Q8EXQ7 · COBDQ_LEPIN

Function

function

Catalyzes two activities which are involved in the adenosylcobalamin biosynthesis: 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, and 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 (By similarity).

Catalytic activity

Cofactor

pyridoxal 5'-phosphate (UniProtKB | Rhea| CHEBI:597326 )

Pathway

Cofactor biosynthesis; adenosylcobalamin biosynthesis.

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site6-7O-phospho-L-threonine (UniProtKB | ChEBI)
Binding site30O-phospho-L-threonine (UniProtKB | ChEBI)
Binding site159O-phospho-L-threonine (UniProtKB | ChEBI)
Binding site323O-phospho-L-threonine (UniProtKB | ChEBI)
Binding site337O-phospho-L-threonine (UniProtKB | ChEBI)
Active site704Nucleophile
Active site802

GO annotations

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

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Adenosylcobalamin biosynthesis bifunctional protein CobDQ

Including 2 domains:

  • Recommended name
    Putative threonine-phosphate decarboxylase
  • EC number
  • Alternative names
    • L-threonine-O-3-phosphate decarboxylase
  • Recommended name
    Cobyric acid synthase

Gene names

    • Name
      cobDQ
    • Ordered locus names
      LB_151

Organism names

Accessions

  • Primary accession
    Q8EXQ7

Proteomes

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00001413051-863Adenosylcobalamin biosynthesis bifunctional protein CobDQ
Modified residue214N6-(pyridoxal phosphate)lysine

Proteomic databases

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-373Putative threonine-phosphate decarboxylase
Region374-863Cobyric acid synthase
Domain622-810GATase cobBQ-type

Sequence similarities

In the N-terminal section; belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family.
In the C-terminal section; belongs to the CobB/CobQ family. CobQ subfamily.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    863
  • Mass (Da)
    97,457
  • Last updated
    2010-10-05 v2
  • Checksum
    40710C6DC23E055E
MNLPEHGGNLIELSKKAGCNPKEILDFSANINPLGFPEWLRPFLHSKIEDLISYPDPNYTSLKKKIHSKYGICTEQIVLGNGASELILQIPFVVQADYALIAVPCYSGYKEAISLLKIPCIEVTLKEEKQFRLDINELRDVLKSKPDQKALVFLGHPNNPTGVTLDKIEVLKIVQEFQNSVFVIDESFIHFCTNESSFLKDKTENMILIQSMTKILALPGLRIGICYASPLICSNISKRLPTWNVNSIAASVYEKAISDEDYIENSKQNIKIWKEKLIYDLSNLEFLNLFSSEANFILIKILDNKNIFDLTQELLIKYKIAVRNCENFSGLSKNFIRIAVRTPEENKKIIDAFSNIFYGTRQRLKSRKKTPSIMFQGTASNVGKSILTAALCRILSQDGIKVAPFKSQNMALNSFVTLNGEEIGRAQALQAQAAKILPDIRMNPILLKPSNEKDSQVIINGKPLNSMNFKDYDQYKPIAFEEVKKSYDSLASEYNVIIIEGAGSASEVNLKKNDIVNMKMAEYAKADVLLVGNIDHGGLFGSLLGTMETLTEWERKLVFGFIINRFRGAKELLKTGINYIEEYTNKPILGIVPYIKNLKLPEEDSLEFKSGALDDTSKLEERLDVVLIDIPRISNHTDIDALRAEPDVRVRIVRTVEDLGEPDVLILPGSKNVISDLNHLYDVGLVNKIFALSRNQKTDIVGICGGYQMLGKNIFDPYRIESDQGSIQGISLLQIETILEKNKSLKRVFATHIPTKTEVEGYEIHHGKTKSIGNTRVILLNEKAEELGHSDPTGRIWGTYIHGIFDKDEFRRKYLDQIRIRKGKSPLVKVQVSYNLEKSLDRLARYVRQSLNINLIYRKLGLG

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AE010301
EMBL· GenBank· DDBJ
AAN51710.2
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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