A5VR62 · COBB_BRUO2
- ProteinHydrogenobyrinate a,c-diamide synthase
- GenecobB
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids436 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of hydrogenobyrinate, using either L-glutamine or ammonia as the nitrogen source.
Miscellaneous
The a and c carboxylates of hydrogenobyrinate are activated for nucleophilic attack via formation of a phosphorylated intermediate by ATP. CobB catalyzes first the amidation of the c-carboxylate, and then that of the a-carboxylate.
Catalytic activity
- 2 ATP + 2 H2O + hydrogenobyrinate + 2 L-glutamine = 2 ADP + 2 H+ + hydrogenobyrinate a,c-diamide + 2 L-glutamate + 2 phosphate
Cofactor
Pathway
Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from precorrin-2 (aerobic route): step 9/10.
Features
Showing features for active site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 327 | Nucleophile | ||||
Sequence: C | ||||||
Site | 427 | Increases nucleophilicity of active site Cys | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | ATP binding | |
Molecular Function | cobyrinic acid a,c-diamide synthase activity | |
Molecular Function | hydrogenobyrinic acid a,c-diamide synthase (glutamine-hydrolysing) activity | |
Biological Process | cobalamin biosynthetic process | |
Biological Process | glutamine metabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameHydrogenobyrinate a,c-diamide synthase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria > Hyphomicrobiales > Brucellaceae > Brucella/Ochrobactrum group > Brucella
Accessions
- Primary accessionA5VR62
Proteomes
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_1000002289 | 1-436 | Hydrogenobyrinate a,c-diamide synthase | |||
Sequence: MKGFMIAAPASGSGKTTVTLGLLRALKRRGEVLAPVKAGPDYIDPAYHRAASGVDCFNLDPWAMRPELISALSSRMTESGARVLVAEGMMGLFDGAIDGKGSSADLARLLDLPVVLVVDCARQSHSIAALVWGFSQFRKDVLIEGVILNRVGSPRHEAMLRGALAPLGVPVLGALPRDPALSLPERHLGLVQADEHAGLESFLEQAADVMEAHIDMDALQTIWLRPKRYDAMANVARLKPLGNRIAVARDDAFAFAYMHLFEGWRRRGAEISFFSPLADEAPKADADAIYLPGGYPELHAQRLAGAPRFRTAIGDAAARGVTAYGECGGYMVLGKTLEDAAGVHHPMLGLLPLETSFARRKLHLGYRLLEPLGGLPWDMPLKAHEFHYASIVREEKADRLFRVRDASGENLGEAGLRVGSVSGSFMHVIDFSGEAA |
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 244-435 | GATase cobBQ-type | ||||
Sequence: RIAVARDDAFAFAYMHLFEGWRRRGAEISFFSPLADEAPKADADAIYLPGGYPELHAQRLAGAPRFRTAIGDAAARGVTAYGECGGYMVLGKTLEDAAGVHHPMLGLLPLETSFARRKLHLGYRLLEPLGGLPWDMPLKAHEFHYASIVREEKADRLFRVRDASGENLGEAGLRVGSVSGSFMHVIDFSGEA |
Domain
Comprises of two domains. The C-terminal domain contains the binding site for glutamine and catalyzes the hydrolysis of this substrate to glutamate and ammonia. The N-terminal domain is anticipated to bind ATP and hydrogenobyrinate and catalyzes the ultimate synthesis of the diamide product. The ammonia produced via the glutaminase domain is probably translocated to the adjacent domain via a molecular tunnel, where it reacts with an activated intermediate.
Sequence similarities
Belongs to the CobB/CbiA family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length436
- Mass (Da)47,016
- Last updated2007-07-10 v1
- ChecksumC1D76603A8FF5D5D
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000708 EMBL· GenBank· DDBJ | ABQ60390.1 EMBL· GenBank· DDBJ | Genomic DNA |