HAMAP rule MF_00987
General rule information
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| Accession | MF_00987 |
| Dates | 22-JAN-2014 (Created)
1-JUN-2023 (Last updated, Version 11) |
| Name | FucA |
| Scope(s) |
Bacteria |
| Template(s) | P0AB87 (FUCA_ECOLI); [ Recover all ] |
| Triggered by |
HAMAP; MF_00987 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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| Identifier | FUCA |
| case <FTGroup:1> | |
| Protein name | RecName: Full=L-fuculose phosphate aldolase; EC=4.1.2.17; AltName: Full=D-ribulose-phosphate aldolase; AltName: Full=L-fuculose-1-phosphate aldolase; |
| end case | |
| case not <FTGroup:1> | |
| Protein name | RecName: Full=Putative L-fuculose phosphate aldolase; |
| end case | |
| Gene name | Name=fucA; |
Comments
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| FUNCTION | Involved in the degradation of L-fucose and D-arabinose. Catalyzes the reversible cleavage of L-fuculose 1-phosphate (Fuc1P) to yield dihydroxyacetone phosphate (DHAP) and L-lactaldehyde. |
| CATALYTIC ACTIVITY | Reaction=L-fuculose 1-phosphate = (S)-lactaldehyde + dihydroxyacetone phosphate; Xref=Rhea:RHEA:12933, ChEBI:CHEBI:18041, ChEBI:CHEBI:57642, ChEBI:CHEBI:57846; EC=4.1.2.17; |
| COFACTOR | Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 1 zinc ion per subunit.; |
| PATHWAY | Carbohydrate degradation; L-fucose degradation; L-lactaldehyde and glycerone phosphate from L-fucose: step 3/3. |
| SUBUNIT | Homotetramer. |
| SIMILARITY | Belongs to the aldolase class II family. AraD/FucA subfamily. |
Keywords
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Gene Ontology
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| GO:0008738; Molecular function:L-fuculose-phosphate aldolase activity |
| GO:0008270; Molecular function:zinc ion binding |
| GO:0042355; Biological process:L-fucose catabolic process |
Cross-references
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Features
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| From: FUCA_ECOLI (P0AB87) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| BINDING | 28 | 29 | /ligand="substrate" | G-N | ||||||||
| BINDING | 43 | 44 | /ligand="substrate" | [TS]-G | ||||||||
| BINDING | 71 | 72 | /ligand="substrate" | S-S | ||||||||
| ACT_SITE | 73 | 73 | /note="Proton donor/acceptor" | E | ||||||||
| BINDING | 73 | 73 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_note="catalytic" |
E | 1 | |||||||
| BINDING | 92 | 92 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_note="catalytic" |
H | 1 | |||||||
| BINDING | 94 | 94 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_note="catalytic" |
H | 1 | |||||||
| BINDING | 155 | 155 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_note="catalytic" |
H | 1 | |||||||
| SITE | 113 | 113 | /note="Plays a key role in the stabilization of the transition state and positioning the aldehyde component" | Y | ||||||||
| SITE | 131 | 131 | /note="Plays a key role in the stabilization of the transition state and positioning the aldehyde component" | F | ||||||||
| SITE | 209 | 209 | /note="Plays a key role in the stabilization of the transition state and positioning the aldehyde component" | Y | ||||||||
Additional information
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| Size range | 195-230 amino acids |
| Related rules |
None |
| Fusion | Nter: None Cter: None |