PFKA_STAA8
ID PFKA_STAA8 Reviewed; 322 AA.
AC Q2FXM8;
DT 03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT 03-SEP-2014, sequence version 2.
DT 03-AUG-2022, entry version 114.
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, ECO:0000269|PubMed:29940104};
DE AltName: Full=Phosphohexokinase {ECO:0000255|HAMAP-Rule:MF_00339};
GN Name=pfkA {ECO:0000255|HAMAP-Rule:MF_00339};
GN OrderedLocusNames=SAOUHSC_01807;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
RN [2]
RP INTERACTION WITH CSHA, AND SUBUNIT.
RC STRAIN=UAMS-1;
RX PubMed=21764917; DOI=10.1128/jb.05485-11;
RA Roux C.M., DeMuth J.P., Dunman P.M.;
RT "Characterization of components of the Staphylococcus aureus mRNA
RT degradosome holoenzyme-like complex.";
RL J. Bacteriol. 193:5520-5526(2011).
RN [3] {ECO:0007744|PDB:5XZ6, ECO:0007744|PDB:5XZ7, ECO:0007744|PDB:5XZ8, ECO:0007744|PDB:5XZ9, ECO:0007744|PDB:5XZA}
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEXES WITH ATP ANALOG;
RP FRUCTOSE-6-PHOSPHATE; ADP AND ATP, FUNCTION, COFACTOR, ACTIVITY REGULATION,
RP SUBUNIT, MUTAGENESIS OF GLY-150; LEU-151; ARG-164 AND ARG-245, AND
RP CATALYTIC ACTIVITY.
RX PubMed=29940104; DOI=10.1021/acs.biochem.8b00028;
RA Tian T., Wang C., Wu M., Zhang X., Zang J.;
RT "Structural insights into the regulation of Staphylococcus aureus
RT phosphofructokinase by tetramer-dimer conversion.";
RL Biochemistry 57:4252-4262(2018).
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 ECO:0000269|PubMed:29940104}.
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, ECO:0000269|PubMed:29940104};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00339,
CC ECO:0000269|PubMed:29940104};
CC -!- ACTIVITY REGULATION: Exists as both a dimer and a tetramer and the
CC equilibrium between the active tetramer and inactive dimer is regulated
CC by several allosteric effectors, including protein concentration, pH,
CC ADP, ATP, AMP-PNP, and F6P. ADP, ATP, low pH, and AMP-PNP shift the
CC equilibrium toward the dimer. {ECO:0000269|PubMed:29940104}.
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 (By similarity). Homodimer, inactive form
CC (PubMed:29940104). Component of a possible RNA degradosome complex
CC composed of cshA, eno, pfkA, pnp, rnjA, rnjB, rnpA and rny. Interacts
CC specifically with RNA helicase CshA. {ECO:0000255|HAMAP-Rule:MF_00339,
CC ECO:0000269|PubMed:21764917, ECO:0000269|PubMed:29940104}.
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=ABD30875.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP000253; ABD30875.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_000717561.1; NZ_LS483365.1.
DR RefSeq; YP_500312.1; NC_007795.1.
DR PDB; 5XOE; X-ray; 2.98 A; A=1-322.
DR PDB; 5XZ6; X-ray; 2.70 A; A=1-322.
DR PDB; 5XZ7; X-ray; 1.60 A; A=1-322.
DR PDB; 5XZ8; X-ray; 1.95 A; A=1-322.
DR PDB; 5XZ9; X-ray; 2.00 A; A=1-322.
DR PDB; 5XZA; X-ray; 1.90 A; A=1-322.
DR PDBsum; 5XOE; -.
DR PDBsum; 5XZ6; -.
DR PDBsum; 5XZ7; -.
DR PDBsum; 5XZ8; -.
DR PDBsum; 5XZ9; -.
DR PDBsum; 5XZA; -.
DR AlphaFoldDB; Q2FXM8; -.
DR SMR; Q2FXM8; -.
DR STRING; 1280.SAXN108_1727; -.
DR EnsemblBacteria; ABD30875; ABD30875; SAOUHSC_01807.
DR GeneID; 3919277; -.
DR KEGG; sao:SAOUHSC_01807; -.
DR PATRIC; fig|93061.5.peg.1647; -.
DR eggNOG; COG0205; Bacteria.
DR HOGENOM; CLU_020655_0_1_9; -.
DR BRENDA; 2.7.1.11; 3352.
DR UniPathway; UPA00109; UER00182.
DR Proteomes; UP000008816; Chromosome.
DR GO; GO:0005945; C:6-phosphofructokinase complex; IBA:GO_Central.
DR GO; GO:0003872; F:6-phosphofructokinase activity; IBA:GO_Central.
DR GO; GO:0016208; F:AMP binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0070095; F:fructose-6-phosphate binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0048029; F:monosaccharide binding; IBA:GO_Central.
DR GO; GO:0061621; P:canonical glycolysis; IBA:GO_Central.
DR GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IBA:GO_Central.
DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Allosteric enzyme; ATP-binding; Cytoplasm; Glycolysis;
KW Kinase; Magnesium; Metal-binding; Nucleotide-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..322
FT /note="ATP-dependent 6-phosphofructokinase"
FT /id="PRO_0000430112"
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 ECO:0000269|PubMed:29940104"
FT BINDING 102..105
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00339,
FT ECO:0000269|PubMed:29940104"
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 ECO:0000269|PubMed:29940104"
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 ECO:0000269|PubMed:29940104"
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 ECO:0000269|PubMed:29940104"
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,
FT ECO:0000269|PubMed:29940104"
FT MUTAGEN 150
FT /note="G->D: Exhibits higher affinity for fructose 6-
FT phosphate and higher catalytic activity with a loss of
FT dimer conversion; in association with A-151."
FT /evidence="ECO:0000269|PubMed:29940104"
FT MUTAGEN 151
FT /note="L->A: Exhibits higher affinity for fructose 6-
FT phosphate and higher catalytic activity with a loss of
FT tetramer-dimer conversion; in association with D-150."
FT /evidence="ECO:0000269|PubMed:29940104"
FT MUTAGEN 164
FT /note="R->A: Complete loss of fructose 6-phosphate
FT binding."
FT /evidence="ECO:0000269|PubMed:29940104"
FT MUTAGEN 245
FT /note="R->A: Complete loss of fructose 6-phosphate
FT binding."
FT /evidence="ECO:0000269|PubMed:29940104"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:5XZ8"
FT HELIX 16..29
FT /evidence="ECO:0007829|PDB:5XZ8"
FT STRAND 33..37
FT /evidence="ECO:0007829|PDB:5XZ8"
FT HELIX 40..45
FT /evidence="ECO:0007829|PDB:5XZ8"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:5XZ8"
FT HELIX 54..57
FT /evidence="ECO:0007829|PDB:5XZ8"
FT HELIX 74..77
FT /evidence="ECO:0007829|PDB:5XZ8"
FT HELIX 79..90
FT /evidence="ECO:0007829|PDB:5XZ8"
FT TURN 91..93
FT /evidence="ECO:0007829|PDB:5XZ8"
FT STRAND 96..101
FT /evidence="ECO:0007829|PDB:5XZ8"
FT HELIX 103..115
FT /evidence="ECO:0007829|PDB:5XZ8"
FT STRAND 120..129
FT /evidence="ECO:0007829|PDB:5XZ8"
FT HELIX 141..161
FT /evidence="ECO:0007829|PDB:5XZ8"
FT STRAND 165..170
FT /evidence="ECO:0007829|PDB:5XZ8"
FT HELIX 177..186
FT /evidence="ECO:0007829|PDB:5XZ8"
FT STRAND 189..192
FT /evidence="ECO:0007829|PDB:5XZ8"
FT HELIX 200..211
FT /evidence="ECO:0007829|PDB:5XZ8"
FT TURN 212..214
FT /evidence="ECO:0007829|PDB:5XZ8"
FT STRAND 219..223
FT /evidence="ECO:0007829|PDB:5XZ8"
FT TURN 224..226
FT /evidence="ECO:0007829|PDB:5XZ8"
FT HELIX 229..239
FT /evidence="ECO:0007829|PDB:5XZ8"
FT STRAND 244..248
FT /evidence="ECO:0007829|PDB:5XZ8"
FT HELIX 250..254
FT /evidence="ECO:0007829|PDB:5XZ8"
FT HELIX 260..278
FT /evidence="ECO:0007829|PDB:5XZ8"
FT STRAND 283..289
FT /evidence="ECO:0007829|PDB:5XZ8"
FT STRAND 292..297
FT /evidence="ECO:0007829|PDB:5XZ8"
FT HELIX 298..302
FT /evidence="ECO:0007829|PDB:5XZ8"
FT HELIX 311..320
FT /evidence="ECO:0007829|PDB:5XZ8"
SQ SEQUENCE 322 AA; 34840 MW; 1FAE41C0BA7CA7F1 CRC64;
MKKIAVLTSG GDSPGMNAAV RAVVRTAIYN EIEVYGVYHG YQGLLNDDIH KLELGSVGDT
IQRGGTFLYS ARCPEFKEQE VRKVAIENLR KRGIEGLVVI GGDGSYRGAQ RISEECKEIQ
TIGIPGTIDN DINGTDFTIG FDTALNTIIG LVDKIRDTAS SHARTFIIEA MGRDCGDLAL
WAGLSVGAET IVVPEVKTDI KEIADKIEQG IKRGKKHSIV LVAEGCMTAQ DCQKELSQYI
NVDNRVSVLG HVQRGGSPTG ADRVLASRLG GYAVDLLMQG ETAKGVGIKN NKIVATSFDE
IFDGKDHKFD YSLYELANKL SI
