Q1YEB0 · Q1YEB0_AURMS
- ProteintRNA-cytidine(32) 2-sulfurtransferase
- GenettcA
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids305 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the ATP-dependent 2-thiolation of cytidine in position 32 of tRNA, to form 2-thiocytidine (s2C32). The sulfur atoms are provided by the cysteine/cysteine desulfurase (IscS) system.
Miscellaneous
The thiolation reaction likely consists of two steps: a first activation step by ATP to form an adenylated intermediate of the target base of tRNA, and a second nucleophilic substitution step of the sulfur (S) atom supplied by the hydrosulfide attached to the Fe-S cluster.
Catalytic activity
- AH2 + ATP + cytidine32 in tRNA + S-sulfanyl-L-cysteinyl-[cysteine desulfurase] = 2-thiocytidine32 in tRNA + A + AMP + diphosphate + H+ + L-cysteinyl-[cysteine desulfurase]
CHEBI:17499 + CHEBI:30616 + RHEA-COMP:10288 CHEBI:82748 Position: 32+ RHEA-COMP:12157 = RHEA-COMP:14821 + CHEBI:13193 + CHEBI:456215 + CHEBI:33019 + CHEBI:15378 + RHEA-COMP:12158
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 [4Fe-4S] cluster per subunit. The cluster is chelated by three Cys residues, the fourth Fe has a free coordination site that may bind a sulfur atom transferred from the persulfide of IscS.
Pathway
tRNA modification.
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | 4 iron, 4 sulfur cluster binding | |
Molecular Function | ATP binding | |
Molecular Function | magnesium ion binding | |
Molecular Function | sulfurtransferase activity | |
Molecular Function | tRNA binding | |
Biological Process | tRNA thio-modification |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nametRNA-cytidine(32) 2-sulfurtransferase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria > Hyphomicrobiales > Aurantimonadaceae > Aurantimonas
Accessions
- Primary accessionQ1YEB0
Proteomes
Subcellular Location
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for region, domain, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 16-38 | Disordered | ||||
Sequence: ADAQDDDAATPAAEDGAGSAHPL | ||||||
Domain | 75-239 | tRNA(Ile)-lysidine/2-thiocytidine synthase N-terminal | ||||
Sequence: WLVGLSGGKDSYALLALLSDLKYRGLLPVDILACNLDQGQPNFPKHVLPDFLSRYDIPHRIEYRDTYSVVTEKVPSNATYCALCSRLRRGNLYRIAREEGCEALVLGHHADDCLETFFMNLFHGGRLSAMPAKLINDEGDLMVLRPLIRSVEEDIAKFSAAMKFP | ||||||
Motif | 80-85 | PP-loop motif | ||||
Sequence: SGGKDS |
Sequence similarities
Belongs to the TtcA family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length305
- Mass (Da)33,754
- Last updated2006-05-02 v1
- Checksum82B2E773A779CECC
Keywords
- Technical term