A0A8J2Z7H7 · A0A8J2Z7H7_9PROT
- ProteinGTP 3',8-cyclase
- GenemoaA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids367 (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
- GTP + AH2 + S-adenosyl-L-methionine = (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate + 5'-deoxyadenosine + L-methionine + A + H+
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 | 50 | GTP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 57 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 61 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 63 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 64 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 99 | GTP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 103 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 133 | GTP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 157 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 193 | GTP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 227 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: M | ||||||
Binding site | 290 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI); 4Fe-4S-substrate | ||||
Sequence: C | ||||||
Binding site | 293 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI); 4Fe-4S-substrate | ||||
Sequence: C | ||||||
Binding site | 295-297 | GTP (UniProtKB | ChEBI) | ||||
Sequence: RVR | ||||||
Binding site | 307 | [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 | cyclic pyranopterin monophosphate synthase activity | |
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 nameGTP 3',8-cyclase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria > Rhodospirillales > Acetobacteraceae > Caldovatus
Accessions
- Primary accessionA0A8J2Z7H7
Proteomes
Interaction
Subunit
Monomer and homodimer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 41-267 | Radical SAM core | ||||
Sequence: PFGRRITYLRVSVTDRCDLRCVYCMAEDMTFLPKAEVLTLEELDRLCGAFIRLGVEKIRLTGGEPLVRKNVISLVRALGARLGAGGLRELTVTTNGTQLARLADGLRAAGVRRINVSLDTLDPAKFTAITRWGRIEQTLDGIFAARAAGLAVKINAVALKGVNEDEFDRMIAWCGEHGFDLCLIETMPLGEISGDRTEQYLPLSLVRARLRQRWTLEETDYRTGGPA |
Sequence similarities
Belongs to the radical SAM superfamily. MoaA family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length367
- Mass (Da)40,177
- Last updated2022-05-25 v1
- Checksum78C6DC8C53506FCB
Keywords
- Technical term