HAMAP rule MF_00989
General rule information
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| PURL | https://purl.expasy.org/hamap/rule/MF_00989 |
| Accession | MF_00989 |
| Dates | 29-JAN-2014 (Created)
1-JUN-2023 (Last updated, Version 10) |
| Name | AraD_entero |
| Scope(s) |
Bacteria Enterobacteriaceae |
| Template(s) | P08203 (ARAD_ECOLI); [ Recover all ] |
| Triggered by |
HAMAP; MF_00989 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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| Identifier | ARAD |
| case <FTGroup:1> | |
| Protein name | RecName: Full=L-ribulose-5-phosphate 4-epimerase; EC=5.1.3.4; AltName: Full=Phosphoribulose isomerase; |
| end case | |
| case not <FTGroup:1> | |
| Protein name | RecName: Full=Putative L-ribulose-5-phosphate 4-epimerase; |
| end case | |
| Gene name | Name=araD; |
Comments
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| FUNCTION | Involved in the degradation of L-arabinose. Catalyzes the interconversion of L-ribulose 5-phosphate (LRu5P) and D-xylulose 5- phosphate (D-Xu5P) via a retroaldol/aldol mechanism (carbon-carbon bond cleavage analogous to a class II aldolase reaction). |
| CATALYTIC ACTIVITY | Reaction=L-ribulose 5-phosphate = D-xylulose 5-phosphate; Xref=Rhea:RHEA:22368, ChEBI:CHEBI:57737, ChEBI:CHEBI:58226; EC=5.1.3.4; |
| COFACTOR | Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 1 zinc ion per subunit.; |
| PATHWAY | Carbohydrate degradation; L-arabinose degradation via L- ribulose; D-xylulose 5-phosphate from L-arabinose (bacterial route): 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:0008742; Molecular function:L-ribulose-phosphate 4-epimerase activity |
| GO:0008270; Molecular function:zinc ion binding |
| GO:0019569; Biological process:L-arabinose catabolic process to xylulose 5-phosphate |
Cross-references
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Features
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| From: ARAD_ECOLI (P08203) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| BINDING | 27 | 28 | /ligand="substrate" | G-N | ||||||||
| BINDING | 44 | 45 | /ligand="substrate" | [TS]-G | ||||||||
| BINDING | 74 | 75 | /ligand="substrate" | S-S | ||||||||
| ACT_SITE | 120 | 120 | /note="Proton donor/acceptor" | D | ||||||||
| ACT_SITE | 229 | 229 | /note="Proton donor/acceptor" | Y | ||||||||
| BINDING | 76 | 76 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" |
D | 1 | |||||||
| BINDING | 95 | 95 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" |
H | 1 | |||||||
| BINDING | 97 | 97 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" |
H | 1 | |||||||
| BINDING | 171 | 171 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" |
H | 1 | |||||||
Additional information
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| Size range | 225-270 amino acids |
| Related rules |
None |
| Fusion | Nter: None Cter: None |