PFKA_BUCCC
ID PFKA_BUCCC Reviewed; 320 AA.
AC Q057P0;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 91.
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=BCc_187;
OS Buchnera aphidicola subsp. Cinara cedri (strain Cc).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=372461;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cc;
RX PubMed=17038625; DOI=10.1126/science.1130441;
RA Perez-Brocal V., Gil R., Ramos S., Lamelas A., Postigo M., Michelena J.M.,
RA Silva F.J., Moya A., Latorre A.;
RT "A small microbial genome: the end of a long symbiotic relationship?";
RL Science 314:312-313(2006).
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; CP000263; ABJ90659.1; -; Genomic_DNA.
DR RefSeq; WP_011672578.1; NC_008513.1.
DR AlphaFoldDB; Q057P0; -.
DR SMR; Q057P0; -.
DR STRING; 372461.BCc_187; -.
DR EnsemblBacteria; ABJ90659; ABJ90659; BCc_187.
DR KEGG; bcc:BCc_187; -.
DR eggNOG; COG0205; Bacteria.
DR HOGENOM; CLU_020655_0_1_6; -.
DR OMA; TNRDNPF; -.
DR OrthoDB; 1421302at2; -.
DR UniPathway; UPA00109; UER00182.
DR Proteomes; UP000000669; 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; Reference proteome; Transferase.
FT CHAIN 1..320
FT /note="ATP-dependent 6-phosphofructokinase"
FT /id="PRO_1000059749"
FT ACT_SITE 128
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00339"
FT BINDING 12
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00339"
FT BINDING 73..74
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00339"
FT BINDING 103..106
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00339"
FT BINDING 104
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00339"
FT BINDING 126..128
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 155
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00339"
FT BINDING 163
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00339"
FT BINDING 170..172
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 186..188
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00339"
FT BINDING 212
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00339"
FT BINDING 223
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 244
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00339"
FT BINDING 250..253
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 320 AA; 35450 MW; 164259B6B644A758 CRC64;
MIKKIGILTS GGDSPGMNAI IRSVVCTALN HNIEVKGIYN GFLGLYNNDM KLLKYSHVAN
LLNQGGTILG SSRFLEFKLE KTRKIAIKNI YKRKIDCLII IGGDGSYKAA NFLTNMGVPC
IGIPGTIDND VSGTDYTVGY FTALETVVDA IDKLRDTSAS HHRISIIEIM GRYCGDLTLS
AAIAGGCEFI VIPEIIYQKE LLLLEIQKSI KKGNKHSIVA ITEHICDVNK LAKYIQKKTF
KETRATILGH IQRGGKPVAY DRILASRMGI YAIQLLLKGY KGQCIGVINN KIVHHNINYA
LKNMKKIFKK DLLNSIKKIY
