Bifunctional adenosylcobalamin biosynthesis protein CobU

NameBifunctional adenosylcobalamin biosynthesis protein CobU
Synonyms
  • Adenosylcobinamide kinase
  • Adenosylcobinamide-phosphate guanylyltransferase
Gene NamecobU
OrganismSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Amino acid sequence
>lcl|BSEQ0005234|Bifunctional adenosylcobalamin biosynthesis protein CobU
MMILVTGGARSGKSRHAEALIGDAPQVLYIATSQILDDEMAARIQHHKDGRPAHWRTAEC
WRHLDTLITADLAPDDAILLECITTMVTNLLFALGGENDPEQWDYAAMERAIDDEIQILI
AACQRCPAKVVLVTNEVGMGIVPENRLARHFRDIAGRVNQRLAAAADEVWLVVSGIGVKI
K
Number of residuesNone
Molecular Weight19901.7
Theoretical pI5.26
GO Classification
Functions
  • ATP binding
  • GTP binding
  • adenosylcobinamide kinase activity
  • cobinamide phosphate guanylyltransferase activity
Processes
  • cobalamin biosynthetic process
  • cofactor biosynthetic process
Components
General FunctionGtp binding
Specific FunctionCatalyzes ATP-dependent phosphorylation of adenosylcobinamide and addition of GMP to adenosylcobinamide phosphate.
Transmembrane Regions
GenBank Protein ID
UniProtKB IDQ05599
UniProtKB Entry Name
Cellular LocationNone
Gene sequence
>lcl|BSEQ0011890|Bifunctional adenosylcobalamin biosynthesis protein CobU (cobU)
ATGATGATTCTGGTGACGGGCGGGGCACGTAGTGGTAAAAGCCGTCATGCTGAAGCCTTA
ATTGGCGATGCGCCGCAGGTACTGTATATCGCCACCTCGCAGATTCTTGATGACGAGATG
GCGGCGAGAATTCAGCATCATAAAGATGGCAGGCCGGCACACTGGCGGACCGCAGAATGC
TGGCGGCATCTTGATACGTTGATTACCGCGGATCTTGCCCCTGACGACGCGATTTTGCTG
GAATGTATTACCACCATGGTGACGAATCTGCTGTTTGCGCTGGGAGGCGAGAACGATCCC
GAACAGTGGGATTACGCGGCGATGGAGCGCGCCATTGACGATGAAATTCAGATTTTAATT
GCAGCCTGCCAGCGCTGCCCGGCGAAAGTGGTACTGGTGACAAATGAGGTGGGAATGGGG
ATCGTCCCGGAAAACCGTCTGGCGCGCCATTTTCGTGATATTGCCGGTCGGGTCAACCAA
CGACTGGCGGCAGCGGCGGATGAGGTCTGGCTGGTAGTCTCAGGTATTGGAGTCAAAATT
AAATGA
GenBank Gene ID
GeneCard IDNone
GenAtlas ID
HGNC ID
Chromosome LocationNone
LocusNone
References
  1. 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. [8501034 ]
  2. 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. [11677609 ]
  3. 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. [7559521 ]
  4. 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. [10869342 ]
  5. 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. [9601028 ]
  6. 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. [10529169 ]

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