ID A0A0N0MT29_9ACTN Unreviewed; 411 AA.
AC A0A0N0MT29;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Cytochrome P450 {ECO:0000313|EMBL:KPI06228.1};
GN ORFNames=OK074_4206 {ECO:0000313|EMBL:KPI06228.1};
OS Actinobacteria bacterium OK074.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1592327 {ECO:0000313|EMBL:KPI06228.1, ECO:0000313|Proteomes:UP000037991};
RN [1] {ECO:0000313|EMBL:KPI06228.1, ECO:0000313|Proteomes:UP000037991}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK074 {ECO:0000313|EMBL:KPI06228.1,
RC ECO:0000313|Proteomes:UP000037991};
RA Brown S.D., Utturkar S.M., Klingeman D.M., Pelletier D.;
RT "Draft genome sequences for four actinobacteria strains OK006 OK074 OV450
RT and OV320.";
RL Submitted (AUG-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:KPI06228.1}.
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DR EMBL; LJCV01000258; KPI06228.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N0MT29; -.
DR PATRIC; fig|1592327.3.peg.6585; -.
DR OrthoDB; 3664945at2; -.
DR Proteomes; UP000037991; 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; cd11030; CYP105-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};
KW Reference proteome {ECO:0000313|Proteomes:UP000037991}.
SQ SEQUENCE 411 AA; 46086 MW; 7398084C90348287 CRC64;
MSDILADAQE ASGLAEYPFP RDLKCPFDPP PELRRRHVEE PVSKVRLWDG TTHWLVTRYE
DQKALYADQR LSVDTTKPGF PYLNEAFRET AAKTPPSFLN MDDPEHARIR RMVTAPFAIK
RIEAMRPAIQ RMTDDLIDKM LAGPNPTDFV EALALPLPSL VICELLGVPY EDHDFFQSNS
KVGLRRDVTA EAVRASFGAI FQYLDKKLDE KIADPAEDML SELGARVQAG ELTKQDATML
GILLLGAGHE TSANMLALGV LAFLEHPEQL AIVRDTDDPK VLAKAADEML RYLTVVHSGQ
RRLALEDLEV GGQQIRAGEG LIIPGATGNW QSDVFPEPEK LDINRDSRLH MAFGFGIHQC
LGQPLARLEL QVVYSTLFRR IPQLRLAVER ETLPYKDDGI VYGVYEMPVA W
//
