A0A0U4B3X5 · A0A0U4B3X5_9CAUD
- ProteinN6-succino-2-amino-2'-deoxyadenylate synthase
- Gene50
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids377 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Involved in the synthesis of the atypical nucleotide dZTP (2-amino-2'-deoxyadenosine-5'-triphosphate). Catalyzes the condensation of aspartate with deoxyguanylate into dSMP (N6-succino-2-amino-2'-deoxyadenylate), which undergoes defumarylation and phosphorylation respectively by host PurB and guanylate/nucleoside diphosphate kinases to give dZTP. dZTP is integrated into the viral genome instead of adenine by the viral DNA polymerase. This Z-base probably completely replaces adenosine and forms a triple bond to the opposite T-base. The resulting non-standard viral DNA is called Z-genome. The chemically modified DNA is probably harder for the host bacteria to digest with nucleases or restriction enzymes.
Catalytic activity
- dGMP + L-aspartate + ATP = (2S)-2-amino-2'-deoxyadenylo-succinate + ADP + phosphate + 2 H+
Cofactor
Pathway
Purine metabolism.
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Active site | 14 | Proton acceptor | |||
Binding site | 14 | ATP (UniProtKB | ChEBI) | |||
Binding site | 14 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 14 | dGMP (UniProtKB | ChEBI) | |||
Binding site | 17 | ATP (UniProtKB | ChEBI) | |||
Binding site | 18 | ATP (UniProtKB | ChEBI) | |||
Binding site | 44 | dGMP (UniProtKB | ChEBI) | |||
Binding site | 46 | ATP (UniProtKB | ChEBI) | |||
Binding site | 46 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 47 | ATP (UniProtKB | ChEBI) | |||
Binding site | 48 | ATP (UniProtKB | ChEBI) | |||
Binding site | 130 | dGMP (UniProtKB | ChEBI) | |||
Binding site | 131 | dGMP (UniProtKB | ChEBI) | |||
Binding site | 145 | dGMP (UniProtKB | ChEBI) | |||
Binding site | 192 | ATP (UniProtKB | ChEBI) | |||
Binding site | 207 | dGMP (UniProtKB | ChEBI) | |||
Binding site | 269 | L-aspartate (UniProtKB | ChEBI) | |||
Binding site | 269 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 270 | L-aspartate (UniProtKB | ChEBI) | |||
Binding site | 275 | L-aspartate (UniProtKB | ChEBI) | |||
Binding site | 359 | ATP (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | adenylosuccinate synthase activity | |
Molecular Function | ATP binding | |
Molecular Function | magnesium ion binding | |
Biological Process | 'de novo' AMP biosynthetic process | |
Biological Process | IMP metabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameN6-succino-2-amino-2'-deoxyadenylate synthase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageViruses > Duplodnaviria > Heunggongvirae > Uroviricota > Caudoviricetes > Korravirus > Korravirus joann
Accessions
- Primary accessionA0A0U4B3X5
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Structure
Sequence
- Sequence statusComplete
- Length377
- Mass (Da)40,745
- Last updated2016-03-16 v1
- ChecksumD9AE826275E9A8E3
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
KU160652 EMBL· GenBank· DDBJ | ALY09453.1 EMBL· GenBank· DDBJ | Genomic DNA |