ID PFKA1_CAEEL Reviewed; 814 AA. AC Q9TZL8; Q95X24; DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2001, sequence version 2. DT 22-FEB-2023, entry version 160. DE RecName: Full=ATP-dependent 6-phosphofructokinase 1 {ECO:0000255|HAMAP-Rule:MF_03184}; DE Short=ATP-PFK 1 {ECO:0000255|HAMAP-Rule:MF_03184}; DE Short=Phosphofructokinase 1 {ECO:0000255|HAMAP-Rule:MF_03184}; DE EC=2.7.1.11 {ECO:0000255|HAMAP-Rule:MF_03184}; DE AltName: Full=Phosphohexokinase 1 {ECO:0000255|HAMAP-Rule:MF_03184}; GN Name=pfk-1.1 {ECO:0000312|WormBase:Y71H10A.1a}; GN ORFNames=Y71H10A.1 {ECO:0000312|WormBase:Y71H10A.1a}; 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:0000255|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; Evidence={ECO:0000255|HAMAP- CC Rule:MF_03184}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_03184}. CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_03184}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|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; FO081433; CCD71595.1; -; Genomic_DNA. DR PIR; T33481; T33481. DR RefSeq; NP_741738.1; NM_171643.3. DR AlphaFoldDB; Q9TZL8; -. DR SMR; Q9TZL8; -. DR BioGRID; 45527; 13. DR STRING; 6239.Y71H10A.1a; -. DR EPD; Q9TZL8; -. DR PaxDb; Q9TZL8; -. DR PeptideAtlas; Q9TZL8; -. DR EnsemblMetazoa; Y71H10A.1a.1; Y71H10A.1a.1; WBGene00022199. DR GeneID; 180583; -. DR KEGG; cel:CELE_Y71H10A.1; -. DR UCSC; Y71H10A.1b.3; c. elegans. DR AGR; WB:WBGene00022199; -. DR CTD; 180583; -. DR WormBase; Y71H10A.1a; CE28266; WBGene00022199; pfk-1.1. DR eggNOG; KOG2440; Eukaryota. DR GeneTree; ENSGT00940000171778; -. DR HOGENOM; CLU_011053_0_0_1; -. DR InParanoid; Q9TZL8; -. DR OMA; FEAYHST; -. DR OrthoDB; 374214at2759; -. DR PhylomeDB; Q9TZL8; -. DR Reactome; R-CEL-6798695; Neutrophil degranulation. DR Reactome; R-CEL-70171; Glycolysis. DR UniPathway; UPA00109; UER00182. DR PRO; PR:Q9TZL8; -. DR Proteomes; UP000001940; Chromosome X. DR Bgee; WBGene00022199; Expressed in material anatomical entity and 5 other tissues. 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 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 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 TIGRFAMs; TIGR02478; 6PF1K_euk; 1. DR PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 2. 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..814 FT /note="ATP-dependent 6-phosphofructokinase 1" FT /id="PRO_0000429718" FT REGION 1..420 FT /note="N-terminal catalytic PFK domain 1" FT REGION 421..435 FT /note="Interdomain linker" FT REGION 436..814 FT /note="C-terminal regulatory PFK domain 2" FT ACT_SITE 196 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184" FT BINDING 55 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184" FT BINDING 118..119 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184" FT BINDING 148..151 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184" FT BINDING 149 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184" FT BINDING 194..196 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184" FT BINDING 231 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184" FT BINDING 238..240 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184" FT BINDING 294 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184" FT BINDING 322 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184" FT BINDING 328..331 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184" FT BINDING 505 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:0000255|HAMAP-Rule:MF_03184" FT BINDING 563..567 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:0000255|HAMAP-Rule:MF_03184" FT BINDING 601 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:0000255|HAMAP-Rule:MF_03184" FT BINDING 608..610 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:0000255|HAMAP-Rule:MF_03184" FT BINDING 664 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:0000255|HAMAP-Rule:MF_03184" FT BINDING 690 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:0000255|HAMAP-Rule:MF_03184" FT BINDING 696..699 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:0000255|HAMAP-Rule:MF_03184" FT BINDING 771 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:0000255|HAMAP-Rule:MF_03184" SQ SEQUENCE 814 AA; 89734 MW; DA829E8969EDF1CE CRC64; MDADASTITP EELDFIRQRA LRRFDSIVPT AGREGTEIAS DIFKGRTLAI YTSGGDSQGM NSAVRSITRM AIYCGCKVYL IYEGYEGMIE GGDFIKEATW NTVSDIIQQG GTIIGSARSS EFRTREGRLK AATNLINRGI GRLVCIGGDG SLTGANTFRL EWTDLVQELV KNQRVTAAAA KKIPYIQIVG LVGSIDNDFC GTDMTIGTDS ALQRIISSID AVVATAQSHQ RAFVIEVMGR HCGYLALVAA LASEADFCFI PEWPAPENWR DVLCDKLSQM RSEGQRLNII IVAEGAIDRD GKAITAEDVK TAVKEKLKYD TRVTILGHVQ RGGAPSAFDR LLGCRMGAEA VFALMEMTEE SEPCVISIDG NVMVRVPLLK CVERTQMVQK AMADKDWTTA VMLRGRSFQR NLETYKLLTK MRTVEKDNLS EGHKFNVAVI NVGAPAGGMN AAVRSYVRMA LYHQCTVYGI EDSFEGLANG SFKQFKWSDV TNWAMNGGSF LGTQKSLPTE KTMPQLAAQL KKHNIQALLL VGGFEAYHST IILAENREKY PEFCIPMCVI PCTISNNVPG TMVSLGSDTA INEICQMIDK IKQSATGTKR RVFIVETMGG YCGYLATLSA LSSGADNAYI FEEPFTVQDL SDDVDVILSK MEVGAKRYLV VRNEWADKNL TTDFVQNLFD SEGKKNFTTR VNVLGHVQQG GSPTPFDRNM GTKLAARALE FLLIQLKENL TADNKVIAKS AHTATLLGLK GRKVVFTPVQ DLKKETDFEH RLPSEQWWMA LRPLLRVLAR HRSTVESSAI LESVEEESAD SHMF //