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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(s) Bacteria
Archaea
Euryarchaeota
Template(s) P0A993 (F16PA_ECOLI); Q59943 (F16PA_SYNE7); [ Recover all ]
Triggered by HAMAP; MF_01855 (Get profile general information and statistics)

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 Name=fbp;

Comments [?]

CATALYTIC ACTIVITY Reaction=beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6- phosphate + phosphate; Xref=Rhea:RHEA:11064, ChEBI:CHEBI:15377, ChEBI:CHEBI:32966, ChEBI:CHEBI:43474, ChEBI:CHEBI:57634; EC=3.1.3.11;
case <FTGroup:1>
COFACTOR Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Note=Binds 2 magnesium ions per subunit.;
end case
case <Property:PHOTOSYN>
PATHWAYCarbohydrate biosynthesis; Calvin cycle.
else
PATHWAYCarbohydrate biosynthesis; gluconeogenesis.
end case
SUBUNITHomotetramer.
SUBCELLULAR LOCATIONCytoplasm.
SIMILARITYBelongs 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 113 116 /ligand="substrate" [DN]-G-S-S
BINDING 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 206 206 /ligand="substrate" N
BINDING 239 239 /ligand="substrate" Y
BINDING 269 269 /ligand="substrate" K

Additional information [?]

Size range 279-378 amino acids
Related rules None
Fusion Nter: None Cter: 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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