D4GSF3 · UBAA_HALVD
- ProteinSAMP-activating enzyme E1
- GeneubaA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids270 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Likely activates multiple ubiquitin-like SAMPs for protein conjugation as well as for sulfur transfer, via ATP-dependent adenylation at their C-terminus (PubMed:21368171, PubMed:24097257, PubMed:24906001).
In fact, it is required for the formation of all three SAMP1-, SAMP2- and SAMP3-protein conjugates, and for molybdenum cofactor (MoCo) biosynthesis and thiolation of tRNAs (PubMed:21368171, PubMed:24097257).
In fact, it is required for the formation of all three SAMP1-, SAMP2- and SAMP3-protein conjugates, and for molybdenum cofactor (MoCo) biosynthesis and thiolation of tRNAs (PubMed:21368171, PubMed:24097257).
Catalytic activity
- [small archaeal modifier protein]-C-terminal Gly-Gly + ATP + H+ = [small archaeal modifier protein]-C-terminal Gly-Gly-AMP + diphosphate
Cofactor
Note: Binds 1 zinc ion per subunit.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 42 | ATP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 63 | ATP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 70-74 | ATP (UniProtKB | ChEBI) | ||||
Sequence: SNLQR | ||||||
Binding site | 87 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 131-132 | ATP (UniProtKB | ChEBI) | ||||
Sequence: DN | ||||||
Binding site | 171 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 174 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Active site | 188 | Glycyl thioester intermediate | ||||
Sequence: C | ||||||
Binding site | 245 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 248 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | ATP binding | |
Molecular Function | metal ion binding | |
Molecular Function | nucleotidyltransferase activity | |
Molecular Function | ubiquitin-like modifier activating enzyme activity |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSAMP-activating enzyme E1
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageArchaea > Euryarchaeota > Stenosarchaea group > Halobacteria > Halobacteriales > Haloferacaceae > Haloferax
Accessions
- Primary accessionD4GSF3
Proteomes
Phenotypes & Variants
Disruption phenotype
Cells lacking this gene are deficient in sampylation, i.e. SAMP-protein conjugates. Moreover, they do not grow anaerobically with DMSO and do not show DMSO reductase activity, but their growth in the presence of oxygen is not affected; however, they are retarded in aerobic growth at 50 degrees Celsius. The lysine tRNAs of the mutant strain appear to be nonthiolated.
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 188 | Loss of activity since this mutant is not able to complement a ubaA deletion in trans to restore sampylation and tRNA thiolation. | ||||
Sequence: C → S |
PTM/Processing
Features
Showing features for chain, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000397107 | 1-270 | SAMP-activating enzyme E1 | |||
Sequence: MTLSLDATQLDRYSRHIIMDEVGPEGQGRLLSSRVVVVGAGGLGAPAIQYLAAVGVGELVVVDDDVVERSNLQRQVVHCDDDVGTPKAESAAAFVRGLNPDVSVEPVEARVDKSNVHEVVAGSDVVVDASDNFPTRYLLNDVCRFEGIPLVHGAIYKFEGQATTLVPDGPCYRCLFPEAPEPGTVPDCATTGVLGVLPGTVGCIQATEAMKLLLDEGEALDGRLLFYDAMDMTFETVPYRTNPDCPVCGEGGVDSIEDIDYVESCAISLD | ||||||
Cross-link | 113 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SAMP2) | ||||
Sequence: K |
Post-translational modification
Sampylated at Lys-113 with the archaeal ubiquitin-like protein SAMP2. Also sampylated with SAMP1.
Keywords
- PTM
Proteomic databases
Interaction
Structure
Sequence
- Sequence statusComplete
- Length270
- Mass (Da)28,704
- Last updated2010-05-18 v1
- ChecksumB9DFDCD37024FA32
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP001956 EMBL· GenBank· DDBJ | ADE04227.1 EMBL· GenBank· DDBJ | Genomic DNA |