TROPD_TALSN
ID TROPD_TALSN Reviewed; 514 AA.
AC B8M9J6; B8M9J7;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Cytochrome P450 monooxygenase tropD {ECO:0000303|PubMed:22508998};
DE EC=1.-.-.- {ECO:0000269|PubMed:22508998};
DE AltName: Full=Tropolone synthesis protein D {ECO:0000303|PubMed:22508998};
GN Name=tropD {ECO:0000303|PubMed:22508998};
GN Synonyms=tsL2 {ECO:0000303|PubMed:22508998}; ORFNames=TSTA_117730;
OS Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS 1006) (Penicillium stipitatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441959;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006;
RX PubMed=22508998; DOI=10.1073/pnas.1201469109;
RA Davison J., al Fahad A., Cai M., Song Z., Yehia S.Y., Lazarus C.M.,
RA Bailey A.M., Simpson T.J., Cox R.J.;
RT "Genetic, molecular, and biochemical basis of fungal tropolone
RT biosynthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:7642-7647(2012).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006;
RX PubMed=24863423; DOI=10.1002/anie.201403450;
RA al Fahad A., Abood A., Simpson T.J., Cox R.J.;
RT "The biosynthesis and catabolism of the maleic anhydride moiety of
RT stipitatonic acid.";
RL Angew. Chem. Int. Ed. 53:7519-7523(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006;
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
CC -!- FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that
CC mediates the biosynthesis of the tropolone class of fungal maleic
CC anhydrides (PubMed:22508998, PubMed:24863423). The pathway begins with
CC the synthesis of 3-methylorcinaldehyde by the non-reducing polyketide
CC synthase (PKS) tropA (PubMed:22508998). 3-methylorcinaldehyde is the
CC substrate for the FAD-dependent monooxygenase tropB to yield a
CC dearomatized hydroxycyclohexadione (PubMed:22508998, PubMed:24863423).
CC The 2-oxoglutarate-dependent dioxygenase tropC then performs the
CC oxidative ring expansion to provide the first tropolone metabolite
CC stipitaldehyde (PubMed:22508998, PubMed:24863423). Trop D converts
CC stipitaldehyde into stipitacetal which is in turn converted to
CC stipitalide by the short-chain dehydrogenase/reductase tropE
CC (PubMed:24863423). The next steps involve tropF, tropG, tropH, tropI
CC and tropJ to form successive tropolone maleic anhydrides including
CC stipitaldehydic, stipitatonic and stipitatic acids (PubMed:24863423).
CC {ECO:0000269|PubMed:22508998, ECO:0000269|PubMed:24863423}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:22508998}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Leads to the accumulation of stipitaldehyde
CC (PubMed:22508998, PubMed:24863423). {ECO:0000269|PubMed:22508998,
CC ECO:0000269|PubMed:24863423}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EED17999.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BK008910; DAA64701.1; -; Genomic_DNA.
DR EMBL; EQ962655; EED17998.1; -; Genomic_DNA.
DR EMBL; EQ962655; EED17999.1; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_002481990.1; XM_002481945.1.
DR RefSeq; XP_002481991.1; XM_002481946.1.
DR AlphaFoldDB; B8M9J6; -.
DR SMR; B8M9J6; -.
DR EnsemblFungi; EED17998; EED17998; TSTA_117730.
DR EnsemblFungi; EED17999; EED17999; TSTA_117730.
DR GeneID; 8105831; -.
DR VEuPathDB; FungiDB:TSTA_117730; -.
DR eggNOG; KOG0158; Eukaryota.
DR HOGENOM; CLU_001570_14_0_1; -.
DR InParanoid; B8M9J6; -.
DR OMA; MEVEAND; -.
DR OrthoDB; 467733at2759; -.
DR PhylomeDB; B8M9J6; -.
DR BioCyc; MetaCyc:MON-19389; -.
DR Proteomes; UP000001745; 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:0008152; P:metabolic process; IEA:UniProt.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00465; EP450IV.
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..514
FT /note="Cytochrome P450 monooxygenase tropD"
FT /id="PRO_0000437130"
FT TRANSMEM 7..27
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 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 346
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 514 AA; 58691 MW; 04509E7ADBA4C1C1 CRC64;
MAYGSQLTLL SGGQSIIILL IVSFLAWRFR VWFRLRHIPG PLGASLTNFV RMSWVFTKKA
HLIHQELHQK YGDVVRFGPN MVSISDPASI HIIYPMRKGL VKNDFYVPLR PYTRNRGAIP
NVFTALDEDL HMKLKYPVAS LFSLSNVSKF EVLVDEVLSV IDEQLDRRFA SHGEIFDLTE
WLQFFAFDVM GTMTFSKRYG FLEEGKDVGG MLNAIGQFMK QAAPVMQNPW LDRVLYKNRI
ADSLKRTPGS DIMKFVVAAI NERQKSASED EDFTKARKGK NDFLDEYIIT QKKDSNIPPW
FVTAWTISNV LAGSDSVGTV MKTTMYNLLT NPRTLEKLHA ELVAANVSRP RPRWSEVHNL
PYLDAVVQEA LRVHPPFALP FERIVPEGGL HISGQYIPAN TVIGASPYVV NRHKPTYGDD
AELWRPERWL EGGPEVRKKR DDGLLTFGAG RRICLGKHIG IFEVKKLIPF LVLNYDISIV
KPETFLAENE WFFRQSNLLA QIRRRPLESV EPNV
