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HAMAP rule MF_00987

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General rule information [?]

Accession MF_00987
Dates 22-JAN-2014 (Created)
19-NOV-2022 (Last updated, Version 10)
Name FucA
Scope
Bacteria
Template P0AB87 (FUCA_ECOLI)
Triggered by

Propagated annotation [?]


Identifier, protein and gene names [?]

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
fucA

Comments [?]

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 RHEA:12933: L-fuculose 1-phosphate = (S)-lactaldehyde + dihydroxyacetone phosphate
EC 4.1.2.17
Cofactor Zn(2+)
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 [?]

Arabinose catabolism
Carbohydrate metabolism
Fucose metabolism
Lyase
Metal-binding
Zinc

Gene Ontology [?]

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 [?]

Pfam PF00596; Aldolase_II; 1;
TIGRFAMs TIGR01086; fucA; 1;

Features [?]

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       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       Plays a key role in the stabilization of the transition state and positioning the aldehyde component     Y  
SITE     131     131       Plays a key role in the stabilization of the transition state and positioning the aldehyde component     F  
SITE     209     209       Plays a key role in the stabilization of the transition state and positioning the aldehyde component     Y  

Additional information [?]

Size range 195-230 amino acids
Related rules None
Fusion None


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