PTMS_PENSI
ID PTMS_PENSI Reviewed; 335 AA.
AC A0A140JWT5;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 11-MAY-2016, sequence version 1.
DT 03-AUG-2022, entry version 11.
DE RecName: Full=NmrA-like family domain-containing oxidoreductase ptmS {ECO:0000303|PubMed:25831977};
DE EC=1.-.-.- {ECO:0000269|PubMed:25831977};
DE AltName: Full=Penitrem biosynthesis cluster 1 protein S {ECO:0000303|PubMed:25831977};
GN Name=ptmS {ECO:0000303|PubMed:25831977};
OS Penicillium simplicissimum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=69488;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION, FUNCTION, AND PATHWAY.
RC STRAIN=AK-40;
RX PubMed=25831977; DOI=10.1002/anie.201501072;
RA Liu C., Tagami K., Minami A., Matsumoto T., Frisvad J.C., Suzuki H.,
RA Ishikawa J., Gomi K., Oikawa H.;
RT "Reconstitution of biosynthetic machinery for the synthesis of the highly
RT elaborated indole diterpene penitrem.";
RL Angew. Chem. Int. Ed. 54:5748-5752(2015).
CC -!- FUNCTION: NmrA-like family domain-containing oxidoreductase; part of
CC the gene cluster that mediates the biosynthesis of the indole
CC diterpenes penitrems (PubMed:25831977). The geranylgeranyl diphosphate
CC (GGPP) synthase ptmG catalyzes the first step in penitrem biosynthesis
CC via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate
CC into geranylgeranyl pyrophosphate (GGPP) (PubMed:25831977).
CC Condensation of indole-3-glycerol phosphate with GGPP by the prenyl
CC transferase ptmC then forms 3-geranylgeranylindole (3-GGI)
CC (PubMed:25831977). Epoxidation by the FAD-dependent monooxygenase ptmM
CC leads to a epoxidized-GGI that is substrate of the terpene cyclase ptmB
CC for cyclization to yield paspaline (PubMed:25831977). Paspaline is
CC subsequently converted to 13-desoxypaxilline by the cytochrome P450
CC monooxygenase ptmP, the latter being then converted to paxilline by the
CC cytochrome P450 monooxygenase ptmQ (PubMed:25831977). Paxilline is
CC converted to beta-paxitriol via C-10 ketoreduction by the short-chain
CC dehydrogenase ptmH which can be monoprenylated at the C-20 by the
CC indole diterpene prenyltransferase ptmD (PubMed:25831977). A two-step
CC elimination (acetylation and elimination) process performed by the O-
CC acetyltransferase ptmV and ptmI leads to the production of the
CC prenylated form of penijanthine (PubMed:25831977). The FAD-linked
CC oxidoreductase ptmO then converts the prenylated form of penijanthine
CC into PC-M5 which is in turn transformed into PC-M4 by the aromatic
CC dimethylallyltransferase ptmE (PubMed:25831977). Five sequential
CC oxidative transformations performed by the cytochrome P450
CC monooxygenases ptmK, ptmU, ptmL, ptmN and ptmJ yield the various
CC penitrem compounds. PtmK, ptmU and ptmM are involved in the formation
CC of the key bicyclic ring of penitrem C via the formation of the
CC intermediates secopenitrem D and penitrem D. PtmL catalyzes the
CC epoxidation of penitrem D and C to yield penitrem B and F,
CC respectively. PtmJ catalyzes the last benzylic hydroxylation to convert
CC penitrem B to prenitrem E and penitrem F to penitrem A
CC (PubMed:25831977). {ECO:0000269|PubMed:25831977}.
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000305|PubMed:25831977}.
CC -!- SIMILARITY: Belongs to the NmrA-type oxidoreductase family.
CC {ECO:0000305}.
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DR EMBL; LC027936; BAU61562.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A140JWT5; -.
DR SMR; A0A140JWT5; -.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR008030; NmrA-like.
DR Pfam; PF05368; NmrA; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 3: Inferred from homology;
KW NADP; Oxidoreductase.
FT CHAIN 1..335
FT /note="NmrA-like family domain-containing oxidoreductase
FT ptmS"
FT /id="PRO_0000446597"
FT REGION 161..206
FT /note="Interaction with ASS1"
FT /evidence="ECO:0000250|UniProtKB:Q9HBL8"
FT BINDING 12..17
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9HBL8"
FT BINDING 39..43
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9HBL8"
FT BINDING 60..61
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9HBL8"
FT BINDING 81..88
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9HBL8"
FT BINDING 139
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9HBL8"
FT BINDING 163..166
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9HBL8"
SQ SEQUENCE 335 AA; 37136 MW; EE45AAD4949FED3B CRC64;
MTQTRKLVTV YGATGNQGRS VVKSLLRAPD SFEVRAITRD PNSVAAQELS ILGANLVQAD
GSQSNQMTEA FQGSWAVFLN INSDDPVFWD PKGPTEFDYG KRIIDSAIVA GVKTLVYSTG
AACTELTKGT VSLRHLDTKN QIEMYARSTG AFENLVPIIP GYFLENFLFK QGAFIMGGFP
WETDAEGYLT WKVPYWGGEE QIPFLSVADD FGDIVHGILI SPSEYHLQVV QAMSEITDYQ
KMTEAFAKVT GKKTRFQPVL PTWKAFDASG NQGFEDVKSM FGFTQETQGH YFGREATDDQ
VSKNLKASAV LDYKESQQSP SLKTVRAWFA REFAA
