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Database: UniProt
Entry: A0A0M8SK08_9ACTN
LinkDB: A0A0M8SK08_9ACTN
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ID   A0A0M8SK08_9ACTN        Unreviewed;       378 AA.
AC   A0A0M8SK08;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=Cytochrome P450 {ECO:0000313|EMBL:KOU35195.1};
GN   ORFNames=ADK54_38625 {ECO:0000313|EMBL:KOU35195.1};
OS   Streptomyces sp. WM6378.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1415557 {ECO:0000313|EMBL:KOU35195.1, ECO:0000313|Proteomes:UP000037774};
RN   [1] {ECO:0000313|Proteomes:UP000037774}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WM6378 {ECO:0000313|Proteomes:UP000037774};
RA   Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC       {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
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:KOU35195.1}.
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DR   EMBL; LGDD01000339; KOU35195.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M8SK08; -.
DR   PATRIC; fig|1415557.3.peg.8497; -.
DR   Proteomes; UP000037774; 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   CDD; cd11029; CYP107-like; 1.
DR   Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR002397; Cyt_P450_B.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   PANTHER; PTHR46696; P450, PUTATIVE (EUROFUNG)-RELATED; 1.
DR   PANTHER; PTHR46696:SF1; P450, PUTATIVE (EUROFUNG)-RELATED; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00359; BP450.
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}.
SQ   SEQUENCE   378 AA;  41629 MW;  C8F7DE42D94ED3AB CRC64;
     MRAEQPVVQA QLPNGETGWL ISRYEDVRAA FADPRLVRPL LSAWPLREGA DAPPPALPTF
     LEMTGEHHER VRRAVLPMFG RRRLEFMRPR IRAMAGELVD AMVAGTADGE AADLVASYAE
     PLPLRVLCET VGLPYEDREI YLPHTLALLG ASGLSMEEVL AALYALQDYA DDLISRREKD
     GEGEDYIGLL LAEALRPGGR LNRDDVVSFV VTMLMAGYKT NIQHTGNALL ALLTRPDELR
     RLRETPEGIG TAVEELLRYV PLMNAINILV ATEDFTLHGQ RIRAGDAVVP VPASANRDPE
     QFVDADRLDL ARTPNAHVAF GHGPHSCMGG HLTRLQLAVA IEVLLERLPG IELAVPARTI
     PWDESTPLRA PAVLPVRW
//
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