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NVFB_ASPN1
ID   NVFB_ASPN1              Reviewed;         316 AA.
AC   A0A2I1BT09;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   28-FEB-2018, sequence version 1.
DT   03-AUG-2022, entry version 15.
DE   RecName: Full=DMOA farnesyltransferase nvfB {ECO:0000303|PubMed:29968715};
DE            EC=2.5.1.- {ECO:0000269|PubMed:29968715};
DE   AltName: Full=Novofumigatonin biosynthesis cluster protein B {ECO:0000303|PubMed:29968715};
GN   Name=nvfB {ECO:0000303|PubMed:29968715}; ORFNames=P174DRAFT_425997;
OS   Aspergillus novofumigatus (strain IBT 16806).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1392255;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 16806;
RX   PubMed=29317534; DOI=10.1073/pnas.1715954115;
RA   Kjaerboelling I., Vesth T.C., Frisvad J.C., Nybo J.L., Theobald S., Kuo A.,
RA   Bowyer P., Matsuda Y., Mondo S., Lyhne E.K., Kogle M.E., Clum A.,
RA   Lipzen A., Salamov A., Ngan C.Y., Daum C., Chiniquy J., Barry K.,
RA   LaButti K., Haridas S., Simmons B.A., Magnuson J.K., Mortensen U.H.,
RA   Larsen T.O., Grigoriev I.V., Baker S.E., Andersen M.R.;
RT   "Linking secondary metabolites to gene clusters through genome sequencing
RT   of six diverse Aspergillus species.";
RL   Proc. Natl. Acad. Sci. U.S.A. 115:E753-E761(2018).
RN   [2]
RP   FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, AND PATHWAY.
RX   PubMed=29968715; DOI=10.1038/s41467-018-04983-2;
RA   Matsuda Y., Bai T., Phippen C.B.W., Noedvig C.S., Kjaerboelling I.,
RA   Vesth T.C., Andersen M.R., Mortensen U.H., Gotfredsen C.H., Abe I.,
RA   Larsen T.O.;
RT   "Novofumigatonin biosynthesis involves a non-heme iron-dependent
RT   endoperoxide isomerase for orthoester formation.";
RL   Nat. Commun. 9:2587-2587(2018).
CC   -!- FUNCTION: DMOA farnesyltransferase; part of the gene cluster that
CC       mediates the biosynthesis of novofumigatonin, a heavily oxygenated
CC       meroterpenoid containing a unique orthoester moiety (PubMed:29968715).
CC       The first step of the pathway is the synthesis of 3,5-
CC       dimethylorsellinic acid (DMOA) by the polyketide synthase nvfA via
CC       condensation of one acetyl-CoA starter unit with 3 malonyl-CoA units
CC       and 2 methylations (PubMed:29968715). DMOA is then converted to
CC       farnesyl-DMOA by the farnesyltransferase nvfB (PubMed:29968715).
CC       Epoxydation by FAD-dependent monooxygenase nvfK, followed by a
CC       protonation-initiated cyclization catalyzed by the terpene cyclase nvfL
CC       leads to the production of asnavolin H (PubMed:29968715). The short
CC       chain dehydrogenase nvfC then as a 3-OH dehydrogenase of asnovolin H to
CC       yield chemesin D (PubMed:29968715). There are two branches to
CC       synthesize asnovolin A from chemesin D (PubMed:29968715). In one
CC       branch, chemesin D undergoes Baeyer-Villiger oxidation by nvfH,
CC       methylation by nvfJ, and enoyl reduction by the nvfM D enoylreductase
CC       that reduces the double bond between C-5'and C-6', to form respectively
CC       asnovolin I, asnovolin K, and asnovolin A (PubMed:29968715). In the
CC       other branch, the methylation precedes the Baeyer-Villiger oxidation
CC       and the enoyl reduction to yield asnovolin A via the asnovolin J
CC       intermediate (PubMed:29968715). Asnovolin A is further converted to
CC       fumigatonoid A by the Fe(II)/2-oxoglutarate-dependent dioxygenase nvfI
CC       that catalyzes an endoperoxidation reaction (PubMed:29968715). The
CC       alpha/beta hydrolase nvfD then acts as an epimerase that converts
CC       fumigatonoid A to its C-5' epimer, which then undergoes spontaneous or
CC       nvfD-catalyzed lactonization (PubMed:29968715). The following step
CC       utilizes the ketoreductase nvfG to produce fumigatonoid B
CC       (PubMed:29968715). The dioxygenase nvfE further converts fumigatonoid B
CC       into fumigatonoid C (PubMed:29968715). Finally the Fe(II)/2-
CC       oxoglutarate-dependent dioxygenase nvfF catalyzes two rounds of
CC       oxidation to transform fumigatonoid C into the end product,
CC       novofumigatonin A (PubMed:29968715). {ECO:0000269|PubMed:29968715}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E)-farnesyl diphosphate + 3,5-dimethylorsellinate = (3R)-
CC         3-farnesyl-6-hydroxy-2,3,5-trimethyl-4-oxocyclohexa-1,5-diene-1-
CC         carboxylate + diphosphate + H(+); Xref=Rhea:RHEA:49632,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:131856,
CC         ChEBI:CHEBI:131857, ChEBI:CHEBI:175763;
CC         Evidence={ECO:0000269|PubMed:29968715};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49633;
CC         Evidence={ECO:0000269|PubMed:29968715};
CC   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC       {ECO:0000269|PubMed:29968715}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- DISRUPTION PHENOTYPE: Completely abolishes the production of
CC       novofumigatonin as well as asnovolin A. {ECO:0000269|PubMed:29968715}.
CC   -!- SIMILARITY: Belongs to the UbiA prenyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; MSZS01000014; PKX88486.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2I1BT09; -.
DR   SMR; A0A2I1BT09; -.
DR   STRING; 1392255.A0A2I1BT09; -.
DR   VEuPathDB; FungiDB:P174DRAFT_425997; -.
DR   OrthoDB; 1343847at2759; -.
DR   UniPathway; UPA00213; -.
DR   Proteomes; UP000234474; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IEA:InterPro.
DR   GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd13959; PT_UbiA_COQ2; 1.
DR   Gene3D; 1.10.357.140; -; 1.
DR   InterPro; IPR039653; Prenyltransferase.
DR   InterPro; IPR000537; UbiA_prenyltransferase.
DR   InterPro; IPR044878; UbiA_sf.
DR   PANTHER; PTHR11048; PTHR11048; 1.
DR   Pfam; PF01040; UbiA; 1.
PE   1: Evidence at protein level;
KW   Membrane; Reference proteome; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..316
FT                   /note="DMOA farnesyltransferase nvfB"
FT                   /id="PRO_0000453077"
FT   TRANSMEM        47..67
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        71..91
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        115..135
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        139..159
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        162..182
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        191..211
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        234..254
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        258..278
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        294..314
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   316 AA;  34871 MW;  B19066EDA5391D75 CRC64;
     MGGKAQNGED EARGKVLSSL PPSLVPYAEL MRVHRPLGYY LNTSPYVVGV VFGAAVAPTK
     LPATILLDRL LILVLWSLFL RSAGCVWNDV IDMDLDRQIA RTRLRPLPRG AVSSWNAVML
     TAGIFACGGS LLSFLPRECA IEALIEIFFA LLYPFGKRFT DFPQLILVNI GWAIPMSMHS
     LGLDPLAYKK PTFFMFLFIA LVIVMIDVVY SRQDTEEDMK VGVKSMAVRF KHSIELLSYA
     FFYASTGALL AAGYYSGLGI PFTVLSVGGH FGGFLYFLKT TGVGKAPQVE SYAKLACLIA
     SLFWVVGLFV EYYLRV
 
 
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