In Salmonella typhimurium LT2, under anaerobic conditions, CobU (EC 126.96.36.199 and EC 188.8.131.52), CobT (EC 184.108.40.206), CobC (EC 220.127.116.11) and CobS (EC 18.104.22.168) catalyse 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 nucleotide loop assembly pathway is the cobinamide (Cbi) activation branch where AdoCbi or adenosylcobinamide-phosphate is converted to the activated intermediate AdoCbi-GDP by Cob U. The final step in adenosylcobalamin biosynthesis is the condensation of AdoCbi-GDP with alpha-ribazole, which is catalysed by EC 22.214.171.124, adenosylcobinamide-GDP ribazoletransferase (CobS), to yield adenosylcobalamin. CobU is a bifunctional enzyme that has both kinase (EC 126.96.36.199) and guanylyltransferase (EC 188.8.131.52, adenosylcobinamide-phosphate guanylyltransferase) 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 .