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Database: UniProt
Entry: A0A125Q160_9ACTN
LinkDB: A0A125Q160_9ACTN
Original site: A0A125Q160_9ACTN 
ID   A0A125Q160_9ACTN        Unreviewed;       402 AA.
AC   A0A125Q160;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Cytochrome P450 {ECO:0000313|EMBL:SCG66094.1};
GN   ORFNames=GA0070623_3173 {ECO:0000313|EMBL:SCG66094.1};
OS   Micromonospora rifamycinica.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=291594 {ECO:0000313|EMBL:SCG66094.1, ECO:0000313|Proteomes:UP000198226};
RN   [1] {ECO:0000313|EMBL:SCG66094.1, ECO:0000313|Proteomes:UP000198226}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44983 {ECO:0000313|EMBL:SCG66094.1,
RC   ECO:0000313|Proteomes:UP000198226};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) 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; LT607752; SCG66094.1; -; Genomic_DNA.
DR   RefSeq; WP_067311303.1; NZ_LT607752.1.
DR   AlphaFoldDB; A0A125Q160; -.
DR   OrthoDB; 4156795at2; -.
DR   Proteomes; UP000198226; Chromosome i.
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; cd11031; Cyp158A-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   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}.
SQ   SEQUENCE   402 AA;  44173 MW;  5489714A67D80F36 CRC64;
     MTETTHATIA RPYPFSDPHR LDVDPRLAEL RRDEPLVRVQ LPFGEPAWLA TRHADVRTVL
     GDLRFSRAAA VGRDEPRSVP YQREAGILGM DPPEHSRLRR LAAKAFTARR VEELRPRTRE
     LAEELVTGML AAGSPADLVT HLATPLPIRV ICDLLGVPVA DQDRFHTWSE AIVSTTSLRP
     EVAQSYLDQL LSYMAGLIAQ RRVTPTDDLI GAMVRARDEN ADRLTEEEMV RLAAGLLAAG
     HETTVTQIPN LVYVLLTEPD AWQRLCADPA LVPSAVEELL RFVPLGATAA FARYALVDVE
     LGGVLVRAGE PVLVSIPSAN RDETVFPDAD RLDLGRETNP HLAFGHGPHH CIGAQLARME
     LQVVLETLLD RTPGLRLAVP ESALTWKTGL LVRGLTALPV GW
//
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