Q8EXQ7 · COBDQ_LEPIN
- ProteinAdenosylcobalamin biosynthesis bifunctional protein CobDQ
- GenecobDQ
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids863 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
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
- O-phospho-L-threonine + H+ = (R)-1-aminopropan-2-yl phosphate + CO2
Cofactor
Pathway
Cofactor biosynthesis; adenosylcobalamin biosynthesis.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 6-7 | O-phospho-L-threonine (UniProtKB | ChEBI) | ||||
Sequence: HG | ||||||
Binding site | 30 | O-phospho-L-threonine (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 159 | O-phospho-L-threonine (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 323 | O-phospho-L-threonine (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 337 | O-phospho-L-threonine (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Active site | 704 | Nucleophile | ||||
Sequence: C | ||||||
Active site | 802 | |||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | ABC-type vitamin B12 transporter activity | |
Molecular Function | pyridoxal phosphate binding | |
Molecular Function | threonine-phosphate decarboxylase activity | |
Biological Process | cobalamin biosynthetic process | |
Biological Process | glutamine metabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAdenosylcobalamin biosynthesis bifunctional protein CobDQ
Including 2 domains:
- Recommended namePutative threonine-phosphate decarboxylase
- EC number
- Alternative names
- Recommended nameCobyric acid synthase
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Spirochaetota > Spirochaetia > Leptospirales > Leptospiraceae > Leptospira
Accessions
- Primary accessionQ8EXQ7
Proteomes
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000141305 | 1-863 | Adenosylcobalamin biosynthesis bifunctional protein CobDQ | |||
Sequence: MNLPEHGGNLIELSKKAGCNPKEILDFSANINPLGFPEWLRPFLHSKIEDLISYPDPNYTSLKKKIHSKYGICTEQIVLGNGASELILQIPFVVQADYALIAVPCYSGYKEAISLLKIPCIEVTLKEEKQFRLDINELRDVLKSKPDQKALVFLGHPNNPTGVTLDKIEVLKIVQEFQNSVFVIDESFIHFCTNESSFLKDKTENMILIQSMTKILALPGLRIGICYASPLICSNISKRLPTWNVNSIAASVYEKAISDEDYIENSKQNIKIWKEKLIYDLSNLEFLNLFSSEANFILIKILDNKNIFDLTQELLIKYKIAVRNCENFSGLSKNFIRIAVRTPEENKKIIDAFSNIFYGTRQRLKSRKKTPSIMFQGTASNVGKSILTAALCRILSQDGIKVAPFKSQNMALNSFVTLNGEEIGRAQALQAQAAKILPDIRMNPILLKPSNEKDSQVIINGKPLNSMNFKDYDQYKPIAFEEVKKSYDSLASEYNVIIIEGAGSASEVNLKKNDIVNMKMAEYAKADVLLVGNIDHGGLFGSLLGTMETLTEWERKLVFGFIINRFRGAKELLKTGINYIEEYTNKPILGIVPYIKNLKLPEEDSLEFKSGALDDTSKLEERLDVVLIDIPRISNHTDIDALRAEPDVRVRIVRTVEDLGEPDVLILPGSKNVISDLNHLYDVGLVNKIFALSRNQKTDIVGICGGYQMLGKNIFDPYRIESDQGSIQGISLLQIETILEKNKSLKRVFATHIPTKTEVEGYEIHHGKTKSIGNTRVILLNEKAEELGHSDPTGRIWGTYIHGIFDKDEFRRKYLDQIRIRKGKSPLVKVQVSYNLEKSLDRLARYVRQSLNINLIYRKLGLG | ||||||
Modified residue | 214 | N6-(pyridoxal phosphate)lysine | ||||
Sequence: K |
Proteomic databases
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-373 | Putative threonine-phosphate decarboxylase | ||||
Sequence: MNLPEHGGNLIELSKKAGCNPKEILDFSANINPLGFPEWLRPFLHSKIEDLISYPDPNYTSLKKKIHSKYGICTEQIVLGNGASELILQIPFVVQADYALIAVPCYSGYKEAISLLKIPCIEVTLKEEKQFRLDINELRDVLKSKPDQKALVFLGHPNNPTGVTLDKIEVLKIVQEFQNSVFVIDESFIHFCTNESSFLKDKTENMILIQSMTKILALPGLRIGICYASPLICSNISKRLPTWNVNSIAASVYEKAISDEDYIENSKQNIKIWKEKLIYDLSNLEFLNLFSSEANFILIKILDNKNIFDLTQELLIKYKIAVRNCENFSGLSKNFIRIAVRTPEENKKIIDAFSNIFYGTRQRLKSRKKTPSI | ||||||
Region | 374-863 | Cobyric acid synthase | ||||
Sequence: MFQGTASNVGKSILTAALCRILSQDGIKVAPFKSQNMALNSFVTLNGEEIGRAQALQAQAAKILPDIRMNPILLKPSNEKDSQVIINGKPLNSMNFKDYDQYKPIAFEEVKKSYDSLASEYNVIIIEGAGSASEVNLKKNDIVNMKMAEYAKADVLLVGNIDHGGLFGSLLGTMETLTEWERKLVFGFIINRFRGAKELLKTGINYIEEYTNKPILGIVPYIKNLKLPEEDSLEFKSGALDDTSKLEERLDVVLIDIPRISNHTDIDALRAEPDVRVRIVRTVEDLGEPDVLILPGSKNVISDLNHLYDVGLVNKIFALSRNQKTDIVGICGGYQMLGKNIFDPYRIESDQGSIQGISLLQIETILEKNKSLKRVFATHIPTKTEVEGYEIHHGKTKSIGNTRVILLNEKAEELGHSDPTGRIWGTYIHGIFDKDEFRRKYLDQIRIRKGKSPLVKVQVSYNLEKSLDRLARYVRQSLNINLIYRKLGLG | ||||||
Domain | 622-810 | GATase cobBQ-type | ||||
Sequence: RLDVVLIDIPRISNHTDIDALRAEPDVRVRIVRTVEDLGEPDVLILPGSKNVISDLNHLYDVGLVNKIFALSRNQKTDIVGICGGYQMLGKNIFDPYRIESDQGSIQGISLLQIETILEKNKSLKRVFATHIPTKTEVEGYEIHHGKTKSIGNTRVILLNEKAEELGHSDPTGRIWGTYIHGIFDKDEF |
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
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length863
- Mass (Da)97,457
- Last updated2010-10-05 v2
- Checksum40710C6DC23E055E
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE010301 EMBL· GenBank· DDBJ | AAN51710.2 EMBL· GenBank· DDBJ | Genomic DNA |