ID A0A166XH31_9PEZI Unreviewed; 495 AA.
AC A0A166XH31;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Averantin oxidoreductase {ECO:0000313|EMBL:KZL76603.1};
GN ORFNames=CI238_03661 {ECO:0000313|EMBL:KZL76603.1};
OS Colletotrichum incanum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum spaethianum species complex.
OX NCBI_TaxID=1573173 {ECO:0000313|EMBL:KZL76603.1, ECO:0000313|Proteomes:UP000076584};
RN [1] {ECO:0000313|EMBL:KZL76603.1, ECO:0000313|Proteomes:UP000076584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAFF 238704 {ECO:0000313|EMBL:KZL76603.1,
RC ECO:0000313|Proteomes:UP000076584};
RA Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA O'Connell R.J.;
RT "Survival trade-offs in plant roots during colonization by closely related
RT pathogenic and mutualistic fungi.";
RL Submitted (JUN-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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KZL76603.1}.
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DR EMBL; LFIW01002278; KZL76603.1; -; Genomic_DNA.
DR STRING; 1573173.A0A166XH31; -.
DR OrthoDB; 2663980at2759; -.
DR Proteomes; UP000076584; 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; cd11058; CYP60B-like; 1.
DR Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR PANTHER; PTHR24305; CYTOCHROME P450; 1.
DR PANTHER; PTHR24305:SF240; CYTOCHROME P450 MONOOXYGENASE STCF-RELATED; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00022617};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022617};
KW Reference proteome {ECO:0000313|Proteomes:UP000076584}.
SQ SEQUENCE 495 AA; 56772 MW; 2BBF622B0842B8CA CRC64;
MSLTLWTLFA LFLLFRIYRI IYNLCFHPLA KVPGPKLYAI SWIPRLWHQQ IRGTHWKDLV
ALHKKYGRIV RTGPDEVSNA SAKAWDDICG SKTFVRDLNF LRVTQLDERH SFISPVKTEH
NTVRRLLQPA FTDRSLLRHE KILGEWTEKL RLNIAKEQGR PVDVAQKLVW MTFDTMGVLS
FGESFGCLDK NRQHPYLKAI ELGAPFLSLL QIILRYEATR GLYDLFLKLP WMRFWNSLRA
TAEAKAAKWI ENADESRGDV MSVIWKAMQD QNTPISQRQA DDLASILCLA GAESTPVLMS
GMMWWILSTP HAHAKLKEEI RTAIRKSSDI TVPNVSKLPY LDACIMESLR QHTPFSVAIP
RIVPEGGAVV DGYFLPAGTV CGVPHWASAH LESHFTDPEM FVPERWLPNP DPRYADDKRD
SFKPFAKGSL DCIGKRLVYH EVRMVMATLF WNFDMELCSE SHNWVAGTNA TVRMMREKGA
LFIKATPSTR NDFEL
//