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
Functions
ATP binding / ATP phosphoribosyltransferase activity / magnesium ion binding
Processes
histidine biosynthetic process
Components
cytosol
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
ResourceLink
UniProtKB IDP60757
UniProtKB Entry NameHIS1_ECOLI
GenBank Protein ID41708
GenBank Gene IDX13462
General References
  1. 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]
  2. 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]
  3. Itoh T, Aiba H, Baba T, Hayashi K, Inada T, Isono K, Kasai H, Kimura S, Kitakawa M, Kitagawa M, Makino K, Miki T, Mizobuchi K, Mori H, Mori T, Motomura K, Nakade S, Nakamura Y, Nashimoto H, Nishio Y, Oshima T, Saito N, Sampei G, Seki Y, Horiuchi T, et al.: A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map. DNA Res. 1996 Dec 31;3(6):379-92. [Article]
  4. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
  5. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
  6. 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]
  7. 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]
  8. 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]
  9. 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]
  10. 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]
  11. 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]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB016611-(5-phospho-D-ribosyl)-ATPexperimentalunknownDetails