ATP phosphoribosyltransferase (P60757)

Identification
Name:ATP phosphoribosyltransferase
Synonyms:
  • ATP-PRT
  • ATP-PRTase
Gene Name:hisG
Enzyme Class:
Biological Properties
General Function:Involved in ATP phosphoribosyltransferase activity
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
Cellular Location:Cytoplasm
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Phosphoribosyl pyrophosphate ↔ 1.0Pyrophosphate + 1.0Phosphoribosyl-ATP
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Phosphoribosyl-ATP + 1.0Pyrophosphate ↔ 1.0Adenosine triphosphate + 1.0Phosphoribosyl pyrophosphate
ReactionCard
SMPDB Reactions:
1.0Thumb+1.0Thumb → 1.0Pyrophosphate+1.0Phosphoribosyl-ATP+1.0Thumb
1.0Phosphoribosyl pyrophosphate + 1.0Hydrogen ion → 1.0Pyrophosphate + 1.0Phosphoribosyl-ATP + 1.0Phosphoribosyl-ATP
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Phosphoribosyl pyrophosphate ↔ 1.0Pyrophosphate + 1.0Phosphoribosyl-ATP
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Phosphoribosyl-ATP + 1.0Pyrophosphate → 1.0Adenosine triphosphate + 1.0Phosphoribosyl pyrophosphate
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB00280Phosphoribosyl pyrophosphateMetaboCard
ECMDB04138Phosphoribosyl-ATPMetaboCard
ECMDB04142PyrophosphateMetaboCard
GO Classification:
Component
cell part
cytoplasm
intracellular part
Function
ATP phosphoribosyltransferase activity
binding
catalytic activity
cation binding
ion binding
magnesium ion binding
metal ion binding
transferase activity
transferase activity, transferring glycosyl groups
transferase activity, transferring pentosyl groups
Process
cellular amino acid and derivative metabolic process
cellular amino acid metabolic process
cellular metabolic process
histidine biosynthetic process
histidine family amino acid metabolic process
histidine metabolic process
metabolic process
Gene Properties
Blattner:b2019
Gene OrientationClockwise
Centisome Percentage:45.01
Left Sequence End2088216
Right Sequence End2089115
Gene Sequence:
>900 bp
ATGAAGCGTGAAGAAATCGCTGATCTGATGGCGTTTGTCGTCGTTGCAGAGGAGCGTAGC
TTCACTCGTGCAGCAGCCCGCCTGAGCATGGCGCAGTCAGCTTTAAGCCAGATAGTGCGT
CGTATAGAAGAACGATTGGGATTGCGGCTTCTGACGCGAACCACGCGCAGCGTTGTTCCA
ACTGAAGCGGGCGAGCATCTTTTGTCTGTTCTTGGCCCTATGTTGCATGACATAGATTCA
GCCATGGCATCCCTGAGCGATCTGCAGAACCGCCCATCCGGGACAATACGTATTACTACT
GTAGAACATGCAGCAAAAACGATATTGTTACCAGCAATGCGCACATTCCTGAAATCGCAT
CCTGAAATTGATATTCAGCTCACCATTGATTATGGTTTGACCGATGTCGTTTCTGAACGT
TTTGATGCAGGCGTCCGTCTGGGTGGGGAGATGGATAAAGATATGATCGCCATTCGAATC
GGGCCAGATATACCAATGGCTATTGTTGGCTCACCGGATTATTTTTCTCGCCGAAGTGTT
CCAACGTCAGTGTCACAATTAATAGATCATCAGGCAATTAATTTGTATCTTCCCACATCG
GGTACAGCAAATCGCTGGAGATTAATACGCGGTGGACGTGAAGTTCGTGTTCGCATGGAA
GGTCAGCTTTTACTGAATACGATAGACCTGATCATTGATGCTGCAATTGATGGGCATGGA
TTGGCGTATCTACCTTATGATCAGGTTGAGCGGGCTATTAAAGAAAAAAAACTGATACGT
GTTTTGGATAAATTCACACCAGATTTACCCGGTTATCACCTGTACTATCCACACCGTCGA
CATGCTGGCTCGGCATTCTCATTATTTATAGATAGGCTGAAGTATAAAGGTGCTGTTTAG
Protein Properties
Pfam Domain Function:
Protein Residues:299
Protein Molecular Weight:33366
Protein Theoretical pI:5
PDB File:1Q1K
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>ATP phosphoribosyltransferase
MTDNTRLRIAMQKSGRLSDDSRELLARCGIKINLHTQRLIAMAENMPIDILRVRDDDIPG
LVMDGVVDLGIIGENVLEEELLNRRAQGEDPRYFTLRRLDFGGCRLSLATPVDEAWDGPL
SLNGKRIATSYPHLLKRYLDQKGISFKSCLLNGSVEVAPRAGLADAICDLVSTGATLEAN
GLREVEVIYRSKACLIQRDGEMEESKQQLIDKLLTRIQGVIQARESKYIMMHAPTERLDE
VIALLPGAERPTILPLAGDQQRVAMHMVSSETLFWETMEKLKALGASSILVLPIEKMME
References
External Links:
ResourceLink
Uniprot ID:P60757
Uniprot Name:HIS1_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:1742185
PDB ID:1Q1K
Ecogene ID:EG10449
Ecocyc:EG10449
ColiBase:b2019
Kegg Gene:b2019
EchoBASE ID:EB0444
CCDB:HIS1_ECOLI
BacMap:16129960
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Carlomagno, M. S., Chiariotti, L., Alifano, P., Nappo, A. G., Bruni, C. B. (1988). "Structure and function of the Salmonella typhimurium and Escherichia coli K-12 histidine operons." J Mol Biol 203:585-606. Pubmed: 3062174
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • 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, a. l. .. (1996). "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 3:379-392. Pubmed: 9097040
  • Jovanovic, G., Kostic, T., Jankovic, M., Savic, D. J. (1994). "Nucleotide sequence of the Escherichia coli K12 histidine operon revisited." J Mol Biol 239:433-435. Pubmed: 8201624
  • Klungsoyr, L., Kryvi, H. (1971). "Sedimentation behaviour of phosphoribosyladenosine triphosphate synthetase. Effects of substrates and modifiers." Biochim Biophys Acta 227:327-336. Pubmed: 4927808
  • Lohkamp, B., Coggins, J. R., Lapthorn, A. J. (2000). "Purification, crystallization and preliminary X-ray crystallographic analysis of ATP-phosphoribosyltransferase from Escherichia coli." Acta Crystallogr D Biol Crystallogr 56:1488-1491. Pubmed: 11185885
  • Lohkamp, B., McDermott, G., Campbell, S. A., Coggins, J. R., Lapthorn, A. J. (2004). "The structure of Escherichia coli ATP-phosphoribosyltransferase: identification of substrate binding sites and mode of AMP inhibition." J Mol Biol 336:131-144. Pubmed: 14741209
  • Tebar, A. R., Fernandez, V. M., Martin Del Rio, R., Ballesteros, A. O. (1973). "Studies on the quaternary structure of the first enzyme for histidine biosynthesis." Experientia 29:1477-1479. Pubmed: 4358959
  • Verde, P., Frunzio, R., di Nocera, P. P., Blasi, F., Bruni, C. B. (1981). "Identification, nucleotide sequence and expression of the regulatory region of the histidine operon of Escherichia coli K-12." Nucleic Acids Res 9:2075-2086. Pubmed: 6170941