ID A0A0F2Q6A9_9CLOT Unreviewed; 363 AA. AC A0A0F2Q6A9; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 08-MAY-2019, entry version 23. DE RecName: Full=ATP-dependent 6-phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_01976}; DE Short=ATP-PFK {ECO:0000256|HAMAP-Rule:MF_01976}; DE Short=Phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_01976}; DE EC=2.7.1.11 {ECO:0000256|HAMAP-Rule:MF_01976}; DE AltName: Full=Phosphohexokinase {ECO:0000256|HAMAP-Rule:MF_01976}; GN Name=pfkA {ECO:0000256|HAMAP-Rule:MF_01976}; GN ORFNames=VR72_12165 {ECO:0000313|EMBL:KJS21066.1}; OS Clostridiaceae bacterium BRH_c20a. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae. OX NCBI_TaxID=1629719 {ECO:0000313|EMBL:KJS21066.1, ECO:0000313|Proteomes:UP000033488}; RN [1] {ECO:0000313|EMBL:KJS21066.1, ECO:0000313|Proteomes:UP000033488} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BRH_c20a {ECO:0000313|EMBL:KJS21066.1}; RA Bagnoud A., Chourey K., Hettich R.L., de Bruijn I., Andersson A.F., RA Leupin O.X., Schwyn B., Bernier-Latmani R.; RT "Microbial metabolic network in the subsurface."; 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_01976}. 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:0000256|HAMAP-Rule:MF_01976}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01976, ECO:0000256|SAAS:SAAS00609123}; 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_01976, ECO:0000256|SAAS:SAAS00041065}. CC -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000256|HAMAP- CC Rule:MF_01976}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01976, CC ECO:0000256|SAAS:SAAS00551378}. CC -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) CC family. Mixed-substrate PFK group III subfamily. CC {ECO:0000256|HAMAP-Rule:MF_01976}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01976}. 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:KJS21066.1}. 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; LADT01000047; KJS21066.1; -; Genomic_DNA. DR PATRIC; fig|1629719.3.peg.1128; -. DR UniPathway; UPA00109; UER00182. DR Proteomes; UP000033488; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003872; F:6-phosphofructokinase activity; IEA:UniProtKB-UniRule. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0047334; F:diphosphate-fructose-6-phosphate 1-phosphotransferase activity; IEA:InterPro. 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_01976; Phosphofructokinase_III; 1. DR InterPro; IPR022953; ATP_PFK. DR InterPro; IPR012003; ATP_PFK_prok-type. DR InterPro; IPR015912; Phosphofructokinase_CS. DR InterPro; IPR000023; Phosphofructokinase_dom. DR InterPro; IPR012829; Phosphofructokinase_III. DR InterPro; IPR035966; PKF_sf. DR Pfam; PF00365; PFK; 1. DR PIRSF; PIRSF000532; ATP_PFK_prok; 1. DR PRINTS; PR00476; PHFRCTKINASE. DR SUPFAM; SSF53784; SSF53784; 1. DR PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01976}; KW Complete proteome {ECO:0000313|Proteomes:UP000033488}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01976, KW ECO:0000256|SAAS:SAAS00436108}; KW Glycolysis {ECO:0000256|HAMAP-Rule:MF_01976, KW ECO:0000256|SAAS:SAAS00436111}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_01976, KW ECO:0000256|SAAS:SAAS00436062, ECO:0000313|EMBL:KJS21066.1}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01976, KW ECO:0000256|SAAS:SAAS00436079}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01976, KW ECO:0000256|SAAS:SAAS00436116}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01976}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01976, KW ECO:0000256|SAAS:SAAS00436075}. FT DOMAIN 7 314 PFK. {ECO:0000259|Pfam:PF00365}. FT NP_BIND 77 78 ATP. {ECO:0000256|HAMAP-Rule:MF_01976}. FT NP_BIND 117 120 ATP. {ECO:0000256|HAMAP-Rule:MF_01976}. FT REGION 141 143 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01976}. FT REGION 185 187 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01976}. FT REGION 288 291 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01976}. FT ACT_SITE 143 143 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_01976}. FT METAL 118 118 Magnesium; catalytic. {ECO:0000256|HAMAP- FT Rule:MF_01976}. FT BINDING 15 15 ATP; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01976}. FT BINDING 178 178 Substrate; shared with dimeric partner. FT {ECO:0000256|HAMAP-Rule:MF_01976}. FT BINDING 238 238 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01976}. FT BINDING 282 282 Substrate; shared with dimeric partner. FT {ECO:0000256|HAMAP-Rule:MF_01976}. FT SITE 119 119 Important for substrate specificity; FT cannot use PPi as phosphoryl donor. FT {ECO:0000256|HAMAP-Rule:MF_01976}. SQ SEQUENCE 363 AA; 38939 MW; 634527F4C2F26364 CRC64; MAVIYLRIGV LTGGGDCPGL NAVIRAVTRT AISNGDTVFG FNDGFKGLIE NRYISLNHDS VSGILIRGGT ILGTTNRDNP MRYEQIINGQ KIYSDMSGII KENYQALGLD TLVVIGGDGT MRMANEIAEK TGIKIVGVPK TIDNDIVGTD LTFGFSSAVD IATDALDRLH STAESHHRVM ILEVMGRDAG WIALHAGIAG GADIILIPEI SYTIEGILNT ITNRIERGKH FSLIIVAEGV KTLEGESIYK DIIKSDIDLV KLGGISNWLV RAIENASSIE CRATILGHLQ RGGSPNSFDR VYCTQLGAKA VELIYQGKFQ EMVALVNNNI TSVPLSIVKG IKLVDPKGPL VSTAKQIGIS FGE //