Phosphoribosylglycinamide formyltransferase

Details

Name
Phosphoribosylglycinamide formyltransferase
Synonyms
  • 2.1.2.2
  • 5'-phosphoribosylglycinamide transformylase
  • GAR transformylase
  • GART
Gene Name
purN
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0020533|Phosphoribosylglycinamide formyltransferase
MNIVVLISGNGSNLQAIIDACKTNKIKGTVRAVFSNKADAFGLERARQAGIATHTLIASA
FDSREAYDRELIHEIDMYAPDVVVLAGFMRILSPAFVSHYAGRLLNIHPSLLPKYPGLHT
HRQALENGDEEHGTSVHFVTDELDGGPVILQAKVPVFAGDSEDDITARVQTQEHAIYPLV
ISWFADGRLKMHENAAWLDGQRLPPQGYAADE
Number of residues
212
Molecular Weight
23238.065
Theoretical pI
5.74
GO Classification
Functions
methyltransferase activity / phosphoribosylglycinamide formyltransferase activity
Processes
'de novo' IMP biosynthetic process / cellular response to DNA damage stimulus
Components
cytosol
General Function
Phosphoribosylglycinamide formyltransferase activity
Specific Function
Catalyzes the transfer of a formyl group from 10-formyltetrahydrofolate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR) and tetrahydrofolate.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0020534|Phosphoribosylglycinamide formyltransferase (purN)
ATGAATATTGTGGTGCTTATTTCCGGCAACGGAAGTAATTTACAGGCAATTATTGACGCC
TGTAAAACCAACAAAATTAAAGGCACCGTACGGGCAGTTTTCAGCAATAAGGCCGACGCG
TTCGGCCTTGAACGCGCCCGCCAGGCGGGTATTGCAACGCATACGCTCATCGCCAGCGCG
TTTGACAGTCGTGAAGCCTATGACCGGGAGTTGATTCATGAAATCGACATGTACGCACCC
GATGTGGTCGTGCTGGCTGGTTTTATGCGCATTCTCAGCCCGGCGTTTGTCTCCCACTAT
GCCGGGCGTTTGCTGAACATTCACCCTTCTCTGCTGCCGAAATATCCCGGATTACACACC
CATCGTCAGGCGCTGGAAAATGGCGATGAAGAGCACGGTACATCGGTGCATTTCGTCACC
GATGAACTGGACGGTGGCCCGGTTATTTTACAGGCGAAAGTCCCGGTATTTGCTGGTGAT
TCGGAAGATGACATCACCGCCCGCGTGCAAACCCAGGAACACGCCATTTATCCACTGGTG
ATTAGCTGGTTTGCCGATGGTCGTCTGAAAATGCACGAAAACGCCGCGTGGCTGGATGGT
CAACGTCTGCCGCCGCAGGGCTACGCTGCCGACGAGTAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP08179
UniProtKB Entry NamePUR3_ECOLI
GenBank Protein ID147425
GenBank Gene IDM13747
General References
  1. Smith JM, Daum HA 3rd: Identification and nucleotide sequence of a gene encoding 5'-phosphoribosylglycinamide transformylase in Escherichia coli K12. J Biol Chem. 1987 Aug 5;262(22):10565-9. [PubMed:3301838]
  2. Yamamoto Y, Aiba H, Baba T, Hayashi K, Inada T, Isono K, Itoh T, Kimura S, Kitagawa M, Makino K, Miki T, Mitsuhashi N, Mizobuchi K, Mori H, Nakade S, Nakamura Y, Nashimoto H, Oshima T, Oyama S, Saito N, Sampei G, Satoh Y, Sivasundaram S, Tagami H, Horiuchi T, et al.: Construction of a contiguous 874-kb sequence of the Escherichia coli -K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features. DNA Res. 1997 Apr 28;4(2):91-113. [PubMed:9205837]
  3. 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. [PubMed:9278503]
  4. 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. [PubMed:16738553]
  5. Pupo GM, Lan R, Reeves PR: Multiple independent origins of Shigella clones of Escherichia coli and convergent evolution of many of their characteristics. Proc Natl Acad Sci U S A. 2000 Sep 12;97(19):10567-72. [PubMed:10954745]
  6. Inglese J, Johnson DL, Shiau A, Smith JM, Benkovic SJ: Subcloning, characterization, and affinity labeling of Escherichia coli glycinamide ribonucleotide transformylase. Biochemistry. 1990 Feb 13;29(6):1436-43. [PubMed:2185839]
  7. Dev IK, Harvey RJ: N10-Formyltetrahydrofolate is the formyl donor for glycinamide ribotide transformylase in Escherichia coli. J Biol Chem. 1978 Jun 25;253(12):4242-4. [PubMed:350869]
  8. Inglese J, Smith JM, Benkovic SJ: Active-site mapping and site-specific mutagenesis of glycinamide ribonucleotide transformylase from Escherichia coli. Biochemistry. 1990 Jul 17;29(28):6678-87. [PubMed:2204419]
  9. Warren MS, Marolewski AE, Benkovic SJ: A rapid screen of active site mutants in glycinamide ribonucleotide transformylase. Biochemistry. 1996 Jul 9;35(27):8855-62. [PubMed:8688421]
  10. Shim JH, Benkovic SJ: Catalytic mechanism of Escherichia coli glycinamide ribonucleotide transformylase probed by site-directed mutagenesis and pH-dependent studies. Biochemistry. 1999 Aug 3;38(31):10024-31. [PubMed:10433709]
  11. Chen P, Schulze-Gahmen U, Stura EA, Inglese J, Johnson DL, Marolewski A, Benkovic SJ, Wilson IA: Crystal structure of glycinamide ribonucleotide transformylase from Escherichia coli at 3.0 A resolution. A target enzyme for chemotherapy. J Mol Biol. 1992 Sep 5;227(1):283-92. [PubMed:1522592]
  12. Almassy RJ, Janson CA, Kan CC, Hostomska Z: Structures of apo and complexed Escherichia coli glycinamide ribonucleotide transformylase. Proc Natl Acad Sci U S A. 1992 Jul 1;89(13):6114-8. [PubMed:1631098]
  13. Su Y, Yamashita MM, Greasley SE, Mullen CA, Shim JH, Jennings PA, Benkovic SJ, Wilson IA: A pH-dependent stabilization of an active site loop observed from low and high pH crystal structures of mutant monomeric glycinamide ribonucleotide transformylase at 1.8 to 1.9 A. J Mol Biol. 1998 Aug 21;281(3):485-99. [PubMed:9698564]
  14. Greasley SE, Yamashita MM, Cai H, Benkovic SJ, Boger DL, Wilson IA: New insights into inhibitor design from the crystal structure and NMR studies of Escherichia coli GAR transformylase in complex with beta-GAR and 10-formyl-5,8,10-trideazafolic acid. Biochemistry. 1999 Dec 21;38(51):16783-93. [PubMed:10606510]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB02236Glycinamide RibonucleotideexperimentalunknownDetails
DB0254010-formyl-5,8,10-trideazafolic acidexperimentalunknownDetails
DB02794(2S)-2-({4-[(2S)-1-(2-Amino-4-oxo-1,4-dihydro-6-quinazolinyl)-3-{[2-({(2R,3R,4S,5R)-3,4-dihydroxy-5-[(phosphonooxy)methyl]tetrahydro-2-furanyl}amino)-2-oxoethyl]amino}-2-hydroxy-2-propanyl]benzoyl}ami no)pentanedioic acidexperimentalunknownDetails
DB04264(10R)-10-formyl-5,8,10-trideazafolic acidexperimentalunknownDetails