PSPC_PENSO
ID PSPC_PENSO Reviewed; 504 AA.
AC P0DUK3;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 02-JUN-2021, sequence version 1.
DT 03-AUG-2022, entry version 5.
DE RecName: Full=Cytochrome P450 monooxygenase pspC {ECO:0000303|PubMed:31086874};
DE EC=1.-.-.- {ECO:0000269|PubMed:31086874};
DE AltName: Full=Soppiline biosynthesis cluster protein C {ECO:0000303|PubMed:31086874};
GN Name=pspC {ECO:0000303|PubMed:31086874};
OS Penicillium soppii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=69789;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PATHWAY.
RX PubMed=31086874; DOI=10.1039/c9ob00807a;
RA Kaneko A., Morishita Y., Tsukada K., Taniguchi T., Asai T.;
RT "Post-genomic approach based discovery of alkylresorcinols from a cricket-
RT associated fungus, Penicillium soppi.";
RL Org. Biomol. Chem. 17:5239-5243(2019).
CC -!- FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that
CC mediates the biosynthesis of the alkylresorcinols called soppilines
CC (PubMed:31086874). The biosynthesis starts with the HR-PKS pspA-
CC catalyzed carbon chain assembly through nine chain elongation cycles,
CC using acetyl CoA and malonyl CoA as a starter and extender units,
CC respectively, to produce the polyketide soppiline A (PubMed:31086874).
CC In the first round, the KR, DH, and CMeT domains work to produce 2-
CC methyl-2-butenyl thioester (PubMed:31086874). In rounds 2 to 5, the KR,
CC DH, and ER domains fully catalyze the reduction of the elongated beta-
CC ketothioester, resulting in the insertion of eight methylene units
CC (PubMed:31086874). The unusual Z,E,Z-triene motif is likely constructed
CC during rounds 6 to 8 (PubMed:31086874). Typically, the DH domain
CC introduces a double bond at an alpha,beta-position of an elongated
CC polyketide chain, with the dehydration of a beta-hydroxy group
CC (PubMed:31086874). The last extension cycle would be carried out with
CC L-oriented beta-ketoreduction by the KR domain to produce beta-hydroxy
CC carboxylic acid soppiline A (PubMed:31086874). The type III PKS pspB
CC intercepts the elongated polyketide chain at round 8 from the HR-PKS
CC pspA, followed by a tri-keto extension and decarboxylative aldol
CC cyclization to produce 1,3,5-trisubstituted alkylresorcinol soppiline B
CC (PubMed:31086874). Subsequently, the cytochrome P450 monooxygenase pspC
CC catalyzes three-step oxidations at the C-4 methyl group to carboxylic
CC acid to yield soppiline C (PubMed:31086874).
CC {ECO:0000269|PubMed:31086874}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3 O2 + 3 reduced [NADPH--hemoprotein reductase] + soppiline B
CC = 4 H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein reductase] +
CC soppiline C; Xref=Rhea:RHEA:66944, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:167549,
CC ChEBI:CHEBI:167551; Evidence={ECO:0000269|PubMed:31086874};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66945;
CC Evidence={ECO:0000269|PubMed:31086874};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:31086874}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR AlphaFoldDB; P0DUK3; -.
DR SMR; P0DUK3; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016712; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen; IEA:InterPro.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002974; Cyt_P450_E_CYP52.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR01239; EP450IICYP52.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW Oxidoreductase; Transmembrane; Transmembrane helix.
FT CHAIN 1..504
FT /note="Cytochrome P450 monooxygenase pspC"
FT /id="PRO_0000452732"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 454
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P04798"
FT CARBOHYD 150
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 385
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 504 AA; 57534 MW; 3EF7EAF634265E59 CRC64;
MAYTLTSIVL GVVVFGLTRI IWGSISWNLR YRRFHSSDGC QQLRSAPSKD PILGLDHFFR
LGKAAHNSRY LEAFQEWFQA VGSTFGVNLM GDYVIFTNEP KNVQAVLVTK FKDFEIGQRR
RDNSAELLGI GVFNADGQTW EHGRALVRPN FTRKQVADLG LFEKHVQRLF EALPKDGTAV
DIQEWTLDTG TDVLFSESSD VLLPSATEVA RKFAWAFNRG IDGIAQRIRL GRFARFYYDP
QYTAACKFVH DYVDEIVAKA VYRAKEWHAE KKDKPVPPDD AEEERYTFLN ALAREGVEPK
QIRDQILNIL VAARDTSACL MSAAVFELAR RPEYQVQLRR EIAEKLSGRQ PTFEDLKDLT
FLNHFVKETL RMYPPVPLNA RVAKNDTVLP RGGGSDGMAP IFVPRGQLVV YQVYSMHRRE
DLWGSDAHIF RPQRWETTRP TFEYLPFNAG PRICPGQQFA LVETSYVLVR LLQEYSNIEA
RGNSAPWREH LTLTCSVGQG VWVS
