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Database: UniProt
Entry: D6EVQ2_STRLI
LinkDB: D6EVQ2_STRLI
Original site: D6EVQ2_STRLI 
ID   D6EVQ2_STRLI            Unreviewed;       398 AA.
AC   D6EVQ2;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   24-JAN-2024, entry version 53.
DE   SubName: Full=Cytochrome P450 {ECO:0000313|EMBL:EFD64764.2};
GN   ORFNames=SSPG_00404 {ECO:0000313|EMBL:EFD64764.2};
OS   Streptomyces lividans TK24.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=457428 {ECO:0000313|EMBL:EFD64764.2};
RN   [1] {ECO:0000313|EMBL:EFD64764.2}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TK24 {ECO:0000313|EMBL:EFD64764.2};
RG   The Broad Institute Genome Sequencing Platform;
RG   Broad Institute Microbial Sequencing Center;
RA   Fischbach M., Godfrey P., Ward D., Young S., Kodira C.D., Zeng Q.,
RA   Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., Chen Z., Engels R.,
RA   Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D.I.,
RA   Hepburn T.A., Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D.,
RA   Pearson M., Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C.,
RA   Sykes S.N., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA   Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA   Galagan J., Nusbaum C., Birren B.;
RT   "The genome sequence of Streptomyces lividans strain TK24.";
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC       {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
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DR   EMBL; GG657756; EFD64764.2; -; Genomic_DNA.
DR   AlphaFoldDB; D6EVQ2; -.
DR   HOGENOM; CLU_707192_0_0_11; -.
DR   Proteomes; UP000002769; 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; cd00302; cytochrome_P450; 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   398 AA;  43984 MW;  93D3F339863B888E CRC64;
     MVQDGRVSAR KADRGRAGPA CPVDRAADGT WRVHDFAVAR ALLRGPGTVQ AGLGIETVEK
     LPPRVRRPVL YRDGPEHREH RRQTARYFTP RRVDEHYREP MVRIAEEQLA VLRSAGEAPL
     SDLAFGLAVG VVSEVVGLRY SRPGIRRRLE RFFPEEFGEP GLTSVRGLYW LVRQNTNWLR
     IHLADVRPAV RAHRRREHDD LISHLIAEGC SDVEILGECL TFAAAGMVTT REFVCLAAWH
     LFSDAELLCH YRSADETGRL AVLQELLRLE PVIGSLRRRA TGPVELSCPD GPVTVRPGEY
     VEVHLDDANA DPKAVGEEPL LVRPQRAGAV GAGLSFGDGP HRCPGAHIAL LETDVFLSRL
     FALDGVRMSG GPRVAFQEAI DGYEIRDLTV ALPRAGRG
//
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