CATH Classification

Domain Context

CATH Clusters

Superfamily Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A
Functional Family

Enzyme Information

2.7.7.62
Adenosylcobinamide-phosphate guanylyltransferase.
based on mapping to UniProt Q58517
GTP + adenosylcobinamide phosphate = diphosphate + adenosylcobinamide- GDP.
-!- In Salmonella typhimurium LT2, under anaerobic conditions, CobU (EC 2.7.7.62 and EC 2.7.1.156), CobT (EC 2.4.2.21), CobC (EC 3.1.3.73) and CobS (EC 2.7.8.26) catalyze reactions in the nucleotide loop assembly pathway, which convert adenosylcobinamide (AdoCbi) into adenosylcobalamin (AdoCbl). -!- CobT and CobC are involved in 5,6-dimethylbenzimidazole activation whereby 5,6-dimethylbenzimidazole is converted to its riboside, alpha-ribazole. -!- The second branch of the nuclotide loop assembly pathway is the cobinamide (Cbi) activation branch where AdoCbi or adenosylcobinamide-phosphate is converted to the activated intermediate AdoCbi-GDP by the bifunctional enzyme CobU. -!- The final step in adenosylcobalamin biosynthesis is the condensation of AdoCbi-GDP with alpha-ribazole, which is catalyzed by CobS (EC 2.7.8.26), to yield adenosylcobalamin. -!- CobU is a bifunctional enzyme that has both kinase (EC 2.7.1.156) and guanylyltransferase (EC 2.7.7.62) activities. -!- However, both activities are not required at all times. -!- The kinase activity has been proposed to function only when S.typhimurium is assimilating cobinamide whereas the guanylyltransferase activity is required for both assimilation of exogenous cobinamide and for de novo synthesis of adenosylcobalamin. -!- The guanylyltransferase reaction is a two-stage reaction with formation of a CobU-GMP intermediate.

UniProtKB Entries (1)

Q58517
COBY_METJA
Methanocaldococcus jannaschii DSM 2661
Adenosylcobinamide-phosphate guanylyltransferase

PDB Structure

PDB 3RSB
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Structure and Mutational Analysis of the Archaeal GTP:AdoCbi-P Guanylyltransferase (CobY) from Methanocaldococcus jannaschii: Insights into GTP Binding and Dimerization.
Newmister, S.A., Otte, M.M., Escalante-Semerena, J.C., Rayment, I.
Biochemistry
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