HAMAP rule MF_01855
General rule information
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| PURL | https://purl.expasy.org/hamap/rule/MF_01855 |
| Accession | MF_01855 |
| Dates | 23-JAN-2009 (Created)
8-OCT-2024 (Last updated, Version 27) |
| Name | FBPase_class1 |
| Scope(s) |
Bacteria Archaea Methanobacteriati |
| Template(s) | P0A993 (F16PA_ECOLI); Q59943 (F16PA_SYNE7); [ Recover all ] |
| Triggered by |
HAMAP; MF_01855 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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| 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
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| 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> | |
| 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
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| case <Property:PHOTOSYN> | |
| Calvin cycle | |
| end case | |
| Carbohydrate metabolism | |
| Cytoplasm | |
| Hydrolase | |
| case <FTGroup:1> | |
| Magnesium | |
| Metal-binding | |
| end case | |
Gene Ontology
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| GO:0042132; Molecular function:fructose 1,6-bisphosphate 1-phosphatase activity | |
| case <FTGroup:1> | |
| GO:0000287; Molecular function:magnesium ion binding | |
| end case | |
| GO:0006094; Biological process:gluconeogenesis | |
| case <Property:PHOTOSYN> | |
| GO:0019253; Biological process:reductive pentose-phosphate cycle | |
| end case | |
| GO:0005737; Cellular component:cytoplasm | |
Cross-references
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Features
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| 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
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| 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. |