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IPR006221 is a Anthranilate synthase/para-aminobenzoate synthase like domain.
<p>This entry represents the anthranilate synthase/para-aminobenzoate synthase domain, which share sequence similarity to the glutamine amidotransferase domain [interpro:IPR017926]. Anthranilate synthase play a role in the tryptophan-biosynthetic pathway, while the para-aminobenzoate synthase is involved in the folate biosynthetic pathway. In at least one case, a single polypeptide from Bacillus subtilis was shown to have both functions.</p> <p>This entry contains proteins similar to para-aminobenzoate (PABA) synthase and ASase. These enzymes catalyze similar reactions and produce similar products, PABA and ortho-aminobenzoate (anthranilate). Each enzyme is composed of non-identical subunits: a glutamine amidotransferase subunit (component II) and a subunit that produces an aminobenzoate products (component I). ASase catalyses the synthesis of anthranilate from chorismate and glutamine and is a tetrameric protein comprising two copies each of components I and II. Component II of ASase belongs to the family of triad GTases which hydrolyse glutamine and transfer nascent ammonia between the active sites. In some bacteria, such as Escherichia coli, component II can be much larger than in other organisms, due to the presence of phosphoribosyl-anthranilate transferase (PRTase) activity. PRTase catalyses the second step in tryptophan biosynthesis and results in the addition of 5-phosphoribosyl-1-pyrophosphate to anthranilate to create N-5'-phosphoribosyl-anthranilate. In E.coli, the first step in the conversion of chorismate to PABA involves two proteins: PabA and PabB which co-operate to transfer the amide nitrogen of glutamine to chorismate forming 4-amino-4 deoxychorismate (ADC). PabA acts as a glutamine amidotransferase, supplying an amino group to PabB, which carries out the amination reaction. A third protein PabC then mediates elimination of pyruvate and aromatisation to give PABA. Several organisms have bipartite proteins containing fused domains homologous to PabA and PabB commonly called PABA synthases. These hybrid PABA synthases may produce ADC and not PABA. [[cite:PUB00003199], [cite:PUB00096162], [cite:PUB00096165], [cite:PUB00096166], [cite:PUB00096163], [cite:PUB00096164]].</p>
This description is obtained from EB-eye REST.
Transcript | Name | Description | Predicted domains | Domain count |
---|---|---|---|---|
– | PREDICTED: anthranilate synthase component II-like [Cicer arietinum] gi|502164732|ref|XP_004513238.1| | 15 | ||
– | PREDICTED: anthranilate synthase component II-like isoform X1 [Cicer arietinum] gi|502168341|ref|XP_004514366.1| | 14 | ||
– | GMP synthase [glutamine]-hydrolyzing]; TAIR: AT1G25220.1 anthranilate synthase beta subunit 1; Swiss-Prot: sp|Q42565|ASB1_ARATH Anthranilate synthase beta subunit 1, chloroplastic; TrEMBL-Plants: tr|B7FJB9|B7FJB9_MEDTR Anthranilate synthase component II; Found in the gene: LotjaGi2g1v0271300 | 15 |
A list of co-occurring predicted domains within the L. japonicus gene space:
Predicted domain | Source | Observations | Saturation (%) |
---|---|---|---|
mobidb-lite | MobiDBLite | 1 | 33.33 |