CATH Classification
Level | CATH Code | Description |
---|---|---|
3 | Alpha Beta | |
3.40 | 3-Layer(aba) Sandwich | |
3.40.50 | Rossmann fold | |
3.40.50.300 | P-loop containing nucleotide triphosphate hydrolases |
Domain Context
CATH Clusters
Superfamily | P-loop containing nucleotide triphosphate hydrolases |
Functional Family | Bifunctional adenosylcobalamin biosynthesis protein |
Enzyme Information
2.7.7.62 |
Adenosylcobinamide-phosphate guanylyltransferase.
based on mapping to UniProt Q05599
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.
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2.7.1.156 |
Adenosylcobinamide kinase.
based on mapping to UniProt Q05599
ATP or GTP + adenosylcobinamide = adenosylcobinamide phosphate + ADP or 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 nucleotide loop assembly pathway is the cobinamide (Cbi) activation branch where AdoCbi or adenosylcobinamide-phosphate is converted to the activated intermediate AdoCbi-GDP by 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.
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UniProtKB Entries (1)
Q05599 |
COBU_SALTY
Salmonella enterica subsp. enterica serovar Typhimurium str. LT2
Bifunctional adenosylcobalamin biosynthesis protein CobU
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PDB Structure
PDB | 1CBU |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | Escherichia |
Primary Citation |
Three-dimensional structure of adenosylcobinamide kinase/adenosylcobinamide phosphate guanylyltransferase from Salmonella typhimurium determined to 2.3 A resolution,.
Biochemistry
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