ID A0A014P2S4_9ACTN Unreviewed; 341 AA. AC A0A014P2S4; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 08-MAY-2019, entry version 33. DE RecName: Full=Pyrophosphate--fructose 6-phosphate 1-phosphotransferase {ECO:0000256|HAMAP-Rule:MF_01976}; DE EC=2.7.1.90 {ECO:0000256|HAMAP-Rule:MF_01976}; DE AltName: Full=6-phosphofructokinase, pyrophosphate dependent {ECO:0000256|HAMAP-Rule:MF_01976}; DE AltName: Full=PPi-dependent phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_01976}; DE Short=PPi-PFK {ECO:0000256|HAMAP-Rule:MF_01976}; DE AltName: Full=Pyrophosphate-dependent 6-phosphofructose-1-kinase {ECO:0000256|HAMAP-Rule:MF_01976}; GN Name=pfp {ECO:0000256|HAMAP-Rule:MF_01976}; GN ORFNames=Z951_25890 {ECO:0000313|EMBL:EXU65302.1}; OS Streptomyces sp. PRh5. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=1158056 {ECO:0000313|EMBL:EXU65302.1, ECO:0000313|Proteomes:UP000019949}; RN [1] {ECO:0000313|EMBL:EXU65302.1, ECO:0000313|Proteomes:UP000019949} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PRh5 {ECO:0000313|EMBL:EXU65302.1, RC ECO:0000313|Proteomes:UP000019949}; RA Zhu D., Yang H., Wang Y., Zhang Z., Yan R.; RT "Whole-genome shotgun assembly and analysis of the genome of RT Streptomyces sp. PRh5, a strain for production of geldanamycin, RT nigericin and nocardamine."; RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate, CC the first committing step of glycolysis. Uses inorganic phosphate CC (PPi) as phosphoryl donor instead of ATP like common ATP-dependent CC phosphofructokinases (ATP-PFKs), which renders the reaction CC reversible, and can thus function both in glycolysis and CC gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of CC both the forward (ATP-PFK) and reverse (fructose-bisphosphatase CC (FBPase)) reactions. {ECO:0000256|HAMAP-Rule:MF_01976}. CC -!- CATALYTIC ACTIVITY: CC Reaction=beta-D-fructose 6-phosphate + diphosphate = beta-D- CC fructose 1,6-bisphosphate + H(+) + phosphate; CC Xref=Rhea:RHEA:13613, ChEBI:CHEBI:15378, ChEBI:CHEBI:32966, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:43474, ChEBI:CHEBI:57634; CC EC=2.7.1.90; 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 -!- ACTIVITY REGULATION: Non-allosteric. {ECO:0000256|HAMAP- CC Rule:MF_01976}. 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:EXU65302.1}. 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; JABQ01000041; EXU65302.1; -; Genomic_DNA. DR RefSeq; WP_037956768.1; NZ_JABQ01000041.1. DR EnsemblBacteria; EXU65302; EXU65302; Z951_25890. DR PATRIC; fig|1158056.3.peg.5190; -. DR UniPathway; UPA00109; UER00182. DR Proteomes; UP000019949; 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:InterPro. DR GO; GO:0047334; F:diphosphate-fructose-6-phosphate 1-phosphotransferase activity; IEA:UniProtKB-EC. 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 Complete proteome {ECO:0000313|Proteomes:UP000019949}; 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:EXU65302.1}; 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 Transferase {ECO:0000256|HAMAP-Rule:MF_01976, KW ECO:0000256|SAAS:SAAS00436075, ECO:0000313|EMBL:EXU65302.1}. FT DOMAIN 2 296 PFK. {ECO:0000259|Pfam:PF00365}. FT REGION 125 127 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01976}. FT REGION 169 171 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01976}. FT REGION 271 274 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01976}. FT ACT_SITE 127 127 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_01976}. FT METAL 103 103 Magnesium; catalytic. {ECO:0000256|HAMAP- FT Rule:MF_01976}. FT BINDING 10 10 Diphosphate; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01976}. FT BINDING 162 162 Substrate; shared with dimeric partner. FT {ECO:0000256|HAMAP-Rule:MF_01976}. FT BINDING 221 221 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01976}. FT BINDING 265 265 Substrate; shared with dimeric partner. FT {ECO:0000256|HAMAP-Rule:MF_01976}. FT SITE 104 104 Important for catalytic activity and FT substrate specificity; stabilizes the FT transition state when the phosphoryl FT donor is PPi; prevents ATP from binding FT by mimicking the alpha-phosphate group of FT ATP. {ECO:0000256|HAMAP-Rule:MF_01976}. FT SITE 124 124 Important for catalytic activity; FT stabilizes the transition state when the FT phosphoryl donor is PPi. FT {ECO:0000256|HAMAP-Rule:MF_01976}. SQ SEQUENCE 341 AA; 35937 MW; B3F5339D3DC077AD CRC64; MRVGVLTGGG DCPGLNAAIR GIVRKGVEVH GFEFVGVRDG WRGALEGAIV PLDVPAVRGI LPRGGTILGS SRTNPLAGEG GVDRVRETLA EYEVDALIAI GGEDTLGVAA ALVGEGIQVV GVPKTIDNDV AGTDYTFGFD TAVNIATEAI DRLHTTAESH TRTLVVEVMG RHSGWIALHS GIAGGANVIL IPEQPFDIGQ VCAWVENRFT IRYAPIVVVA EGAVPKEGQM VVKDSSLDEF GHVRLSGIGE WLSHEIADHT GKEARTTVLG HVQRGGTPSA FDRWLATRFG LRAIDAVKDR DFGTMVALRG TDIVRIPLAD ATVGTKGVDP ALYSEFGVFF G //