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HAMAP rule MF_01855

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General rule information [?]

Accession MF_01855
Dates 23-JAN-2009 (Created)
17-JAN-2023 (Last updated, Version 24)
Name FBPase_class1
Scope
Bacteria
Archaea; Euryarchaeota
Templates P0A993 (F16PA_ECOLI); Q59943 (F16PA_SYNE7): [Recover all]
Triggered by

Propagated annotation [?]


Identifier, protein and gene names [?]

Identifier
F16PA
Protein name
RecName: Full=Fructose-1,6-bisphosphatase class 1;
Short=FBPase class 1;
EC 3.1.3.11;
AltName: Full=D-fructose-1,6-bisphosphate 1-phosphohydrolase class 1;
Gene name
fbp

Comments [?]

Catalytic activity RHEA:11064: beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-phosphate + phosphate
EC 3.1.3.11
case <FTGroup:1>
Cofactor Mg(2+)
Note: Binds 2 magnesium ions per subunit.
end case
case <Property:PHOTOSYN>
Pathway Carbohydrate biosynthesis; Calvin cycle.
else
Pathway Carbohydrate biosynthesis; gluconeogenesis.
end case
Subunit Homotetramer.
Subcellular location Cytoplasm.
Similarity Belongs to the FBPase class 1 family.

Keywords [?]

case <Property:PHOTOSYN>
Calvin cycle
end case
Carbohydrate metabolism
Cytoplasm
Hydrolase
case <FTGroup:1>
Magnesium
Metal-binding
end case

Gene Ontology [?]

GO:0042132; Molecular function: fructose 1,6-bisphosphate 1-phosphatase activity.
case <FTGroup:1>
GO:0000287; Molecular function: magnesium ion binding.
end case
GO:0016051; Biological process: carbohydrate biosynthetic process.
case <Property:PHOTOSYN>
GO:0019253; Biological process: reductive pentose-phosphate cycle.
end case
GO:0005737; Cellular component: cytoplasm.

Cross-references [?]

Pfam PF00316; FBPase; 1;
PRINTS PR00115; F16BPHPHTASE; 1;
PROSITE PS00124; FBPASE; 1;

Features [?]

From: F16PA_ECOLI (P0A993)
Key     From     To       Description   Tag   Condition   FTGroup
BINDING (Optional)     113     116       /ligand="substrate     [DN]-G-S-S  
BINDING (Optional)     257     259       /ligand="substrate     Y-L-Y  
BINDING     89     89       /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" /ligand_label="1     E   1
BINDING     110     110       /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" /ligand_label="1     D   1
BINDING     110     110       /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" /ligand_label="2     D   1
BINDING     112     112       /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" /ligand_label="1     [LIV]   1
BINDING     113     113       /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" /ligand_label="2     D   1
BINDING     275     275       /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" /ligand_label="2     [ED]   1
BINDING (Optional)     206     206       /ligand="substrate     N  
BINDING (Optional)     239     239       /ligand="substrate     Y  
BINDING (Optional)     269     269       /ligand="substrate     K  

Additional information [?]

Size range 279-378 amino acids
Related rules None
Fusion None
Comments The E.coli protein is subject to complex allosteric regulation. This may be the case for other members of this family. Conserved metal binding sites are missing in METS4 and in second and third copies in PARP8. Sequences are not shown in alignment.


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