PFKA_LACDE
ID PFKA_LACDE Reviewed; 319 AA.
AC P80019;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 2.
DT 03-AUG-2022, entry version 128.
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};
OS Lactobacillus delbrueckii subsp. bulgaricus.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=1585;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8366023; DOI=10.1128/jb.175.17.5344-5349.1993;
RA Branny P., de la Torre F., Garel J.R.;
RT "Cloning, sequencing, and expression in Escherichia coli of the gene coding
RT for phosphofructokinase in Lactobacillus bulgaricus.";
RL J. Bacteriol. 175:5344-5349(1993).
RN [2]
RP PROTEIN SEQUENCE OF 1-38, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION.
RC STRAIN=B107;
RX PubMed=1828763; DOI=10.1111/j.1432-1033.1991.tb16067.x;
RA le Bras G., Deville-Bonne D., Garel J.R.;
RT "Purification and properties of the phosphofructokinase from Lactobacillus
RT bulgaricus. A non-allosteric analog of the enzyme from Escherichia coli.";
RL Eur. J. Biochem. 198:683-687(1991).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS), AND ACTIVITY REGULATION.
RC STRAIN=B107;
RX PubMed=16285731; DOI=10.1021/bi051283g;
RA Paricharttanakul N.M., Ye S., Menefee A.L., Javid-Majd F.,
RA Sacchettini J.C., Reinhart G.D.;
RT "Kinetic and structural characterization of phosphofructokinase from
RT Lactobacillus bulgaricus.";
RL Biochemistry 44:15280-15286(2005).
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:1828763}.
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. The binding affinities for these effectors are
CC decreased however, and therefore the allosteric effect becomes apparent
CC only at high effector concentrations. {ECO:0000255|HAMAP-Rule:MF_00339,
CC ECO:0000269|PubMed:16285731, ECO:0000269|PubMed:1828763}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.2 mM for ATP (at pH 8.2) {ECO:0000269|PubMed:1828763};
CC KM=0.07 mM for ATP (at pH 6.0) {ECO:0000269|PubMed:1828763};
CC KM=0.3 mM for fructose 6-phosphate (at pH 6.0 and 8.2)
CC {ECO:0000269|PubMed:1828763};
CC Vmax=90 umol/min/mg enzyme (at pH 8.2) {ECO:0000269|PubMed:1828763};
CC pH dependence:
CC Optimum pH is 8.2. {ECO:0000269|PubMed:1828763};
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:1828763}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00339,
CC ECO:0000269|PubMed:1828763}.
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; X71403; CAA50526.1; -; Genomic_DNA.
DR PIR; A48663; S35928.
DR RefSeq; WP_003619813.1; NZ_QOVB01000006.1.
DR PDB; 1ZXX; X-ray; 1.85 A; A=1-319.
DR PDBsum; 1ZXX; -.
DR AlphaFoldDB; P80019; -.
DR SMR; P80019; -.
DR GeneID; 66399781; -.
DR OMA; KFAVICV; -.
DR SABIO-RK; P80019; -.
DR UniPathway; UPA00109; UER00182.
DR EvolutionaryTrace; P80019; -.
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 CDD; cd00763; Bacterial_PFK; 1.
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;
KW Direct protein sequencing; Glycolysis; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Transferase.
FT CHAIN 1..319
FT /note="ATP-dependent 6-phosphofructokinase"
FT /id="PRO_0000111957"
FT ACT_SITE 127
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 125..127
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 154
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 162
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00339"
FT BINDING 169..171
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 185..187
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..215
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 222
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 243
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00339"
FT BINDING 249..252
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 STRAND 3..8
FT /evidence="ECO:0007829|PDB:1ZXX"
FT HELIX 16..28
FT /evidence="ECO:0007829|PDB:1ZXX"
FT TURN 29..31
FT /evidence="ECO:0007829|PDB:1ZXX"
FT STRAND 33..37
FT /evidence="ECO:0007829|PDB:1ZXX"
FT HELIX 40..46
FT /evidence="ECO:0007829|PDB:1ZXX"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:1ZXX"
FT HELIX 54..57
FT /evidence="ECO:0007829|PDB:1ZXX"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:1ZXX"
FT HELIX 79..91
FT /evidence="ECO:0007829|PDB:1ZXX"
FT STRAND 96..101
FT /evidence="ECO:0007829|PDB:1ZXX"
FT HELIX 103..114
FT /evidence="ECO:0007829|PDB:1ZXX"
FT STRAND 119..125
FT /evidence="ECO:0007829|PDB:1ZXX"
FT HELIX 139..159
FT /evidence="ECO:0007829|PDB:1ZXX"
FT STRAND 163..168
FT /evidence="ECO:0007829|PDB:1ZXX"
FT HELIX 175..183
FT /evidence="ECO:0007829|PDB:1ZXX"
FT STRAND 187..190
FT /evidence="ECO:0007829|PDB:1ZXX"
FT HELIX 198..210
FT /evidence="ECO:0007829|PDB:1ZXX"
FT STRAND 216..221
FT /evidence="ECO:0007829|PDB:1ZXX"
FT TURN 222..224
FT /evidence="ECO:0007829|PDB:1ZXX"
FT HELIX 227..236
FT /evidence="ECO:0007829|PDB:1ZXX"
FT STRAND 242..246
FT /evidence="ECO:0007829|PDB:1ZXX"
FT HELIX 248..252
FT /evidence="ECO:0007829|PDB:1ZXX"
FT HELIX 258..276
FT /evidence="ECO:0007829|PDB:1ZXX"
FT STRAND 281..287
FT /evidence="ECO:0007829|PDB:1ZXX"
FT STRAND 290..295
FT /evidence="ECO:0007829|PDB:1ZXX"
FT HELIX 296..299
FT /evidence="ECO:0007829|PDB:1ZXX"
FT HELIX 309..317
FT /evidence="ECO:0007829|PDB:1ZXX"
SQ SEQUENCE 319 AA; 34009 MW; 555C5FE1D522BC9C CRC64;
MKRIGILTSG GDAPGMNAAV RAVTRVAIAN GLEVFGIRYG FAGLVAGDIF PLESEDVAHL
INVSGTFLYS ARYPEFAEEE GQLAGIEQLK KHGIDAVVVI GGDGSYHGAL QLTRHGFNSI
GLPGTIDNDI PYTDATIGYD TACMTAMDAI DKIRDTASSH HRVFIVNVMG RNCGDIAMRV
GVACGADAIV IPERPYDVEE IANRLKQAQE SGKDHGLVVV AEGVMTADQF MAELKKYGDF
DVRANVLGHM QRGGTPTVSD RVLASKLGSE AVHLLLEGKG GLAVGIENGK VTSHDILDLF
DESHRGDYDL LKLNADLSR
