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Database: UniProt
Entry: A0A1C5JI26_9ACTN
LinkDB: A0A1C5JI26_9ACTN
Original site: A0A1C5JI26_9ACTN 
ID   A0A1C5JI26_9ACTN        Unreviewed;       423 AA.
AC   A0A1C5JI26;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Cytochrome P450 {ECO:0000313|EMBL:SCG69869.1};
GN   ORFNames=GA0070213_11159 {ECO:0000313|EMBL:SCG69869.1};
OS   Micromonospora humi.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=745366 {ECO:0000313|EMBL:SCG69869.1, ECO:0000313|Proteomes:UP000199360};
RN   [1] {ECO:0000313|EMBL:SCG69869.1, ECO:0000313|Proteomes:UP000199360}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45647 {ECO:0000313|EMBL:SCG69869.1,
RC   ECO:0000313|Proteomes:UP000199360};
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; FMDM01000011; SCG69869.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C5JI26; -.
DR   STRING; 745366.GA0070213_11159; -.
DR   Proteomes; UP000199360; 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; cd20625; CYP164-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   423 AA;  45321 MW;  85643F653D7C0C13 CRC64;
     MDPADALALL MSPAGRVDPY PTYERLRAHG PVVQAGPVFY AVTGYAEADA ILRDARFGVM
     DDGLRDQFMP GWRESPAVLS ISRSMLRTNP PDHSRMRRLA AGAFTPRRIA AMRGVVEAQA
     DALVDAMLAG GRGGAPVDFM AEFAYPLPVG VICALLGVPA ADRPLFRRWA TDLTGVLEPE
     ITMDELAVAD RGAAELRAYF TELVAARRRA PADDLTTALV QAHDGGDRLT GDELLANLIV
     LLVAGFETTT NLLGNGLVAL LDHPRAAATL REHPEFAPAY VDELLRYDSP VQLTSRMSTA
     PSTYGGVDLP AESWVIVMLG AANRDPRRYP EPGRFDPWRP QIHPLSFGAG PHYCLGAALA
     RLEAQVAVPL LLRRLPELAV AGTPERRVRL TLRGYATLPV TPGREAAPVT VAGTPPGAAG
     PTP
//
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