PFKA_STAES
ID PFKA_STAES Reviewed; 322 AA.
AC Q8CS68;
DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2003, sequence version 2.
DT 03-AUG-2022, entry version 124.
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=SE_1374;
OS Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176280;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12228 / FDA PCI 1200;
RX PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT "Genome-based analysis of virulence genes in a non-biofilm-forming
RT Staphylococcus epidermidis strain (ATCC 12228).";
RL Mol. Microbiol. 49:1577-1593(2003).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO04973.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE015929; AAO04973.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_764929.1; NC_004461.1.
DR RefSeq; WP_002440192.1; NZ_WBME01000042.1.
DR AlphaFoldDB; Q8CS68; -.
DR SMR; Q8CS68; -.
DR STRING; 176280.SE_1374; -.
DR EnsemblBacteria; AAO04973; AAO04973; SE_1374.
DR GeneID; 50018512; -.
DR KEGG; sep:SE_1374; -.
DR PATRIC; fig|176280.10.peg.1342; -.
DR eggNOG; COG0205; Bacteria.
DR HOGENOM; CLU_020655_0_1_9; -.
DR UniPathway; UPA00109; UER00182.
DR Proteomes; UP000001411; 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_0000111982"
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; 34882 MW; BC40971A7BDD042E CRC64;
MKKIAVLTSG GDSPGMNAAV RAVTRTAIYN NIEVYGVYQG YQGLLDDDIH KLELGSVGDT
IQRGGTFLFS ARCPQFKEED VRKKAIENLR KRGIEGLVVI GGDGSYRGAQ RISEECKEIQ
TIGIPGTIDN DINGTDFTIG FDTALNTIIE SVDKIRDTAS SHARTFIVEV MGRDCGDLAL
WAGLSVGAET IVLPEVNTDI KDVAEKIEQG IKRGKKHSIV MVAEGCMSGQ ECADELTKYI
NIDTRVSVLG HIQRGGSPSG ADRVLASRLG GYAVELLKQG ETAKGVGIRN NQLTSTPFDE
IFAESDRKFN SQMYELAKEL SI
