A5VR62 · COBB_BRUO2

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

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

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.

TypeIDPosition(s)Description
Active site327Nucleophile
Site427Increases nucleophilicity of active site Cys

GO annotations

AspectTerm
Molecular FunctionATP binding
Molecular Functioncobyrinic acid a,c-diamide synthase activity
Molecular Functionhydrogenobyrinic acid a,c-diamide synthase (glutamine-hydrolysing) activity
Biological Processcobalamin biosynthetic process
Biological Processglutamine metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Hydrogenobyrinate a,c-diamide synthase
  • EC number
  • Alternative names
    • Hydrogenobyrinic acid a,c-diamide synthase

Gene names

    • Name
      cobB
    • Ordered locus names
      BOV_1259

Organism names

Accessions

  • Primary accession
    A5VR62

Proteomes

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_10000022891-436Hydrogenobyrinate a,c-diamide synthase

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain244-435GATase cobBQ-type

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

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    436
  • Mass (Da)
    47,016
  • Last updated
    2007-07-10 v1
  • Checksum
    C1D76603A8FF5D5D
MKGFMIAAPASGSGKTTVTLGLLRALKRRGEVLAPVKAGPDYIDPAYHRAASGVDCFNLDPWAMRPELISALSSRMTESGARVLVAEGMMGLFDGAIDGKGSSADLARLLDLPVVLVVDCARQSHSIAALVWGFSQFRKDVLIEGVILNRVGSPRHEAMLRGALAPLGVPVLGALPRDPALSLPERHLGLVQADEHAGLESFLEQAADVMEAHIDMDALQTIWLRPKRYDAMANVARLKPLGNRIAVARDDAFAFAYMHLFEGWRRRGAEISFFSPLADEAPKADADAIYLPGGYPELHAQRLAGAPRFRTAIGDAAARGVTAYGECGGYMVLGKTLEDAAGVHHPMLGLLPLETSFARRKLHLGYRLLEPLGGLPWDMPLKAHEFHYASIVREEKADRLFRVRDASGENLGEAGLRVGSVSGSFMHVIDFSGEAA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000708
EMBL· GenBank· DDBJ
ABQ60390.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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