P9WJS3 · MOAA1_MYCTU
- ProteinGTP 3',8-cyclase 1
- GenemoaA1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids359 (go to sequence)
- Protein existenceEvidence at transcript level
- 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 | 30 | GTP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 37 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 41 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 43 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 44 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 80 | GTP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 84 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 115 | GTP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 139 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 176 | GTP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 210 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: M | ||||||
Binding site | 273 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI); 4Fe-4S-substrate | ||||
Sequence: C | ||||||
Binding site | 276 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI); 4Fe-4S-substrate | ||||
Sequence: C | ||||||
Binding site | 278-280 | GTP (UniProtKB | ChEBI) | ||||
Sequence: RSR | ||||||
Binding site | 290 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI); 4Fe-4S-substrate | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | plasma membrane | |
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 1
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Mycobacteriales > Mycobacteriaceae > Mycobacterium > Mycobacterium tuberculosis complex
Accessions
- Primary accessionP9WJS3
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Phenotypes & Variants
Miscellaneous
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000152976 | 1-359 | GTP 3',8-cyclase 1 | |||
Sequence: MSTPTLPDMVAPSPRVRVKDRCRRMMGDLRLSVIDQCNLRCRYCMPEEHYTWLPRQDLLSVKEISAIVDVFLSVGVSKVRITGGEPLIRPDLPEIVRTLSAKVGEDSGLRDLAITTNGVLLADRVDGLKAAGMKRITVSLDTLQPERFKAISQRNSHDKVIAGIKAVAAAGFTDTKIDTTVMRGANHDELADLIEFARTVNAEVRFIEYMDVGGATHWAWEKVFTKANMLESLEKRYGRIEPLPKHDTAPANRYALPDGTTFGIIASTTEPFCATCDRSRLTADGLWLHCLYAISGINLREPLRAGATHDDLVETVTTGWRRRTDRGAEQRLAQRERGVFLPLSTLKADPHLEMHTRGG |
Proteomic databases
Expression
Induction
Expression is positively regulated by the transcriptional regulator MoaR1.
Interaction
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 21-241 | Radical SAM core | ||||
Sequence: RCRRMMGDLRLSVIDQCNLRCRYCMPEEHYTWLPRQDLLSVKEISAIVDVFLSVGVSKVRITGGEPLIRPDLPEIVRTLSAKVGEDSGLRDLAITTNGVLLADRVDGLKAAGMKRITVSLDTLQPERFKAISQRNSHDKVIAGIKAVAAAGFTDTKIDTTVMRGANHDELADLIEFARTVNAEVRFIEYMDVGGATHWAWEKVFTKANMLESLEKRYGRIE |
Sequence similarities
Belongs to the radical SAM superfamily. MoaA family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length359
- Mass (Da)39,960
- Last updated2014-04-16 v1
- ChecksumD6176DCBD467AE66
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AL123456 EMBL· GenBank· DDBJ | CCP45919.1 EMBL· GenBank· DDBJ | Genomic DNA |