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 16-OCT-2019, entry version 148. 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 RT investigating biology."; RL Science 282:2012-2018(1998). CC -!- FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate CC to 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 CC 1,6-bisphosphate + H(+); Xref=Rhea:RHEA:16109, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:32966, CC ChEBI:CHEBI:57634, ChEBI:CHEBI:456216; EC=2.7.1.11; CC Evidence={ECO:0000255|HAMAP-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 CC fructose 2,6-bisphosphate, and allosterically inhibited by ATP or CC citrate. {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) CC family. ATP-dependent PFK group I subfamily. Eukaryotic two domain CC clade 'E' 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; 12. DR STRING; 6239.Y71H10A.1a; -. DR EPD; Q9TZL8; -. DR PaxDb; Q9TZL8; -. DR PeptideAtlas; Q9TZL8; -. DR PRIDE; 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 eggNOG; COG0205; LUCA. DR GeneTree; ENSGT00940000171778; -. DR HOGENOM; HOG000200154; -. DR InParanoid; Q9TZL8; -. DR KO; K00850; -. DR OMA; AEWPSLI; -. 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 5 organ(s), highest expression level in multi-cellular organism. 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 GO; GO:0006007; P:glucose catabolic process; IBA:GO_Central. DR GO; GO:0051289; P:protein homotetramerization; IBA:GO_Central. 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; Complete proteome; Cytoplasm; KW Glycolysis; Kinase; Magnesium; Metal-binding; Nucleotide-binding; KW Reference proteome; Transferase. FT CHAIN 1 814 ATP-dependent 6-phosphofructokinase 1. FT /FTId=PRO_0000429718. FT NP_BIND 118 119 ATP. {ECO:0000255|HAMAP-Rule:MF_03184}. FT NP_BIND 148 151 ATP. {ECO:0000255|HAMAP-Rule:MF_03184}. FT REGION 1 420 N-terminal catalytic PFK domain 1. FT REGION 194 196 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_03184}. FT REGION 238 240 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_03184}. FT REGION 328 331 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_03184}. FT REGION 421 435 Interdomain linker. FT REGION 436 814 C-terminal regulatory PFK domain 2. FT REGION 563 567 Allosteric activator fructose 2,6- FT bisphosphate binding. {ECO:0000255|HAMAP- FT Rule:MF_03184}. FT REGION 608 610 Allosteric activator fructose 2,6- FT bisphosphate binding. {ECO:0000255|HAMAP- FT Rule:MF_03184}. FT REGION 696 699 Allosteric activator fructose 2,6- FT bisphosphate binding. {ECO:0000255|HAMAP- FT Rule:MF_03184}. FT ACT_SITE 196 196 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_03184}. FT METAL 149 149 Magnesium; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_03184}. FT BINDING 55 55 ATP; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_03184}. FT BINDING 231 231 Substrate; shared with dimeric partner. FT {ECO:0000255|HAMAP-Rule:MF_03184}. FT BINDING 294 294 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_03184}. FT BINDING 322 322 Substrate; shared with dimeric partner. FT {ECO:0000255|HAMAP-Rule:MF_03184}. FT BINDING 505 505 Allosteric activator fructose 2,6- FT bisphosphate. {ECO:0000255|HAMAP- FT Rule:MF_03184}. FT BINDING 601 601 Allosteric activator fructose 2,6- FT bisphosphate; shared with dimeric FT partner. {ECO:0000255|HAMAP- FT Rule:MF_03184}. FT BINDING 664 664 Allosteric activator fructose 2,6- FT bisphosphate. {ECO:0000255|HAMAP- FT Rule:MF_03184}. FT BINDING 690 690 Allosteric activator fructose 2,6- FT bisphosphate; shared with dimeric FT partner. {ECO:0000255|HAMAP- FT Rule:MF_03184}. FT BINDING 771 771 Allosteric activator fructose 2,6- FT bisphosphate. {ECO:0000255|HAMAP- FT 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 //