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Database: UniProt
Entry: A0A1B8SK78_9MYCO
LinkDB: A0A1B8SK78_9MYCO
Original site: A0A1B8SK78_9MYCO 
ID   A0A1B8SK78_9MYCO        Unreviewed;       396 AA.
AC   A0A1B8SK78;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Cytochrome P450 {ECO:0000313|EMBL:OBY33130.1};
GN   ORFNames=ACT18_03610 {ECO:0000313|EMBL:OBY33130.1};
OS   Mycolicibacter kumamotonensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacter.
OX   NCBI_TaxID=354243 {ECO:0000313|EMBL:OBY33130.1, ECO:0000313|Proteomes:UP000092668};
RN   [1] {ECO:0000313|EMBL:OBY33130.1, ECO:0000313|Proteomes:UP000092668}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Roo {ECO:0000313|EMBL:OBY33130.1,
RC   ECO:0000313|Proteomes:UP000092668};
RA   Greninger A.L., Cunningham G., Miller S.;
RT   "Genome sequence of Mycobacterium kumamotonense strain Roo.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|ARBA:ARBA00001971};
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:OBY33130.1}.
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DR   EMBL; LFOE01000003; OBY33130.1; -; Genomic_DNA.
DR   RefSeq; WP_065287288.1; NZ_LFOE01000003.1.
DR   AlphaFoldDB; A0A1B8SK78; -.
DR   STRING; 354243.BST28_09335; -.
DR   PATRIC; fig|354243.3.peg.768; -.
DR   OrthoDB; 3664945at2; -.
DR   Proteomes; UP000092668; 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};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000461}.
SQ   SEQUENCE   396 AA;  43610 MW;  5FD0B653094BB198 CRC64;
     MSRDGRCPFD PPPETMALAA QAPLSRVRIW DGSTPWLITG YEAVRALFSD PRVSVDDHQP
     GFPHWNEMMR ASVDHRPKSV FTTDGAEHIR YRRILSPALT MKRVDALTPV AQRITDEHID
     AILAGPQPAD LIEGFALPIP SLVISELLGV PYEDHAFFQQ HATMGVDRNA TSDDLAEGAT
     ELSKYLVRLL ETRMAEPADD MVSALGQRVQ NGELSVREAT QLGTGMLIAG HETTANMIGL
     GIVALLGEPD KIDEKTAVFR GDDDAAIANA VEELLRYLSI IHTGQRRVAL EDIEIAGETI
     RAGEGIIIDL APANWDASVF PEPEVLDLAR PARQHMAFGF GPHQCVGQQL ARAEMVIAFR
     TLFRRIPTLK LAVGIDEIPF KDDRLAYGVY ELPVTW
//
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