A0A1H0NKS3 · SAND_SELRU
- ProteinS-adenosylmethionine-dependent nucleotide dehydratase
- Genevip6
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids274 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
function
Expression of pVip6 in E.coli (strain MG1655) confers resistance to phages lambda, P1, SECphi6, SECphi8 and T7. Catalyzes the conversion of cytidine triphosphate (CTP) to 3'-deoxy-3',4'-didehydro-CTP (ddhCTP), probably via a SAM-dependent radical mechanism (PubMed:32937646).
The modified nucleotide represses transcription from T7 RNA polymerase-directed genes (possibly by acting as chain terminators), strongly suggesting these nucleotides block viral polymerase transcription (By similarity).
The modified nucleotide represses transcription from T7 RNA polymerase-directed genes (possibly by acting as chain terminators), strongly suggesting these nucleotides block viral polymerase transcription (By similarity).
Miscellaneous
How this protein allows bacteria to resist viruses that do not encode their own RNA polymerase (such as lambda, P1) is unknown.
Catalytic activity
- AH2 + CTP + S-adenosyl-L-methionine = 3'-deoxy-3',4'-didehydro-CTP + 5'-deoxyadenosine + A + H+ + H2O + L-methionineThis reaction proceeds in the forward direction.
Cofactor
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | 4 iron, 4 sulfur cluster binding | |
Molecular Function | lyase activity | |
Molecular Function | metal ion binding | |
Biological Process | defense response to virus |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameS-adenosylmethionine-dependent nucleotide dehydratase
- EC number
- Short namesSAND
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacillota > Negativicutes > Selenomonadales > Selenomonadaceae > Selenomonas
Accessions
- Primary accessionA0A1H0NKS3
Proteomes
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000456417 | 1-274 | S-adenosylmethionine-dependent nucleotide dehydratase | |||
Sequence: MAYKVNLHITQKCNYACKYCFAHFDHHNDLTLGQWKHIIDNLKTSGLVDAINFAGGEPVLHRDFAAIVNYAYDQGFKLSIITNGSLMLNPKLMPPELFAKFDTLGISVDSINPKTLIALGACNNSQEVLSYDKLSHLITLARSVNPTIRIKLNTVITNLNADEDLTIIGQELDIARWKMLRMKLFIHEGFNNAPLLVSQADFDGFVERHAEVSHDIVPENDLTRSYIMVDNQGRLLDDETEEYKVVGSLLAEDFGTVFDRYHFDEATYASRYAG |
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-215 | Radical SAM core | ||||
Sequence: MAYKVNLHITQKCNYACKYCFAHFDHHNDLTLGQWKHIIDNLKTSGLVDAINFAGGEPVLHRDFAAIVNYAYDQGFKLSIITNGSLMLNPKLMPPELFAKFDTLGISVDSINPKTLIALGACNNSQEVLSYDKLSHLITLARSVNPTIRIKLNTVITNLNADEDLTIIGQELDIARWKMLRMKLFIHEGFNNAPLLVSQADFDGFVERHAEVSHD |
Sequence similarities
Belongs to the radical SAM superfamily. Prokaryotic viperin family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length274
- Mass (Da)30,933
- Last updated2017-04-12 v1
- ChecksumF3694907EEEFB6A4