A0A6M4JFL7 · A0A6M4JFL7_BACSU
- Protein7-carboxy-7-deazaguanine synthase
- GenequeE
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids243 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the complex heterocyclic radical-mediated conversion of 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) to 7-carboxy-7-deazaguanine (CDG), a step common to the biosynthetic pathways of all 7-deazapurine-containing compounds.
Catalytic activity
- 6-carboxy-5,6,7,8-tetrahydropterin + H+ = 7-carboxy-7-deazaguanine + NH4+
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 S-adenosyl-L-methionine per subunit.
Note: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Pathway
Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 15-17 | substrate | ||||
Sequence: IQG | ||||||
Binding site | 30 | substrate | ||||
Sequence: R | ||||||
Binding site | 34 | [4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 38 | [4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 40-42 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: WCD | ||||||
Binding site | 41 | [4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 43 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 81 | substrate | ||||
Sequence: S | ||||||
Binding site | 83 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 127-129 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: SPK |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | 4 iron, 4 sulfur cluster binding | |
Molecular Function | carbon-nitrogen lyase activity | |
Molecular Function | magnesium ion binding | |
Molecular Function | S-adenosyl-L-methionine binding | |
Biological Process | queuosine biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name7-carboxy-7-deazaguanine synthase
- EC number
- Short namesCDG synthase
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Bacillales > Bacillaceae > Bacillus
Accessions
- Primary accessionA0A6M4JFL7
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 21-239 | Radical SAM core | ||||
Sequence: VIGQKTMFVRTAGCDYSCSWCDSAFTWDGSAKKDIRWMTAEEIFAELKDIGGDAFSHVTISGGNPALLKQLDAFIELLKENNIRAALETQGTVYQDWFTLIDDLTISPKPPSSKMVTNFQKLDHILTSLQENDRQHAVSLKVVIFNDEDLEFAKTVHKRYPGIPFYLQVGNDDVHTTDDQSLIAHLLGKYEALVDKVAVDAELNLVRVLPQLHTLLWGN |
Sequence similarities
Belongs to the radical SAM superfamily. 7-carboxy-7-deazaguanine synthase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length243
- Mass (Da)27,122
- Last updated2020-10-07 v1
- Checksum8F44E27D21A7B1FD
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP052842 EMBL· GenBank· DDBJ | QJP87884.1 EMBL· GenBank· DDBJ | Genomic DNA |