ID U5VXN2_9ACTN Unreviewed; 390 AA.
AC U5VXN2;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE SubName: Full=Cytochrome P450 {ECO:0000313|EMBL:AGZ41614.1};
GN ORFNames=AFR_16680 {ECO:0000313|EMBL:AGZ41614.1};
OS Actinoplanes friuliensis DSM 7358.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=1246995 {ECO:0000313|EMBL:AGZ41614.1, ECO:0000313|Proteomes:UP000017746};
RN [1] {ECO:0000313|EMBL:AGZ41614.1, ECO:0000313|Proteomes:UP000017746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7358 {ECO:0000313|EMBL:AGZ41614.1,
RC ECO:0000313|Proteomes:UP000017746};
RX PubMed=24637369; DOI=10.1016/j.jbiotec.2014.03.011;
RA Ruckert C., Szczepanowski R., Albersmeier A., Goesmann A., Fischer N.,
RA Steinkamper A., Puhler A., Biener R., Schwartz D., Kalinowski J.;
RT "Complete genome sequence of the actinobacterium Actinoplanes friuliensis
RT HAG 010964, producer of the lipopeptide antibiotic friulimycin.";
RL J. Biotechnol. 178:41-42(2014).
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
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DR EMBL; CP006272; AGZ41614.1; -; Genomic_DNA.
DR RefSeq; WP_023361702.1; NC_022657.1.
DR AlphaFoldDB; U5VXN2; -.
DR STRING; 1246995.AFR_16680; -.
DR KEGG; afs:AFR_16680; -.
DR PATRIC; fig|1246995.3.peg.3382; -.
DR eggNOG; COG2124; Bacteria.
DR HOGENOM; CLU_033716_0_2_11; -.
DR OrthoDB; 4156795at2; -.
DR Proteomes; UP000017746; 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:UP000017746}.
SQ SEQUENCE 390 AA; 42310 MW; D6131704D94652E2 CRC64;
MEVDFADPGF VRDPYPVLGL LREQAPVSRH EPTGRWLAAS HAAANAVLRD RRLGRFWQDR
EPAEVYEPFN LLHRHQMMEN EPPVHTRLRS LVAKAFVRGH VERLRPAVAA EAGALLRAAG
PEFDLLADVA EPLAVTVIAE LLGVPVADRH RLRPWSAAIV RMYEVTRTPE VEAAALTAAA
EFADYLRDLA DRRRAEPRDD LVSHLVTVRD GTDKLSADEL VASAILLLNA GHEASVNALG
GGVVALLRHP DQLARLRADR GLIPAAGEEM IRYDPPLHMF VRIAAADVQV EGVTIPAGAE
VAALLGAANR DPAVFAEPDT FDVGRDPNPH LGFGAGLHFC LGAPLARIEL QAGLAALLDL
PALALAAEPV QRPTFVLRAY TAVRLTTRQT
//
