ID A0A024K097_9MYCO Unreviewed; 391 AA.
AC A0A024K097;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Cytochrome P450 superfamily protein {ECO:0000313|EMBL:CDO89341.1};
GN ORFNames=BN973_03716 {ECO:0000313|EMBL:CDO89341.1};
OS Mycobacterium triplex.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium simiae complex.
OX NCBI_TaxID=47839 {ECO:0000313|EMBL:CDO89341.1};
RN [1] {ECO:0000313|EMBL:CDO89341.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44626 {ECO:0000313|EMBL:CDO89341.1};
RX PubMed=24874681; DOI=10.1128/genomeA.00499-14;
RA Sassi M., Croce O., Robert C., Raoult D., Drancourt M.;
RT "Draft Genome Sequence of Mycobacterium triplex DSM 44626.";
RL Genome Announc. Announc.2:e00499-e00414(2014).
RN [2] {ECO:0000313|EMBL:CDO89341.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 44626 {ECO:0000313|EMBL:CDO89341.1};
RA Urmite Genomes U.;
RL Submitted (APR-2014) 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; HG964446; CDO89341.1; -; Genomic_DNA.
DR RefSeq; WP_036469910.1; NZ_LQPY01000017.1.
DR AlphaFoldDB; A0A024K097; -.
DR STRING; 47839.BN973_03716; -.
DR eggNOG; COG2124; Bacteria.
DR HOGENOM; CLU_033716_0_1_11; -.
DR OrthoDB; 3599725at2; -.
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; cd11035; P450cam-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: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}.
SQ SEQUENCE 391 AA; 43929 MW; 601E3D71817DBE6A CRC64;
MTEAQGFVDQ TMMGIAEPQP MYKTLRESSP VFRSDQAVVL SRLADIEMAL KHTELFSSNM
DAVNLGNIRP LIPLQIDPPE HAKYRRVLDP LFTPREMARR EPRVTELVNE MIDRFAGRGE
CDFHAEFAVP LPCTVFLQLL GLPLADLDKF LEWKDGVIRP EGDSGFNRRH ESSAPVAQQI
YDYFERAIDD HIANPRDDVL SAMIAANLNA EGRPLSREEL LDICFLFLIA GLDTVTDSLD
CFFVYLARHP GHRHQLVEQP DVLPHAVEEL LRWETPVPGV ARVAMQDVEV GGCPISKGER
VSPLLGAANT DPAEFPDPEV VDFTRNPNRH RAFGGGPHRC LGSHLARMEL RVALREFHRR
IPDYEIKPGT QLAYTAALRS VESLPLIFAV S
//
