Q5V341 · CBIA_HALMA

Function

function

Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source.

Miscellaneous

The a and c carboxylates of cobyrinate are activated for nucleophilic attack via formation of a phosphorylated intermediate by ATP. CbiA 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 sirohydrochlorin (anaerobic route): step 10/10.

Features

Showing features for active site, site.

TypeIDPosition(s)Description
Active site317Nucleophile
Site420Increases nucleophilicity of active site Cys

GO annotations

AspectTerm
Molecular FunctionATP binding
Molecular Functioncobyrinic acid a,c-diamide synthase activity
Biological Processcobalamin biosynthetic process
Biological Processglutamine metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Cobyrinate a,c-diamide synthase
  • EC number
  • Alternative names
    • Cobyrinic acid a,c-diamide synthetase

Gene names

    • Name
      cbiA
    • Ordered locus names
      rrnAC1102

Organism names

Accessions

  • Primary accession
    Q5V341

Proteomes

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001412741-439Cobyrinate a,c-diamide synthase

Proteomic databases

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region214-235Disordered
Domain237-428GATase 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 cobyrinate 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
    439
  • Mass (Da)
    46,284
  • Last updated
    2004-12-07 v1
  • Checksum
    F49FFAFC63D97D5C
MEGFVLAGTSSGVGKTVATLATLTALEDAGYQPQPAKAGPDFIDPSHHEALVDTPSRTLDPWLAGEDGMRRTYWRGTGDICVVEGVMGLYDGTKTSTAAVAEGLDLPVVLVVDAKAGMESVAATALGFAQYADRIGVDIEVAGILAQRAHGGRHADGIRDALPEDLTYFGRIPPMSDLEIPDRHLGLHMGSEAGLDRDALSTAAETIDIERLVETARAPPEVATTERNTGDSPADRRVAVAQDSAFCFIYPSVLERLRSEASVEPFSPVAGDSVPDADAIYLPGGYPELHGESLETGGTLDEIAVRAADGVPVYGECGGLMALSESLTTTDGDTYEMAGVLPADIEMQDRYQALDHVELEARADTVAATSGAHRRGHEFHYSAATLGSDASFAFDMVRGDGIDGEHDGLTEYSTIGTYCHCHGESGAFDRLLAVPSKDI

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AY596297
EMBL· GenBank· DDBJ
AAV46061.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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