A0A4R1AGC7 · A0A4R1AGC7_9ACTN

  • 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.

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.

Type
IDPosition(s)Description
Active site335Nucleophile
Site426Increases 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
Molecular Functionpyridoxal phosphate binding
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
      E0W78_11535

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • IC_218
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Propionibacteriales > Nocardioidaceae > Aeromicrobium

Accessions

  • Primary accession
    A0A4R1AGC7

Proteomes

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain7-191CobQ/CobB/MinD/ParA nucleotide binding
Domain253-432CobB/CobQ-like glutamine amidotransferase
Domain485-797Aminotransferase class I/classII large

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.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    806
  • Mass (Da)
    84,007
  • Last updated
    2019-07-31 v1
  • MD5 Checksum
    A0630C816CA935347CF8282530BB5800
MSLPRVLVAAPASGHGKTTVATGLMAALAARGHAVSGHKVGPDYIDPGYHALATGRPGRNLDPHLTDPALMVPLLLHGARGADVAVVEGVMGLFDGQIGGDGFASSAHVATLTRTPVVLVVDVSHASRSVGAVVHGMATFEPGVTVAGVILNKAGSPRHAAEARAAVERTGIPVLGVLQRDHGVSAPSRHLGLVPAEERDEAAGSLDRLAAQVAEHVDLDAVLEIARSASPLTETAWDPTDHVRPAGTDAPVVAVAAGRAFTFRYAETTELLEAAGCTVVPFDPARDRHLPAGTRGLYLGGGFPEVHAAALSANSSLRADLRQAVLDGVPTVAECAGLLYLCRSVDGHPMIGALDADAVMTPRLTLSYRTPRLGTDQLLGAAGTAATAHEFHRTTVHPVHGDRPAWSLDAGDVGFAGPTLSASYLHLHWAGHPHLAQSFADAVHGSTATARPATPVAATVAVVEPVAAPSDPLRHHGDVEATKGLLDLAVNVSRLPRPEWLEQALRDGTAASTAYPDATAAHAAVARRHGRDVDEVLVTAGAAEAFFLVARARRWHRPVVVHPQFTEPDVALRAAGHRVAHVLCRAADDFALDPALVPDDADLVVVGNPTNPTGRLHPAATLRALCRPGRVVVVDEAFMDHVPGERQTLTAHRLPGLVVVRSLTKTWSMPGVRAGYVVGDPAVVADLREQQPPWSVGTAALHAVVATSGPQALAEADHRARLAVQHRRVLVDGLAELGVEVVPTEAPFVLARLGSGGHARLRAAGVAVRRADTFPGLDDTWARLAVREPAVTRHLLTTLGVEAAWS

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
SJXM01000009
EMBL· GenBank· DDBJ
TCI97672.1
EMBL· GenBank· DDBJ
Genomic DNA

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.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
Help