A4FW46 · CBIA_METM5

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. Involved in the biosynthesis of the unique nickel-containing tetrapyrrole coenzyme F430, the prosthetic group of methyl-coenzyme M reductase (MCR), which plays a key role in methanogenesis and anaerobic methane oxidation. Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of Ni-sirohydrochlorin, using L-glutamine or ammonia as the nitrogen source.

Miscellaneous

The a and c carboxylates of cobyrinate and Ni-sirohydrochlorin 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 site331Nucleophile
Site431Increases 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
Biological Processmethanogenesis

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
    • Ni-sirohydrochlorin a,c-diamide synthase
      (EC:6.3.5.12
      ) . EC:6.3.5.12 (UniProtKB | ENZYME | Rhea)
    • Ni-sirohydrochlorin a,c-diamide synthetase

Gene names

    • Name
      cbiA
    • Synonyms
      cfbB
    • Ordered locus names
      MmarC5_0100

Organism names

Accessions

  • Primary accession
    A4FW46

Proteomes

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_10000743901-447Cobyrinate a,c-diamide synthase

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain252-439GATase 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 or Ni-sirohydrochlorin, 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
    447
  • Mass (Da)
    50,199
  • Last updated
    2007-04-17 v1
  • Checksum
    9C238529B7F8F076
MKRVVIAGTSSMVGKTTISTGIMKALSKKNNVQPYKIGPDYIDPTYHTEATKNKSRNLDSFFMDEMQVRSIFKRHSKNKDINVIEGVRGLYEGISPYNDVGSTASVSKTLNAPVILLMDARSLTRSAAAIIKGFKSFDTELNIKGVIFNKIRGEGHLNKLKEAVKYYDNDIEIIGAIPRDDGLSVSQRHLGLVPTPENKQKLLERIDLWGNTVEECLDIEKIVELSDESFDFEVDEKNKEETLWKVEKNNSKIAVAFDESFNFYYWDNFDALEENGAKIKFFSPLNDVEVPDCDTIYLGGGYPELFSEKLSNNKSMIDSIRNFDGKIYGECGGLMYLTNSIDGKEMLKLIDADAVMTPNVQGLSYVKGTFEKDCIIGEKSKEFKAHEFHYSKLININENDFSYRINRGKGIINSMDGITSKDGDIVGGYAHQHCIGNPYFAANLSKT

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000609
EMBL· GenBank· DDBJ
ABO34417.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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