A0A7U5Y357 · A0A7U5Y357_9BURK

  • 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.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.

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 site318Nucleophile
Site411Increases 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
    • ORF names
      DPH57_24170

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • YMA4
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Betaproteobacteria > Burkholderiales > Oxalobacteraceae > Telluria group > Massilia

Accessions

  • Primary accession
    A0A7U5Y357

Proteomes

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain7-172CobQ/CobB/MinD/ParA nucleotide binding
Domain235-417CobB/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
    430
  • Mass (Da)
    45,002
  • Last updated
    2021-06-02 v1
  • Checksum
    FF6218FC457E3A0D
MGARAVLIAAVSSGQGKTTVTAALARKLARAGERVRVFKCGPDFIDPMVLQRASGAPVETLDLWMVGRERCHQLLAQAALEADTILIEGVMGLYDGTPSAADLAREFGVPVLAVIDAGAMAQTAGALVHGLRDYGPVEMAGVIANRVGSAGHAAMVQASLRGIPLFGTLPKQGRSLPERHLGLVLPHEVEGIDDLLDELATQMTFDSAAWATLPALTFAAPASSAPTEPLLAGRTIAIARDESFLFVYHANTELLRQLGAHIVYFAPLQDDAVPADADAVYLPGGYPELHCERLAGATRWRASIQAAHAAGKPIVAECGGMMALADALADGAGHDWPMAGLLPGRVTVQKKLAGLGPQALVTPQGILRGHTFHYSRLESTTPVFAHTSKNPSGAQGEAVYRVGSLTASYFHAYFPSNPAAVAALFSRSDA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP030092
EMBL· GenBank· DDBJ
AXA93960.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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