Bifunctional adenosylcobalamin biosynthesis protein CobU
Details
- Name
- Bifunctional adenosylcobalamin biosynthesis protein CobU
- Synonyms
- Adenosylcobinamide kinase
- Adenosylcobinamide-phosphate guanylyltransferase
- Gene Name
- cobU
- Organism
- Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
- Amino acid sequence
>lcl|BSEQ0005234|Bifunctional adenosylcobalamin biosynthesis protein CobU MMILVTGGARSGKSRHAEALIGDAPQVLYIATSQILDDEMAARIQHHKDGRPAHWRTAEC WRHLDTLITADLAPDDAILLECITTMVTNLLFALGGENDPEQWDYAAMERAIDDEIQILI AACQRCPAKVVLVTNEVGMGIVPENRLARHFRDIAGRVNQRLAAAADEVWLVVSGIGVKI K
- Number of residues
- 181
- Molecular Weight
- 19901.7
- Theoretical pI
- 5.26
- GO Classification
- Functionsadenosylcobinamide kinase activity / ATP binding / cobinamide phosphate guanylyltransferase activity / GTP bindingProcessescobalamin biosynthetic process / cofactor biosynthetic process
- General Function
- Gtp binding
- Specific Function
- Catalyzes ATP-dependent phosphorylation of adenosylcobinamide and addition of GMP to adenosylcobinamide phosphate.
- Pfam Domain Function
- CobU (PF02283)
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0011890|Bifunctional adenosylcobalamin biosynthesis protein CobU (cobU) ATGATGATTCTGGTGACGGGCGGGGCACGTAGTGGTAAAAGCCGTCATGCTGAAGCCTTA ATTGGCGATGCGCCGCAGGTACTGTATATCGCCACCTCGCAGATTCTTGATGACGAGATG GCGGCGAGAATTCAGCATCATAAAGATGGCAGGCCGGCACACTGGCGGACCGCAGAATGC TGGCGGCATCTTGATACGTTGATTACCGCGGATCTTGCCCCTGACGACGCGATTTTGCTG GAATGTATTACCACCATGGTGACGAATCTGCTGTTTGCGCTGGGAGGCGAGAACGATCCC GAACAGTGGGATTACGCGGCGATGGAGCGCGCCATTGACGATGAAATTCAGATTTTAATT GCAGCCTGCCAGCGCTGCCCGGCGAAAGTGGTACTGGTGACAAATGAGGTGGGAATGGGG ATCGTCCCGGAAAACCGTCTGGCGCGCCATTTTCGTGATATTGCCGGTCGGGTCAACCAA CGACTGGCGGCAGCGGCGGATGAGGTCTGGCTGGTAGTCTCAGGTATTGGAGTCAAAATT AAATGA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID Q05599 UniProtKB Entry Name COBU_SALTY GenBank Gene ID AE008789 - General References
- Roth JR, Lawrence JG, Rubenfield M, Kieffer-Higgins S, Church GM: Characterization of the cobalamin (vitamin B12) biosynthetic genes of Salmonella typhimurium. J Bacteriol. 1993 Jun;175(11):3303-16. [Article]
- McClelland M, Sanderson KE, Spieth J, Clifton SW, Latreille P, Courtney L, Porwollik S, Ali J, Dante M, Du F, Hou S, Layman D, Leonard S, Nguyen C, Scott K, Holmes A, Grewal N, Mulvaney E, Ryan E, Sun H, Florea L, Miller W, Stoneking T, Nhan M, Waterston R, Wilson RK: Complete genome sequence of Salmonella enterica serovar Typhimurium LT2. Nature. 2001 Oct 25;413(6858):852-6. [Article]
- O'Toole GA, Escalante-Semerena JC: Purification and characterization of the bifunctional CobU enzyme of Salmonella typhimurium LT2. Evidence for a CobU-GMP intermediate. J Biol Chem. 1995 Oct 6;270(40):23560-9. [Article]
- Thomas MG, Thompson TB, Rayment I, Escalante-Semerena JC: Analysis of the adenosylcobinamide kinase/adenosylcobinamide-phosphate guanylyltransferase (CobU) enzyme of Salmonella typhimurium LT2. Identification of residue His-46 as the site of guanylylation. J Biol Chem. 2000 Sep 8;275(36):27576-86. [Article]
- Thompson TB, Thomas MG, Escalante-Semerena JC, Rayment I: Three-dimensional structure of adenosylcobinamide kinase/adenosylcobinamide phosphate guanylyltransferase from Salmonella typhimurium determined to 2.3 A resolution,. Biochemistry. 1998 May 26;37(21):7686-95. [Article]
- Thompson TB, Thomas MG, Escalante-Semerena JC, Rayment I: Three-dimensional structure of adenosylcobinamide kinase/adenosylcobinamide phosphate guanylyltransferase (CobU) complexed with GMP: evidence for a substrate-induced transferase active site. Biochemistry. 1999 Oct 5;38(40):12995-3005. [Article]