ID A0A165LMH9_EXIGL Unreviewed; 540 AA.
AC A0A165LMH9;
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=Cytochrome P450 {ECO:0000313|EMBL:KZV98058.1};
GN ORFNames=EXIGLDRAFT_641801 {ECO:0000313|EMBL:KZV98058.1};
OS Exidia glandulosa HHB12029.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Exidiaceae; Exidia.
OX NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV98058.1, ECO:0000313|Proteomes:UP000077266};
RN [1] {ECO:0000313|EMBL:KZV98058.1, ECO:0000313|Proteomes:UP000077266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12029 {ECO:0000313|EMBL:KZV98058.1,
RC ECO:0000313|Proteomes:UP000077266};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005179}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|RuleBase:RU000461}.
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DR EMBL; KV425923; KZV98058.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165LMH9; -.
DR STRING; 1314781.A0A165LMH9; -.
DR InParanoid; A0A165LMH9; -.
DR OrthoDB; 5472594at2759; -.
DR Proteomes; UP000077266; 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: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; PTHR24305; CYTOCHROME P450; 1.
DR PANTHER; PTHR24305:SF166; CYTOCHROME P450 12A4, MITOCHONDRIAL-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 Metal-binding {ECO:0000256|RuleBase:RU000461};
KW Monooxygenase {ECO:0000256|RuleBase:RU000461};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000461};
KW Reference proteome {ECO:0000313|Proteomes:UP000077266}.
SQ SEQUENCE 540 AA; 60144 MW; CB8167054B226323 CRC64;
MHVPLVALAL GAVFWTLSTY RAFQRNRQLA IASGLPFICL PVDTFSPFWQ VAGPVLVPLL
RFLPFGLGAW ADDARAAWVL KHELHSKYGR VFIVVCPWQN VVHVADPDVV VDVVTRRTEF
PKPAHFYKIV EVYGRSVVTT DGADWVRYRK ITGPPFSEKN NHLVWRSTLE QTSQFLEALK
MTPIVPATAS NRPGRVLPQL QRDMKTIALH IIAEAGFGVA LPFAAADLEN TASIHTLLRF
LIPVMVIPKP LLRAIPIPAW RSAYTAYAEF QKYTALLTSR AKEDGMDNDG SRANLLHALV
ANAEVAGEKS ERLSDAEVLA HLFVFILAGH ETTANALSYA ILNLAIHSDV QEWFIQRLDD
ELSSNRGIEP RDWGYDSVFG QAQAALCIMN ETLRLFPTVA GVPKWTDSSS VALAWNERKF
LVPPKTPVVF NTIAMHRDPT LWGPDAAEFK PQRWLKDQPR KGQFMAFSEG ARACLGKKFA
QVEFVAVLAT IFSRFRAELE CAPGQTMDDA KKKAMAAFDS SVVLATLGMT KQVPVRFVPR
//
