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Pyrophosphate--fructose 6-phosphate 1-phosphotransferase (EC 2.7.1.90) (6-phosphofructokinase, pyrophosphate dependent) (PPi-dependent phosphofructokinase) (PPi-PFK) (Pyrophosphate-dependent 6-phosphofructose-1-kinase)

 U1R1S3_9ACTO            Unreviewed;       404 AA.
U1R1S3;
13-NOV-2013, integrated into UniProtKB/TrEMBL.
13-NOV-2013, sequence version 1.
27-SEP-2017, entry version 22.
RecName: Full=Pyrophosphate--fructose 6-phosphate 1-phosphotransferase {ECO:0000256|HAMAP-Rule:MF_01977};
EC=2.7.1.90 {ECO:0000256|HAMAP-Rule:MF_01977};
AltName: Full=6-phosphofructokinase, pyrophosphate dependent {ECO:0000256|HAMAP-Rule:MF_01977};
AltName: Full=PPi-dependent phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_01977};
Short=PPi-PFK {ECO:0000256|HAMAP-Rule:MF_01977};
AltName: Full=Pyrophosphate-dependent 6-phosphofructose-1-kinase {ECO:0000256|HAMAP-Rule:MF_01977};
Name=pfp {ECO:0000256|HAMAP-Rule:MF_01977};
ORFNames=HMPREF1550_02203 {ECO:0000313|EMBL:ERH27971.1};
Actinomyces sp. oral taxon 877 str. F0543.
Bacteria; Actinobacteria; Actinomycetales; Actinomycetaceae;
Actinomyces.
NCBI_TaxID=1227264 {ECO:0000313|EMBL:ERH27971.1, ECO:0000313|Proteomes:UP000016532};
[1] {ECO:0000313|EMBL:ERH27971.1, ECO:0000313|Proteomes:UP000016532}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=F0543 {ECO:0000313|EMBL:ERH27971.1,
ECO:0000313|Proteomes:UP000016532};
Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R.,
Courtney L., Fronick C., O'Laughlin M., Godfrey J., Wilson R.M.,
Miner T., Farmer C., Delehaunty K., Cordes M., Minx P., Tomlinson C.,
Chen J., Wollam A., Pepin K.H., Bhonagiri V., Zhang X., Warren W.,
Mitreva M., Mardis E.R., Wilson R.K.;
Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate,
the first committing step of glycolysis. Uses inorganic phosphate
(PPi) as phosphoryl donor instead of ATP like common ATP-dependent
phosphofructokinases (ATP-PFKs), which renders the reaction
reversible, and can thus function both in glycolysis and
gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of
both the forward (ATP-PFK) and reverse (fructose-bisphosphatase
(FBPase)) reactions. {ECO:0000256|HAMAP-Rule:MF_01977}.
-!- CATALYTIC ACTIVITY: Diphosphate + D-fructose 6-phosphate =
phosphate + D-fructose 1,6-bisphosphate. {ECO:0000256|HAMAP-
Rule:MF_01977}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000256|HAMAP-Rule:MF_01977};
-!- ENZYME REGULATION: Non-allosteric. {ECO:0000256|HAMAP-
Rule:MF_01977}.
-!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
phosphate and glycerone phosphate from D-glucose: step 3/4.
{ECO:0000256|HAMAP-Rule:MF_01977}.
-!- SUBUNIT: Homodimer or homotetramer. {ECO:0000256|HAMAP-
Rule:MF_01977}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01977}.
-!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA)
family. PPi-dependent PFK group II subfamily. Clade "P" sub-
subfamily. {ECO:0000256|HAMAP-Rule:MF_01977}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:ERH27971.1}.
-----------------------------------------------------------------------
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EMBL; AWSG01000154; ERH27971.1; -; Genomic_DNA.
RefSeq; WP_021613014.1; NZ_KE952330.1.
EnsemblBacteria; ERH27971; ERH27971; HMPREF1550_02203.
PATRIC; fig|1227264.3.peg.1891; -.
OrthoDB; POG091H01AC; -.
UniPathway; UPA00109; UER00182.
Proteomes; UP000016532; Unassembled WGS sequence.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0003872; F:6-phosphofructokinase activity; IEA:UniProtKB-UniRule.
GO; GO:0047334; F:diphosphate-fructose-6-phosphate 1-phosphotransferase activity; IEA:UniProtKB-EC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:InterPro.
HAMAP; MF_01977; Phosphofructokinase_II_P; 1.
InterPro; IPR022953; ATP_PFK.
InterPro; IPR000023; Phosphofructokinase_dom.
InterPro; IPR011405; PPi-PFK_SMc01852.
Pfam; PF00365; PFK; 1.
PIRSF; PIRSF036484; PPi-PFK_SMc01852; 1.
PRINTS; PR00476; PHFRCTKINASE.
SUPFAM; SSF53784; SSF53784; 1.
3: Inferred from homology;
Complete proteome {ECO:0000313|Proteomes:UP000016532};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01977};
Glycolysis {ECO:0000256|HAMAP-Rule:MF_01977};
Kinase {ECO:0000256|HAMAP-Rule:MF_01977};
Magnesium {ECO:0000256|HAMAP-Rule:MF_01977};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_01977};
Transferase {ECO:0000256|HAMAP-Rule:MF_01977}.
DOMAIN 5 349 PFK. {ECO:0000259|Pfam:PF00365}.
REGION 150 152 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_01977}.
REGION 195 197 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_01977}.
REGION 324 327 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_01977}.
ACT_SITE 152 152 Proton acceptor. {ECO:0000256|HAMAP-
Rule:MF_01977}.
METAL 122 122 Magnesium; catalytic. {ECO:0000256|HAMAP-
Rule:MF_01977}.
BINDING 13 13 Diphosphate; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_01977}.
BINDING 267 267 Substrate. {ECO:0000256|HAMAP-
Rule:MF_01977}.
SITE 123 123 Important for catalytic activity and
substrate specificity; stabilizes the
transition state when the phosphoryl
donor is PPi; prevents ATP from binding
by mimicking the alpha-phosphate group of
ATP. {ECO:0000256|HAMAP-Rule:MF_01977}.
SITE 149 149 Important for catalytic activity;
stabilizes the transition state when the
phosphoryl donor is PPi.
{ECO:0000256|HAMAP-Rule:MF_01977}.
SEQUENCE 404 AA; 44439 MW; 7B00727DDD207309 CRC64;
MSVRRVALLT AGGFAPCLSS AVGGLIERYT EIDPTVEIIA YQNGYHGLLT GNYVVVDEDA
RAHAAVLHRF GGSPIGNSRV KLTNKKNLVE RGLVAEDENP LEKAAEQLRK DGVDVLHTIG
GDDTNTTAAD LAAYLEEHDY HLTVVGLPKT IDNDVVPIRQ SLGAWTAAEE VSEYSQNVIG
EHRSNPRMLI IHEIMGRNCG WLTAAGSRCY HEWLKTQEWV PSIGLSKERW DIHAIFLPEM
KIDLDAEAKR LKAIMDEQGN VNIFLSEGAG VPEIIAEIEA AGGEVQRDPF GHVKLDTINP
GQWFAKQFAE KIDAEKVMVQ KSGYFSRSSR ANADDLRLIK SMTDLAVECA FKGESGVIGH
DEEDGDRLKA IPFPRIAGGK PFDITQKWFI DLMAEIGQDV VPAK


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