ID A0A0M3UAY0_9PSEU Unreviewed; 444 AA.
AC A0A0M3UAY0;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Cytochrome P450 {ECO:0000313|EMBL:ALE83275.1};
GN ORFNames=XF36_08970 {ECO:0000313|EMBL:ALE83275.1};
OS Pseudonocardia sp. HH130629-09.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Pseudonocardia.
OX NCBI_TaxID=1641402 {ECO:0000313|EMBL:ALE83275.1, ECO:0000313|Proteomes:UP000062082};
RN [1] {ECO:0000313|EMBL:ALE83275.1, ECO:0000313|Proteomes:UP000062082}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HH130629-09 {ECO:0000313|EMBL:ALE83275.1,
RC ECO:0000313|Proteomes:UP000062082};
RX PubMed=26438860; DOI=10.1073/pnas.1515348112;
RA Sit C.S., Van Arnam E.B., Ramadhar T.R.;
RT "Variable genetic architectures produce virtually identical molecules in
RT bacterial symbionts of fungus-growing ants.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:13150-13154(2015).
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
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DR EMBL; CP011868; ALE83275.1; -; Genomic_DNA.
DR RefSeq; WP_060711638.1; NZ_CP011868.1.
DR AlphaFoldDB; A0A0M3UAY0; -.
DR KEGG; pseh:XF36_08970; -.
DR PATRIC; fig|1641402.3.peg.1920; -.
DR Proteomes; UP000062082; 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; cd20625; CYP164-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; P450, PUTATIVE (EUROFUNG)-RELATED; 1.
DR PANTHER; PTHR46696:SF1; 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};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000461};
KW Reference proteome {ECO:0000313|Proteomes:UP000062082}.
SQ SEQUENCE 444 AA; 49110 MW; 2AEC2280FAE0D716 CRC64;
MAASRGARRW IRWVLRHGAM RQEVTRQAGK GDLGAHMIIS PEVVRDPYPA YEQIRGQGRM
VRSALTWTTV DHEITTEVLR SPDFCVGMRM PENAPGLLRA LLAAGGTWPL GPAEPPSLLS
IDPPDHNRIR KLVTRSFSAK AISSLRGRTE EIAAQLLAEL EAGTDRRTDV ISGYASLLPA
TVITEMLGAP VEMRERFLEW GEGGAYSLDM GLDYATFRRS ERDIDALTEW MSGHFERLRR
EPNDSILSSL VATYDEEEGR LTHDELLSLA MLLLAAGFET TVNLIGNGTR LLLTHPDQLA
RLQADPALWP NAVDEVLRFD SPVQRTGRVA ARDTELCGFP VRRGSLVLTH LGGANRDPDV
FPDPARFDVG REGADRHVAF SQGIHYCLGA ALAKMEGEVG LRALFDRYPD LRADGPAELR
GTRVLRGYRT LPVRLGDARV HVDA
//
