A4SVU3 · MOBA_POLAQ
- ProteinMolybdenum cofactor guanylyltransferase
- GenemobA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids199 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
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
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 | 71 | GTP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 101 | GTP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 101 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | GTP binding | |
Molecular Function | metal ion binding | |
Molecular Function | molybdenum cofactor guanylyltransferase activity | |
Biological Process | bis(molybdopterin guanine dinucleotide)molybdenum 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
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Betaproteobacteria > Burkholderiales > Burkholderiaceae > Polynucleobacter
Accessions
- Primary accessionA4SVU3
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_1000115805 | 1-199 | Molybdenum cofactor guanylyltransferase | |||
Sequence: MISPENITGLILAGGRAQRMGGIDKGLISFHQKPLIESAINRLKNQVGPILINANRNITKYAGYGYPVVMDETPDFSGPLAGFSVGLKACKTSYLLTSPCDSPLLPLDLAARLAAEMERGPFDLVYASSLESGKTWAQPVFCLMRANLQDSLTAFLTKGDLKIDRWFKELKSSTVIFDDAQAFANVNTPEELKILEAAL |
Interaction
Subunit
Monomer.
Structure
Family & Domains
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.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length199
- Mass (Da)21,653
- Last updated2007-05-15 v1
- ChecksumBA8F07248C345AB6
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000655 EMBL· GenBank· DDBJ | ABP33607.1 EMBL· GenBank· DDBJ | Genomic DNA |