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Database: UniProt
Entry: A0A0F7JK56_9DEIO
LinkDB: A0A0F7JK56_9DEIO
Original site: A0A0F7JK56_9DEIO 
ID   A0A0F7JK56_9DEIO        Unreviewed;       405 AA.
AC   A0A0F7JK56;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=Cytochrome P450 {ECO:0000313|EMBL:AKH16516.1};
GN   ORFNames=SY84_04975 {ECO:0000313|EMBL:AKH16516.1};
OS   Deinococcus soli (ex Cha et al. 2016).
OC   Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=1309411 {ECO:0000313|EMBL:AKH16516.1, ECO:0000313|Proteomes:UP000034024};
RN   [1] {ECO:0000313|EMBL:AKH16516.1, ECO:0000313|Proteomes:UP000034024}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N5 {ECO:0000313|EMBL:AKH16516.1,
RC   ECO:0000313|Proteomes:UP000034024};
RA   Kim M.K., Srinivasan S., Lee J.-J.;
RT   "Deinococcus soli/N5/whole genome sequencing.";
RL   Submitted (JAN-2015) 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; CP011389; AKH16516.1; -; Genomic_DNA.
DR   RefSeq; WP_046843091.1; NZ_CP011389.1.
DR   AlphaFoldDB; A0A0F7JK56; -.
DR   KEGG; dch:SY84_04975; -.
DR   PATRIC; fig|1309411.5.peg.1022; -.
DR   OrthoDB; 54272at2; -.
DR   Proteomes; UP000034024; Chromosome.
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:SF2; CYTOCHROME P450 130; 1.
DR   PANTHER; PTHR46696; 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:UP000034024}.
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   405 AA;  44382 MW;  37FF988424EDAE9B CRC64;
     MTINESSPPE PARCPFGGDS LTRRDTAQPG AAPQADARGV VQVRSFQAAR DVLRSEAVTQ
     AGFNAETVND AGILKRRPVL FTEGEEHHEM RRDTARYFTP AAVAGYQPMI AALADRLIGQ
     LAARGEANID DLSLTLAVQV ASQVVGLTSS RLPGLERRVM TFVEHDGNSE PGMSPEKGRL
     AGILDQRHLL AFYLLDVKPA IQARRKQRRD DLISHLLDRD YSDLEILTEC LTYGTAGMVT
     TREFITVATW HLLRAPELRA AYVHGTEKER LDILHEILRV EPVVSTLYRR AQAELTVDGH
     TVPQGTLLAL NLADANTDPA VAGEQAGSVC PARPLPRGVQ APVMAFGDGH HRCPGAFLAI
     KETDTFLRRL LIWQDLRLVA EPRVTFNEVV KGYELRGLRV ALGGA
//
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