ID A0A0D2BU67_9EURO Unreviewed; 536 AA.
AC A0A0D2BU67;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Pisatin demethylase {ECO:0008006|Google:ProtNLM};
GN ORFNames=PV06_06586 {ECO:0000313|EMBL:KIW40987.1};
OS Exophiala oligosperma.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=215243 {ECO:0000313|EMBL:KIW40987.1, ECO:0000313|Proteomes:UP000053342};
RN [1] {ECO:0000313|EMBL:KIW40987.1, ECO:0000313|Proteomes:UP000053342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 72588 {ECO:0000313|EMBL:KIW40987.1,
RC ECO:0000313|Proteomes:UP000053342};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala oligosperma CBS72588.";
RL Submitted (JAN-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; KN847337; KIW40987.1; -; Genomic_DNA.
DR RefSeq; XP_016261203.1; XM_016407723.1.
DR AlphaFoldDB; A0A0D2BU67; -.
DR STRING; 215243.A0A0D2BU67; -.
DR GeneID; 27358660; -.
DR VEuPathDB; FungiDB:PV06_06586; -.
DR HOGENOM; CLU_001570_14_0_1; -.
DR OrthoDB; 408598at2759; -.
DR Proteomes; UP000053342; 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; cd11060; CYP57A1-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:SF215; CYTOCHROME P450 MONOOXYGENASE CICH-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:UP000053342};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..41
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 536 AA; 60731 MW; AF44A815B5862F4D CRC64;
MAMDTSTATP PSNSFEPWSS SYWTVVLLLA LSITTGIIYI LTQRYQPYLR SIPGPFLASF
TDLWRFVKVN QLRFELTLQE LHDRYGDLVR VGPNCISVGD PREIRQIYGI SRLFQKSEYY
RVAQPLINGK PVASLFMITN EDAHKAAKRP IAHAYAMTSL LDYEPFVDNT STVLVERLTS
LYADSDKVCD IGEWLQWYAF DVIGEMTMSR RFGFLEQGRD VGTIIKTLNK SGAYTAIVGQ
MPWLDYLLAK NRWWGHLFSR DKMGVSKFVL SFLQPRIDEA ALRRRERKKD DNDDDDADVT
TSTDHRKDFT AKFIAASERY SGKIPPSQLL GWSLSNINAG SDTTAITLRA IFHFLLLHPA
CLSRLLDELH SAELGDAPTF RETSTLPYLG AVIKESLRLH TPVGLILERV VPQGGVTLCG
RHFPAGTVVG CNPAVIHQDA RVFGRRYGVR EFRPERWLEP PSGGEELAEM ERCFMAFGAG
KRTCIGKNIS LLEVHKLVPL LLMKFKFTLV DPEKSLTIWN TFFVHQKGLE VYVEKA
//
