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Database: UniProt
Entry: A0A2K9EJX6_9RHOB
LinkDB: A0A2K9EJX6_9RHOB
Original site: A0A2K9EJX6_9RHOB 
ID   A0A2K9EJX6_9RHOB        Unreviewed;       448 AA.
AC   A0A2K9EJX6;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=Cytochrome P450 {ECO:0000313|EMBL:AUH34689.1};
GN   ORFNames=CUV01_16025 {ECO:0000313|EMBL:AUH34689.1};
OS   Paracoccus tegillarcae.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Paracoccus.
OX   NCBI_TaxID=1529068 {ECO:0000313|EMBL:AUH34689.1, ECO:0000313|Proteomes:UP000233742};
RN   [1] {ECO:0000313|EMBL:AUH34689.1, ECO:0000313|Proteomes:UP000233742}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BM15 {ECO:0000313|EMBL:AUH34689.1,
RC   ECO:0000313|Proteomes:UP000233742};
RA   Hurst M.R.H.;
RL   Submitted (DEC-2017) 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|RuleBase:RU000461}.
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DR   EMBL; CP025408; AUH34689.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2K9EJX6; -.
DR   KEGG; paro:CUV01_16025; -.
DR   OrthoDB; 9764248at2; -.
DR   Proteomes; UP000233742; 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   Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002401; Cyt_P450_E_grp-I.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   PANTHER; PTHR24305; CYTOCHROME P450; 1.
DR   PANTHER; PTHR24305:SF166; CYTOCHROME P450 12A4, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233742}.
SQ   SEQUENCE   448 AA;  50060 MW;  DB6945177FBAB480 CRC64;
     MIPPKPQASP KRGGILRMVR GFRRDLLSAL PANLFHAWMA EFRNPLIHSF VCNDPALVRL
     ILQERPAEFP KSNRLREGLA PLLGNSVFLT NGEEWQSQRR IIDPAFEGGR LREVFPALLD
     AAQAVAARLP VGEIDIEPEA SHAAADAIFR TLFSLPIEHQ VAERVFGAFR AHQAAQPIVN
     LAALLPLPNW LPRLHSRRTR ETAAEIRGLI RGLVEDRMRA ITEGTAPDDL ATKIMTTPDP
     QTGRTFTAPE MIDQVAIFFL AGHETSASAL SWALWLLAAN PEWQDLVAQE AATMTEDMAG
     LSRLKVTRAV FREALRLYPP VPMMVREAAC PQHFRDREVP RGAQLILSPW HLHRHDRLWD
     RPDTFDPGRW DSDAGRVSAR NAYIPFSAGQ RVCPGAGFAM LEGVLMLALI TRAFRLSPGQ
     VDPVPVARLT LRGRDGILIK LERRQERA
//
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