Q3A7A0 · Q3A7A0_SYNC1

Function

function

Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH2 groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation.
Decarboxylates L-threonine-O-3-phosphate to yield (R)-1-amino-2-propanol O-2-phosphate, the precursor for the linkage between the nucleotide loop and the corrin ring in cobalamin.

Catalytic activity

Pathway

Cofactor biosynthesis; adenosylcobalamin biosynthesis.

Features

Showing features for active site.

TypeIDPosition(s)Description
Active site706Nucleophile
Active site803

GO annotations

AspectTerm
Molecular FunctionABC-type vitamin B12 transporter activity
Molecular Functionmethyltransferase activity
Molecular Functionpyridoxal phosphate binding
Molecular Functionthreonine-phosphate decarboxylase activity
Biological Processcobalamin biosynthetic process
Biological Processglutamine metabolic process
Biological Processmethylation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Cobyric acid synthase

Gene names

    • Name
      cobQ
    • Ordered locus names
      Pcar_0484

Organism names

Accessions

  • Primary accession
    Q3A7A0

Proteomes

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain27-356Aminotransferase class I/classII large
Domain375-600CobQ/CobB/MinD/ParA nucleotide binding
Domain626-809CobB/CobQ-like glutamine amidotransferase

Sequence similarities

Belongs to the CobB/CobQ family. CobQ subfamily.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    864
  • Mass (Da)
    94,910
  • Last updated
    2005-11-22 v1
  • Checksum
    1A96C41A09CDCDC3
MTESGNWRHGGHLRQLAMAAGVNPESLLDFSANINPLGPPEWLRSRISGSISSLVHYPDPEGLALVDAACRRYGVDADEILIGNGSTELFYLLPHALGVRHALIPVPSYVDYATAADIAGLTVHTLPLTADNGFAFDFEILETALEELKGSPVIVPIGHPNNPTGRSLDAQRLRALARRFPTTTFVVDEAFADFVEDFDSLTINRPANVVVMLSLTKIFAIPGLRLGLAVASPALVRKVKSLQPPWSVNTIAQQVGEAALRDAEYIHASRTAVTALRDTLRHELEKIPYLTVYPGQANFLLLRCDRKSMDARTLANRLIKRGLAIRICENFEGLDRRFFRVAVRTEPENRQLVAALRQELFLAPLVTTRRHTPAIMFQGTSSNAGKSVLAAALCRIMLQDGYRVAPFKSQNMSLNSFVTRDGGEMGRAQVVQAQAARLDPDVRMNPILLKPSSETGSQVVLCGKPVGNMKVMDYFRYKAEAFERVKECYDSLASEHDAMVLEGAGSPAEVNLKAHDIVNMKMALFAQAPVLMVGDIDCGGVFASFVGSMEVLSERERAQVAGFIVNRFRGQADLLKDALDYTLQHTGRPILGVVPYVKDLGLPEEDSVGFKEGMFNDTRSSEDAVDIAVLDLPHISNFTDIEPLHIEPDVRIRTVRRIQDLGQPDAVIVPGSKNVIGDLTFLRAVGLDRSLEQLAAEGRCEIIGICGGYQILGRSIDDPHGIESPGTELTGLGLLPIDTVLEQDKTLTRSEARHRISGLKVHGYEIHHGQSHSDPIPPALIGSDGEAMGACRDDGLVWGSYLHGLFDADGFRRWFIDRLRQRKGLKPYGTVQVCYDLEPAFERLADIVRQSIDIPALYRLMGLR

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000142
EMBL· GenBank· DDBJ
ABA87744.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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