173
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 187..189
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
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 215..217
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 224
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 245
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00339"
FT BINDING 251..254
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 322 AA; 34567 MW; 262DC5A660B65663 CRC64;
MKKIAVLTSG GDAPGMNAAI RAVVRTAIYN GIEVYGVYQG YLGLINDDLK KLELGSVGDT
IQRGGTFLYS ARCPEFKDKE VRAKAIENLR SRGIDGLVVI GGDGSYRGAQ RISEECPEIQ
TIGIPGTIDN DIPGTDYTIG FDSALNTIIE SVDKIRDTAS SHARTFIVEV MGRDCGDLAL
WAGLAVGAET IIVPEEKVDI KDVAEKIESG IKRGKKHSIV VVAEGVMGGQ LCADELAKYI
HVDARVSVLG HIQRGGSPTG QDRVLASRLG GHAVELLMDG KTALGVGIKQ NQLTQTKFED
IFNNKGSKFD KQMYKLAQEL SI
