B1VB59 · B1VB59_CITFR

  • Protein
    Cobyrinate a,c-diamide synthase
  • Gene
    cbiA
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

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 site334Nucleophile
Site438Increases 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

Organism names

  • Taxonomic identifier
  • Organism
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Citrobacter > Citrobacter freundii complex

Accessions

  • Primary accession
    B1VB59

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain9-194CobQ/CobB/MinD/ParA nucleotide binding
Domain253-444CobB/CobQ-like glutamine amidotransferase

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.
Belongs to the CobB/CobQ family. CobQ subfamily.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    459
  • Mass (Da)
    49,782
  • Last updated
    2008-05-20 v1
  • Checksum
    D381FE981936382E
MAANFHAFVLAGTGSGCGKTTVTLGLLSLLKKRGLRVQPCKVGPDYLDTGWHTAVCGTASRNLDSFMLPVPTLNALFREHMQHADIAVIEGVMGLYDGYGTDPNYCSTAAMAKQLGCPVILLVDGKAVSTSIAATVMGFQHFDPTLNIAGVIVNRVNSETHYQLLKVAIERYCAVPVLGYVPRMAGVALPERHLGLVTARESVINQQPWQAFAATLEQTLDIDALLRLSQLDTLPAGEWPALPAADAGAGLTLAIADDEAFNFYYPDNITLLERTGLKIVRFSPLHDTCLPDCQMIWLGGGYPELHAAALARNIAMLNQLRAAHQQGVAIYAECGGLMYLGSSLEDSQGDTWLMADIIPGHSKMGKRLTRFGYCEAQAAQQTLLAAEGEVLRGHEFHYSDFTPETPAVMNCRKVRDGKTLQAWSGGWQVGNTFASYLHVHFAQRPQMLNHWLAAARSAL

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AM498294
EMBL· GenBank· DDBJ
CAM57280.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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