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Database: UniProt
Entry: A0A285E656_9ACTN
LinkDB: A0A285E656_9ACTN
Original site: A0A285E656_9ACTN 
ID   A0A285E656_9ACTN        Unreviewed;       403 AA.
AC   A0A285E656;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=Cytochrome P450 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=SAMN06893097_101385 {ECO:0000313|EMBL:SNX94588.1};
OS   Geodermatophilus sabuli.
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Geodermatophilus.
OX   NCBI_TaxID=1564158 {ECO:0000313|EMBL:SNX94588.1, ECO:0000313|Proteomes:UP000219514};
RN   [1] {ECO:0000313|EMBL:SNX94588.1, ECO:0000313|Proteomes:UP000219514}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 46844 {ECO:0000313|EMBL:SNX94588.1,
RC   ECO:0000313|Proteomes:UP000219514};
RA   Ehlers B., Leendertz F.H.;
RL   Submitted (SEP-2017) 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; OBDO01000001; SNX94588.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A285E656; -.
DR   OrthoDB; 9801155at2; -.
DR   Proteomes; UP000219514; 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   CDD; cd11037; CYP199A2-like; 1.
DR   Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR   InterPro; IPR001128; Cyt_P450.
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   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:UP000219514}.
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   403 AA;  44200 MW;  C8DC97937623A39C CRC64;
     MTATVDTGTD LPTNNTDPFS HEVLEDPAPL HHELREAGPV VRLTAYGVYA LARYEQVHAA
     LVDWQGFQSA AGVGLSNFRF EEPWRPPSLL LEADPPRHDA PRRVLQKVLS PRSLRRLRDQ
     WLADGDTLVE EVLARGTEFD AVPALAEAFP LRVFPDAVGL SPEGRENLLP LGDHNFNAFG
     PANDLVAKGA PRVAELMGWA TARCQRDALS PGGFGAQIWS AADRGEITTQ QAPLVTRSLL
     LAGVDTTVHG LSAVLYAFAT NPDQWRRLRA QPGLARVAFD EAVRWESPVQ TFFRTATSDI
     RVGEHVIPDG QKILMFLGAA NRDPRRWTDP DVFDLGRDPS GHVGFGMGIH QCIGQHVARL
     EAEALLTALA KRVRTIELAA PTKRHHNNTL RAWASIPLRV GLA
//
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