ID A8LAQ2_FRASN Unreviewed; 398 AA.
AC A8LAQ2;
DT 04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT 04-DEC-2007, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE SubName: Full=Cytochrome P450 {ECO:0000313|EMBL:ABW13827.1};
GN ORFNames=Franean1_4449 {ECO:0000313|EMBL:ABW13827.1};
OS Frankia sp. (strain EAN1pec).
OC Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; Frankia.
OX NCBI_TaxID=298653 {ECO:0000313|EMBL:ABW13827.1};
RN [1] {ECO:0000313|EMBL:ABW13827.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=EAN1.pec {ECO:0000313|EMBL:ABW13827.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Hammon N.,
RA Israni S., Dalin E., Tice H., Pitluck S., Saunders E., Brettin T.,
RA Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Kim E., Rawnsley T., Niemann J., Benson D.R., Huang Y.,
RA Mastronunzio J., Bassi C.A., Tisa L.S., Richardson P.;
RT "Complete sequence of Frankia sp. EAN1pec.";
RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
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DR EMBL; CP000820; ABW13827.1; -; Genomic_DNA.
DR AlphaFoldDB; A8LAQ2; -.
DR STRING; 298653.Franean1_4449; -.
DR KEGG; fre:Franean1_4449; -.
DR eggNOG; COG2124; Bacteria.
DR HOGENOM; CLU_033716_2_0_11; -.
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}.
SQ SEQUENCE 398 AA; 45250 MW; 794A00F9AFCD18A7 CRC64;
MRFDPTAAAI KADPYPAYAR LRAEAPVEWN DLGFWTVARH QDCLFALRDK RLGKEHPFAW
AIENPDLPLI QIHDAMMIFH DGQAHRRVRR LFTSAFTTRA ADRLRPDIAA IVDELLAELV
ERDEFDLVSQ FCYPVTLRTI CYMLGVPRSD IDWCHSLTKN VQRLLEQDLS RAELVQISDS
TVTLSEYFAE HVRDRRRNPK DDLISLLVQA EIDGERLTEE EIIANSILLY LGGEDTNANL
MANSTLALLA APDQAELLRH DAGVVHATAF DELLRYDSSF QMLTRYANEP VEIGGQRIEE
GQTVMCLLGS ANRDEREYER PDELDLRRVV KRGVSFGGGP HLCVGAPLAR AQLQEALPRL
FRAFPWMQNL TEELEYPLLV VRGPKELTLA TGKQRVMA
//