ID A0A0N4TMH1_BRUPA Unreviewed; 813 AA. AC A0A0N4TMH1; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 24-JAN-2024, entry version 36. 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 ORFNames=BPAG_LOCUS9605 {ECO:0000313|EMBL:VDN90791.1}; OS Brugia pahangi (Filarial nematode worm). OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia. OX NCBI_TaxID=6280 {ECO:0000313|Proteomes:UP000038020, ECO:0000313|WBParaSite:BPAG_0000964301-mRNA-1}; RN [1] {ECO:0000313|WBParaSite:BPAG_0000964301-mRNA-1} RP IDENTIFICATION. RG WormBaseParasite; RL Submitted (FEB-2017) to UniProtKB. RN [2] {ECO:0000313|EMBL:VDN90791.1, ECO:0000313|Proteomes:UP000278627} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RG Pathogen Informatics; RL Submitted (NOV-2018) 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|ARBA:ARBA00002659, ECO:0000256|HAMAP- CC 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: Homotetramer. {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 EMBL; UZAD01013160; VDN90791.1; -; Genomic_DNA. DR AlphaFoldDB; A0A0N4TMH1; -. DR STRING; 6280.A0A0N4TMH1; -. DR WBParaSite; BPAG_0000964301-mRNA-1; BPAG_0000964301-mRNA-1; BPAG_0000964301. DR UniPathway; UPA00109; UER00182. DR Proteomes; UP000038020; Unplaced. DR Proteomes; UP000278627; Unassembled WGS sequence. 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; -; 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; IPR015912; Phosphofructokinase_CS. DR InterPro; IPR000023; Phosphofructokinase_dom. DR InterPro; IPR035966; PKF_sf. DR NCBIfam; TIGR02478; 6PF1K_euk; 1. DR PANTHER; PTHR13697:SF4; ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE, MUSCLE 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 Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533, ECO:0000256|HAMAP- KW Rule:MF_03184}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_03184}; 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|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_03184}; Reference proteome {ECO:0000313|Proteomes:UP000278627}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_03184}. FT DOMAIN 55..360 FT /note="Phosphofructokinase" FT /evidence="ECO:0000259|Pfam:PF00365" FT DOMAIN 441..724 FT /note="Phosphofructokinase" FT /evidence="ECO:0000259|Pfam:PF00365" FT REGION 1..427 FT /note="N-terminal catalytic PFK domain 1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184" FT REGION 441..813 FT /note="C-terminal regulatory PFK domain 2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184" FT ACT_SITE 203 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184" FT BINDING 62 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184" FT BINDING 125..126 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184" FT BINDING 155..158 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184" FT BINDING 156 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184" FT BINDING 201..203 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 238 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184" FT BINDING 245..247 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 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 329 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184" FT BINDING 335..338 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 508 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 565..569 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 603 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 610..612 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 666 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 692 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 698..701 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 774 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 813 AA; 89500 MW; 71CBBC91579D7CC8 CRC64; MKNSGLPITS LDDDFGPPTT DMHRMKFSIR SDSIVPSAGR EGTSIAPQIY KGRTMAVFTS GGDASGMNSA VRSVVRMGVY LGCRVFLIYE GYQGMVDGGD NIKEADWQSV SDIIQRGGTV IGSARCKVFQ ERWGRLQAAE NLIKHRITNL VCIGGDGSLT GANLFRQEWQ GLVKELLLSG KITREEAVEC GNIQIVGLVG SIDNDFCGTD MTIGTDTALQ RICEAIDCVM STAQSHQRTF VIEVMGRHCG YLALVAALAS EADFCFIPEW PVPTDWPTVL CQKLRMMREA GSRLNIVIVA EGALDREGKC ITAESVRAVV KETLHYDTRV TVLGHVQRGG SPSAFDRLLG CRMGAEAVLA LMEMTPQSEP CVVSIDGNVI VRVPLMQCVQ RTQAVKKAMD ERDWETAVKL RGRSFQRNLE TYRLLTKVEP KKVDPNVPVY NVAIVNVGAP AGGMNAVVRS YVRMALYHGC KVYGIKNSFE GLCRGEDMAW GDVCNWVMYG GSFLGTQKQL PGKIMDKVAD AFEKYNFHGL LLVGGFEAFH SCLLLSRARD KYPSLRIPMC VIPCTISNNV PGTSLSLGSD TAVNEICEMI DKIKLSATGT KRRVFIVETM GGFCGYLATI SALASGADNA YIFEEQFKVS DIMDDVKVIS RKMRTGVQRY LIVRNECANK NYTTEFVNQL FAEEGKGAFS TRTNVLGHAQ QGGNPTPFDR NMGTKLAARA LEFIISQILK YIDPKTGILN AVSPDSATLL GLMGRRTVFT PVEELSLETD FEHRVPKHQW WMKMRPLLRI LAKHDSTYQT EAMVVPEVEG ESA //