A0AA96XVW8 · A0AA96XVW8_9PSED

  • Protein
    Hydrogenobyrinate a,c-diamide synthase
  • Gene
    cobB
  • 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 hydrogenobyrinate, using either L-glutamine or ammonia as the nitrogen source.

Miscellaneous

The a and c carboxylates of hydrogenobyrinate are activated for nucleophilic attack via formation of a phosphorylated intermediate by ATP. CobB 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 precorrin-2 (aerobic route): step 9/10.

Features

Showing features for active site, site.

Type
IDPosition(s)Description
Active site326Nucleophile
Site419Increases nucleophilicity of active site Cys

GO annotations

AspectTerm
Molecular FunctionATP binding
Molecular Functioncobyrinic acid a,c-diamide synthase activity
Molecular Functionhydrogenobyrinic acid a,c-diamide synthase (glutamine-hydrolysing) activity
Biological Processcobalamin biosynthetic process
Biological Processglutamine metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Hydrogenobyrinate a,c-diamide synthase
  • EC number
  • Alternative names
    • Hydrogenobyrinic acid a,c-diamide synthase

Gene names

    • Name
      cobB
    • ORF names
      QOM08_21175

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • P105
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Pseudomonadales > Pseudomonadaceae > Pseudomonas

Accessions

  • Primary accession
    A0AA96XVW8

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain15-192CobQ/CobB/MinD/ParA nucleotide binding
Domain245-424CobB/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 hydrogenobyrinate 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
    464
  • Mass (Da)
    49,220
  • Last updated
    2024-03-27 v1
  • Checksum
    35719D5F28195325
MSDVPLASRHCPAVLIAAPASGQGKTTVTAALARLHRKQGRRVRVFKCGPDFLDPMILERASGAPVYQLDMWMVGEQESRRLLWEAAAEADLILIEGVMGLFDGTPSSADLARHFGVPVLAVIDGTAMAQTFGALALGLARYQPDLPFAGVLANRVGTLRHAQLLEGSLTEGLRWYGALSRETGIELPSRHLGLVQASELNDLDLRLDAAADALAGSCEVALPPAVEFVAPAVIAAQPWLEGVHIAVARDEAFAFTYGASLDLLRAMGAQLSFFSPIHDSELPAADSLYLPGGYPELHHVALAQNAPMLAAIRAHHQAGKPLLAECGGMLYLLDSLTDVDGTRAELLGLLAGDAQMQKRLAALALQSVELPEGTLRGHTYHHSLTSTGLEPIARGHSPNGGRGAEAVFRQGRMTASYVHFYFPSNPRAIAALFAPDPEAAIANRLAPTSDHLTPVGASLLAKRP

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP126693
EMBL· GenBank· DDBJ
WNZ77198.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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