Q30ZX9 · DAPAT_OLEA2
- ProteinLL-diaminopimelate aminotransferase
- GenedapL
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids388 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Involved in the synthesis of meso-diaminopimelate (m-DAP or DL-DAP), required for both lysine and peptidoglycan biosynthesis. Catalyzes the direct conversion of tetrahydrodipicolinate to LL-diaminopimelate.
Catalytic activity
- (2S,6S)-2,6-diaminoheptanedioate + 2-oxoglutarate = (S)-2,3,4,5-tetrahydrodipicolinate + H+ + H2O + L-glutamate
Cofactor
Pathway
Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (aminotransferase route): step 1/1.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 16 | substrate | ||||
Sequence: Y | ||||||
Binding site | 41 | substrate | ||||
Sequence: G | ||||||
Binding site | 70 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 104-105 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: SK | ||||||
Binding site | 105 | substrate | ||||
Sequence: K | ||||||
Binding site | 129 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 129 | substrate | ||||
Sequence: Y | ||||||
Binding site | 179 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 179 | substrate | ||||
Sequence: N | ||||||
Binding site | 210 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 239-241 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: SLS | ||||||
Binding site | 250 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 368 | substrate | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | L,L-diaminopimelate aminotransferase activity | |
Molecular Function | pyridoxal phosphate binding | |
Biological Process | lysine biosynthetic process via diaminopimelate |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameLL-diaminopimelate aminotransferase
- EC number
- Short namesDAP-AT ; DAP-aminotransferase ; LL-DAP-aminotransferase
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Thermodesulfobacteriota > Desulfovibrionia > Desulfovibrionales > Desulfovibrionaceae > Oleidesulfovibrio
Accessions
- Primary accessionQ30ZX9
Proteomes
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000342235 | 1-388 | LL-diaminopimelate aminotransferase | |||
Sequence: MTQFTLADRLATLPPYLFAQIDKVKAEVAARGVDIISLGIGDPDMPTPDFVIEALKKAAEKPANHQYPSYTGMLAFRQEVANWYKRRYAVELDPKTEVLTLIGSKEGIAHFPTAFVNPGDLVLVCPPCYPVYAIASRFMGGVVQELPLLEENDFLPDLDAVDEATWEKARCIFVNYPNNPTAAMAPRSFFEKLIGIARKHNVIVVHDAAYTEMYYNENNRPLSIMEIPGAMDVAIEFNSLSKPYNMTGWRIAMAVGNASLVAGLGKVKENMDSGAFQAVQEAAIVALRDGDAFLAEIRDIYRKRRDTVIAALNKIGITCRVPEASLYVWARVPEGYTSSDFVTRVLQETGVVMTPGNGFGAAGEGYFRISLTVNDERLEEAVSRIASL | ||||||
Modified residue | 242 | N6-(pyridoxal phosphate)lysine | ||||
Sequence: K |
Interaction
Structure
Sequence
- Sequence statusComplete
- Length388
- Mass (Da)42,773
- Last updated2005-12-06 v1
- Checksum68CA2F7BA4A6942C
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000112 EMBL· GenBank· DDBJ | ABB38767.1 EMBL· GenBank· DDBJ | Genomic DNA |