HAMAP rule MF_00197
General rule information
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| PURL | https://purl.expasy.org/hamap/rule/MF_00197 |
| Accession | MF_00197 |
| Dates | 28-FEB-2005 (Created)
09-JAN-2025 (Last updated, Version 27) |
| Name | DAP_epimerase |
| Scope(s) |
Bacteria Archaea |
| Template(s) | P0A6K1; P44859; Q8NP73; P9WP19; [ Recover all ] |
| Triggered by |
HAMAP; MF_00197 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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| Identifier | DAPF |
| Protein name | RecName: Full=Diaminopimelate epimerase; Short=DAP epimerase; EC=5.1.1.7; AltName: Full=PLP-independent amino acid racemase; |
| Gene name | Name=dapF; |
Comments
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| case <OC:Bacteria> | |
| FUNCTION | Catalyzes the stereoinversion of LL-2,6-diaminopimelate (L,L- DAP) to meso-diaminopimelate (meso-DAP), a precursor of L-lysine and an essential component of the bacterial peptidoglycan. |
| end case | |
| case <OC:Archaea> | |
| FUNCTION | Catalyzes the stereoinversion of LL-2,6-diaminopimelate (L,L- DAP) to meso-diaminopimelate (meso-DAP), a precursor of L-lysine. |
| end case | |
| CATALYTIC ACTIVITY | Reaction=(2S,6S)-2,6-diaminopimelate = meso-2,6-diaminopimelate; Xref=Rhea:RHEA:15393, ChEBI:CHEBI:57609, ChEBI:CHEBI:57791; EC=5.1.1.7; |
| PATHWAY | Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; DL-2,6-diaminopimelate from LL-2,6-diaminopimelate: step 1/1. |
| SUBUNIT | Homodimer. |
| SUBCELLULAR LOCATION | Cytoplasm. |
| SIMILARITY | Belongs to the diaminopimelate epimerase family. |
Keywords
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Gene Ontology
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| GO:0008837; Molecular function:diaminopimelate epimerase activity |
| GO:0009089; Biological process:lysine biosynthetic process via diaminopimelate |
| GO:0005737; Cellular component:cytoplasm |
Cross-references
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Features
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| From: DAPF_HAEIN (P44859) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| BINDING | 74 | 75 | /ligand="substrate" | [GI]-N | ||||||||
| BINDING | 208 | 209 | /ligand="substrate" | E-R | ||||||||
| BINDING | 218 | 219 | /ligand="substrate" | G-[ST] | ||||||||
| ACT_SITE | 73 | 73 | /note="Proton donor" | C | ||||||||
| ACT_SITE | 217 | 217 | /note="Proton acceptor" | C | ||||||||
| BINDING | 11 | 11 | /ligand="substrate" | N | ||||||||
| BINDING | 44 | 44 | /ligand="substrate" | Q | ||||||||
| BINDING | 64 | 64 | /ligand="substrate" | [NQ] | ||||||||
| BINDING | 157 | 157 | /ligand="substrate" | N | ||||||||
| BINDING | 190 | 190 | /ligand="substrate" | N | ||||||||
| SITE | 159 | 159 | /note="Could be important to modulate the pK values of the two catalytic cysteine residues" | H | ||||||||
| SITE | 208 | 208 | /note="Could be important to modulate the pK values of the two catalytic cysteine residues" | E | ||||||||
| case <OC:Gammaproteobacteria> | ||||||||||||
| SITE | 268 | 268 | /note="Important for dimerization" | [YF] | ||||||||
| end case | ||||||||||||
Additional information
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| Size range | 249-333 amino acids |
| Related rules |
None |
| Fusion | Nter: None Cter: None |
| Comments | DcsC (S.lavendulae) belongs to the same group of racemases/epimerases as diaminopimelate epimerase (DapF) and also utilizes a two-base mechanism involving a pair of cysteine residues, however it function as racemase with O-ureido-L-serine as a substrate. |