Q3ZWJ9 · CBIA_DEHMC

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 physiological significance of this enzyme is not known since D.mccartyi is cobalamin auxotroph.

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Features

Showing features for active site, site.

TypeIDPosition(s)Description
Active site335Nucleophile
Site440Increases 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
    • Synonyms
      cobB
    • Ordered locus names
      cbdbA149

Organism names

Accessions

  • Primary accession
    Q3ZWJ9

Proteomes

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_10000022911-463Cobyrinate a,c-diamide synthase

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain252-448GATase 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
    463
  • Mass (Da)
    50,361
  • Last updated
    2005-09-27 v1
  • Checksum
    E8FD6EBD46492544
MNFPRIVIAGVSSSSGKTTISSGLTAALAQRGHKVAAYKCGPDYIDPGYLTLASNNPCHNLDSWMLSKDAMTEVFFHGLKNRDIALVEGVMGLYDGYSGERPGGSTAEIARLLSAPVILLVNISHMAESAAAIVLGYKNLDPRINIAGVILNQAGSTRHYEICRKAIEKYASTPVIGYLLRNKDLVIPERHLGLKTTSEGGELETFIQNLATRIESTIDIDRILEIARNAPPLPEKPLPCLFPETPACPVTRIAVAKDEAFSFYYQANLDMLSDWGAELCYFSPVHDTCLPPDIGGIYIGGGFPEIMAAELSANQPMKDTLTKAAADGMPIYAECGGLMYLSEAIEDFDSTKYLMLGLLPGISVMQKKLHRLGYTRAAVQNDNILSAKGTELRGHIFHWSKLPSPQTKPAYTLLEPAEFVGQNEGFIIGGSTNVLASYLHLHFGTNPDLAKNFIRISKDFCTI

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AJ965256
EMBL· GenBank· DDBJ
CAI82403.1
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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