M0FL95 · M0FL95_9EURY

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

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

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 site322Nucleophile
Site424Increases nucleophilicity of active site Cys
Active site426
Active site428

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
      C459_17961

Organism names

  • Taxonomic identifier
  • Strain
    • ATCC BAA-645
  • Taxonomic lineage
    Archaea > Euryarchaeota > Stenosarchaea group > Halobacteria > Halobacteriales > Haloferacaceae > Haloferax

Accessions

  • Primary accession
    M0FL95

Proteomes

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain4-184CobQ/CobB/MinD/ParA nucleotide binding
Domain242-430CobB/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.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    441
  • Mass (Da)
    46,445
  • Last updated
    2013-04-03 v1
  • Checksum
    0C28985BE96E3E36
MRGVVVAGTASGVGKTVTTLAVCRALEREGYAVQPAKAGPDFIDPSHHAAVVGKPSRSLDPWLEGEAGMLRTYARGEGDICVVEGMMGLYDGDTSTARVAALLDLPVVLVADARAGMQSVAATAYGFRTYADRMGIDADVAGVIASRAHGGRHAEGIRDALPEELPYLGRIPPSDDLEIPERHLGLHLGDEAPLSDAALDAAADGIRADALAEVAREPDWDTEAFESGRGEAAQATDSDSPTVAVARDEAFCFVYPSTLERLETLGAVSYFSPVAGDDLPDCDGVYLPGGYPERFAAELASSPTLPALSDRAADGLPVFGECGGLMALSESLTTTDGDTHEMAGILPADVTMQDRYQALDHVELRATDGTLTADAGETLRGHEFHYSSADPATDARFAFDVERGDGIDGREGLTEYRTLGTYAHVHPESGAFDRFVSRLAD

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AOLE01000038
EMBL· GenBank· DDBJ
ELZ60042.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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