ID   A0A1H9X3T1_9PSEU        Unreviewed;       472 AA.
AC   A0A1H9X3T1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Cytochrome P450 {ECO:0000313|EMBL:SES40701.1};
GN   ORFNames=SAMN04488000_12722 {ECO:0000313|EMBL:SES40701.1};
OS   Lentzea albida.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Lentzea.
OX   NCBI_TaxID=65499 {ECO:0000313|EMBL:SES40701.1, ECO:0000313|Proteomes:UP000199503};
RN   [1] {ECO:0000313|EMBL:SES40701.1, ECO:0000313|Proteomes:UP000199503}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44437 {ECO:0000313|EMBL:SES40701.1,
RC   ECO:0000313|Proteomes:UP000199503};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|ARBA:ARBA00001971,
CC         ECO:0000256|PIRSR:PIRSR602403-1};
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC       {ECO:0000256|RuleBase:RU000461}.
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DR   EMBL; FOFV01000027; SES40701.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H9X3T1; -.
DR   STRING; 65499.SAMN04488000_12722; -.
DR   OrthoDB; 5290182at2; -.
DR   Proteomes; UP000199503; 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   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; PTHR24305; CYTOCHROME P450; 1.
DR   PANTHER; PTHR24305:SF166; CYTOCHROME P450 12A4, MITOCHONDRIAL-RELATED; 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|PIRSR:PIRSR602403-1, ECO:0000256|RuleBase:RU000461};
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          30..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         420
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   472 AA;  52407 MW;  868905CF3D0F0625 CRC64;
     MTHEQETRRL SIGTVPVPRW LETRALRGGA ARTRHLAEPP PGSGLRAVPG DAGLPLVGHG
     LEWMRYGPRF ERARVTRYGP VSWMKAFGVK MAVVGGADAT QAVLTNKDKA FSQAGWNLFL
     DPFFKRGLLM LDDEHLQHRR IMQQAFTRPR LAGYAEVAGR VVRAGLADLP DRFTVHPAMA
     RLTMGIGSQV FMASSIDTNE PVLRAFRAAV DGTTALARFS VPGGKWQAGS RGRRKLEEYF
     TAALPGKRNS AGNDLFSVLA SAQDEDGQRF TDTEVVDHMI FLMVAALDTS ATTATAAMYH
     LARRPEWQER ARAESVALGP APDLDGLDRL TTLDLVVKES LRLVAPVPTF VRRTVRDVDL
     TGYHVPAGTT TIVMPAANHY DPAYWHDPDA FDPDRFAEPR REDRAHRFAF VPFGGGAHKC
     IGMVLGFLEV KTILHELLLR HRWRLPEGYR MRWDWSNTPS PAGGLPVHLD RI
//