ID A0A0N4TMH1_BRUPA Unreviewed; 813 AA. AC A0A0N4TMH1; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 17-FEB-2016, entry version 3. DE RecName: Full=ATP-dependent 6-phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_03184}; DE Short=ATP-PFK {ECO:0000256|HAMAP-Rule:MF_03184}; DE Short=Phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_03184}; DE EC=2.7.1.11 {ECO:0000256|HAMAP-Rule:MF_03184}; DE AltName: Full=Phosphohexokinase {ECO:0000256|HAMAP-Rule:MF_03184}; OS Brugia pahangi (Filarial nematode worm). OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Spirurida; OC Filarioidea; Onchocercidae; Brugia. OX NCBI_TaxID=6280 {ECO:0000313|Proteomes:UP000038020, ECO:0000313|WBParaSite:BPAG_0000964301-mRNA-1}; RN [1] {ECO:0000313|Proteomes:UP000038020, ECO:0000313|WBParaSite:BPAG_0000964301-mRNA-1} RP NUCLEOTIDE SEQUENCE. RG Helminth Genomes Consortium; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. 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:0000256|HAMAP-Rule:MF_03184}. CC -!- CATALYTIC ACTIVITY: ATP + D-fructose 6-phosphate = ADP + D- CC fructose 1,6-bisphosphate. {ECO:0000256|HAMAP-Rule:MF_03184, CC ECO:0000256|PIRNR:PIRNR000533}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_03184}; CC -!- ENZYME REGULATION: Allosterically activated by ADP, AMP, or CC fructose 2,6-bisphosphate, and allosterically inhibited by ATP or CC citrate. {ECO:0000256|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:0000256|HAMAP-Rule:MF_03184, ECO:0000256|PIRNR:PIRNR000533}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_03184}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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:0000256|HAMAP-Rule:MF_03184, CC ECO:0000256|PIRNR:PIRNR000533}. 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 WBParaSite; BPAG_0000964301-mRNA-1; BPAG_0000964301-mRNA-1; BPAG_0000964301. DR UniPathway; UPA00109; UER00182. DR Proteomes; UP000038020; Genome Assembly. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-HAMAP. DR GO; GO:0003872; F:6-phosphofructokinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:InterPro. 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 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 {ECO:0000256|HAMAP-Rule:MF_03184}; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_03184, KW ECO:0000256|PIRNR:PIRNR000533}; KW Complete proteome {ECO:0000313|Proteomes:UP000038020}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03184}; KW Glycolysis {ECO:0000256|HAMAP-Rule:MF_03184, KW ECO:0000256|PIRNR:PIRNR000533}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_03184, KW ECO:0000256|PIRNR:PIRNR000533}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_03184}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_03184}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03184, KW ECO:0000256|PIRNR:PIRNR000533}; KW Reference proteome {ECO:0000313|Proteomes:UP000038020}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_03184, KW ECO:0000256|PIRNR:PIRNR000533}. FT DOMAIN 55 360 PFK. {ECO:0000259|Pfam:PF00365}. FT DOMAIN 441 724 PFK. {ECO:0000259|Pfam:PF00365}. FT NP_BIND 125 126 ATP. {ECO:0000256|HAMAP-Rule:MF_03184}. FT NP_BIND 155 158 ATP. {ECO:0000256|HAMAP-Rule:MF_03184}. FT REGION 1 427 N-terminal catalytic PFK domain 1. FT {ECO:0000256|HAMAP-Rule:MF_03184}. FT REGION 201 203 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_03184}. FT REGION 245 247 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_03184}. FT REGION 335 338 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_03184}. FT REGION 428 440 Interdomain linker. {ECO:0000256|HAMAP- FT Rule:MF_03184}. FT REGION 441 813 C-terminal regulatory PFK domain 2. FT {ECO:0000256|HAMAP-Rule:MF_03184}. FT REGION 565 569 Allosteric activator fructose 2,6- FT bisphosphate binding. {ECO:0000256|HAMAP- FT Rule:MF_03184}. FT REGION 610 612 Allosteric activator fructose 2,6- FT bisphosphate binding. {ECO:0000256|HAMAP- FT Rule:MF_03184}. FT REGION 698 701 Allosteric activator fructose 2,6- FT bisphosphate binding. {ECO:0000256|HAMAP- FT Rule:MF_03184}. FT ACT_SITE 203 203 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_03184}. FT METAL 156 156 Magnesium; catalytic. {ECO:0000256|HAMAP- FT Rule:MF_03184}. FT BINDING 62 62 ATP; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_03184}. FT BINDING 238 238 Substrate; shared with dimeric partner. FT {ECO:0000256|HAMAP-Rule:MF_03184}. FT BINDING 301 301 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_03184}. FT BINDING 329 329 Substrate; shared with dimeric partner. FT {ECO:0000256|HAMAP-Rule:MF_03184}. FT BINDING 508 508 Allosteric activator fructose 2,6- FT bisphosphate. {ECO:0000256|HAMAP-Rule: FT MF_03184}. FT BINDING 603 603 Allosteric activator fructose 2,6- FT bisphosphate; shared with dimeric FT partner. {ECO:0000256|HAMAP-Rule: FT MF_03184}. FT BINDING 666 666 Allosteric activator fructose 2,6- FT bisphosphate. {ECO:0000256|HAMAP-Rule: FT MF_03184}. FT BINDING 692 692 Allosteric activator fructose 2,6- FT bisphosphate; shared with dimeric FT partner. {ECO:0000256|HAMAP-Rule: FT MF_03184}. FT BINDING 774 774 Allosteric activator fructose 2,6- FT bisphosphate. {ECO:0000256|HAMAP-Rule: FT MF_03184}. SQ SEQUENCE 813 AA; 89500 MW; 71CBBC91579D7CC8 CRC64; MKNSGLPITS LDDDFGPPTT DMHRMKFSIR SDSIVPSAGR EGTSIAPQIY KGRTMAVFTS GGDASGMNSA VRSVVRMGVY LGCRVFLIYE GYQGMVDGGD NIKEADWQSV SDIIQRGGTV IGSARCKVFQ ERWGRLQAAE NLIKHRITNL VCIGGDGSLT GANLFRQEWQ GLVKELLLSG KITREEAVEC GNIQIVGLVG SIDNDFCGTD MTIGTDTALQ RICEAIDCVM STAQSHQRTF VIEVMGRHCG YLALVAALAS EADFCFIPEW PVPTDWPTVL CQKLRMMREA GSRLNIVIVA EGALDREGKC ITAESVRAVV KETLHYDTRV TVLGHVQRGG SPSAFDRLLG CRMGAEAVLA LMEMTPQSEP CVVSIDGNVI VRVPLMQCVQ RTQAVKKAMD ERDWETAVKL RGRSFQRNLE TYRLLTKVEP KKVDPNVPVY NVAIVNVGAP AGGMNAVVRS YVRMALYHGC KVYGIKNSFE GLCRGEDMAW GDVCNWVMYG GSFLGTQKQL PGKIMDKVAD AFEKYNFHGL LLVGGFEAFH SCLLLSRARD KYPSLRIPMC VIPCTISNNV PGTSLSLGSD TAVNEICEMI DKIKLSATGT KRRVFIVETM GGFCGYLATI SALASGADNA YIFEEQFKVS DIMDDVKVIS RKMRTGVQRY LIVRNECANK NYTTEFVNQL FAEEGKGAFS TRTNVLGHAQ QGGNPTPFDR NMGTKLAARA LEFIISQILK YIDPKTGILN AVSPDSATLL GLMGRRTVFT PVEELSLETD FEHRVPKHQW WMKMRPLLRI LAKHDSTYQT EAMVVPEVEG ESA //