ID A0A431MRQ0_9SPHI Unreviewed; 330 AA. AC A0A431MRQ0; DT 08-MAY-2019, integrated into UniProtKB/TrEMBL. DT 08-MAY-2019, sequence version 1. DT 05-JUN-2019, entry version 2. 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 ECO:0000313|EMBL:RTL59307.1}; GN ORFNames=EKK37_13500 {ECO:0000313|EMBL:RTL59307.1}; OS Sphingobacteriales bacterium. OC Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales. OX NCBI_TaxID=2044944 {ECO:0000313|EMBL:RTL59307.1, ECO:0000313|Proteomes:UP000268352}; RN [1] {ECO:0000313|EMBL:RTL59307.1, ECO:0000313|Proteomes:UP000268352} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AWTP1-9 {ECO:0000313|EMBL:RTL59307.1}; RA Kantor R.S., Miller S.E., Nelson K.L.; RT "The water microbiome through an advanced treatment facility for RT direct potable reuse."; 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_00339, CC ECO:0000256|SAAS:SAAS01078966}. 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_00339, CC ECO:0000256|SAAS:SAAS01116210}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00339, ECO:0000256|SAAS:SAAS00609123}; CC -!- ACTIVITY REGULATION: Allosterically activated by ADP and other CC diphosphonucleosides, and allosterically inhibited by CC phosphoenolpyruvate. {ECO:0000256|HAMAP-Rule:MF_00339, CC ECO:0000256|SAAS:SAAS01070487}. 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:SAAS00041065}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00339, CC ECO:0000256|SAAS:SAAS00557934}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00339, CC ECO:0000256|SAAS:SAAS00551378}. 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:SAAS00541548}. 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:RTL59307.1}. 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; RXJG01000004; RTL59307.1; -; Genomic_DNA. DR UniPathway; UPA00109; UER00182. DR Proteomes; UP000268352; Unassembled WGS sequence. 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 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; 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:SAAS00016785}; KW Complete proteome {ECO:0000313|Proteomes:UP000268352}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00339, KW ECO:0000256|SAAS:SAAS00436108}; KW Glycolysis {ECO:0000256|HAMAP-Rule:MF_00339, KW ECO:0000256|SAAS:SAAS00436111}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_00339, KW ECO:0000256|SAAS:SAAS00436062, ECO:0000313|EMBL:RTL59307.1}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00339, KW ECO:0000256|SAAS:SAAS00436079}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00339, KW ECO:0000256|SAAS:SAAS00436116}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00339, KW ECO:0000256|SAAS:SAAS00016719}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00339, KW ECO:0000256|SAAS:SAAS00436075, ECO:0000313|EMBL:RTL59307.1}. FT DOMAIN 7 283 PFK. {ECO:0000259|Pfam:PF00365}. FT NP_BIND 76 77 ATP. {ECO:0000256|HAMAP-Rule:MF_00339}. FT NP_BIND 106 109 ATP. {ECO:0000256|HAMAP-Rule:MF_00339}. FT REGION 25 29 Allosteric activator ADP binding; shared FT with dimeric partner. {ECO:0000256|HAMAP- FT Rule:MF_00339}. FT REGION 130 132 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_00339}. FT REGION 174 176 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_00339}. FT REGION 190 192 Allosteric activator ADP binding. FT {ECO:0000256|HAMAP-Rule:MF_00339}. FT REGION 218 220 Allosteric activator ADP binding. FT {ECO:0000256|HAMAP-Rule:MF_00339}. FT REGION 257 260 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_00339}. FT ACT_SITE 132 132 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_00339}. FT METAL 107 107 Magnesium; catalytic. {ECO:0000256|HAMAP- FT Rule:MF_00339}. FT BINDING 15 15 ATP; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_00339}. FT BINDING 159 159 Allosteric activator ADP. FT {ECO:0000256|HAMAP-Rule:MF_00339}. FT BINDING 167 167 Substrate; shared with dimeric partner. FT {ECO:0000256|HAMAP-Rule:MF_00339}. FT BINDING 216 216 Allosteric activator ADP. FT {ECO:0000256|HAMAP-Rule:MF_00339}. FT BINDING 227 227 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00339}. FT BINDING 251 251 Substrate; shared with dimeric partner. FT {ECO:0000256|HAMAP-Rule:MF_00339}. SQ SEQUENCE 330 AA; 35934 MW; 67C5CCFADD287CC2 CRC64; MTKKVSNIGV LTSGGDSPGM NACIRAVVRT GLYHGLEMFG IMRGYQGMID DDIVPMHSRS VANIIQRGGT ILKTARCKEF FELSGRKKAY ENLKKHGIDG LVIIGGDGSF RGAQKFSHEF DIPCIGLPGT IDKDIAGTDF TIGFDTAVNT AVECIDKIRD TADAHDRLFI IEVMGRDAGY IALHSGIATG AEHILIPERK TDIEAVISSL EEKEKRKKLV NMIVVAEGDD FGGADEVAKV VKERLPMADV RVCILGHIQR GGAPSCIDRL IASRMGYAAV EALLDPTGTH HNHMIGILNN RIHFTPLDKA IKAKQKISDE WMKIVKILAS //