Protein name |
Phosphoribosylformylglycinamidine synthase subunit PurS (FGAM synthase) (EC 6.3.5.3) (Formylglycinamide ribonucleotide amidotransferase subunit III) (FGAR amidotransferase III) (FGAR-AT III) (Phosphoribosylformylglycinamidine synthase subunit III) |
NCBI Accession ID |
AE000512.1 |
Organism |
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099) |
Left |
1269604 |
Right |
1269852 |
Strand |
+ |
Nucleotide Sequence |
TTGCCGCTCTTTAAATTCGCAATAGACGTTCAGTACAGGAGCAACGTGAGGGATCCGCGCGGAGAAACGATCGAACGTGTTCTGAGGGAAGAAAAAGGTCTTCCCGTGAAAAAGTTGAGACTTGGGAAGTCCATCCACCTCGAAGTAGAAGCAGAAAACAAAGAAAAAGCGTACGAAATCGTAAAGAAAGCCTGCGAAGAACTCCTGGTGAACCCGGTTGTTGAGGAATATGAGGTGAGGGAGCTGTGA |
Sequence |
MPLFKFAIDVQYRSNVRDPRGETIERVLREEKGLPVKKLRLGKSIHLEVEAENKEKAYEIVKKACEELLVNPVVEEYEVREL |
Source of smORF |
Swiss-Prot |
Function |
Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to PurL. {ECO:0000255|HAMAP-Rule:MF_01926, ECO:0000269|Pubmed:18597481}. |
Pubmed ID |
10360571
23637642
16865708
18597481
|
Domain |
CDD:412569 |
Functional Category |
Others |
Uniprot ID |
Q9X0X1
|
ORF Length (Amino Acid) |
82 |