_EC 2.5.1.17 Cob(I)yrinic acid a,c-diamide adenosyltransferase. 8 PDB entries  
EC 2.-.-.- Transferases. [17,949 PDB entries]
EC 2.5.-.- Transferring alkyl or aryl groups, other than methyl groups. [1,301 PDB entries]
EC 2.5.1.- Transferring alkyl or aryl groups, other than methyl groups. [1,301 PDB entries]
EC 2.5.1.17 Cob(I)yrinic acid a,c-diamide adenosyltransferase. [8 PDB entries]    
1g5r

Pathway: Corrin Biosynthesis (part 5)
Reaction: (1) Atp + cob(I)yrinic acid a,c-diamide = triphosphate + adenosylcob(III)yrinic acid a,c-diamide. (2) Atp + cobinamide = triphosphate + adenosylcobinamide.
 


ATP
+
cob(I)yrinic acid a,c-diamide
=
triphosphate
+
adenosylcob(III)yrinic acid a,c-diamide

ATP
+
cobinamide
=
triphosphate
+
adenosylcobinamide
Molecule diagrams generated from .mol files obtained from the KEGG ftp site.

Other name(s): Aquacob(I)alamin adenosyltransferase. Aquocob(I)alamin vitamin B12s adenosyltransferase. ATP:cob(I)alamin Co-beta-adenosyltransferase. ATP:corrinoid adenosyltransferase. Cob(I)alamin adenosyltransferase.
Comments: The corrinoid adenosylation pathway comprises three steps: (1) Reduction of Co(III) to Co(II) by a one-electron transfer; this can be carried out by Ec 1.16.1.3, or non-enzymically in the presence of dihydroflavin nucleotides. (2) Co(II) is reduced to Co(I) in a second single-electron transfer by Ec 1.16.1.4. (3) The Co(I) conducts a nucleophilic attack on the adenosyl moiety of Atp to leave the cobalt atom in a Co(III) state (EC 2.5.1.17). The enzyme responsible for the adenosylation reaction is the product of the gene cobO in the aerobic bacterium Pseudomonas denitrificans
Links:   [IntEnz]   [ExPASy]   [KEGG]  

There are 8 PDB entries in enzyme class E.C.2.5.1.17

  PDB code Protein
1g5r
The three-dimensional structure of atp:corrinoid adenosyltra from salmonella typhimurium. Apo form
Source: Salmonella typhimurium. Organism_taxid: 602. Gene: coba. Expressed in: salmonella typhimurium. Expression_system_taxid: 602
Chain: A (157 residues) CATH domain: 3.40.50.300
1g5t
The three-dimensional structure of atp:corrinoid adenosyltra from salmonella typhimurium. Apo-atp form
Source: Salmonella typhimurium. Organism_taxid: 602. Gene: coba. Expressed in: salmonella typhimurium. Expression_system_taxid: 602
Chain: A (157 residues) CATH domain: 3.40.50.300
Bound ligands:   Het Group ATP corresponds to enzyme reactant ATP
  Het Group ATP corresponds to enzyme reactant ATP
1g64
The three-dimensional structure of atp:corrinoid adenosyltra from salmonella typhimurium. Cobalamin/atp ternary complex
Source: Salmonella typhimurium. Organism_taxid: 602. Gene: coba. Expressed in: salmonella typhimurium. Expression_system_taxid: 602
Chains: A, B (169 residues) CATH domain: 3.40.50.300
Bound ligands:   Het Group ATP corresponds to enzyme reactant ATP
  Het Group B12 is 59.79% similar to enzyme reactant cob(I)yrinic
  Het Group ATP corresponds to enzyme reactant ATP
  Het Group B12 is 72.83% similar to enzyme reactant cobinamide
1rty
Crystal structure of bacillus subtilis yvqk, a putative atp- binding cobalamin adenosyltransferase, the north east structural genomics target sr128
Source: Bacillus subtilis. Organism_taxid: 1423. Strain: 168. Gene: yvqk. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C (158 residues) CATH domain: 1.20.1200.10
1woz
Crystal structure of uncharacterized protein st1454 from sul tokodaii
Source: Sulfolobus tokodaii. Organism_taxid: 273063. Strain: 7. Gene: st1454. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (159 residues) CATH domain: 1.20.1200.10
2g2d
Crystal structure of a putative pduo-type atp:cobalamin adenosyltransferase from mycobacterium tuberculosis
Source: Mycobacterium tuberculosis. Organism_taxid: 1773. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Chain: A (160 residues) CATH domain: 1.20.1200.10
2idx
Structure of human atp:cobalamin adenosyltransferase bound to atp.
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: mmab. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C (148 residues) CATH domain: 1.20.1200.10
Bound ligands:   Het Group ATP corresponds to enzyme reactant ATP
  Het Group ATP corresponds to enzyme reactant ATP
4hut
Structure of atp:co(i)rrinoid adenosyltransferase (coba) fro salmonella enterica in complex with four and five-coordinat alamin and atp
Source: Salmonella enterica subsp. Enterica se typhimurium. Organism_taxid: 99287. Strain: lt2. Gene: btur, coba, stm1718. Expressed in: salmonella enterica subsp. Enterica sero expression_system_taxid: 90371.
Chains: A, B (191 residues) CATH domain: 3.40.50.300
Bound ligands:   Het Group ATP corresponds to enzyme reactant ATP
  Het Group B12 is 59.79% similar to enzyme reactant cob(I)yrinic
  Het Group ATP corresponds to enzyme reactant ATP
  Het Group B12 is 72.83% similar to enzyme reactant cobinamide