ID A0A4V0ZH02_9BACT Unreviewed; 367 AA. AC A0A4V0ZH02; DT 31-JUL-2019, integrated into UniProtKB/TrEMBL. DT 31-JUL-2019, sequence version 1. DT 18-SEP-2019, entry version 2. 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=EGM51_06525 {ECO:0000313|EMBL:QBG47064.1}; OS Verrucomicrobia bacterium S94. OC Bacteria; Verrucomicrobia; unclassified Verrucomicrobia. OX NCBI_TaxID=2488809 {ECO:0000313|EMBL:QBG47064.1, ECO:0000313|Proteomes:UP000289135}; RN [1] {ECO:0000313|EMBL:QBG47064.1, ECO:0000313|Proteomes:UP000289135} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S94 {ECO:0000313|EMBL:QBG47064.1, RC ECO:0000313|Proteomes:UP000289135}; RA Baek K.; RT "Verrucomicrobia bacterium S94."; RL Submitted (NOV-2018) 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 --------------------------------------------------------------------------- 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; CP036201; QBG47064.1; -; Genomic_DNA. DR UniPathway; UPA00109; UER00182. DR Proteomes; UP000289135; Chromosome. 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:UP000289135}; 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:QBG47064.1}; 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 8 312 PFK. {ECO:0000259|Pfam:PF00365}. FT NP_BIND 76 77 ATP. {ECO:0000256|HAMAP-Rule:MF_01976}. FT NP_BIND 112 115 ATP. {ECO:0000256|HAMAP-Rule:MF_01976}. FT REGION 135 137 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01976}. FT REGION 179 181 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01976}. FT REGION 287 290 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01976}. FT ACT_SITE 137 137 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_01976}. FT METAL 113 113 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 172 172 Substrate; shared with dimeric partner. FT {ECO:0000256|HAMAP-Rule:MF_01976}. FT BINDING 232 232 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01976}. FT BINDING 281 281 Substrate; shared with dimeric partner. FT {ECO:0000256|HAMAP-Rule:MF_01976}. FT SITE 114 114 Important for substrate specificity; FT cannot use PPi as phosphoryl donor. FT {ECO:0000256|HAMAP-Rule:MF_01976}. SQ SEQUENCE 367 AA; 39111 MW; 39922D1BF34170E2 CRC64; MATKTKTIGI LTSGGDCPGL NAAIRGVAKA ALAQGTKVIG ILDGFRGLVE NRTMTLEDKD VSGILTHGGT FLGSSRDKPH KMPMGEKVLD MTEVAVSNAR KNHIDCLVCL GGNGTQKNAM RLHEAGLDVL TLPKTIDNDV AGTDITFGFD SSMAIATEAI DRLHTTASSH HRAIVCEIMG HKAGWLALGA GIAGGADVIL LPEIPYDLDY IVEHLMARRH HSKRFSIIAI AEGAISKEEA AEGRKKKKPV RKKENGMMLI EEPVASRIAR QIQQAAGIEV RFTSLGHVQR GGSPTATDRL LSTRLGTKAG ELLHDGVYNV MVGLKGERCV AVPLEDVAGR TKVVPAGHPW LKTAVLVDTC LGDKLDF //