AC   MF_00989;
DC   Protein; auto
TR   HAMAP; MF_00989; -; 1; level=0
XX
Names: AraD_entero
XX
ID   ARAD
case <FTGroup:1>
DE   RecName: Full=L-ribulose-5-phosphate 4-epimerase;
DE            EC=5.1.3.4;
DE   AltName: Full=Phosphoribulose isomerase;
end case
case not <FTGroup:1>
DE   RecName: Full=Putative L-ribulose-5-phosphate 4-epimerase;
end case
GN   Name=araD;
XX
CC   -!- FUNCTION: Involved in the degradation of L-arabinose. Catalyzes the
CC       interconversion of L-ribulose 5-phosphate (LRu5P) and D-xylulose 5-
CC       phosphate (D-Xu5P) via a retroaldol/aldol mechanism (carbon-carbon bond
CC       cleavage analogous to a class II aldolase reaction).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-ribulose 5-phosphate = D-xylulose 5-phosphate;
CC         Xref=Rhea:RHEA:22368, ChEBI:CHEBI:57737, ChEBI:CHEBI:58226;
CC         EC=5.1.3.4;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC       Note=Binds 1 zinc ion per subunit.;
CC   -!- PATHWAY: Carbohydrate degradation; L-arabinose degradation via L-
CC       ribulose; D-xylulose 5-phosphate from L-arabinose (bacterial route):
CC       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; TIGR00760; araD; 1; trigger=no
XX
KW   Arabinose catabolism
KW   Carbohydrate metabolism
KW   Isomerase
KW   Metal-binding
KW   Zinc
XX
GO   GO:0008742; F:L-ribulose-phosphate 4-epimerase activity
GO   GO:0008270; F:zinc ion binding
GO   GO:0019569; P:L-arabinose catabolic process to xylulose 5-phosphate
XX
FT   From: ARAD_ECOLI (P08203)
FT   BINDING         27..28
FT                   /ligand="substrate"
FT   Condition: G-N
FT   BINDING         44..45
FT                   /ligand="substrate"
FT   Condition: [TS]-G
FT   BINDING         74..75
FT                   /ligand="substrate"
FT   Condition: S-S
FT   ACT_SITE        120
FT                   /note="Proton donor/acceptor"
FT   Condition: D
FT   ACT_SITE        229
FT                   /note="Proton donor/acceptor"
FT   Condition: Y
FT   BINDING         76
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   Group: 1; Condition: D
FT   BINDING         95
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   Group: 1; Condition: H
FT   BINDING         97
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   Group: 1; Condition: H
FT   BINDING         171
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   Group: 1; Condition: H
XX
Size: 225-270;
Related: None;
Template: P08203;
Scope:
 Bacteria; Enterobacteriaceae
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None
XX
# Revision 1.10 2023/06/01
//