A0A1W6K1P7 · A0A1W6K1P7_9CREN
- ProteinProbable GTP 3',8-cyclase
- GenemoaA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids308 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate.
Catalytic activity
- AH2 + GTP + S-adenosyl-L-methionine = (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate + 5'-deoxyadenosine + A + H+ + L-methionine
Cofactor
Note: Binds 2 [4Fe-4S] clusters. Binds 1 [4Fe-4S] cluster coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine and 1 [4Fe-4S] cluster coordinated with 3 cysteines and the GTP-derived substrate.
Pathway
Cofactor biosynthesis; molybdopterin biosynthesis.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 13 | GTP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 20 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 24 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 27 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 61 | GTP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 65 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 90 | GTP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 114 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 151 | GTP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 245 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI); 4Fe-4S-substrate | ||||
Sequence: C | ||||||
Binding site | 248 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI); 4Fe-4S-substrate | ||||
Sequence: C | ||||||
Binding site | 250-252 | GTP (UniProtKB | ChEBI) | ||||
Sequence: RIR | ||||||
Binding site | 262 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI); 4Fe-4S-substrate | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | 4 iron, 4 sulfur cluster binding | |
Molecular Function | GTP 3',8'-cyclase activity | |
Molecular Function | GTP binding | |
Molecular Function | metal ion binding | |
Molecular Function | S-adenosyl-L-methionine binding | |
Biological Process | Mo-molybdopterin cofactor biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProbable GTP 3',8-cyclase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageArchaea > Thermoproteota > Thermoprotei > Sulfolobales > Sulfolobaceae > Acidianus
Accessions
- Primary accessionA0A1W6K1P7
Proteomes
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 4-224 | Radical SAM core | ||||
Sequence: RYGRELEDLRITLTHVCNFSCFFCHMEGEGDLYVNGLTPDEIELVAEVSKEYGIKYVKLTGGEPTLRRDLTEIIYRLRNLGLEVSMTTNGYMLSKIASKLKEAGLNRVNISLHTLDKEKFKKITGVDGMDRVIEGIKEAINVGLKPVKLNFVATKMNINEAFNVIDFAEKIGVNELHLIELHPVGMGKIAFSYHEKLNNLENVLKEKALREGTRNKHYRPR |
Sequence similarities
Belongs to the radical SAM superfamily. MoaA family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length308
- Mass (Da)35,274
- Last updated2017-07-05 v1
- ChecksumAC6C7D2D2D5165FB
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP020477 EMBL· GenBank· DDBJ | ARM76463.1 EMBL· GenBank· DDBJ | Genomic DNA |