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Database: UniProt
Entry: E6JBA3_9ACTN
LinkDB: E6JBA3_9ACTN
Original site: E6JBA3_9ACTN 
ID   E6JBA3_9ACTN            Unreviewed;       405 AA.
AC   E6JBA3;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   SubName: Full=Cytochrome P450 monooxygenase {ECO:0000313|EMBL:EFV91134.1};
GN   ORFNames=ES5_12575 {ECO:0000313|EMBL:EFV91134.1};
OS   Dietzia cinnamea P4.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Dietziaceae;
OC   Dietzia.
OX   NCBI_TaxID=910954 {ECO:0000313|EMBL:EFV91134.1, ECO:0000313|Proteomes:UP000004165};
RN   [1] {ECO:0000313|EMBL:EFV91134.1, ECO:0000313|Proteomes:UP000004165}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P4 {ECO:0000313|EMBL:EFV91134.1,
RC   ECO:0000313|Proteomes:UP000004165};
RX   PubMed=21901521; DOI=10.1007/s10482-011-9633-7;
RA   Procopio L., Alvarez V.M., Jurelevicius D.A., Hansen L., Sorensen S.J.,
RA   Cardoso J.S., Padula M., Leitao A.C., Seldin L., van Elsas J.D.;
RT   "Insight from the draft genome of Dietzia cinnamea P4 reveals mechanisms of
RT   survival in complex tropical soil habitats and biotechnology potential.";
RL   Antonie Van Leeuwenhoek 101:289-302(2012).
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:EFV91134.1}.
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DR   EMBL; AEKG01000309; EFV91134.1; -; Genomic_DNA.
DR   RefSeq; WP_007631658.1; NZ_AEKG01000309.1.
DR   AlphaFoldDB; E6JBA3; -.
DR   Proteomes; UP000004165; 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; cd11078; CYP130-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, ECO:0000313|EMBL:EFV91134.1};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000461}.
SQ   SEQUENCE   405 AA;  45301 MW;  18F08CA009C280F8 CRC64;
     MTTSAPTPLV FSPYDYAVHE DPYPYYARLR AEAPVYHNAE LGFWALSRHA DVREAFRAPD
     VFSNAMGVSL DPAAYGPHAY KTMSFLAMDD PRHARLRKLV SKGFTSRRVD ALSDGIAAIS
     RQYWDECLAR SRDGEAFDFV EDYAGKLPMD VISDLMGVPE ADRAELRRLA DLVMHREEGV
     EDVPQESMVA ALDLITYYQG MVAERRRVRT EDLTSALLDA EIDGEKLDED EILSFLFLMV
     VAGNETTTKL LANALFWGHE NPDQSRAVLD DPELAPAWVE ETLRFDTSSQ LVLRTTTQET
     TVRGVTIPAD RKVLLLIGSA NRDEEVFERG DTFDLARDTS ASLSFGQGPH FCLGAHLARL
     EGRIALDMIS RSITGYELLP GAQRVHSSNV RGFAHLPMRV EVARR
//
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