ID K6PF_CALFI Reviewed; 184 AA. AC Q27543; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 16-JUN-2009, entry version 43. DE RecName: Full=6-phosphofructokinase; DE Short=Phosphofructokinase; DE EC=2.7.1.11; DE AltName: Full=Phosphohexokinase; DE Flags: Fragment; GN Name=PFK; OS Calanus finmarchicus. OC Eukaryota; Metazoa; Arthropoda; Crustacea; Maxillopoda; Copepoda; OC Calanoida; Calanidae; Calanus. OX NCBI_TaxID=6837; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=95400449; PubMed=7670600; RA Crawford D.L.; RT "Nuclear genes from the copepod Calanus finmarchicus."; RL Mol. Mar. Biol. Biotechnol. 4:241-247(1995). CC -!- CATALYTIC ACTIVITY: ATP + D-fructose 6-phosphate = ADP + D- CC fructose 1,6-bisphosphate. CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- CC phosphate and glycerone phosphate from D-glucose: step 3/4. CC -!- SIMILARITY: Belongs to the phosphofructokinase family. Two domains CC subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U21244; AAA85287.1; -; mRNA. DR HSSP; P00512; 3PFK. DR BRENDA; 2.7.1.11; 297876. DR GO; GO:0005945; C:6-phosphofructokinase complex; IEA:InterPro. DR GO; GO:0003872; F:6-phosphofructokinase activity; IEA:EC. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0006096; P:glycolysis; IEA:UniProtKB-KW. DR InterPro; IPR000023; Phosphofructokinase. DR InterPro; IPR015912; Phosphofructokinase_CS. DR Pfam; PF00365; PFK; 1. DR PRINTS; PR00476; PHFRCTKINASE. DR ProDom; PD000707; Ppfruckinase; 1. DR PROSITE; PS00433; PHOSPHOFRUCTOKINASE; PARTIAL. PE 2: Evidence at transcript level; KW ATP-binding; Glycolysis; Kinase; Nucleotide-binding; Transferase. FT CHAIN <1 >184 6-phosphofructokinase. FT /FTId=PRO_0000112028. FT NP_BIND 77 81 ATP (By similarity). FT NP_BIND 94 110 ATP (By similarity). FT ACT_SITE 50 50 Proton acceptor (By similarity). FT BINDING 85 85 Substrate (By similarity). FT BINDING 176 176 Substrate (By similarity). FT BINDING 182 182 Substrate (By similarity). FT NON_TER 1 1 FT NON_TER 184 184 SQ SEQUENCE 184 AA; 20208 MW; E9B71F095A5DF2AD CRC64; GGDGSLTGAN RFKGEWSSLV KELLETGKIT KEVAEKHSHL NIVGMVGSID NDFCGTDMTI GTDSALHRIV EVADNIIPTA YSHQRAFVLE VMGRHCGYLA LVAGIVTEAD FVFAPEWPPE EDWPEKLCKK LELERQSGQR LNIIIVAEGA IDRQGNPITA EGVKKIIVDR LEMDTRTTVL GHIQ //