ID A0A8M9PRJ5_DANRE Unreviewed; 787 AA. AC A0A8M9PRJ5; DT 03-AUG-2022, integrated into UniProtKB/TrEMBL. DT 03-AUG-2022, sequence version 1. DT 03-MAY-2023, entry version 5. 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}; GN Name=pfkpb {ECO:0000313|RefSeq:XP_021323740.1}; OS Danio rerio (Zebrafish) (Brachydanio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Danionidae; Danioninae; Danio. OX NCBI_TaxID=7955 {ECO:0000313|Proteomes:UP000000437, ECO:0000313|RefSeq:XP_021323740.1}; RN [1] {ECO:0000313|RefSeq:XP_021323740.1} RP IDENTIFICATION. RC STRAIN=Tuebingen {ECO:0000313|RefSeq:XP_021323740.1}; RG RefSeq; RL Submitted (JAN-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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR RefSeq; XP_021323740.1; XM_021468065.1. DR UniPathway; UPA00109; UER00182. DR Proteomes; UP000000437; Chromosome 2. 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 PANTHER; PTHR13697:SF53; ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE; 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 TIGRFAMs; TIGR02478; 6PF1K_euk; 1. DR PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 2. PE 1: Evidence at protein level; 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 Proteomics identification {ECO:0007829|PeptideAtlas:A0A8M9PRJ5}; KW Reference proteome {ECO:0000313|Proteomes:UP000000437}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_03184}. FT DOMAIN 18..323 FT /note="Phosphofructokinase" FT /evidence="ECO:0000259|Pfam:PF00365" FT DOMAIN 409..693 FT /note="Phosphofructokinase" FT /evidence="ECO:0000259|Pfam:PF00365" FT REGION 1..390 FT /note="N-terminal catalytic PFK domain 1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184" FT REGION 408..787 FT /note="C-terminal regulatory PFK domain 2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184" FT ACT_SITE 166 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184" FT BINDING 25 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184" FT BINDING 88..89 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184" FT BINDING 118..121 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184" FT BINDING 119 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184" FT BINDING 164..166 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 201 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184" FT BINDING 208..210 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 264 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 292 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184" FT BINDING 298..301 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 477 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 534..538 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 572 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 579..581 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 635 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 661 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 667..670 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 741 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 787 AA; 86034 MW; 65D6298AEAD98FE0 CRC64; MPDTKKYIEN LSGAGKCIGV LTSGGDAQGM NAAVRAVVRM GIYVGAKVYF IHEGYQGMVD GGDNIKEASW ESVSSMLQVG GTVIGSARCK DFRTHEGRLC AALNLVQRGI TNLCVIGGDG SLTGANLFRE EWSGLLDELV QSGQISEDAA QTHSALHIVG MVGSIDNDFC GTDMTIGTDS ALHRIIEVVD AIMTTAQSHQ RTFVLEVMGR HCGYLALVSA LACGADWVLI PERPPKDGWE EQMCQKLSEN RADKKRLNII IVAEGAIDQN NKPITTDHIK DLVVSRLGFD TRVTILGHVQ RGGTPSAFDR ILASRMGVEA VLALLEASPG TPACVVSLCG NQAVRVPLME CVQMTQEVQK AMDEKRFEEA VKLRGRSFEN NLNTYKLLSH RKIDTELPHD GQCRSSFNVA VLNVGAPAAG MNAAVRSAVR VGITEGHTMF AVSDGFEGFY KGQIKEIKWG DVGGWTGQGG SLLGTKRTLP AKHVDKIAEQ MRIHNINALL VIGGFEAYLG LMELQAARSK HAELCVPMVM VPATVSNNIP GSDLSIGADT AINAITDTCD RIKQSASGTK RRVFIIETMG GYCGYLATVG GLAAGADAAY IYEEPFDIRD LQSNVEHLTE KMKTSIQRGL VLRNENSNEN YTTDFIYQLY SEEGKGVFDC RKNVLGHMQQ GGAPSPFDRN FGTKIAAKAM QWISKKLKEF YRDGRVFANT EDSACLLGMR RRALLFQPVV QLKDETDFVH RIPKEQWWLR LRPLMKILAK YKTSYDVSDS GQLEHIVRLR AKDSSAI //