AC   MF_00987;
DC   Protein; auto
TR   HAMAP; MF_00987; -; 1; level=0
XX
Names: FucA
XX
ID   FUCA
case <FTGroup:1>
DE   RecName: Full=L-fuculose phosphate aldolase;
DE            EC=4.1.2.17;
DE   AltName: Full=D-ribulose-phosphate aldolase;
DE   AltName: Full=L-fuculose-1-phosphate aldolase;
end case
case not <FTGroup:1>
DE   RecName: Full=Putative L-fuculose phosphate aldolase;
end case
GN   Name=fucA;
XX
CC   -!- FUNCTION: Involved in the degradation of L-fucose and D-arabinose.
CC       Catalyzes the reversible cleavage of L-fuculose 1-phosphate (Fuc1P) to
CC       yield dihydroxyacetone phosphate (DHAP) and L-lactaldehyde.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-fuculose 1-phosphate = (S)-lactaldehyde + dihydroxyacetone
CC         phosphate; Xref=Rhea:RHEA:12933, ChEBI:CHEBI:18041,
CC         ChEBI:CHEBI:57642, ChEBI:CHEBI:57846; EC=4.1.2.17;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC       Note=Binds 1 zinc ion per subunit.;
CC   -!- PATHWAY: Carbohydrate degradation; L-fucose degradation; L-lactaldehyde
CC       and glycerone phosphate from L-fucose: step 3/3.
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SIMILARITY: Belongs to the aldolase class II family. AraD/FucA
CC       subfamily.
XX
DR   Pfam; PF00596; Aldolase_II; 1; trigger=no
DR   NCBIfam; TIGR01086; fucA; 1; trigger=no
XX
KW   Arabinose catabolism
KW   Carbohydrate metabolism
KW   Fucose metabolism
KW   Lyase
KW   Metal-binding
KW   Zinc
XX
GO   GO:0008738; F:L-fuculose-phosphate aldolase activity
GO   GO:0008270; F:zinc ion binding
GO   GO:0042355; P:L-fucose catabolic process
XX
FT   From: FUCA_ECOLI (P0AB87)
FT   BINDING         28..29
FT                   /ligand="substrate"
FT   Condition: G-N
FT   BINDING         43..44
FT                   /ligand="substrate"
FT   Condition: [TS]-G
FT   BINDING         71..72
FT                   /ligand="substrate"
FT   Condition: S-S
FT   ACT_SITE        73
FT                   /note="Proton donor/acceptor"
FT   Condition: E
FT   BINDING         73
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT   Group: 1; Condition: E
FT   BINDING         92
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT   Group: 1; Condition: H
FT   BINDING         94
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT   Group: 1; Condition: H
FT   BINDING         155
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT   Group: 1; Condition: H
FT   SITE            113
FT                   /note="Plays a key role in the stabilization of the
FT                   transition state and positioning the aldehyde component"
FT   Condition: Y
FT   SITE            131
FT                   /note="Plays a key role in the stabilization of the
FT                   transition state and positioning the aldehyde component"
FT   Condition: F
FT   SITE            209
FT                   /note="Plays a key role in the stabilization of the
FT                   transition state and positioning the aldehyde component"
FT   Condition: Y
XX
Size: 195-230;
Related: None;
Template: P0AB87;
Scope:
 Bacteria
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None
XX
# Revision 1.11 2023/06/01
//