PFP_AMYME
ID PFP_AMYME Reviewed; 341 AA.
AC Q59126;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2003, sequence version 2.
DT 03-AUG-2022, entry version 101.
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};
OS Amycolatopsis methanolica.
OC Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC Amycolatopsis; Amycolatopsis methanolica group.
OX NCBI_TaxID=1814;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 44096 / JCM 8087 / NBRC 15065 / NCIMB 11946 / NRRL B-24139 / LMD
RC 80.32 / 239;
RX PubMed=8550409; DOI=10.1128/jb.178.1.149-155.1996;
RA Alves A.M., Meijer W.G., Vrijbloed J.W., Dijkhuizen L.;
RT "Characterization and phylogeny of the pfp gene of Amycolatopsis
RT methanolica encoding PPi-dependent phosphofructokinase.";
RL J. Bacteriol. 178:149-155(1996).
RN [2]
RP PROTEIN SEQUENCE OF 1-40, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION.
RC STRAIN=DSM 44096 / JCM 8087 / NBRC 15065 / NCIMB 11946 / NRRL B-24139 / LMD
RC 80.32 / 239;
RX PubMed=7961441; DOI=10.1128/jb.176.22.6827-6835.1994;
RA Alves A.M., Euverink G.J., Hektor H.J., Hessels G.I., van der Vlag J.,
RA Vrijbloed J.W., Hondmann D., Visser J., Dijkhuizen L.;
RT "Enzymes of glucose and methanol metabolism in the actinomycete
RT Amycolatopsis methanolica.";
RL J. Bacteriol. 176:6827-6835(1994).
RN [3]
RP FUNCTION, AND INDUCTION.
RC STRAIN=DSM 44096 / JCM 8087 / NBRC 15065 / NCIMB 11946 / NRRL B-24139 / LMD
RC 80.32 / 239;
RX PubMed=11717283; DOI=10.1128/jb.183.24.7231-7240.2001;
RA Alves A.M., Euverink G.J., Santos H., Dijkhuizen L.;
RT "Different physiological roles of ATP- and PP(i)-dependent
RT phosphofructokinase isoenzymes in the methylotrophic actinomycete
RT Amycolatopsis methanolica.";
RL J. Bacteriol. 183:7231-7240(2001).
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, ECO:0000269|PubMed:11717283,
CC ECO:0000269|PubMed:7961441}.
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 ECO:0000269|PubMed:7961441};
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 ECO:0000269|PubMed:7961441}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.84 mM for phosphate {ECO:0000269|PubMed:7961441};
CC KM=0.2 mM for diphosphate {ECO:0000269|PubMed:7961441};
CC KM=0.4 mM for fructose 6-phosphate {ECO:0000269|PubMed:7961441};
CC KM=0.025 mM for fructose 1,6-bisphosphate
CC {ECO:0000269|PubMed:7961441};
CC Vmax=58 umol/min/mg enzyme for the forward reaction
CC {ECO:0000269|PubMed:7961441};
CC Vmax=59 umol/min/mg enzyme for the reverse reaction
CC {ECO:0000269|PubMed:7961441};
CC pH dependence:
CC Optimum pH is 7.5 for both the forward and the reverse reactions.
CC {ECO:0000269|PubMed:7961441};
CC Temperature dependence:
CC Optimum temperature is 35-46 degrees Celsius.
CC {ECO:0000269|PubMed:7961441};
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: Homotetramer. {ECO:0000269|PubMed:7961441}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01976}.
CC -!- INDUCTION: Present when grown on glucose.
CC {ECO:0000269|PubMed:11717283}.
CC -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family.
CC Mixed-substrate PFK group III subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_01976}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB01683.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U31277; AAB01683.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q59126; -.
DR SMR; Q59126; -.
DR BRENDA; 2.7.1.90; 314.
DR SABIO-RK; Q59126; -.
DR UniPathway; UPA00109; UER00182.
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 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Glycolysis; Kinase; Magnesium;
KW Metal-binding; Transferase.
FT CHAIN 1..341
FT /note="Pyrophosphate--fructose 6-phosphate 1-
FT phosphotransferase"
FT /id="PRO_0000112011"
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; 36229 MW; 306613246172D36B CRC64;
MRVGVLTGGG DCPGLNAVIR AVVRKGIEAH GWEIVGFRSG WRGPLTGDSR PLGLDDVEEI
LIRGGTILGS SRTNPYKEEG GVEKIRAVLA DQGVDALIAI GGEDTLGVAK KLTDDGIGVV
GVPKTIDNDL AATDYTFGFD TAVHIATEAI DRLRTTAESH YRAMVVEVMG RHAGWIALHA
GLAGGANVIL VPERPFSVEQ VVEWVERRFE KMYAPIIVVA EGAVPEGGAE VLRTGEKDAF
GHVQLGGVGT WLADEIAERT GKESRAVVLG HTQRGGTPTA YDRVLATRFG LHAVDAVADG
DFGTMVALRG TDIVRVKLAE ATAELKTVPP ERYEEAEVFF G
