Q4JAP9 · LYSX_SULAC
- ProteinAlpha-aminoadipate--LysW ligase LysX
- GenelysX
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids276 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Catalyzes the ATP-dependent formation of a covalent bond between the amino group of alpha-aminoadipate (AAA) and the gamma-carboxyl group of the C-terminal glutamate residue in LysW.
Catalytic activity
- [amino-group carrier protein]-C-terminal-L-glutamate + ATP + L-2-aminoadipate = [amino-group carrier protein]-C-terminal-N-(1,4-dicarboxybutan-1-yl)-L-glutamine + ADP + H+ + phosphate
Cofactor
Note: Binds 2 magnesium ions per subunit.
Pathway
Amino-acid biosynthesis; L-lysine biosynthesis via AAA pathway; L-lysine from L-alpha-aminoadipate (Thermus route): step 1/5.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 82 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 122 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 126-132 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GSWGRMV | ||||||
Binding site | 162-173 | ATP (UniProtKB | ChEBI) | ||||
Sequence: QEFVKKPNRDIR | ||||||
Binding site | 187 | ATP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 196 | ATP (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 231 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 244 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 244 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 246 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: N |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | ATP binding | |
Molecular Function | ligase activity | |
Molecular Function | metal ion binding | |
Biological Process | lysine biosynthetic process via aminoadipic acid | |
Biological Process | protein modification process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAlpha-aminoadipate--LysW ligase LysX
- EC number
- Short namesAAA--LysW ligase LysX
Gene names
Organism names
- Strain
- Taxonomic lineageArchaea > Thermoproteota > Thermoprotei > Sulfolobales > Sulfolobaceae > Sulfolobus
Accessions
- Primary accessionQ4JAP9
Proteomes
Phenotypes & Variants
Disruption phenotype
Cells lacking this gene require lysine for growth.
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 253-254 | Alters substrate specificity, so that glutamate is preferred over alpha-aminoadipate. | ||||
Sequence: NT → GF |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000422992 | 1-276 | Alpha-aminoadipate--LysW ligase LysX | |||
Sequence: MRWEEKDIITEAKKSGFKAIPIFTKDFYSAIGVGENYSELEADVIIQRNTSHARALTTSLIFEGWNYNVVNDATSLFKCGNKLYTLSLLAKHNIKTPRTIVTFSKDKAVDLAKKIGFPAVIKPIEGSWGRMVAKAVDEDILYSFLEYQEYTTSQFRQIYLVQEFVKKPNRDIRIFVMGDEAPVGIYRVNERNWKTNTALGARALPLKIDDELRDLALKVRDIMGGFFLGIDIFEDPERGYLVNEVNGVPEYKNTVRVNNFNVSSYLLNKLREWIKK |
Interaction
Structure
Family & Domains
Features
Showing features for domain, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 86-271 | ATP-grasp | ||||
Sequence: LSLLAKHNIKTPRTIVTFSKDKAVDLAKKIGFPAVIKPIEGSWGRMVAKAVDEDILYSFLEYQEYTTSQFRQIYLVQEFVKKPNRDIRIFVMGDEAPVGIYRVNERNWKTNTALGARALPLKIDDELRDLALKVRDIMGGFFLGIDIFEDPERGYLVNEVNGVPEYKNTVRVNNFNVSSYLLNKLR | ||||||
Motif | 253-254 | N-[TS] motif that is essential for LysX substrate specificity | ||||
Sequence: NT |
Sequence similarities
Belongs to the RimK family. LysX subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length276
- Mass (Da)31,712
- Last updated2005-08-02 v1
- Checksum3BA4CE0980E8B635
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000077 EMBL· GenBank· DDBJ | AAY80130.1 EMBL· GenBank· DDBJ | Genomic DNA |