ID PFKA2_CAEEL Reviewed; 756 AA. AC Q27483; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 27-MAR-2024, entry version 144. DE RecName: Full=ATP-dependent 6-phosphofructokinase 2; DE Short=ATP-PFK 2; DE Short=Phosphofructokinase 2; DE EC=2.7.1.11 {ECO:0000250|UniProtKB:P16861}; DE AltName: Full=Phosphohexokinase 2; GN Name=pfk-1.2 {ECO:0000312|WormBase:C50F4.2}; GN ORFNames=C50F4.2 {ECO:0000312|WormBase:C50F4.2}; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae; OC Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bristol N2; RX PubMed=9851916; DOI=10.1126/science.282.5396.2012; RG The C. elegans sequencing consortium; RT "Genome sequence of the nematode C. elegans: a platform for investigating RT biology."; RL Science 282:2012-2018(1998). 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:0000250|UniProtKB:P16861}. 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:0000250|UniProtKB:P16861}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:P16861}; CC -!- ACTIVITY REGULATION: Allosterically activated by ADP, AMP, or fructose CC 2,6-bisphosphate, and allosterically inhibited by ATP or citrate. CC {ECO:0000250|UniProtKB:P16861}. CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- CC phosphate and glycerone phosphate from D-glucose: step 3/4. CC {ECO:0000250|UniProtKB:P16861}. CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P16861}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P16861}. 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:0000305}. 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; Z70750; CAA94737.1; -; Genomic_DNA. DR PIR; T20109; T20109. DR RefSeq; NP_505457.1; NM_073056.3. DR AlphaFoldDB; Q27483; -. DR SMR; Q27483; -. DR STRING; 6239.C50F4.2.1; -. DR EPD; Q27483; -. DR PaxDb; 6239-C50F4-2; -. DR PeptideAtlas; Q27483; -. DR EnsemblMetazoa; C50F4.2.1; C50F4.2.1; WBGene00008230. DR GeneID; 179335; -. DR KEGG; cel:CELE_C50F4.2; -. DR UCSC; C50F4.2; c. elegans. DR AGR; WB:WBGene00008230; -. DR WormBase; C50F4.2; CE05467; WBGene00008230; pfk-1.2. DR eggNOG; KOG2440; Eukaryota. DR HOGENOM; CLU_011053_0_0_1; -. DR InParanoid; Q27483; -. DR OMA; RCYLIRE; -. DR OrthoDB; 374214at2759; -. DR PhylomeDB; Q27483; -. DR Reactome; R-CEL-6798695; Neutrophil degranulation. DR Reactome; R-CEL-70171; Glycolysis. DR UniPathway; UPA00109; UER00182. DR PRO; PR:Q27483; -. DR Proteomes; UP000001940; Chromosome V. DR Bgee; WBGene00008230; Expressed in larva and 1 other cell type or tissue. DR GO; GO:0005945; C:6-phosphofructokinase complex; IBA:GO_Central. DR GO; GO:0003872; F:6-phosphofructokinase activity; IBA:GO_Central. DR GO; GO:0016208; F:AMP binding; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IBA:GO_Central. DR GO; GO:0070095; F:fructose-6-phosphate binding; IBA:GO_Central. DR GO; GO:0042802; F:identical protein binding; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0048029; F:monosaccharide binding; IBA:GO_Central. DR GO; GO:0061621; P:canonical glycolysis; IBA:GO_Central. DR GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IBA:GO_Central. DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IBA:GO_Central. DR Gene3D; 3.40.50.450; -; 2. DR Gene3D; 3.40.50.460; Phosphofructokinase domain; 2. 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:SF8; ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE 2; 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; 1. PE 3: Inferred from homology; KW Allosteric enzyme; ATP-binding; Cytoplasm; Glycolysis; Kinase; Magnesium; KW Metal-binding; Nucleotide-binding; Reference proteome; Transferase. FT CHAIN 1..756 FT /note="ATP-dependent 6-phosphofructokinase 2" FT /id="PRO_0000112029" FT REGION 1..393 FT /note="N-terminal catalytic PFK domain 1" FT /evidence="ECO:0000250|UniProtKB:P16861" FT REGION 394..404 FT /note="Interdomain linker" FT /evidence="ECO:0000250|UniProtKB:P16861" FT REGION 405..756 FT /note="C-terminal regulatory PFK domain 2" FT /evidence="ECO:0000250|UniProtKB:P16861" FT ACT_SITE 159 FT /note="Proton acceptor" FT /evidence="ECO:0000250|UniProtKB:P16861" FT BINDING 20 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P16861" FT BINDING 81..82 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P16861" FT BINDING 111..114 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P16861" FT BINDING 112 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="catalytic" FT /evidence="ECO:0000250|UniProtKB:P16861" FT BINDING 157..159 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000250|UniProtKB:P16861" FT BINDING 194 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000250|UniProtKB:P16861" FT BINDING 201..203 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000250|UniProtKB:P16861" FT BINDING 257 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000250|UniProtKB:P16861" FT BINDING 285 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000250|UniProtKB:P16861" FT BINDING 291..294 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000250|UniProtKB:P16861" FT BINDING 474 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:0000250|UniProtKB:P16861" FT BINDING 530..534 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:0000250|UniProtKB:P16861" FT BINDING 575..577 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:0000250|UniProtKB:P16861" FT BINDING 632 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:0000250|UniProtKB:P16861" FT BINDING 658 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:0000250|UniProtKB:P16861" FT BINDING 664..667 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:0000250|UniProtKB:P16861" SQ SEQUENCE 756 AA; 83301 MW; 26A89B801D286534 CRC64; MEQKFKKGKD HGVGVLTSGG DSQGMNAAVR SVVRETIRQG HRCYLIREGY NGLINGNIEL AKWAHVANVT HLGGSMIGTS RCDEFRTTDG RKKAAAIMFD KRIFHLIVIG GDGSLMGAQK LKEEWGRFGE ELFAEGKITE EVANEGRELH LAGIVGSIDN DCIESDKSIG SDTALHRICE AIDGLVMTAQ SHQRVFVVEV MGRHCGYLAL TAAIAVEADY VFYPEIPPDE KWPEQLCHQL GSVRKMGKRQ NVIILGEGVT NSKGQRIDVR QVKEEIETRL QLEVRIATLG HLQRGGAPSF LDRLIGLRMG YEAVQEVLKG KEEKEGAVVT GQKTIAKVMC LRGHNIQRNE LSRVIRQTET ANEEIMQRHS DLACRLRGFG FLDKQTYLNF VSIPLSTTMP SRTKTFAVVH IGSPCAGMNA ATYSFTRMAN HSGIQVIGIK HGWDGLKNKD VKLLTWANVQ GWAQFGGSML GTKRQLPSEM DLIAEGLNSN NVDGLVIIGG FMAFESALIL QQNRSEYTCL SIPIVVIPAT ISNNCPGTCM SLGVDTALNE ICRQVDNISQ NAIGSKNKVM IIETMGSRSG FLATMTALST GSQFALIRQV ETNEKDLEKL AIETKERLDS GNLEKFLLIR SEGASDEIYS PDVKKIFDKV MKNKYGVRIT NLGYSQLGGH PSCFDRQMGI RMGVRAFEGI VNPVKMGDRD CCVIGLRGSS LRYVPVQGLG KKVCFEHGVP HNMWWLDLHP LVEAMTKKPQ EAVLSS //