A0A6A7N4N6 · A0A6A7N4N6_9BURK
- ProteinMolybdenum cofactor guanylyltransferase
- GenemobA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids633 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP.
Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor.
Catalytic activity
- GTP + H+ + Mo-molybdopterin = diphosphate + Mo-molybdopterin guanine dinucleotide
Cofactor
Pathway
Cofactor biosynthesis; molybdopterin biosynthesis.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 12-14 | GTP (UniProtKB | ChEBI) | ||||
Sequence: LAG | ||||||
Binding site | 25 | GTP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 53 | GTP (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 73 | GTP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 103 | GTP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 103 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | GTP binding | |
Molecular Function | metal ion binding | |
Molecular Function | molybdenum cofactor guanylyltransferase activity | |
Molecular Function | molybdopterin molybdotransferase activity | |
Biological Process | Mo-molybdopterin cofactor biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMolybdenum cofactor guanylyltransferase
- EC number
- Short namesMoCo guanylyltransferase
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Betaproteobacteria > Burkholderiales > Oxalobacteraceae > Telluria group > Rugamonas
Accessions
- Primary accessionA0A6A7N4N6
Proteomes
Subcellular Location
Interaction
Subunit
Monomer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 404-545 | MoaB/Mog | ||||
Sequence: AFFSTGDELRSLGDPLDDGCVYDSNRYTLFGMLTRLGCEVIDMGIVRDDPAALEAALRQACTKADAIITSGGVSEGAADYTRDIMARLGDVAFWKLAMRPGRPLAFGKIQTEADSAWLFGLPGNPVAVMVSFYMFARPALLR |
Domain
The N-terminal domain determines nucleotide recognition and specific binding, while the C-terminal domain determines the specific binding to the target protein.
Sequence similarities
Belongs to the MobA family.
Belongs to the MoeA family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length633
- Mass (Da)67,224
- Last updated2020-06-17 v1
- Checksum5CD52C308992D555