VERC1_PENPO
ID VERC1_PENPO Reviewed; 805 AA.
AC A0A1V6NWP3;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2017, sequence version 1.
DT 03-AUG-2022, entry version 13.
DE RecName: Full=FAD-dependent monooxygenase verC1 {ECO:0000303|PubMed:34093475};
DE EC=1.-.-.- {ECO:0000305|PubMed:34093475};
DE AltName: Full=Cluster 4 protein C1 {ECO:0000303|PubMed:34093475};
DE AltName: Full=Verrucosidin biosynthesis cluster protein C1 {ECO:0000303|PubMed:34093475};
DE Flags: Precursor;
GN Name=verC1 {ECO:0000303|PubMed:34093475};
GN Synonyms=cl4C1 {ECO:0000303|PubMed:34093475}; ORFNames=PENPOL_c002G07872;
OS Penicillium polonicum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=60169;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 4502;
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
RN [2]
RP FUNCTION.
RX PubMed=34093475; DOI=10.3389/fmicb.2021.660871;
RA Valente S., Piombo E., Schroeckh V., Meloni G.R., Heinekamp T.,
RA Brakhage A.A., Spadaro D.;
RT "CRISPR-Cas9-Based Discovery of the Verrucosidin Biosynthesis Gene Cluster
RT in Penicillium polonicum.";
RL Front. Microbiol. 12:660871-660871(2021).
CC -!- FUNCTION: FAD-dependent monooxygenase; part of the gene cluster that
CC mediates the biosynthesis of the neurotoxin verrucosidin, a methylated
CC alpha-pyrone polyketide that inhibits oxidative phosphorylation in
CC mitochondria and thereby causes neurological diseases
CC (PubMed:34093475). The carbon backbone of verrucosidin is synthesized
CC by the HR-PKS verA, and further modified by the other verrucodidin
CC cluster enzymes (Probable). {ECO:0000269|PubMed:34093475,
CC ECO:0000305|PubMed:34093475}.
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000305|PubMed:34093475}.
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000305|PubMed:34093475}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.
CC {ECO:0000305}.
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DR EMBL; MDYM01000002; OQD69144.1; -; Genomic_DNA.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000191408; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR Pfam; PF01494; FAD_binding_3; 2.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 3: Inferred from homology;
KW FAD; Flavoprotein; Glycoprotein; Membrane; Monooxygenase; Oxidoreductase;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..805
FT /note="FAD-dependent monooxygenase verC1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000455359"
FT TRANSMEM 551..571
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 604..624
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 632..652
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 671..691
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 703..723
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 726..746
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 761..781
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 35..36
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 130
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 306
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 316..320
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT CARBOHYD 132
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 805 AA; 89545 MW; C5FBEF398B41362A CRC64;
MTFRVIIVGG GVAGLTLASA FEKAGIDYIL LECRPAFDVA VGASIALSPN GARILDQLGA
WEKWLKIAQP LVRWGDRNSK GELIMPRSAS TPLAKALTGY DMTFGLRRSL LQTLYDNIED
KSMLLPKKSV INVTCSQEGV AVQCADGCSY EGDILVGADG TYSKVREYMW RLADRDEPGL
MDPDKKAMTA EYQCLFGISK ASGSIAIGDA DFIYDHDRSS FIFSDNCGRI CYFILQKMDR
VYEMVEIPRF SQANAQAYAQ RHADIQIRPD LTFGNLYEHS ESSILVALEE AKFKQWSWGR
IVCVGDSIHK MTPNLGAGAS ASIESAAALL NSIKAMFDHS PEEGPTETQI RECFAQYQKS
REVRATAIVD ASSMTTRLQA LRGWFEFLFV RLGMPIMGSF AADMASEIWV GATMLENLAP
PKASLRGTLP FNPTQGQGQR ESKLKRALLG LPFLALLLVA KTATDAKYAS ALRGYIWESG
GMTSAMGSVP LLQRFYSMKG VGDLWSLRYI NYLPDFYETN YESLSQAVSS SIDVGIVMSI
WSFESIRRAN ALTMAQIPTL FTFYGQMAGL GRVSPLYYIL YYINSPIEVF KGADMRLMHL
NYAIAVLPAI IVSYYIPLSA AFFWPTVSGR KSWLFVWQMH PIWTAITLYL FSRIFPSTVK
EDRVHGLRRD LPVIKFSMTV LVIGAAGFWM WSRWTSPSSV ARVFFPTAVP STQAPFAACV
CAILKWDMLS TFGSTFLWLG YLIWDLKYAG MMQATWVRVA IYGVAAFVAL GPGAAIGLGW
LWRENILAHK RHKDAVTEEN LAQTR
