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 29-SEP-2021, entry version 156. 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 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 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; GTPCAYD; -. DR OrthoDB; 172878at2759; -. 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 multi-cellular organism 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; 3.40.50.460; -; 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 Pfam; PF00365; PFK; 2. DR PIRSF; PIRSF000533; ATP_PFK_euk; 1. DR PRINTS; PR00476; PHFRCTKINASE. DR SUPFAM; SSF53784; SSF53784; 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 NP_BIND 118..119 FT /note="ATP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184" FT NP_BIND 148..151 FT /note="ATP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184" FT REGION 1..420 FT /note="N-terminal catalytic PFK domain 1" FT REGION 194..196 FT /note="Substrate binding" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184" FT REGION 238..240 FT /note="Substrate binding" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184" FT REGION 328..331 FT /note="Substrate binding" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184" FT REGION 421..435 FT /note="Interdomain linker" FT REGION 436..814 FT /note="C-terminal regulatory PFK domain 2" FT REGION 563..567 FT /note="Fructose 2,6-bisphosphate binding; allosteric FT activator" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184" FT REGION 608..610 FT /note="Fructose 2,6-bisphosphate binding; allosteric FT activator" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184" FT REGION 696..699 FT /note="Fructose 2,6-bisphosphate binding; allosteric FT activator" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184" FT ACT_SITE 196 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184" FT METAL 149 FT /note="Magnesium; catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184" FT BINDING 55 FT /note="ATP; via amide nitrogen" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184" FT BINDING 231 FT /note="Substrate; shared with dimeric partner" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184" FT BINDING 294 FT /note="Substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184" FT BINDING 322 FT /note="Substrate; shared with dimeric partner" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184" FT BINDING 505 FT /note="Fructose 2,6-bisphosphate; allosteric activator" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184" FT BINDING 601 FT /note="Fructose 2,6-bisphosphate; allosteric activator; FT shared with dimeric partner" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184" FT BINDING 664 FT /note="Fructose 2,6-bisphosphate; allosteric activator" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184" FT BINDING 690 FT /note="Fructose 2,6-bisphosphate; allosteric activator; FT shared with dimeric partner" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184" FT BINDING 771 FT /note="Fructose 2,6-bisphosphate; allosteric activator" 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 //