PFKA1_THET8
ID PFKA1_THET8 Reviewed; 322 AA.
AC P21777; Q5SGW8;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 3.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=ATP-dependent 6-phosphofructokinase 1 {ECO:0000255|HAMAP-Rule:MF_00339};
DE Short=ATP-PFK 1 {ECO:0000255|HAMAP-Rule:MF_00339};
DE Short=Phosphofructokinase 1 {ECO:0000255|HAMAP-Rule:MF_00339};
DE EC=2.7.1.11 {ECO:0000255|HAMAP-Rule:MF_00339};
DE AltName: Full=Phosphohexokinase 1 {ECO:0000255|HAMAP-Rule:MF_00339};
GN Name=pfkA {ECO:0000255|HAMAP-Rule:MF_00339}; OrderedLocusNames=TTHA1962;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1828151; DOI=10.1016/0006-291x(91)90429-b;
RA Xu J., Seki M., Denda K., Yoshida M.;
RT "Molecular cloning of phosphofructokinase 1 gene from a thermophilic
RT bacterium, Thermus thermophilus.";
RL Biochem. Biophys. Res. Commun. 176:1313-1318(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 1-25.
RX PubMed=1830879;
RA Xu J., Oshima T., Yoshida M.;
RT "Phosphoenolpyruvate-insensitive phosphofructokinase isozyme from Thermus
RT thermophilus HB8.";
RL J. Biochem. 109:199-203(1991).
RN [4]
RP FUNCTION, ACTIVITY REGULATION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RX PubMed=4335287; DOI=10.1021/bi00756a022;
RA Yoshida M.;
RT "Allosteric nature of thermostable phosphofructokinase from an extreme
RT thermophilic bacterium.";
RL Biochemistry 11:1087-1093(1972).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RX PubMed=2146397; DOI=10.1016/s0022-2836(05)80171-8;
RA Xu J., Oshima T., Yoshida M.;
RT "Tetramer-dimer conversion of phosphofructokinase from Thermus thermophilus
RT induced by its allosteric effectors.";
RL J. Mol. Biol. 215:597-606(1990).
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:2146397, ECO:0000269|PubMed:4335287}.
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:2146397,
CC ECO:0000269|PubMed:4335287};
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 (By similarity). Allosterically inhibited by
CC phosphoenolpyruvate which induces the dissociation of the active
CC tetramer into an inactive two-subunit forms. {ECO:0000250,
CC ECO:0000269|PubMed:4335287}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.08 mM for ATP {ECO:0000269|PubMed:4335287};
CC KM=0.025 mM for fructose 6-phosphate {ECO:0000269|PubMed:4335287};
CC pH dependence:
CC Optimum pH is 8.4. {ECO:0000269|PubMed:4335287};
CC Temperature dependence:
CC Optimum temperature is 85 degrees Celsius.
CC {ECO:0000269|PubMed:4335287};
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 ECO:0000269|PubMed:2146397}.
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; M71213; AAA27501.1; -; Genomic_DNA.
DR EMBL; AP008226; BAD71785.1; -; Genomic_DNA.
DR RefSeq; WP_011173968.1; NC_006461.1.
DR RefSeq; YP_145228.1; NC_006461.1.
DR AlphaFoldDB; P21777; -.
DR SMR; P21777; -.
DR STRING; 300852.55773344; -.
DR EnsemblBacteria; BAD71785; BAD71785; BAD71785.
DR GeneID; 3169721; -.
DR KEGG; ttj:TTHA1962; -.
DR PATRIC; fig|300852.9.peg.1933; -.
DR eggNOG; COG0205; Bacteria.
DR HOGENOM; CLU_020655_0_1_0; -.
DR OMA; KFAVICV; -.
DR PhylomeDB; P21777; -.
DR BRENDA; 2.7.1.11; 2305.
DR UniPathway; UPA00109; UER00182.
DR Proteomes; UP000000532; 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 1: Evidence at protein level;
KW Allosteric enzyme; ATP-binding; Cytoplasm; Direct protein sequencing;
KW Glycolysis; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..322
FT /note="ATP-dependent 6-phosphofructokinase 1"
FT /id="PRO_0000112001"
FT ACT_SITE 128
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 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; ligand shared between
FT dimeric partners"
FT /note="in other chain"
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; ligand shared between
FT dimeric partners"
FT /note="in other chain"
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; ligand shared between
FT dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00339"
FT BINDING 214..216
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 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 246
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00339"
FT BINDING 252..255
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 CONFLICT 111
FT /note="C -> F (in Ref. 1; AAA27501)"
FT /evidence="ECO:0000305"
FT CONFLICT 273
FT /note="A -> P (in Ref. 1; AAA27501)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 322 AA; 33537 MW; 608CD4053E6ACEA3 CRC64;
MKRIGVFTSG GDAPGMNAAI RAVVRQAHAL GVEVIGIRRG YAGMIQGEMV PLGVRDVANI
IQRGGTILLT ARSQEFLTEE GRAKAYAKLQ AAGIEGLVAI GGDGTFRGAL CLVEEHGMPV
VGVPGTIDND LYGTDYTIGF DTAVNTALEA IDRIRDTAAS HERVFFIEVM GRHAGFIALD
VGLAGGAEVI AVPEEPVDPK AVAEVLEASQ RRGKKSSIVV VAEGAYPGGA AGLLAAIREH
LQVEARVTVL GHIQRGGSPT AKDRILASRL GAAAVEALVG GASGVMVGEV EGEVDLTPLK
EAVERRKDIN RALLRLSQVL AL
