FolP (PA4750) is the dihydropteroate synthase (EC 2.5.1.15) of Pseudomonas aeruginosa. It condenses 4-aminobenzoate with 6-hydroxymethyl-7,8-dihydropterin diphosphate to form 7,8-dihydropteroate, the precursor of dihydrofolate, in the de novo tetrahydrofolate biosynthesis pathway. It belongs to the DHPS family (pterin-binding domain, TIGR01496) and is a soluble cytoplasmic enzyme; in bacteria this enzyme is the target of the sulfonamide antibiotics. Its activity has not been studied on the P. aeruginosa protein itself; the assignment rests on strong family conservation.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0004156 dihydropteroate synthase activity | IBA GO_REF:0000033 | ACCEPT | Summary: IBA from PTN000468650 (DHPS clade, six seeds: E. coli FolP P0AC13, S. pneumoniae SulA P59655, M. tuberculosis FolP1 P9WND1, yeast FOL1, Arabidopsis AT1G69190 and PA4750 itself). Reason: Core activity. The IBD stands on the five other seeds, which include classic biochemically characterized DHPS enzymes, so the wrong-organism PseudoCAP seed does not weaken it. Supporting Evidence: file:PSEAE/folP/folP-uniprot.txt Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. file:PSEAE/folP/folP-uniprot.txt TIGR01496; DHPS file:PSEAE/folP/folP-uniprot.txt PS00792; DHPS_1 |
| GO:0004156 dihydropteroate synthase activity | IDA PMID:1657875 Purification and partial characterization of 7,8-dihydro-6-h... | ACCEPT | Summary: PseudoCAP IDA citing Talarico et al. 1991, which purified HPPK and DHPS from E. coli MC4100. No P. aeruginosa protein was assayed. Reason: The claim is true for PA4750 by family conservation and the IBA, so it is kept; the cited paper is about the E. coli enzyme and a source defect is recorded (seed verdict WRONG). Supporting Evidence: file:PSEAE/folP/folP-uniprot.txt Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. file:PSEAE/folP/folP-uniprot.txt TIGR01496; DHPS |
| GO:0004156 dihydropteroate synthase activity | IEA GO_REF:0000120 | ACCEPT | Summary: InterPro/EC/RHEA mapping; same claim. Reason: DHPS family signatures are present. Supporting Evidence: file:PSEAE/folP/folP-uniprot.txt TIGR01496; DHPS file:PSEAE/folP/folP-uniprot.txt PS00792; DHPS_1 |
| GO:0005829 cytosol | IBA GO_REF:0000033 | ACCEPT | Summary: IBA cytosol from PTN000468680, seeded by E. coli FolP. Reason: Soluble enzyme with no signal peptide or transmembrane segment. Supporting Evidence: file:PSEAE/folP/folP-uniprot.txt Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. |
| GO:0009396 folic acid-containing compound biosynthetic process | IEA GO_REF:0000002 | TOO GENERAL | Summary: InterPro2GO folic acid-containing compound biosynthetic process. Reason: True, but entailed by the accepted tetrahydrofolate biosynthetic process rows. Supporting Evidence: file:PSEAE/folP/folP-uniprot.txt Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. |
| GO:0042558 pteridine-containing compound metabolic process | IEA GO_REF:0000002 | TOO GENERAL | Summary: InterPro2GO pteridine-containing compound metabolic process (pterin-binding domain). Reason: True, but entailed by the accepted tetrahydrofolate biosynthetic process rows. Supporting Evidence: file:PSEAE/folP/folP-uniprot.txt Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. |
| GO:0046654 tetrahydrofolate biosynthetic process | IBA GO_REF:0000033 | ACCEPT | Summary: IBA tetrahydrofolate biosynthetic process from PTN000468650 (yeast, M. tuberculosis, Arabidopsis seeds). Reason: Dihydropteroate is the direct precursor of dihydrofolate. Supporting Evidence: file:PSEAE/folP/folP-uniprot.txt Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. |
| GO:0046654 tetrahydrofolate biosynthetic process | IEA GO_REF:0000041 | ACCEPT | Summary: UniPathway mapping to tetrahydrofolate biosynthesis. Reason: Same claim as the IBA row. Supporting Evidence: file:PSEAE/folP/folP-uniprot.txt Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. |
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Download this section (compressed HTML)Experiment: Purify recombinant PA4750 and measure dihydropteroate synthase activity and sulfonamide inhibition, to give the P. aeruginosa enzyme its own experimental evidence.
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