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Annotation rule MF_03185 |
General rule information
[?]
Accession |
MF_03185 |
Dates |
16-MAY-2014 (Created) 20-NOV-2019 (Last updated, Version 8) |
Name |
Phosphofructokinase_II_Long_euk |
case <OC:Eukaryota>
end case
Propagated annotation
[?]
Identifier, protein and gene names
[?]
case <OC:Viridiplantae> and not (<FT:1> or <FT:2>)
Protein name |
RecName:
|
Full=Pyrophosphate--fructose 6-phosphate 1-phosphotransferase subunit alpha;
|
|
Short=PFP;
|
AltName:
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Full=6-phosphofructokinase, pyrophosphate dependent;
|
AltName:
|
Full=PPi-PFK;
|
AltName:
|
Full=Pyrophosphate-dependent 6-phosphofructose-1-kinase;
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|
else case (<OC:Viridiplantae>) and <FT:1>
Protein name |
RecName:
|
Full=Pyrophosphate--fructose 6-phosphate 1-phosphotransferase subunit beta;
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Short=PFP;
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|
EC 2.7.1.90;
|
AltName:
|
Full=6-phosphofructokinase, pyrophosphate dependent;
|
AltName:
|
Full=PPi-PFK;
|
AltName:
|
Full=Pyrophosphate-dependent 6-phosphofructose-1-kinase;
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|
else case <FT:1>
Protein name |
RecName:
|
Full=Pyrophosphate--fructose 6-phosphate 1-phosphotransferase;
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|
EC 2.7.1.90;
|
AltName:
|
Full=6-phosphofructokinase, pyrophosphate dependent;
|
AltName:
|
Full=PPi-dependent phosphofructokinase;
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Short=PPi-PFK;
|
AltName:
|
Full=Pyrophosphate-dependent 6-phosphofructose-1-kinase;
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|
else case <FT:2>
Protein name |
RecName:
|
Full=Probable ATP-dependent 6-phosphofructokinase;
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Short=ATP-PFK;
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Short=Phosphofructokinase;
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EC 2.7.1.11;
|
AltName:
|
Full=Phosphohexokinase;
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|
else
end case
case <OC:Viridiplantae> and not (<FT:1> or <FT:2>)
Function |
Regulatory subunit of pyrophosphate--fructose 6-phosphate 1-phosphotransferase. |
else case <OC:Viridiplantae> and <FT:1>
Function |
Catalytic subunit of pyrophosphate--fructose 6-phosphate 1-phosphotransferase. 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. |
Catalytic activity |
RHEA:13613: beta-D-fructose 6-phosphate + diphosphate = beta-D-fructose 1,6-bisphosphate + H(+) + phosphate
EC 2.7.1.90
|
else case <FT:1>
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. |
Catalytic activity |
RHEA:13613: beta-D-fructose 6-phosphate + diphosphate = beta-D-fructose 1,6-bisphosphate + H(+) + phosphate
EC 2.7.1.90
|
Activity regulation |
Non-allosteric. |
else case <FT:2>
Function |
Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis. |
Catalytic activity |
RHEA:16109: ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H(+)
EC 2.7.1.11
|
else
Function |
Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate, the first committing step of glycolysis. |
end case
case <OC:Viridiplantae>
Activity regulation |
Allosterically activated by fructose 2,6-bisphosphate. |
end case
case <FT:1> or <FT:2>
end case
Pathway |
Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4. |
case (<OC:Viridiplantae> or <OC:Apicomplexa>)
Subunit |
Tetramer of two alpha (regulatory) and two beta (catalytic) chains. |
else
Subunit |
Homodimer or monomer. |
end case
Subcellular location |
Cytoplasm. |
Similarity |
Belongs to the phosphofructokinase type A (PFKA) family. PPi-dependent PFK group II subfamily. Clade 'Long' sub-subfamily. |
case <OC:Viridiplantae>
end case
case <FT:2>
end case
GO:0003872; Molecular function: 6-phosphofructokinase activity.
GO:0006096; Biological process: glycolytic process.
GO:0005737; Cellular component: cytoplasm.
From: PFP_ENTHI (C4LZC2) |
Key
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From
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To
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Description
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Tag
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Condition
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FTGroup
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SITE (Optional)
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175
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175
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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
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[DN]
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SITE (Optional)
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175
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175
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Important for substrate specificity; cannot use PPi as phosphoryl donor
|
|
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G
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case <FT:1>
BINDING
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80
|
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80
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Diphosphate; via amide nitrogen
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|
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G
|
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SITE
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201
|
|
201
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|
Important for catalytic activity; stabilizes the transition state when the phosphoryl donor is PPi
|
|
|
|
K
|
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|
else case <FT:2>
NP_BIND
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144
|
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145
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ATP
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|
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[RK]-x
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|
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NP_BIND
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173
|
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176
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|
ATP
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G-[DE]-G-[ST]
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|
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BINDING
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80
|
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80
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ATP; via amide nitrogen
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|
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G
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end case
case <FT:1> or <FT:2>
REGION
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202
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204
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Substrate binding
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T-x-D
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REGION (Optional)
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241
|
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242
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Substrate binding; shared with dimeric partner
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|
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K-Y
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REGION
|
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249
|
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251
|
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Substrate binding
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|
|
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M-G-[RH]
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REGION
|
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420
|
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423
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Substrate binding
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[HY]-x(2)-R
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ACT_SITE
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204
|
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204
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Proton acceptor
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D
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METAL
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174
|
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174
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Magnesium; catalytic
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[DE]
|
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BINDING
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310
|
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310
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Substrate
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|
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E
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end case
Additional information
[?]
Size range |
544-1426 amino acids |
Related rules |
MF_01980 (PFP) |
Fusion |
None |
Comments |
Classification of type A phosphofructokinases into subfamilies was done according to Mueller at al.(2001) (PubMed:11673446) and Bapteste et al.(2003) (PubMed:14585511). Phosphoryl donor specificity (ATP or PPi) seems to be determined by a single residue, Asp or Gly-175 (PFP_ENTHI numbering) according to Chi et al.(2000) (PubMeed:11001940), Moore et al.(2002) (PubMed:12015149), and Bapteste et al.(2003) (PubMed:14585511) and references therein. |