HAMAP rule MF_00197
General rule information
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Accession | MF_00197 |
Dates | 1-JUN-2001 (Created)
1-JUN-2023 (Last updated, Version 36) |
Name | DAP_epimerase |
Scope(s) |
Bacteria Archaea |
Template(s) | P0A6K1 (DAPF_ECOLI); P44859 (DAPF_HAEIN); Q8NP73 (DAPF_CORGL); P9WP19 (DAPF_MYCTU); [ 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-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (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-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L- lysine. |
end case | |
CATALYTIC ACTIVITY | Reaction=(2S,6S)-2,6-diaminoheptanedioate = meso-2,6- diaminoheptanedioate; 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. |