Accession | TIGR00639 |
Name | PurN |
Function | phosphoribosylglycinamide formyltransferase |
Gene Symbol | purN |
Trusted Cutoff | 150.10 |
Domain Trusted Cutoff | 150.10 |
Noise Cutoff | 127.00 |
Domain Noise Cutoff | 127.00 |
Isology Type | equivalog |
EC Number | 2.1.2.2 |
HMM Length | 192 |
Mainrole Category | Purines, pyrimidines, nucleosides, and nucleotides |
Subrole Category | Purine ribonucleotide biosynthesis |
Gene Ontology Term | GO:0004644: phosphoribosylglycinamide formyltransferase activity molecular_function |
| GO:0009152: purine ribonucleotide biosynthetic process biological_process |
Author | Haft DH |
Entry Date | Oct 25 1999 11:40AM |
Last Modified | Feb 14 2011 3:27PM |
Comment | This HMM describes phosphoribosylglycinamide formyltransferase (GAR transformylase), one of several proteins in formyl_transf (Pfam family PF00551). This enzyme uses formyl tetrahydrofolate as a formyl group donor to produce 5'-phosphoribosyl-N-formylglycinamide. PurT, a different GAR transformylase, uses ATP and formate rather than formyl tetrahydrofolate. Experimental proof includes complementation of E. coli purN mutants by orthologs from vertebrates (where it is a domain of a multifunctional protein), Bacillus subtilis, and Arabidopsis.
No archaeal example was detected.
In phylogenetic analyses, the member from Saccharomyces cerevisiae shows a long branch length but membership in the family, while the formyltetrahydrofolate deformylases form a closely related outgroup. |
References | A2 hmmalign
GA hmmsearch
DR PFAM; PF00551; formyl_transf
DR YPD; ADE8
DR OUTGROUP; EGAD|15350|EC1232
DR OUTGROUP; EGAD|156449|AA1257
RM 87280114
RT Identification and nucleotide sequence of a gene encoding 5'-phosphoribosylglycinamide transformylase in Escherichia coli K12.
RA Smith JM, Daum HA 3d
RL J Biol Chem 1987 Aug 5;262(22):10565-9 |
Genome Property | GenProp0110: purine (inosine-5'-phosphate) biosynthesis from ribose-5-phosphate (HMM) |