HAMAP rule MF_01288
General rule information
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| Accession | MF_01288 |
| Dates | 19-SEP-2008 (Created)
26-JAN-2023 (Last updated, Version 14) |
| Name | Rhamnon_dehydrat |
| Scope(s) |
Bacteria Actinomycetota Pseudomonadota Archaea |
| Template(s) | Q8ZNF9 (RHMD_SALTY); P77215 (RHMD_ECOLI); Q12DF1 (RHMD_POLSJ); [ Recover all ] |
| Triggered by |
HAMAP; MF_01288 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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| Identifier | RHMD |
| case <OC:Bacteria> | |
| Protein name | RecName: Full=L-rhamnonate dehydratase; Short=RhamD; EC=4.2.1.90; |
| end case | |
| case <OC:Archaea> | |
| Protein name | RecName: Full=Putative L-rhamnonate dehydratase; Short=RhamD; EC=4.2.1.90; |
| end case | |
| Gene name | Name=rhmD; |
Comments
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| FUNCTION | Catalyzes the dehydration of L-rhamnonate to 2-keto-3-deoxy- L-rhamnonate (KDR). |
| CATALYTIC ACTIVITY | Reaction=L-rhamnonate = 2-dehydro-3-deoxy-L-rhamnonate + H2O; Xref=Rhea:RHEA:23080, ChEBI:CHEBI:15377, ChEBI:CHEBI:58118, ChEBI:CHEBI:58371; EC=4.2.1.90; |
| case <FTGroup:1> | |
| COFACTOR | Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Note=Binds 1 Mg(2+) ion per subunit.; |
| end case | |
| case <OC:Pseudomonadota> | |
| SUBUNIT | Homooctamer; tetramer of dimers. |
| end case | |
| MISCELLANEOUS | Reaction proceeds via a syn dehydration. |
| SIMILARITY | Belongs to the mandelate racemase/muconate lactonizing enzyme family. RhamD subfamily. |
Keywords
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| Lyase | |
| case <FTGroup:1> | |
| Magnesium | |
| Metal-binding | |
| end case | |
Gene Ontology
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| case <FTGroup:1> | |
| GO:0000287; Molecular function:magnesium ion binding | |
| end case | |
| GO:0050032; Molecular function:L-rhamnonate dehydratase activity | |
Cross-references
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| PROSITE | PS00908; MR_MLE_1; 1; |
| PROSITE | PS00909; MR_MLE_2; 1; |
| Pfam | PF01188; MR_MLE; 1; |
| Pfam | PF02746; MR_MLE_N; 1; |
Features
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| From: RHMD_SALTY (Q8ZNF9) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| ACT_SITE | 329 | 329 | /note="Proton acceptor" | H | ||||||||
| BINDING | 226 | 226 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" |
D | 1 | |||||||
| BINDING | 252 | 252 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" |
E | 1 | |||||||
| BINDING | 280 | 280 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" |
E | 1 | |||||||
| BINDING | 33 | 33 | /ligand="substrate" | H | ||||||||
| BINDING | 59 | 59 | /ligand="substrate" | R | ||||||||
| BINDING | 349 | 349 | /ligand="substrate" | E | ||||||||
| SITE | 302 | 302 | /note="Increases basicity of active site His" | D | ||||||||
| SITE | 349 | 349 | /note="Transition state stabilizer" | E | ||||||||
Additional information
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| Size range | 390-428 amino acids |
| Related rules |
None |
| Fusion | Nter: None Cter: None |