PBCG_EMENI
ID PBCG_EMENI Reviewed; 534 AA.
AC C8VN91; Q5BCY2;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Cytochrome P450 monooxygenase AN1598 {ECO:0000303|PubMed:22506079};
DE EC=1.-.-.- {ECO:0000305|PubMed:22506079};
DE AltName: Full=Pimaradiene biosynthesis cluster protein AN1598 {ECO:0000303|PubMed:22506079};
GN ORFNames=AN1598, ANIA_01598;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
RN [3]
RP FUNCTION, INDUCTION, AND PATHWAY.
RX PubMed=22506079; DOI=10.1371/journal.pone.0035450;
RA Bromann K., Toivari M., Viljanen K., Vuoristo A., Ruohonen L.,
RA Nakari-Setaelae T.;
RT "Identification and characterization of a novel diterpene gene cluster in
RT Aspergillus nidulans.";
RL PLoS ONE 7:e35450-e35450(2012).
RN [4]
RP FUNCTION, AND INDUCTION.
RX PubMed=27098256; DOI=10.1007/s00253-016-7517-5;
RA Bromann K., Toivari M., Viljanen K., Ruohonen L., Nakari-Setaelae T.;
RT "Engineering Aspergillus nidulans for heterologous ent-kaurene and gamma-
RT terpinene production.";
RL Appl. Microbiol. Biotechnol. 100:6345-6359(2016).
CC -!- FUNCTION: Bifunctional terpene synthase; part of the gene cluster that
CC mediates the biosynthesis of the diterpene ent-pimara-8(14),15-diene
CC (PD) (PubMed:22506079, PubMed:27098256). Within the cluster, the HMG-
CC CoA reductase AN1593 functions in the mevalonate pathway, which
CC produces isoprenoid precursors (PubMed:22506079, PubMed:27098256). The
CC geranylgeranyl pyrophosphate (GGPP) synthase AN1592 is needed in the
CC formation of GGPP, the precursor for diterpenes (PubMed:22506079,
CC PubMed:27098256). Lastly, the pimaradiene synthase pbcA performs the 2
CC cyclization steps that convert GGPP to ent-pimara-8(14),15-diene
CC (PubMed:22506079, PubMed:27098256). The putative roles of the remaining
CC cluster enzymes in ent-pimara-8(14),15-diene biosynthesis is unclear
CC (Probable). The cytochrome P450 monooxygenase AN1598, the glutathione
CC S-transferase AN1595, the oxidoreductases AN1596 and AN1597 probably
CC function as decorative enzymes (Probable). It is possible that in
CC biological conditions the compound is oxidized to ent-pimara-8(14),15-
CC dien-19-oic acid, which is a bioactive diterpene compound predominant
CC in many plant extracts (Probable). {ECO:0000269|PubMed:22506079,
CC ECO:0000269|PubMed:27098256, ECO:0000305|PubMed:22506079}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000305|PubMed:22506079}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Expression is positively regulated by the cluster-specific
CC transcription factor pbcR. {ECO:0000269|PubMed:22506079,
CC ECO:0000269|PubMed:27098256}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAA64305.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AACD01000025; EAA64305.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BN001307; CBF85188.1; -; Genomic_DNA.
DR RefSeq; XP_659202.1; XM_654110.1.
DR AlphaFoldDB; C8VN91; -.
DR SMR; C8VN91; -.
DR STRING; 227321.C8VN91; -.
DR EnsemblFungi; CBF85188; CBF85188; ANIA_01598.
DR EnsemblFungi; EAA64305; EAA64305; AN1598.2.
DR GeneID; 2875700; -.
DR KEGG; ani:AN1598.2; -.
DR VEuPathDB; FungiDB:AN1598; -.
DR eggNOG; KOG0156; Eukaryota.
DR HOGENOM; CLU_022195_0_1_1; -.
DR InParanoid; C8VN91; -.
DR OMA; PECKDEW; -.
DR OrthoDB; 614788at2759; -.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000000560; Chromosome VII.
DR Proteomes; UP000005890; 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:0019748; P:secondary metabolic process; IEP:AspGD.
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; IPR002403; Cyt_P450_E_grp-IV.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00465; EP450IV.
DR SUPFAM; SSF48264; SSF48264; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..534
FT /note="Cytochrome P450 monooxygenase AN1598"
FT /id="PRO_0000450845"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 464
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 3
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 498
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 534 AA; 61207 MW; 06921449276122F0 CRC64;
MDNYTWHSGT LIPSDSPSSI DRSQLYLEIL GVLSVVYLLQ TLVAYSKSFK APFVGFRFWY
EPKWLVGLRF SQGALAQVNE GYAKYKNAMF KVARNDSDIL VIPNKYVEEL RSLPDEKISA
IRAHIKNLLG KYSTTLILLE SDLHTRMLQT KLTPNLGSFI EVIESELLFA MDQEIPANLD
DWQSVNVFHI VLRIVARISA RVFLGVPACR NEEWLQTSIH YTENVFATVM LLRRFPKWMH
PIVGHLLPSY WAIHRNLRTA KRIISPMVRQ RRAEEAKRNP DYVKPNDLLQ WMMDGANEND
GQPDKLAHRQ LLLSLASIHT TTMAAAHCFY DLCQHPEYFE PLREEINDVI AQDGGWKKTT
LNKMRKLDSF LKESQRINPP SLLAFNRIVS EDLTLSDGTL LPKGTHFSMP SAAILQDNGV
EPGADQFDGF RYYKKRLNPE EANKHQFAMT DNNNLHFGHG KYSCPGRFFA SNEIKIIMAH
LLTDYEFKYP RGATRPRNLT ADENLYPDPS ARLLMRRRVV APPQASITPQ LVSA
