ID A0A075K5Z6_9FIRM Unreviewed; 359 AA. AC A0A075K5Z6; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 26-FEB-2020, entry version 33. 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=UFO1_0080 {ECO:0000313|EMBL:AIF49641.1}; OS Pelosinus sp. UFO1. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Sporomusaceae; OC Pelosinus; unclassified Pelosinus. OX NCBI_TaxID=484770 {ECO:0000313|EMBL:AIF49641.1, ECO:0000313|Proteomes:UP000027983}; RN [1] {ECO:0000313|EMBL:AIF49641.1, ECO:0000313|Proteomes:UP000027983} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UFO1 {ECO:0000313|EMBL:AIF49641.1}; RX PubMed=25189589; RA Brown S.D., Utturkar S.M., Magnuson T.S., Ray A.E., Poole F.L., RA Lancaster W.A., Thorgersen M.P., Adams M.W., Elias D.A.; RT "Complete Genome Sequence of Pelosinus sp. Strain UFO1 Assembled Using RT Single-Molecule Real-Time DNA Sequencing Technology."; RL Genome Announc. 2:e00881-14(2014). CC -!- FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate to CC 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 1,6- CC bisphosphate + H(+); Xref=Rhea:RHEA:16109, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:32966, ChEBI:CHEBI:57634, CC ChEBI:CHEBI:456216; EC=2.7.1.11; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01976}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01976, CC 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-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) family. CC Mixed-substrate PFK group III subfamily. {ECO:0000256|HAMAP- CC Rule:MF_01976}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01976}. 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; CP008852; AIF49641.1; -; Genomic_DNA. DR RefSeq; WP_038666473.1; NZ_CP008852.1. DR STRING; 484770.UFO1_0080; -. DR EnsemblBacteria; AIF49641; AIF49641; UFO1_0080. DR KEGG; puf:UFO1_0080; -. DR HOGENOM; CLU_020655_0_0_9; -. DR KO; K21071; -. DR OrthoDB; 1421302at2; -. DR UniPathway; UPA00109; UER00182. DR Proteomes; UP000027983; Chromosome. 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 TIGRFAMs; TIGR02483; PFK_mixed; 1. DR PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01976}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01976, 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, ECO:0000256|SAAS:SAAS00436062, KW ECO:0000313|EMBL:AIF49641.1}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01976, 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 Reference proteome {ECO:0000313|Proteomes:UP000027983}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01976, KW ECO:0000256|SAAS:SAAS00436075, ECO:0000313|EMBL:AIF49641.1}. FT DOMAIN 4..309 FT /note="PFK" FT /evidence="ECO:0000259|Pfam:PF00365" FT NP_BIND 73..74 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01976" FT NP_BIND 113..116 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01976" FT REGION 180..182 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01976" FT REGION 283..286 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01976" FT ACT_SITE 138 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01976" FT METAL 114 FT /note="Magnesium; catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01976" FT BINDING 11 FT /note="ATP; via amide nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01976" FT BINDING 173 FT /note="Substrate; shared with dimeric partner" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01976" FT BINDING 233 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01976" FT BINDING 277 FT /note="Substrate; shared with dimeric partner" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01976" FT SITE 115 FT /note="Important for substrate specificity; cannot use PPi FT as phosphoryl donor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01976" SQ SEQUENCE 359 AA; 38688 MW; 51F987544EA83107 CRC64; MKTIAVLTGG GDCPGLNAVI RAVYKTAHSN GIEVYGVKNG FKGLVEDDLS ILGPESVSGI LPRGGTILGT TNRDNPFKYQ CIDHGELVYK DMSRQVLFNL KQRDIEALIV IGGDGTLKIA SKIAELGFPV VGVPKSIDND LPKTERTFGF DTAVSIATEA LDRLHTTAES HHRVMILEVM GRYAGWIALH SGIAGGADCI IIPEIPFKWD SIIEKIKLRQ QKGTLFSIIV VAEGAKPING NLSVARIVNN CPETIRLGGI SDKIAHELEN LLPVECRSTV LGHLQRGGSP TAYDRVLSTR YGEAAVNAII NKNFKTMVAL QNNEIVSVNL IDVVGIPYLV PTTHDLIKTG RSLGISFGD //