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Database: UniProt
Entry: E9RHV2_9BASI
LinkDB: E9RHV2_9BASI
Original site: E9RHV2_9BASI 
ID   E9RHV2_9BASI            Unreviewed;       435 AA.
AC   E9RHV2;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Putative P450 oxidoreductase {ECO:0000313|EMBL:BAJ78285.1};
DE   Flags: Fragment;
GN   Name=cyp1 {ECO:0000313|EMBL:BAJ78285.1};
OS   Sporisorium graminicola.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Sporisorium.
OX   NCBI_TaxID=280036 {ECO:0000313|EMBL:BAJ78285.1};
RN   [1] {ECO:0000313|EMBL:BAJ78285.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Morita T., Fukuoka T., Imura T., Kitamoto D.;
RT   "Accumulation of cellobiose lipids under nitrogen-limiting conditions by
RT   two ustilaginomycetous yeasts, Pseudozyma aphidis and Pseudozyma
RT   hubeiensis.";
RL   FEMS Yeast Res. 13:44-49(2013).
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC       {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
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DR   EMBL; AB602448; BAJ78285.1; -; Genomic_DNA.
DR   AlphaFoldDB; E9RHV2; -.
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   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; PTHR24296; CYTOCHROME P450; 1.
DR   PANTHER; PTHR24296:SF8; CYTOCHROME P450 704B1; 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};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU000461};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU000461};
KW   Monooxygenase {ECO:0000256|RuleBase:RU000461};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU000461}.
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:BAJ78285.1"
FT   NON_TER         435
FT                   /evidence="ECO:0000313|EMBL:BAJ78285.1"
SQ   SEQUENCE   435 AA;  49808 MW;  A6B9001245028716 CRC64;
     NTHSLPGLGR LIDISRPDWI EHVQKTKFAS YVKGEQFHDQ MRDVLGDGIF TSDGERWKMQ
     RKVASRIFTV SSFKAIITHT IREDCKLVEK LIESYAKDGS VFNLQELYFK FTLSSFVKIA
     FSQDIKALSE PDRPDTFGDA FNYAQKVLDM RFVQPWWKIA ERFSETGKKM RAARKVVEEF
     TNNIVESRRS ETEALGEKAK PEGSRKDLLD LFMAYRSSDG QGLSNQQLKD TILNLMIAGR
     DTTAEALSWM SWHMLTKPDV YSSIREEIDA SLEADGQQEG LEIDYDVFEQ HTAKLTTFHE
     TLRLHPSIPK NIRRALQDDV LPNGGPRVRK GDLVLYSDWA MARNPEIWGP DACEFKPSRW
     IDDKTGSTVK YSQFQAHFFN GGPRLCLGQK LASYEVVQLI HHIFAKFDLE LVDHGPKKSA
     GFDKVPDYLN SLTHP
//
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