A0A009ZBJ7 · A0A009ZBJ7_9GAMM
- ProteinL-lysine 2,3-aminomutase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids334 (go to sequence)
- Protein existenceInferred from homology
- Annotation score2/5
Function
Catalytic activity
- L-lysine = D-beta-lysine
Cofactor
Protein has several cofactor binding sites:
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 113 | [4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | |||
Binding site | 117 | [4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | |||
Binding site | 120 | [4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | |||
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | 4 iron, 4 sulfur cluster binding | |
Molecular Function | isomerase activity | |
Molecular Function | metal ion binding |
Keywords
- Molecular function
- Ligand
Names & Taxonomy
Protein names
- Recommended nameL-lysine 2,3-aminomutase
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Moraxellales > Moraxellaceae > Acinetobacter > Acinetobacter calcoaceticus/baumannii complex
Accessions
- Primary accessionA0A009ZBJ7
Proteomes
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Modified residue | 325 | N6-(pyridoxal phosphate)lysine | |||
Structure
Sequence
- Sequence statusComplete
- Length334
- Mass (Da)38,341
- Last updated2014-06-11 v1
- MD5 ChecksumD04F6B79B26537FF4B461DBCF4305AE7
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
JEZN01000001 EMBL· GenBank· DDBJ | EXD37695.1 EMBL· GenBank· DDBJ | Genomic DNA |