ID A0A124FN52_9CHLR Unreviewed; 322 AA. AC A0A124FN52; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=ATP-dependent 6-phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_00339}; DE Short=ATP-PFK {ECO:0000256|HAMAP-Rule:MF_00339}; DE Short=Phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_00339}; DE EC=2.7.1.11 {ECO:0000256|HAMAP-Rule:MF_00339}; DE AltName: Full=Phosphohexokinase {ECO:0000256|HAMAP-Rule:MF_00339}; GN Name=pfkA {ECO:0000256|HAMAP-Rule:MF_00339}; GN ORFNames=XD73_0337 {ECO:0000313|EMBL:KUK46811.1}; OS Anaerolinea thermophila. OC Bacteria; Chloroflexi; Anaerolineae; Anaerolineales; Anaerolineaceae; OC Anaerolinea. OX NCBI_TaxID=167964 {ECO:0000313|EMBL:KUK46811.1, ECO:0000313|Proteomes:UP000064249}; RN [1] {ECO:0000313|EMBL:KUK46811.1, ECO:0000313|Proteomes:UP000064249} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=46_16 {ECO:0000313|EMBL:KUK46811.1}; RX PubMed=26787827; RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M., RA Andersen G.L., Banfield J.F.; RT "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate RT Phyla and Other Microbial Community Members in Biogeochemical RT Transformations in Oil Reservoirs."; RL MBio 7:0-0(2016). 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_00339, CC ECO:0000256|SAAS:SAAS00729178}. CC -!- CATALYTIC ACTIVITY: ATP + D-fructose 6-phosphate = ADP + D- CC fructose 1,6-bisphosphate. {ECO:0000256|HAMAP-Rule:MF_00339, CC ECO:0000256|SAAS:SAAS00728855}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00339, ECO:0000256|SAAS:SAAS00640094}; CC -!- ENZYME REGULATION: Allosterically activated by ADP and other CC diphosphonucleosides, and allosterically inhibited by CC phosphoenolpyruvate. {ECO:0000256|HAMAP-Rule:MF_00339}. 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_00339, ECO:0000256|SAAS:SAAS00640117}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00339, CC ECO:0000256|SAAS:SAAS00643582}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00339, CC ECO:0000256|SAAS:SAAS00640112}. CC -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) CC family. ATP-dependent PFK group I subfamily. Prokaryotic clade CC "B1" sub-subfamily. {ECO:0000256|HAMAP-Rule:MF_00339, CC ECO:0000256|SAAS:SAAS00634686}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00339}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KUK46811.1}. 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; LGFU01000007; KUK46811.1; -; Genomic_DNA. DR PATRIC; fig|167964.4.peg.283; -. DR UniPathway; UPA00109; UER00182. DR Proteomes; UP000064249; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003872; F:6-phosphofructokinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:InterPro. DR HAMAP; MF_00339; Phosphofructokinase_I_B1; 1. DR InterPro; IPR022953; ATP_PFK. DR InterPro; IPR012003; ATP_PFK_prok-type. DR InterPro; IPR012828; PFKA_ATP_prok. DR InterPro; IPR015912; Phosphofructokinase_CS. DR InterPro; IPR000023; Phosphofructokinase_dom. DR Pfam; PF00365; PFK; 1. DR PIRSF; PIRSF000532; ATP_PFK_prok; 1. DR PRINTS; PR00476; PHFRCTKINASE. DR SUPFAM; SSF53784; SSF53784; 1. DR TIGRFAMs; TIGR02482; PFKA_ATP; 1. DR PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 1. PE 3: Inferred from homology; KW Allosteric enzyme {ECO:0000256|HAMAP-Rule:MF_00339}; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00339, KW ECO:0000256|SAAS:SAAS00728960}; KW Complete proteome {ECO:0000313|Proteomes:UP000064249}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00339, KW ECO:0000256|SAAS:SAAS00640104}; KW Glycolysis {ECO:0000256|HAMAP-Rule:MF_00339, KW ECO:0000256|SAAS:SAAS00640111}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_00339, KW ECO:0000256|SAAS:SAAS00640102, ECO:0000313|EMBL:KUK46811.1}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00339, KW ECO:0000256|SAAS:SAAS00640121}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00339, KW ECO:0000256|SAAS:SAAS00640110}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00339, KW ECO:0000256|SAAS:SAAS00728832}; KW Reference proteome {ECO:0000313|Proteomes:UP000064249}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00339, KW ECO:0000256|SAAS:SAAS00640113}. FT DOMAIN 3 277 PFK. {ECO:0000259|Pfam:PF00365}. FT NP_BIND 72 73 ATP. {ECO:0000256|HAMAP-Rule:MF_00339}. FT NP_BIND 102 105 ATP. {ECO:0000256|HAMAP-Rule:MF_00339}. FT REGION 21 25 Allosteric activator ADP binding; shared FT with dimeric partner. {ECO:0000256|HAMAP- FT Rule:MF_00339}. FT REGION 125 127 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_00339}. FT REGION 169 171 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_00339}. FT REGION 185 187 Allosteric activator ADP binding. FT {ECO:0000256|HAMAP-Rule:MF_00339}. FT REGION 213 215 Allosteric activator ADP binding. FT {ECO:0000256|HAMAP-Rule:MF_00339}. FT REGION 253 256 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_00339}. FT ACT_SITE 127 127 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_00339}. FT METAL 103 103 Magnesium; catalytic. {ECO:0000256|HAMAP- FT Rule:MF_00339}. FT BINDING 11 11 ATP; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_00339}. FT BINDING 154 154 Allosteric activator ADP. FT {ECO:0000256|HAMAP-Rule:MF_00339}. FT BINDING 162 162 Substrate; shared with dimeric partner. FT {ECO:0000256|HAMAP-Rule:MF_00339}. FT BINDING 211 211 Allosteric activator ADP. FT {ECO:0000256|HAMAP-Rule:MF_00339}. FT BINDING 222 222 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00339}. FT BINDING 247 247 Substrate; shared with dimeric partner. FT {ECO:0000256|HAMAP-Rule:MF_00339}. SQ SEQUENCE 322 AA; 33828 MW; 79F8332DBFA60490 CRC64; MKKIAVLTSG GDAPGMNAAI RAVVRTGVQN GLEVYGVPLG YQGLIDGKFI PLGPRDVGGI IQKGGTFLGS ARCEEFKTEA GRKTALRALN GNGIEGLVVI GGNGSQTGSY LLSEMGFPVV GVASTIDNDL VGSDITIGVD TALNIALEAI DRLKVTGSSH QRAFLIEVMG RKCGYLALMA AIAGGAETVT LPEIDVEPEE IVKVLSEAYE RGKSHAIVVV AEGAKYNATK LAEYFTKHHE EIGFALRVTI LGHVQRGGSP SAQDRILASR LGAGAVTSLL KGEYGVLVGW VNNALKTTPL KDVVGKKKQL DMELFELARV LD //