A0AA42GTJ8 · A0AA42GTJ8_9HYPH

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.

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 precorrin-2 (aerobic route): step 9/10.

Features

Showing features for active site, site.

TypeIDPosition(s)Description
Active site327Nucleophile
Site427Increases 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
      N7376_01860

Organism names

  • Taxonomic identifier
  • Strain
    • GD04153
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Alphaproteobacteria > Hyphomicrobiales > Brucellaceae > Brucella/Ochrobactrum group > Brucella

Accessions

  • Primary accession
    A0AA42GTJ8

Proteomes

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain5-188CobQ/CobB/MinD/ParA nucleotide binding
Domain245-429CobB/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
    436
  • Mass (Da)
    47,231
  • Last updated
    2024-01-24 v1
  • Checksum
    8F1649BB02BFDF73
MKGFMIAAPASGSGKTTVTLGLLRVLKRRGVALAPAKAGPDYIDPAYHKAASGADCFNLDPWAMRPELISALSSRMTESSAKLLVAEGMMGLFDGAMDGKGSSADLARVLELPVVLVVDCARQSHSVAALVWGFSQFRKDVLIAGIILNRVGSPRHEAMLRGALEPLGIPVLGALPRDTDLSLPERHLGLVQAGEHSDLETFLDHAADVIEAHIDLDTLQSIWSRPKRYDAMANVPRLKPLGNHIAVARDDAFAFAYAHLFEGWRRRGVEISFFSPLADEAPRQDADAIYLPGGYPELYAGRLAQAARFQTAIRDAATRGATVYGECGGYMVLGESLQDAEGVAHPMLGLLPLETSFAKRKLHLGYRLLEPLEGSPWKEPLKAHEFHYASILREGEADRLFRVRDAARDELGEAGLRVGSVSGSFMHVIDFCGDKA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JAODYY010000001
EMBL· GenBank· DDBJ
MDH0122733.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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