ID A0A075K5Z6_9FIRM Unreviewed; 359 AA. AC A0A075K5Z6; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 06-JUL-2016, entry version 17. 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. 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 CC to fructose 1,6-bisphosphate by ATP, the first committing step of CC glycolysis. {ECO:0000256|HAMAP-Rule:MF_01976}. CC -!- CATALYTIC ACTIVITY: ATP + D-fructose 6-phosphate = ADP + D- CC fructose 1,6-bisphosphate. {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 --------------------------------------------------------------------------- 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 EnsemblBacteria; AIF49641; AIF49641; UFO1_0080. DR KEGG; puf:UFO1_0080; -. DR KO; K00850; -. 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-HAMAP. 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 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 Complete proteome {ECO:0000313|Proteomes:UP000027983}; 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|RuleBase:RU004092, ECO:0000256|SAAS:SAAS00436062, KW ECO:0000313|EMBL:AIF49641.1}; 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 Reference proteome {ECO:0000313|Proteomes:UP000027983}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01976, KW ECO:0000256|RuleBase:RU004092, ECO:0000256|SAAS:SAAS00436075, KW ECO:0000313|EMBL:AIF49641.1}. FT DOMAIN 4 309 PFK. {ECO:0000259|Pfam:PF00365}. FT NP_BIND 73 74 ATP. {ECO:0000256|HAMAP-Rule:MF_01976}. FT NP_BIND 113 116 ATP. {ECO:0000256|HAMAP-Rule:MF_01976}. FT REGION 180 182 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01976}. FT REGION 283 286 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01976}. FT ACT_SITE 138 138 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_01976}. FT METAL 114 114 Magnesium; catalytic. {ECO:0000256|HAMAP- FT Rule:MF_01976}. FT BINDING 11 11 ATP; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01976}. FT BINDING 173 173 Substrate; shared with dimeric partner. FT {ECO:0000256|HAMAP-Rule:MF_01976}. FT BINDING 233 233 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01976}. FT BINDING 277 277 Substrate; shared with dimeric partner. FT {ECO:0000256|HAMAP-Rule:MF_01976}. FT SITE 115 115 Important for substrate specificity; FT cannot use PPi as phosphoryl donor. FT {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 //