ID A0A0N1G360_9ACTN Unreviewed; 413 AA.
AC A0A0N1G360;
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=Linalool 8-monooxygenase {ECO:0000313|EMBL:KPI09634.1};
DE EC=1.14.13.151 {ECO:0000313|EMBL:KPI09634.1};
GN ORFNames=OK006_0297 {ECO:0000313|EMBL:KPI09634.1};
OS Actinobacteria bacterium OK006.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1592326 {ECO:0000313|EMBL:KPI09634.1, ECO:0000313|Proteomes:UP000037912};
RN [1] {ECO:0000313|EMBL:KPI09634.1, ECO:0000313|Proteomes:UP000037912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK006 {ECO:0000313|EMBL:KPI09634.1,
RC ECO:0000313|Proteomes:UP000037912};
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 (SEP-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:KPI09634.1}.
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DR EMBL; LJCU01000215; KPI09634.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N1G360; -.
DR PATRIC; fig|1592326.3.peg.4258; -.
DR Proteomes; UP000037912; 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 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, ECO:0000313|EMBL:KPI09634.1};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000461,
KW ECO:0000313|EMBL:KPI09634.1}.
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 413 AA; 45573 MW; 07937E9B9072E921 CRC64;
MTENVADTET AEATPEYPSP RSAQCPFAPP PGLLDLHDSG KSVVRARTWD GSTPWIVTRH
AALREILADP RVSADIGGPG YPHTTEAMKA HAAEMQPSIN NTDGAEHSRW RRMLTSSFTR
HRMEKLRPAI RQITDDLIDK MLAGPNPTDL NTALSLPLPS LMICELLGVP YEDHEFFQEH
AGVTNARFKS PQEAAETTRE LRRYISGLIE AKMDDPAEDV LSDLGARVKE GDLSLAEAAP
LGHILLVAGH DTSANMITLG TALLLQNPDQ LAALRENCDD PKFVANAVEE LLRYLTIPHL
LARRAVVEDI EIDGETIRAG EGVIAALPAA NWDPLAFPEP EKLDLARRAA HHVAFSWGPH
QCIGQQLARI ELHIVFSTLF RRVPTLRLAV DVSELKFKED SQAYGIYELP VTW
//
