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Annotation rule MF_01855 |
General rule information
[?]
Accession |
MF_01855 |
Dates |
23-JAN-2009 (Created) 21-AUG-2020 (Last updated, Version 16) |
Scope |
Bacteria
Archaea; Euryarchaeota |
Propagated annotation
[?]
Identifier, protein and gene names
[?]
Protein name |
RecName:
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Full=Fructose-1,6-bisphosphatase class 1;
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Short=FBPase class 1;
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EC 3.1.3.11;
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AltName:
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Full=D-fructose-1,6-bisphosphate 1-phosphohydrolase class 1;
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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. |
case <Property:PHOTOSYN>
end case
case <FTGroup:1>
end case
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
From: F16PA_ECOLI (P0A993) |
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
|
|
FTGroup
|
REGION (Optional)
|
|
113
|
|
116
|
|
Substrate binding
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|
|
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[DN]-G-S-S
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|
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REGION (Optional)
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257
|
|
259
|
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Substrate binding
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|
|
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Y-L-Y
|
|
|
METAL
|
|
89
|
|
89
|
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Magnesium 1
|
|
|
|
E
|
|
1
|
METAL
|
|
110
|
|
110
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|
Magnesium 1
|
|
|
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D
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|
1
|
METAL
|
|
110
|
|
110
|
|
Magnesium 2
|
|
|
|
D
|
|
1
|
METAL
|
|
112
|
|
112
|
|
Magnesium 1; via carbonyl oxygen
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|
|
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[LIV]
|
|
1
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METAL
|
|
113
|
|
113
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Magnesium 2
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|
|
|
D
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|
1
|
METAL
|
|
275
|
|
275
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|
Magnesium 2
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|
|
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[ED]
|
|
1
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BINDING (Optional)
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206
|
|
206
|
|
Substrate
|
|
|
|
N
|
|
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BINDING (Optional)
|
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239
|
|
239
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Substrate
|
|
|
|
Y
|
|
|
BINDING (Optional)
|
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269
|
|
269
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Substrate
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|
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K
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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. |