B2TCD6 · B2TCD6_PARPJ

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 site320Nucleophile
Site413Increases nucleophilicity of active site Cys

GO annotations

AspectTerm
Molecular FunctionATP binding
Molecular Functioncobyrinic acid a,c-diamide synthase activity
Molecular Functiontransferase 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
      Bphyt_4996

Organism names

Accessions

  • Primary accession
    B2TCD6

Proteomes

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain8-175CobQ/CobB/MinD/ParA nucleotide binding
Domain237-418CobB/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

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    432
  • Mass (Da)
    45,563
  • Last updated
    2008-07-01 v1
  • Checksum
    0BE6399C72411C7A
MAACPALFISAPASGQGKTTITAGLARYHRRLGRRVRVFKTGPDFLDPMILARASGAPVLSLDLWMVGEAACRTLLAQAAAEADLILIEGVMGLFDGTPSSADLATTFGVPVLAVISAKAMAQTFGAVAFGLAQFRPQVPFYGVLANRVGSARHAQMLEEALSPALRWCGHIAASDEITLPDRHLGLHQADEIDDLDARLDHAADTLGRTALAELPPPVEFGAPTPEVLPRLLDGKTIAVARDAAFSFIYPANLALLEVLGAQVAFFSPLADEALPEHADAVYLPGGYPELHAAALANNNRSAASIHAHAAAGKPLVAECGGMLYLLDQLTDTHGVTTPMLGLLPGHATMQTRFTALGMQQIDSLHGPMTGHTFHYSKLNTSLTPLRSATRPQGDAPGEAVYRAGSIVATYMHAYWPSNPAFTAALFHGEAF

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP001053
EMBL· GenBank· DDBJ
ACD19360.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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