| Accession | TIGR00655 |
| Name | PurU |
| Function | formyltetrahydrofolate deformylase |
| Gene Symbol | purU |
| Trusted Cutoff | 285.95 |
| Domain Trusted Cutoff | 285.95 |
| Noise Cutoff | 170.60 |
| Domain Noise Cutoff | 170.60 |
| Isology Type | equivalog |
| EC Number | 3.5.1.10 |
| HMM Length | 280 |
| Mainrole Category | Purines, pyrimidines, nucleosides, and nucleotides |
| Subrole Category | Purine ribonucleotide biosynthesis |
| Gene Ontology Term | GO:0008864: formyltetrahydrofolate deformylase activity molecular_function |
| | GO:0009152: purine ribonucleotide biosynthetic process biological_process |
| Author | Haft DH |
| Entry Date | Dec 1 1999 10:45AM |
| Last Modified | Feb 14 2011 3:27PM |
| Comment | This HMM describes formyltetrahydrofolate deformylases. The enzyme is a homohexamer. Sequences from a related enzyme formyl tetrahydrofolate-specific enzyme, phosphoribosylglycinamide formyltransferase, serve as an outgroup for phylogenetic analysis. Putative members of this family, scoring below the trusted cutoff, include a sequence from Rhodobacter capsulatus that lacks an otherwise conserved C-terminal region.
|
| References | A2 hmmalign
AL Clustalw
DR PFAM; PF00551; formyl_transf
RN [1]
RM 95173107
RT Formyltetrahydrofolate hydrolase, a regulatory enzyme that functions to balance pools of tetrahydrofolate and one-carbon tetrahydrofolate adducts in Escherichia coli.
RA Nagy PL, Marolewski A, Benkovic SJ, Zalkin H
RL J Bacteriol 1995 Mar;177(5):1292-8
RN [2]
RM 94042872
RT purU, a source of formate for purT-dependent phosphoribosyl-N-formylglycinamide synthesis.
RA Nagy PL, McCorkle GM, Zalkin H
RL J Bacteriol 1993 Nov;175(21):7066-73
DR SWISSPROT; P37051; PURU_ECOLI;
DR OUTGROUP; EGAD|18449|EC2500;
DR EXPERIMENTAL; EGAD|15350|EC1232;
|
