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The PKS-NRPS hybrid synthetase psoA is responsible for the biosynthesis of azaspirene, one of the first intermediates having the 1-oxa-7-azaspiro[4,4]-non-2-ene-4,6-dione core of pseurotin, via condensation of one acetyl-CoA, 4 malonyl-CoA, and a L-phenylalanine molecule (PubMed:24082142, PubMed:24939566). The dual-functional monooxygenase/methyltransferase psoF seems to be involved in the addition of the C3 methyl group onto the pseurotin scaffold (PubMed:24939566). Azaspirene is then converted to synerazol through 4 steps including oxidation of C17 by the cytochrome P450 monooxygenase psoD, O-methylation of the hydroxy group of C8 by the methyltransferase psoC, and the trans-to-cis isomerization of the C13 olefin by the glutathione S-transferase psoE (PubMed:24939566). The fourth step of synerazol production is performed by the dual-functional monooxygenase/methyltransferase psoF which seems to catalyze the epoxidation of the intermediate deepoxy-synerazol (PubMed:24939566). Synerazol can be attacked by a water molecule nonenzymatically at two different positions to yield two diol products, pseurotin A and pseurotin D (PubMed:24939566)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24082142"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24939566"}],"value":"Secondary metabolite biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16207816"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21388144"}],"value":"Expression is under the control of StuA, which is responsible for transcriptional activation during acquisition of developmental competence (PubMed:16207816). Expression is also induced under hypoxic conditions (PubMed:21388144)"}],"commentType":"INDUCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17464044"}],"value":"NRP synthetases are composed of discrete domains (adenylation (A), thiolation (T) or peptidyl carrier protein (PCP) and condensation (C) domains) which when grouped together are referred to as a single module (PubMed:17464044). Each module is responsible for the recognition (via the A domain) and incorporation of a single amino acid into the growing peptide product (PubMed:17464044). Thus, an NRP synthetase is generally composed of one or more modules and can terminate in a thioesterase domain (TE) that releases the newly synthesized peptide from the enzyme. Occasionally, epimerase (E) domains (responsible for l- to d- amino acid conversion) are present within the NRP synthetase (PubMed:17464044). NRPS14 also contains a ketoacyl synthase domain (KS), an acyl transferase domain (AT), a dehydratase domain (DH), and 2 ketoreductase domains (KR) (PubMed:17464044). NRPS14 has the following architecture: KS-AT-DH-KR-T-C-A-T-KR (PubMed:17464044)"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17722120"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24082142"}],"value":"Abolishes the production of pseurotin (PubMed:17722120, PubMed:24082142)"}],"commentType":"DISRUPTION PHENOTYPE"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"In the C-terminal section; belongs to the NRP synthetase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":4007,"modifier":"EXACT"}},"description":"PKS-NRPS hybrid synthetase psoA","featureId":"PRO_0000416555"},{"type":"Domain","location":{"start":{"value":8,"modifier":"EXACT"},"end":{"value":444,"modifier":"EXACT"}},"description":"Ketosynthase family 3 (KS3)","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU01348"}]},{"type":"Domain","location":{"start":{"value":969,"modifier":"EXACT"},"end":{"value":1276,"modifier":"EXACT"}},"description":"PKS/mFAS DH","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU01363"}]},{"type":"Domain","location":{"start":{"value":2418,"modifier":"EXACT"},"end":{"value":2495,"modifier":"EXACT"}},"description":"Carrier 1","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00258"}]},{"type":"Domain","location":{"start":{"value":3576,"modifier":"EXACT"},"end":{"value":3652,"modifier":"EXACT"}},"description":"Carrier 2","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00258"}]},{"type":"Region","location":{"start":{"value":575,"modifier":"EXACT"},"end":{"value":897,"modifier":"EXACT"}},"description":"Malonyl-CoA:ACP transacylase (MAT) domain","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Region","location":{"start":{"value":969,"modifier":"EXACT"},"end":{"value":1147,"modifier":"EXACT"}},"description":"Dehydratase (DH) domain","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Region","location":{"start":{"value":969,"modifier":"EXACT"},"end":{"value":1105,"modifier":"EXACT"}},"description":"N-terminal hotdog fold","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU01363"}]},{"type":"Region","location":{"start":{"value":1120,"modifier":"EXACT"},"end":{"value":1276,"modifier":"EXACT"}},"description":"C-terminal hotdog fold","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU01363"}]},{"type":"Region","location":{"start":{"value":2131,"modifier":"EXACT"},"end":{"value":2305,"modifier":"EXACT"}},"description":"Ketoreductase (KR) domain","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Region","location":{"start":{"value":2513,"modifier":"EXACT"},"end":{"value":2550,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":2589,"modifier":"EXACT"},"end":{"value":2885,"modifier":"EXACT"}},"description":"Condensation (C) domain","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Region","location":{"start":{"value":3076,"modifier":"EXACT"},"end":{"value":3478,"modifier":"EXACT"}},"description":"Adenylation (A) domain","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Region","location":{"start":{"value":3696,"modifier":"EXACT"},"end":{"value":3920,"modifier":"EXACT"}},"description":"Reductase (R) domain","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Compositional bias","location":{"start":{"value":2518,"modifier":"EXACT"},"end":{"value":2531,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":182,"modifier":"EXACT"},"end":{"value":182,"modifier":"EXACT"}},"description":"For beta-ketoacyl synthase activity","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU01348"}]},{"type":"Active site","location":{"start":{"value":321,"modifier":"EXACT"},"end":{"value":321,"modifier":"EXACT"}},"description":"For beta-ketoacyl synthase activity","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU01348"}]},{"type":"Active site","location":{"start":{"value":364,"modifier":"EXACT"},"end":{"value":364,"modifier":"EXACT"}},"description":"For beta-ketoacyl synthase activity","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU01348"}]},{"type":"Active site","location":{"start":{"value":1001,"modifier":"EXACT"},"end":{"value":1001,"modifier":"EXACT"}},"description":"Proton acceptor; 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