ID   NF450_NEOFI             Reviewed;         547 AA.
AC   A1DN29;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   29-SEP-2021, sequence version 2.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Sesterfisheric acid synthase {ECO:0000303|PubMed:26332841};
DE            EC=1.-.-.- {ECO:0000269|PubMed:26332841};
DE   AltName: Full=Cytochrome P450 monooxygenase NfP450 {ECO:0000303|PubMed:26332841};
DE   AltName: Full=Sesterfisheric acid biosynthesis cluster protein NfP450 {ECO:0000303|PubMed:26332841};
GN   Name=NfP450 {ECO:0000303|PubMed:26332841}; ORFNames=NFIA_055490;
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC   / WB 181;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX   PubMed=26332841; DOI=10.1021/jacs.5b08319;
RA   Ye Y., Minami A., Mandi A., Liu C., Taniguchi T., Kuzuyama T., Monde K.,
RA   Gomi K., Oikawa H.;
RT   "Genome mining for sesterterpenes using bifunctional terpene synthases
RT   reveals a unified intermediate of di/sesterterpenes.";
RL   J. Am. Chem. Soc. 137:11846-11853(2015).
RN   [3]
RP   FUNCTION.
RX   PubMed=29410538; DOI=10.1038/s41598-018-20916-x;
RA   Sato H., Narita K., Minami A., Yamazaki M., Wang C., Suemune H., Nagano S.,
RA   Tomita T., Oikawa H., Uchiyama M.;
RT   "Theoretical Study of Sesterfisherol Biosynthesis: Computational Prediction
RT   of Key Amino Acid Residue in Terpene Synthase.";
RL   Sci. Rep. 8:2473-2473(2018).
CC   -!- FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that
CC       mediates the biosynthesis of sesterfisheric acid (PubMed:26332841). The
CC       bifunctional terpene synthase NfSS converts DMAPP and IPP, and also
CC       GGPP, into sesterfisherol (PubMed:26332841, PubMed:29410538). The C-
CC       terminal prenyltransferase (PT) domain of NfSS catalyzes formation of
CC       GFPP, whereas the N-terminal terpene cyclase (TC) domain catalyzes the
CC       cyclization of GFPP to sesterfisherol (PubMed:26332841,
CC       PubMed:29410538). The cyotochrome P450 monooxygenase NfP450 then
CC       catalyzes oxidative modifications of sesterfisherol into sesterfisheric
CC       acid (PubMed:26332841). {ECO:0000269|PubMed:26332841,
CC       ECO:0000269|PubMed:29410538}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
CC   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC       {ECO:0000269|PubMed:26332841}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAW16200.1; Type=Erroneous gene model prediction; Evidence={ECO:0000269|PubMed:26332841};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DS027698; EAW16200.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_001258097.1; XM_001258096.1.
DR   SMR; A1DN29; -.
DR   EnsemblFungi; EAW16200; EAW16200; NFIA_055490.
DR   GeneID; 4584612; -.
DR   KEGG; nfi:NFIA_055490; -.
DR   VEuPathDB; FungiDB:NFIA_055490; -.
DR   eggNOG; KOG0158; Eukaryota.
DR   HOGENOM; CLU_001570_14_11_1; -.
DR   OMA; PQYWHAP; -.
DR   OrthoDB; 467733at2759; -.
DR   UniPathway; UPA00213; -.
DR   Proteomes; UP000006702; Unassembled WGS sequence.
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:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.10.630.10; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002401; Cyt_P450_E_grp-I.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW   Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..547
FT                   /note="Sesterfisheric acid synthase"
FT                   /id="PRO_0000453641"
FT   TRANSMEM        19..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         490
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        341
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        404
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   547 AA;  61473 MW;  1720C595042C569F CRC64;
     MDAQHLMTMS GISLEQVAIM GCSLGTGLLV SMIIYNYFFH PLARVPGPCT GAIFPFWSMS
     SLYRRRLNPD LAELHKKYGQ ILSLLSGYGG LLMCPRNTGP IVRVGPNQLS FATVEAQKMI
     YNAKPTHTGS DELFGRDGTL QDVLLSMILG AANIGSLSNR AEHKKMRKRL QPGFTSKALF
     EQESLLRMHM DRLLQGLAQD TGVIDLTEYF SRFLWDLIGD LSFGEPLVPE KHGRRTDTLR
     SLVGVYQGCF PILEAINYAV PQIEGVLKLA LQLVPPATLR AVLPSATFRE YDHPAINSHT
     TPLQCCINRQ DGRSDFLTHI MGDKSSNPTE LELSYDELHS NATVLMIAGY KTTETSLSAL
     FYRLLSTPGV LEKLQTELFS NFQSIDEITG KKLLSLPYLN GCVNESLRLT PAVAGKFASR
     RSPGAIIEGF YVPSGTEVYT ETYTMQRSPQ YWHAPDEYRP ERWFERGEGS PYAQDVHEAF
     KPFSSGPRAC LGREMALQTL RLTAALLVYR FHLKIVNEDR FVWEQDTDSR MIYSKYHIKA
     IVQERLT