ATP phosphoribosyltransferase
Details
- Name
- ATP phosphoribosyltransferase
- Synonyms
- 2.4.2.17
- ATP-PRT
- Gene Name
- hisG
- Organism
- Escherichia coli (strain K12)
- Amino acid sequence
>lcl|BSEQ0010854|ATP phosphoribosyltransferase MTDNTRLRIAMQKSGRLSDDSRELLARCGIKINLHTQRLIAMAENMPIDILRVRDDDIPG LVMDGVVDLGIIGENVLEEELLNRRAQGEDPRYFTLRRLDFGGCRLSLATPVDEAWDGPL SLNGKRIATSYPHLLKRYLDQKGISFKSCLLNGSVEVAPRAGLADAICDLVSTGATLEAN GLREVEVIYRSKACLIQRDGEMEESKQQLIDKLLTRIQGVIQARESKYIMMHAPTERLDE VIALLPGAERPTILPLAGDQQRVAMHMVSSETLFWETMEKLKALGASSILVLPIEKMME
- Number of residues
- 299
- Molecular Weight
- 33366.32
- Theoretical pI
- 5.29
- GO Classification
- FunctionsATP binding / ATP phosphoribosyltransferase activity / magnesium ion bindingProcesseshistidine biosynthetic processComponentscytosol
- General Function
- Magnesium ion binding
- Specific Function
- Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity.
- Pfam Domain Function
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasm
- Gene sequence
>lcl|BSEQ0010855|ATP phosphoribosyltransferase (hisG) ATGACAGACAACACTCGTTTACGCATAGCTATGCAGAAATCCGGCCGTTTAAGTGATGAC TCACGCGAATTGCTGGCGCGCTGTGGCATTAAAATTAATCTTCACACCCAGCGCCTGATC GCGATGGCAGAAAACATGCCGATTGATATTCTGCGCGTGCGTGACGACGACATTCCCGGT CTGGTAATGGATGGCGTGGTAGACCTTGGGATTATCGGCGAAAACGTGCTGGAAGAAGAG CTGCTTAACCGCCGCGCCCAGGGTGAAGATCCACGCTACTTTACCCTGCGTCGTCTGGAT TTCGGCGGCTGTCGTCTTTCGCTGGCAACGCCGGTTGATGAAGCCTGGGACGGTCCGCTC TCCTTAAACGGTAAACGTATCGCCACCTCTTATCCTCACCTGCTCAAGCGTTATCTCGAC CAGAAAGGCATCTCTTTTAAATCCTGCTTACTGAACGGTTCTGTTGAAGTCGCCCCGCGT GCCGGACTGGCGGATGCGATTTGCGATCTGGTTTCCACCGGTGCCACGCTGGAAGCTAAC GGCCTGCGCGAAGTCGAAGTTATCTATCGCTCGAAAGCCTGCCTGATTCAACGCGATGGC GAAATGGAAGAATCCAAACAGCAACTGATCGACAAACTGCTGACCCGTATTCAGGGTGTG ATCCAGGCGCGCGAATCAAAATACATCATGATGCACGCACCGACCGAACGTCTGGATGAA GTCATCGCCCTGCTGCCAGGTGCCGAACGCCCAACTATTCTGCCGCTGGCGGGTGACCAA CAGCGCGTAGCGATGCACATGGTCAGCAGCGAAACCCTGTTCTGGGAAACCATGGAAAAA CTGAAAGCGCTGGGTGCCAGTTCAATTCTGGTCCTGCCGATTGAGAAGATGATGGAGTGA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P60757 UniProtKB Entry Name HIS1_ECOLI GenBank Protein ID 41708 GenBank Gene ID X13462 - General References
- Carlomagno MS, Chiariotti L, Alifano P, Nappo AG, Bruni CB: Structure and function of the Salmonella typhimurium and Escherichia coli K-12 histidine operons. J Mol Biol. 1988 Oct 5;203(3):585-606. [Article]
- Jovanovic G, Kostic T, Jankovic M, Savic DJ: Nucleotide sequence of the Escherichia coli K12 histidine operon revisited. J Mol Biol. 1994 Jun 10;239(3):433-5. [Article]
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- Verde P, Frunzio R, di Nocera PP, Blasi F, Bruni CB: Identification, nucleotide sequence and expression of the regulatory region of the histidine operon of Escherichia coli K-12. Nucleic Acids Res. 1981 May 11;9(9):2075-86. [Article]
- Klungsoyr L, Atkinson DE: Regulatory properties of phosphoribosyladenosine triphosphate synthetase. Synergism between adenosine monophosphate, phosphoribosyladenosine triphosphate, and histidine. Biochemistry. 1970 Apr 28;9(9):2021-7. [Article]
- Klungsoyr L, Kryvi H: Sedimentation behaviour of phosphoribosyladenosine triphosphate synthetase. Effects of substrates and modifiers. Biochim Biophys Acta. 1971 Feb 10;227(2):327-36. [Article]
- Tebar AR, Fernandez VM, Martin Del Rio R, Ballesteros AO: Studies on the quaternary structure of the first enzyme for histidine biosynthesis. Experientia. 1973 Dec;29(12):1477-9. [Article]
- Lohkamp B, Coggins JR, Lapthorn AJ: Purification, crystallization and preliminary X-ray crystallographic analysis of ATP-phosphoribosyltransferase from Escherichia coli. Acta Crystallogr D Biol Crystallogr. 2000 Nov;56(Pt 11):1488-91. [Article]
- Lohkamp B, McDermott G, Campbell SA, Coggins JR, Lapthorn AJ: The structure of Escherichia coli ATP-phosphoribosyltransferase: identification of substrate binding sites and mode of AMP inhibition. J Mol Biol. 2004 Feb 6;336(1):131-44. [Article]