ID A0A0U1LYR5_TALIS Unreviewed; 511 AA.
AC A0A0U1LYR5;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Trichodiene oxygenase {ECO:0000313|EMBL:CRG88473.1};
GN ORFNames=PISL3812_05503 {ECO:0000313|EMBL:CRG88473.1};
OS Talaromyces islandicus (Penicillium islandicum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Islandici.
OX NCBI_TaxID=28573 {ECO:0000313|EMBL:CRG88473.1, ECO:0000313|Proteomes:UP000054383};
RN [1] {ECO:0000313|EMBL:CRG88473.1, ECO:0000313|Proteomes:UP000054383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WF-38-12 {ECO:0000313|EMBL:CRG88473.1};
RA Syromyatnikov M.Y., Popov V.N.;
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971};
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
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DR EMBL; CVMT01000004; CRG88473.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0U1LYR5; -.
DR STRING; 28573.A0A0U1LYR5; -.
DR OMA; MQASSME; -.
DR OrthoDB; 3184603at2759; -.
DR Proteomes; UP000054383; Unassembled WGS sequence.
DR GO; GO:0016020; C: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 CDD; cd11062; CYP58-like; 1.
DR Gene3D; 1.10.630.10; Cytochrome P450; 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 PANTHER; PTHR24305; CYTOCHROME P450; 1.
DR PANTHER; PTHR24305:SF157; N-ACETYLTRYPTOPHAN 6-HYDROXYLASE IVOC-RELATED; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|RuleBase:RU000461}; Iron {ECO:0000256|RuleBase:RU000461};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|RuleBase:RU000461};
KW Monooxygenase {ECO:0000256|RuleBase:RU000461};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000461};
KW Reference proteome {ECO:0000313|Proteomes:UP000054383};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 511 AA; 58003 MW; 61CBE22C016702C6 CRC64;
MLSYVSDLFP SCGAIAVGLL AWLATLAIYR LYLHPLARAG FPGPRLAAVS TWYEAYFDVF
LQGQYILQIE RMHQKYGPIV RIGPNELHVL DHEYYNKLYN MSNRLDKSAY FYCMLGNPKA
SFGTISAHLH RIRRSALSPF FSQQAVSRFS SHVQSIVDRL IDRMGKCAER GEPVPLFYAY
RCVTVDIITE YIFGHQFNLL DRPDWGKEFY SAWRSLWELS PTIRQFPPMM DAFMAMPRWL
TALINPKALE VVDLFASVDS QTKRLLSMNP AAIKTKRHPI VVWELSKTDA LPPDEKTLER
LSVEANGLLA AGFETTGGVL SYVTYLVLAH PDAHRKLLAE LVDAIPNPAH IPSFQQLEKL
PFLRGVVKEG LRLSVGAWSR LPRVNPNEDM HYKNWVVPAG TAIGMSALFV EKSPILFPDP
EAFIPERWID GATGESHLDQ YILTFGKGTR SCVGINLAYA ELYSILATLF RRFPDIQLHE
TSFRDVEHVH DYFAGMTRRE SQGLQVITGK K
//
