ID A0A3B4DK23_PYGNA Unreviewed; 768 AA.
AC A0A3B4DK23;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=ATP-dependent 6-phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_03184};
DE Short=ATP-PFK {ECO:0000256|HAMAP-Rule:MF_03184};
DE Short=Phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_03184};
DE EC=2.7.1.11 {ECO:0000256|HAMAP-Rule:MF_03184};
DE AltName: Full=Phosphohexokinase {ECO:0000256|HAMAP-Rule:MF_03184};
OS Pygocentrus nattereri (Red-bellied piranha).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Pygocentrus.
OX NCBI_TaxID=42514 {ECO:0000313|Ensembl:ENSPNAP00000023456.1, ECO:0000313|Proteomes:UP000261440};
RN [1] {ECO:0000313|Ensembl:ENSPNAP00000023456.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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_03184}.
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_03184, ECO:0000256|PIRNR:PIRNR000533};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|HAMAP-Rule:MF_03184};
CC -!- ACTIVITY REGULATION: Allosterically activated by ADP, AMP, or fructose
CC 2,6-bisphosphate, and allosterically inhibited by ATP or citrate.
CC {ECO:0000256|HAMAP-Rule:MF_03184}.
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_03184,
CC ECO:0000256|PIRNR:PIRNR000533}.
CC -!- SUBUNIT: Homo- and heterotetramers. {ECO:0000256|HAMAP-Rule:MF_03184}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03184}.
CC -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family.
CC ATP-dependent PFK group I subfamily. Eukaryotic two domain clade "E"
CC sub-subfamily. {ECO:0000256|PIRNR:PIRNR000533}.
CC -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family.
CC ATP-dependent PFK group I subfamily. Eukaryotic two domain clade 'E'
CC sub-subfamily. {ECO:0000256|HAMAP-Rule:MF_03184}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_03184}.
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DR AlphaFoldDB; A0A3B4DK23; -.
DR Ensembl; ENSPNAT00000012598.1; ENSPNAP00000023456.1; ENSPNAG00000008024.1.
DR GeneTree; ENSGT00940000159292; -.
DR OMA; CERLGEX; -.
DR UniPathway; UPA00109; UER00182.
DR Proteomes; UP000261440; Unplaced.
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; cd00764; Eukaryotic_PFK; 1.
DR Gene3D; 3.40.50.450; -; 2.
DR Gene3D; 3.40.50.460; Phosphofructokinase domain; 2.
DR HAMAP; MF_03184; Phosphofructokinase_I_E; 1.
DR InterPro; IPR009161; 6-Pfructokinase_euk.
DR InterPro; IPR022953; ATP_PFK.
DR InterPro; IPR041914; PFK_vert-type.
DR InterPro; IPR015912; Phosphofructokinase_CS.
DR InterPro; IPR000023; Phosphofructokinase_dom.
DR InterPro; IPR035966; PKF_sf.
DR NCBIfam; TIGR02478; 6PF1K_euk; 1.
DR PANTHER; PTHR13697:SF14; ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE, LIVER TYPE; 1.
DR PANTHER; PTHR13697; PHOSPHOFRUCTOKINASE; 1.
DR Pfam; PF00365; PFK; 2.
DR PIRSF; PIRSF000533; ATP_PFK_euk; 1.
DR PRINTS; PR00476; PHFRCTKINASE.
DR SUPFAM; SSF53784; Phosphofructokinase; 2.
DR PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 2.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Allosteric enzyme {ECO:0000256|HAMAP-Rule:MF_03184};
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_03184,
KW ECO:0000256|PIRNR:PIRNR000533};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03184};
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|HAMAP-
KW Rule:MF_03184};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_03184};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_03184};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_03184};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03184,
KW ECO:0000256|PIRNR:PIRNR000533};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_03184}.
FT DOMAIN 17..311
FT /note="Phosphofructokinase"
FT /evidence="ECO:0000259|Pfam:PF00365"
FT DOMAIN 390..673
FT /note="Phosphofructokinase"
FT /evidence="ECO:0000259|Pfam:PF00365"
FT REGION 1..378
FT /note="N-terminal catalytic PFK domain 1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184"
FT REGION 389..768
FT /note="C-terminal regulatory PFK domain 2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184"
FT ACT_SITE 165
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184"
FT BINDING 24
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184"
FT BINDING 87..88
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184"
FT BINDING 117..120
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184"
FT BINDING 118
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184"
FT BINDING 163..165
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184"
FT BINDING 252
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184"
FT BINDING 280
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184"
FT BINDING 286..289
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184"
FT BINDING 458
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /ligand_note="allosteric activator; ligand shared between
FT dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184"
FT BINDING 515..519
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /ligand_note="allosteric activator; ligand shared between
FT dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184"
FT BINDING 553
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /ligand_note="allosteric activator; ligand shared between
FT dimeric partners"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184"
FT BINDING 560..562
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /ligand_note="allosteric activator; ligand shared between
FT dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184"
FT BINDING 616
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /ligand_note="allosteric activator; ligand shared between
FT dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184"
FT BINDING 642
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /ligand_note="allosteric activator; ligand shared between
FT dimeric partners"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184"
FT BINDING 648..651
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /ligand_note="allosteric activator; ligand shared between
FT dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184"
FT BINDING 722
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /ligand_note="allosteric activator; ligand shared between
FT dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184"
SQ SEQUENCE 768 AA; 84018 MW; BC3F660823287651 CRC64;
MFLDFEKLRM AGAGKAIAVL TSGGDAQGMN AAVRAVTRMG IYVGAKVYLI YEGYEGLVDG
GDNIKIANWQ SVSNIIQLGG TVIGSARCKA FTAREGRLAA AFHLVQRGIT NLCVCGGDGS
LTGANIFRNE WSDLLAQLVQ EGRITDSLAQ QYTHLNIVGL VGSIDNDFCG TDMTIGADSA
LHRIMEVIDA ISTTAQRHNV RYLAVVSALA SGADWVFIPE APPEEGWEDH MCARLGESRS
KGSRLNIVII AEGAIDKHGE PITSNYVKDL VVQRLGYDTR VTVLGHVQRG GTPSAFDRVL
SSKLGVEAVV ALLEATPETS ACVIGLSGNQ AMRLPLMECV NMTKEVQKAM NEKRFEEAIQ
LRGKSFENNW NTYKLLAHQK PAQSKSDHSM AILNVGAPAA GMNAAVRSAV RVGLAQGLRV
YNVNDGFEGL AKGMVTEVHW HDVAGWTGQG GSLLGTKRTL PNSCMEQIVE TISKYNIQSL
LVIGGFEAYE GVLQLVEARG HYDELCIVMC VIPATISNNV PGTDFSLGAD TAVNAAMESC
DKIKQSASGT KRRVFIVETM GGYCGYLATT TGIAVGADAA YIFEESFNIR DLEMNVEHLT
EKMKKDIQRG LVLRNEKCHK HYTTDFIHNL YSAEGKGIFD CRVNVLGHLQ QGGVPTPFDR
NFGTKMGVKA VLWLTEKMKE THRQGRVFAN APETACVIGM NRKVMSFSPV TELKDHTDFE
HRMPKEQWWI NLRVMLKMLA KYQTHFDEYV TGDIEHVTRR TLSIETGF
//
