PFP_AMYMS
ID PFP_AMYMS Reviewed; 341 AA.
AC Q9AGC0; G0G7F4;
DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Pyrophosphate--fructose 6-phosphate 1-phosphotransferase {ECO:0000255|HAMAP-Rule:MF_01976};
DE EC=2.7.1.90 {ECO:0000255|HAMAP-Rule:MF_01976};
DE AltName: Full=6-phosphofructokinase, pyrophosphate dependent {ECO:0000255|HAMAP-Rule:MF_01976};
DE AltName: Full=PPi-dependent phosphofructokinase {ECO:0000255|HAMAP-Rule:MF_01976};
DE Short=PPi-PFK {ECO:0000255|HAMAP-Rule:MF_01976};
DE AltName: Full=Pyrophosphate-dependent 6-phosphofructose-1-kinase {ECO:0000255|HAMAP-Rule:MF_01976};
GN Name=pfp {ECO:0000255|HAMAP-Rule:MF_01976}; Synonyms=pfk, pfkA;
GN OrderedLocusNames=RAM_12510, AMES_2433;
OS Amycolatopsis mediterranei (strain S699) (Nocardia mediterranei).
OC Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC Amycolatopsis.
OX NCBI_TaxID=713604;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=S699;
RA Kuan L., Mueller M., August P.R., Pogosova-Agadjanyan E., Floss H.G.,
RA Yu T.;
RT "Characterization and cloning of three 3-deoxy D-arabinoheptulosonate 7-
RT phosphate synthase isoenzymes from Amycolatopsis mediterranei S699.";
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S699;
RX PubMed=21914879; DOI=10.1128/jb.05819-11;
RA Verma M., Kaur J., Kumar M., Kumari K., Saxena A., Anand S., Nigam A.,
RA Ravi V., Raghuvanshi S., Khurana P., Tyagi A.K., Khurana J.P., Lal R.;
RT "Whole genome sequence of the rifamycin B-producing strain Amycolatopsis
RT mediterranei S699.";
RL J. Bacteriol. 193:5562-5563(2011).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S699;
RX PubMed=23012281; DOI=10.1128/jb.01295-12;
RA Tang B., Zhao W., Zheng H., Zhuo Y., Zhang L., Zhao G.P.;
RT "Complete genome sequence of Amycolatopsis mediterranei S699 based on de
RT novo assembly via a combinatorial sequencing strategy.";
RL J. Bacteriol. 194:5699-5700(2012).
CC -!- FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate, the
CC first committing step of glycolysis. Uses inorganic phosphate (PPi) as
CC phosphoryl donor instead of ATP like common ATP-dependent
CC phosphofructokinases (ATP-PFKs), which renders the reaction reversible,
CC and can thus function both in glycolysis and gluconeogenesis.
CC Consistently, PPi-PFK can replace the enzymes of both the forward (ATP-
CC PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions.
CC {ECO:0000255|HAMAP-Rule:MF_01976}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-fructose 6-phosphate + diphosphate = beta-D-fructose
CC 1,6-bisphosphate + H(+) + phosphate; Xref=Rhea:RHEA:13613,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:32966, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57634; EC=2.7.1.90;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01976};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01976};
CC -!- ACTIVITY REGULATION: Non-allosteric. {ECO:0000255|HAMAP-Rule:MF_01976}.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 3/4.
CC {ECO:0000255|HAMAP-Rule:MF_01976}.
CC -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000255|HAMAP-Rule:MF_01976}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01976}.
CC -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family.
CC Mixed-substrate PFK group III subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_01976}.
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DR EMBL; AF336847; AAK28147.1; -; Genomic_DNA.
DR EMBL; CP002896; AEK40992.1; -; Genomic_DNA.
DR EMBL; CP003729; AFO75969.1; -; Genomic_DNA.
DR RefSeq; WP_013224333.1; NC_018266.1.
DR AlphaFoldDB; Q9AGC0; -.
DR SMR; Q9AGC0; -.
DR STRING; 713604.RAM_12510; -.
DR EnsemblBacteria; AEK40992; AEK40992; RAM_12510.
DR KEGG; amm:AMES_2433; -.
DR KEGG; amn:RAM_12510; -.
DR PATRIC; fig|713604.12.peg.2579; -.
DR HOGENOM; CLU_020655_0_0_11; -.
DR OMA; TNRDNPF; -.
DR OrthoDB; 1421302at2; -.
DR UniPathway; UPA00109; UER00182.
DR Proteomes; UP000006138; Chromosome.
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 Gene3D; 3.40.50.460; -; 1.
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 Cytoplasm; Glycolysis; Kinase; Magnesium; Metal-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..341
FT /note="Pyrophosphate--fructose 6-phosphate 1-
FT phosphotransferase"
FT /id="PRO_0000112010"
FT ACT_SITE 127
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
FT BINDING 10
FT /ligand="diphosphate"
FT /ligand_id="ChEBI:CHEBI:33019"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
FT BINDING 103
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
FT BINDING 125..127
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
FT BINDING 162
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
FT BINDING 169..171
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
FT BINDING 221
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
FT BINDING 265
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
FT BINDING 271..274
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
FT SITE 104
FT /note="Important for catalytic activity and substrate
FT specificity; stabilizes the transition state when the
FT phosphoryl donor is PPi; prevents ATP from binding by
FT mimicking the alpha-phosphate group of ATP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
FT SITE 124
FT /note="Important for catalytic activity; stabilizes the
FT transition state when the phosphoryl donor is PPi"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
SQ SEQUENCE 341 AA; 36272 MW; 2B5C28E7BBD57065 CRC64;
MRVGVLTGGG DCPGLNAVIR AVVRKGIEVH GWDFVGFRNG WNGPLTGDSR PLGLNDVEDI
LTRGGTILRS SRTNPYKVEG GVDKIKQVLA DQGVDALIAI GGEDTLGVAK RLTDDGIGVV
GVPKTIDNDL GATDYTFGFD TAVSIATEAI DRLHTTAESH HRALVVEVMG RHAGWIALHS
GLAGGASVIL VPERHFNVDQ VVSWVERRFE KEFAPIIVVA EGALPEGGEE KLLTGEKDAF
GHVRLGGIGT WLADEIAHRT GKESRAVVLG HVQRGGTPTA YDRVLATRFG LNAVDAVADG
DFGVMVALKG TDIVRVKLSE ATAELKTVPV ERYQEAEVFF G
