ID A0A024JZQ2_9MYCO Unreviewed; 414 AA.
AC A0A024JZQ2;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Cytochrome P450 {ECO:0000313|EMBL:CDO89141.1};
GN ORFNames=BN973_03512 {ECO:0000313|EMBL:CDO89141.1};
OS Mycobacterium triplex.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium simiae complex.
OX NCBI_TaxID=47839 {ECO:0000313|EMBL:CDO89141.1};
RN [1] {ECO:0000313|EMBL:CDO89141.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44626 {ECO:0000313|EMBL:CDO89141.1};
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:CDO89141.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 44626 {ECO:0000313|EMBL:CDO89141.1};
RA Xu Y.W., Yang Q.;
RL Submitted (APR-2014) 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}.
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DR EMBL; HG964446; CDO89141.1; -; Genomic_DNA.
DR RefSeq; WP_036469630.1; NZ_LQPY01000015.1.
DR AlphaFoldDB; A0A024JZQ2; -.
DR STRING; 47839.BN973_03512; -.
DR eggNOG; COG2124; Bacteria.
DR HOGENOM; CLU_033716_2_0_11; -.
DR OrthoDB; 3455208at2; -.
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 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; 2.
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 414 AA; 45716 MW; 7FE775084A2004BF CRC64;
MTVGTAKPSI FDADLPVLDY AVTDTPQQIY PQFRAAQQVA PIALGPVGPE TLSYELARTV
LGDPRFGIPP GIHLTAHGVT SGELWDRVVA SILCMEGTEH RRLRSLVSKA FTPRATARMD
STIHAVINEL TDAVVAAGNC EFVEEIARPY PIPVICALLG APREDWQLFS TWAEDIFKIV
SFDCNLAEEE PKVLKAWDAF DEYIDGMIAE RRKSLTDDLL SELIRAEDRG DRLNASEVRM
LAFSILVAGT DTTRTQLAAS MQVLSEHPEQ WALLRDNPEL GMKAVEETMR HSPSMCSTLR
SAIDDVTIGE YTFPAGTFII VNTYAANRDP SIYDDPTRFD ITRNDPPPIL TFGGGAHYCL
GANLARRELS EALKILAHRL PHPRCTENPP WRPLLGMSGP TRLQLEFDTS AAAE
//
