Orotate phosphoribosyltransferase
Details
- Name
- Orotate phosphoribosyltransferase
- Synonyms
- 2.4.2.10
- OPRT
- Gene Name
- pyrE
- Organism
- Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
- Amino acid sequence
>lcl|BSEQ0011085|Orotate phosphoribosyltransferase MKPYQRQFIEFALNKQVLKFGEFTLKSGRKSPYFFNAGLFNTGRDLALLGRFYAEALVDS GIEFDLLFGPAYKGIPIATTTAVALAEHHDKDLPYCFNRKEAKDHGEGGSLVGSALQGRV MLVDDVITAGTAIRESMEIIQAHGATLAGVLISLDRQERGRGEISAIQEVERDYGCKVIS IITLKDLIAYLEEKPDMAEHLAAVRAYREEFGV
- Number of residues
- 213
- Molecular Weight
- 23561.74
- Theoretical pI
- 5.68
- GO Classification
- Functionsmagnesium ion binding / orotate phosphoribosyltransferase activityProcesses'de novo' UMP biosynthetic process
- General Function
- Orotate phosphoribosyltransferase activity
- Specific Function
- Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP).
- Pfam Domain Function
- Pribosyltran (PF00156)
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0011086|Orotate phosphoribosyltransferase (pyrE) ATGAAACCGTATCAGCGCCAGTTTATTGAGTTTGCGCTTAACAAGCAGGTACTAAAGTTT GGCGAGTTTACGCTGAAATCCGGGCGCAAAAGCCCCTATTTCTTCAACGCCGGGCTGTTT AATACCGGGCGCGACCTGGCGTTGTTAGGCCGTTTTTATGCCGAAGCGCTGGTGGATTCC GGTATTGAATTTGATCTGCTGTTTGGCCCCGCGTACAAAGGTATTCCGATCGCGACGACG ACGGCGGTTGCGCTGGCGGAACATCACGATAAAGACCTGCCGTACTGCTTTAACCGCAAA GAGGCAAAAGATCATGGTGAAGGCGGGAGCCTGGTGGGCAGCGCGCTACAGGGCCGCGTG ATGCTGGTGGATGACGTGATTACCGCAGGTACGGCGATTCGCGAGTCAATGGAGATTATT CAGGCGCACGGGGCTACGCTGGCTGGCGTACTGATTTCGCTGGATCGTCAGGAACGTGGC CGCGGCGAGATTTCCGCGATTCAGGAAGTGGAGCGCGACTATGGTTGTAAGGTTATCTCC ATCATTACGCTGAAAGACCTGATTGCCTATCTGGAAGAAAAACCTGATATGGCTGAGCAT CTGGCGGCTGTGCGAGCATACCGGGAAGAATTTGGCGTGTAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P08870 UniProtKB Entry Name PYRE_SALTY GenBank Protein ID 47812 GenBank Gene ID Z19547 - General References
- Scapin G, Sacchettini JC, Dessen A, Bhatia M, Grubmeyer C: Primary structure and crystallization of orotate phosphoribosyltransferase from Salmonella typhimurium. J Mol Biol. 1993 Apr 20;230(4):1304-8. [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]
- Neuhard J, Stauning E, Kelln RA: Cloning and characterization of the pyrE gene and of PyrE::Mud1 (Ap lac) fusions from Salmonella typhimurium. Eur J Biochem. 1985 Feb 1;146(3):597-603. [Article]
- Bhatia MB, Vinitsky A, Grubmeyer C: Kinetic mechanism of orotate phosphoribosyltransferase from Salmonella typhimurium. Biochemistry. 1990 Nov 20;29(46):10480-7. [Article]
- Bhatia MB, Grubmeyer C: The role of divalent magnesium in activating the reaction catalyzed by orotate phosphoribosyltransferase. Arch Biochem Biophys. 1993 Jun;303(2):321-5. [Article]
- Grubmeyer C, Segura E, Dorfman R: Active site lysines in orotate phosphoribosyltransferase. J Biol Chem. 1993 Sep 25;268(27):20299-304. [Article]
- Ozturk DH, Dorfman RH, Scapin G, Sacchettini JC, Grubmeyer C: Locations and functional roles of conserved lysine residues in Salmonella typhimurium orotate phosphoribosyltransferase. Biochemistry. 1995 Aug 29;34(34):10755-63. [Article]
- Ozturk DH, Dorfman RH, Scapin G, Sacchettini JC, Grubmeyer C: Structure and function of Salmonella typhimurium orotate phosphoribosyltransferase: protein complementation reveals shared active sites. Biochemistry. 1995 Aug 29;34(34):10764-70. [Article]
- Scapin G, Grubmeyer C, Sacchettini JC: Crystal structure of orotate phosphoribosyltransferase. Biochemistry. 1994 Feb 15;33(6):1287-94. [Article]
- Scapin G, Ozturk DH, Grubmeyer C, Sacchettini JC: The crystal structure of the orotate phosphoribosyltransferase complexed with orotate and alpha-D-5-phosphoribosyl-1-pyrophosphate. Biochemistry. 1995 Aug 29;34(34):10744-54. [Article]