ID L0K8E7_HALHC Unreviewed; 334 AA.
AC L0K8E7;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=ATP-dependent 6-phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_00339};
DE Short=ATP-PFK {ECO:0000256|HAMAP-Rule:MF_00339};
DE Short=Phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_00339};
DE EC=2.7.1.11 {ECO:0000256|HAMAP-Rule:MF_00339};
DE AltName: Full=Phosphohexokinase {ECO:0000256|HAMAP-Rule:MF_00339};
GN Name=pfkA {ECO:0000256|HAMAP-Rule:MF_00339};
GN OrderedLocusNames=Halha_0398 {ECO:0000313|EMBL:AGB40393.1};
OS Halobacteroides halobius (strain ATCC 35273 / DSM 5150 / MD-1).
OC Bacteria; Bacillota; Clostridia; Halanaerobiales; Halobacteroidaceae;
OC Halobacteroides.
OX NCBI_TaxID=748449 {ECO:0000313|EMBL:AGB40393.1, ECO:0000313|Proteomes:UP000010880};
RN [1] {ECO:0000313|Proteomes:UP000010880}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35273 / DSM 5150 / MD-1
RC {ECO:0000313|Proteomes:UP000010880};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Gu W.,
RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Tindall B., Pomrenke H., Brambilla E., Klenk H.-P.,
RA Eisen J.A.;
RT "The complete genome of Halobacteroides halobius DSM 5150.";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
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:0000256|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;
CC Evidence={ECO:0000256|ARBA:ARBA00000432, ECO:0000256|HAMAP-
CC Rule:MF_00339};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|HAMAP-Rule:MF_00339};
CC -!- ACTIVITY REGULATION: Allosterically activated by ADP and other
CC diphosphonucleosides, and allosterically inhibited by
CC phosphoenolpyruvate. {ECO:0000256|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:0000256|ARBA:ARBA00004679, ECO:0000256|HAMAP-Rule:MF_00339}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00339}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|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:0000256|HAMAP-Rule:MF_00339}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00339}.
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DR EMBL; CP003359; AGB40393.1; -; Genomic_DNA.
DR RefSeq; WP_015326119.1; NC_019978.1.
DR AlphaFoldDB; L0K8E7; -.
DR STRING; 748449.Halha_0398; -.
DR KEGG; hhl:Halha_0398; -.
DR PATRIC; fig|748449.3.peg.370; -.
DR eggNOG; COG0205; Bacteria.
DR HOGENOM; CLU_020655_0_1_9; -.
DR OrthoDB; 9802503at2; -.
DR UniPathway; UPA00109; UER00182.
DR Proteomes; UP000010880; 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; 3.40.50.450; -; 1.
DR Gene3D; 3.40.50.460; Phosphofructokinase domain; 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 NCBIfam; TIGR02482; PFKA_ATP; 1.
DR PANTHER; PTHR13697:SF4; ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE; 1.
DR PANTHER; PTHR13697; PHOSPHOFRUCTOKINASE; 1.
DR Pfam; PF00365; PFK; 1.
DR PIRSF; PIRSF000532; ATP_PFK_prok; 1.
DR PRINTS; PR00476; PHFRCTKINASE.
DR SUPFAM; SSF53784; Phosphofructokinase; 1.
DR PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 1.
PE 3: Inferred from homology;
KW Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533, ECO:0000256|HAMAP-
KW Rule:MF_00339};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00339};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00339};
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|HAMAP-
KW Rule:MF_00339};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00339};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00339};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00339};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00339}; Reference proteome {ECO:0000313|Proteomes:UP000010880};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00339}.
FT DOMAIN 3..290
FT /note="Phosphofructokinase"
FT /evidence="ECO:0000259|Pfam:PF00365"
FT ACT_SITE 128
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339"
FT BINDING 11
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|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:0000256|HAMAP-Rule:MF_00339"
FT BINDING 72..73
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339"
FT BINDING 102..105
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339"
FT BINDING 103
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_00339"
FT BINDING 163
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000256|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:0000256|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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_00339"
FT BINDING 259
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339"
FT BINDING 265..268
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00339"
SQ SEQUENCE 334 AA; 35870 MW; 2608999DACF850A8 CRC64;
MNKIGVLTSG GDAPGMNAAV RAVVRKALHE GLEVVGIKRG YSGVIEGDFI TLDRSSVSDI
IQRGGTFLRS ARCEEFRTKE GRKRAAKKLR EEGIEGLVVI GGDGSFTGAK LLNEETGIKT
IGVPATIDND IACTDDSIGY DTAMNTIIDA ITKIRDTASS HERAFVIEAM GRHAGFLTLA
AGLAGGAESI LVPEIDFEMD EVCEKIQHDY EEGKIHSIVL VAEGVELGNV EFETNRNPDE
SPAFLIGREI NERTGFETRV TILGHIQRGG APTGRDRLLA SRLGASAVDQ LLAGKSNKMV
GLIHNTVKVA PIEEAIESNK ELNEEVYKLA NILT
//
