ID A0A0L6WPG1_9AGAR Unreviewed; 502 AA.
AC A0A0L6WPG1;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Secologanin synthase {ECO:0000313|EMBL:KNZ77019.1};
GN ORFNames=J132_07740 {ECO:0000313|EMBL:KNZ77019.1};
OS Termitomyces sp. J132.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Tricholomatineae; Lyophyllaceae;
OC Termitomyces.
OX NCBI_TaxID=1306850 {ECO:0000313|EMBL:KNZ77019.1, ECO:0000313|Proteomes:UP000053712};
RN [1] {ECO:0000313|Proteomes:UP000053712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J132 {ECO:0000313|Proteomes:UP000053712};
RA Hu H., Poulsen M.;
RT "The genome of Termitomyces.";
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971,
CC ECO:0000256|PIRSR:PIRSR602403-1};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005179}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|ARBA:ARBA00010617}.
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DR EMBL; KQ412558; KNZ77019.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L6WPG1; -.
DR STRING; 1306850.A0A0L6WPG1; -.
DR OrthoDB; 3640568at2759; -.
DR Proteomes; UP000053712; Unassembled WGS sequence.
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:InterPro.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR CDD; cd11069; CYP_FUM15-like; 1.
DR Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR InterPro; IPR036396; Cyt_P450_sf.
DR PANTHER; PTHR24305; CYTOCHROME P450; 1.
DR PANTHER; PTHR24305:SF242; CYTOCHROME P450 MONOOXYGENASE ATNE-RELATED; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00465; EP450IV.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Heme {ECO:0000256|PIRSR:PIRSR602403-1};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR602403-1};
KW Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR602403-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053712};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT BINDING 438
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:0000256|PIRSR:PIRSR602403-1"
SQ SEQUENCE 502 AA; 56758 MW; 0291D923DAFD7320 CRC64;
MGGRVRLNHS IQGILWCKFK STSGLSKWRF KILQFRRLYT TDTKALNHIL MTTSVYQKPE
AARHNLSRIL GEGVLVVEGE KHKQQRKVMN PAFGPSQIRE LTEIFVSKAI QLRDAWASEN
DRKDGQDWID ALSWLSRTTL DVIGLAGLFF CFPTALTLTG LHAGFNYKFD ALSEDPKKNE
LNAAFALMFK AGTRLSLIPM IRAYFPFLRF LKTEQDVKAA EARKTMTRIS HELLRGSKNS
VHEKGEKRDL LTLLVKSNMD TDIPEHQRMS DQDVLAQIPT FLVAGHETTS TGTTWALYAL
TQDKAVQNKL REELFSVDTD NPTMDQLNAL PYLDMVVRET LRVHSPVPST IRIAVKDDLL
PLGHPITDRK GVVHNFIKVT KGQMLFIPIL AINRDKSIWG EDAAEFRPER WEHVPEAAAN
VPGVWGNMLT FLGGPRACIG YRFSLVETKA LLFTLVRAFE FDLAVPAKDI IKKSSIVQRP
VLVTDPDGSN KMPLLIRPIE RS
//
