ID J9RQN4_9ACTN Unreviewed; 455 AA.
AC J9RQN4;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Cytochrome P450 {ECO:0000313|EMBL:AFR50417.1};
GN ORFNames=KTR9_3783 {ECO:0000313|EMBL:AFR50417.1};
OS Gordonia sp. KTR9.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=337191 {ECO:0000313|EMBL:AFR50417.1, ECO:0000313|Proteomes:UP000003281};
RN [1] {ECO:0000313|EMBL:AFR50417.1, ECO:0000313|Proteomes:UP000003281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KTR9 {ECO:0000313|EMBL:AFR50417.1,
RC ECO:0000313|Proteomes:UP000003281};
RX PubMed=22923396; DOI=10.1128/AEM.02120-12;
RA Chen H.P., Zhu S.H., Casabon I., Hallam S.J., Crocker F.H., Mohn W.W.,
RA Indest K.J., Eltis L.D.;
RT "Genomic and transcriptomic studies of an RDX (hexahydro-1,3,5-
RT trinitro-1,3,5-triazine)-degrading actinobacterium.";
RL Appl. Environ. Microbiol. 78:7798-7800(2012).
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|PIRSR:PIRSR602403-1};
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
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DR EMBL; CP002907; AFR50417.1; -; Genomic_DNA.
DR RefSeq; WP_014927909.1; NC_018581.1.
DR AlphaFoldDB; J9RQN4; -.
DR STRING; 337191.KTR9_3783; -.
DR KEGG; gor:KTR9_3783; -.
DR PATRIC; fig|337191.3.peg.4159; -.
DR eggNOG; COG2124; Bacteria.
DR HOGENOM; CLU_001570_15_0_11; -.
DR Proteomes; UP000003281; 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 CDD; cd11042; CYP51-like; 1.
DR Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR InterPro; IPR036396; Cyt_P450_sf.
DR PANTHER; PTHR24304:SF2; 24-HYDROXYCHOLESTEROL 7-ALPHA-HYDROXYLASE; 1.
DR PANTHER; PTHR24304; CYTOCHROME P450 FAMILY 7; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00465; EP450IV.
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|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR602403-1};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR602403-1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR602403-1};
KW Monooxygenase {ECO:0000256|RuleBase:RU000461};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000461}.
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 398
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR602403-1"
SQ SEQUENCE 455 AA; 51793 MW; 184BF2651C94A5BC CRC64;
MTAITESGLR QPNRVSGGEG EHGHLDELAT DPISLFWRVR EECGDVGLFQ LADREVVLVS
GSAANEEFFR APEEDLDQAA AYPFMTPVFG EGVVFDTSPE ERSKAIHNSA LKGAHMKQHA
VTIPNEVERI IAGWGDEGEI DLLDFFAELT LYTSSSCLIG RKFRERLNGH IAHLFHDLEK
GTDPIAYVDY KADIESFRKR DEARAELVEF IQGVMDERIA NPTEDKEDRD LMDVLVQVGF
DANTVTGMFI SMMFAGHHTT SGTAAWTLIE LLRNPDYMRR VYDELDEIYG ETPPGERPEY
TFAHTRQMPQ LENALKEALR LHPPLIILMR VVQHDFHVED FEVKAGQSIA VSPAISNRLP
EDFPGADSFD PDRYDKPRQE DLVNRWTWIP FGAGRHRCVG AQFAIMQLKA IFSVLFQNYE
FEMLQPPESY RNDHSKMVVQ LQQPCRVAYR KRQDA
//
