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Database: UniProt
Entry: A0A1Q5CDR5_9ACTN
LinkDB: A0A1Q5CDR5_9ACTN
Original site: A0A1Q5CDR5_9ACTN 
ID   A0A1Q5CDR5_9ACTN        Unreviewed;       432 AA.
AC   A0A1Q5CDR5;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=Cytochrome {ECO:0000313|EMBL:OKI81742.1};
GN   ORFNames=A6A27_16625 {ECO:0000313|EMBL:OKI81742.1};
OS   Micromonospora sp. CB01531.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=1718947 {ECO:0000313|EMBL:OKI81742.1, ECO:0000313|Proteomes:UP000186700};
RN   [1] {ECO:0000313|EMBL:OKI81742.1, ECO:0000313|Proteomes:UP000186700}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CB01531 {ECO:0000313|EMBL:OKI81742.1,
RC   ECO:0000313|Proteomes:UP000186700};
RX   PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA   Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA   Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA   Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT   "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL   MBio 7:e02104-e02116(2016).
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC       {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OKI81742.1}.
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DR   EMBL; LWLS01000024; OKI81742.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q5CDR5; -.
DR   STRING; 1718947.A6A27_16625; -.
DR   Proteomes; UP000186700; 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; cd11033; CYP142-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:UP000186700}.
SQ   SEQUENCE   432 AA;  47867 MW;  FA5D07ED3994A18A CRC64;
     MVDPRTYVDG VPYHLLATLR AAGPVAWVEE PPLLGLSGGP GFWLVLRHAE VTDVLKQPRL
     FSSWLGATQI RDPATPEDLG YVRRMMLNMD PPEHGRLRRP VARSFTPRAV GALEASIRAT
     AAALVERTLG DADEGTFDFA RDLAADLPLL TLADVLGMPE PDRWLLYDWS NRVIGFQDPD
     HAGSAAFDPR AGTAAAREAL RHRPAPDADG RMPDPRTRAG MADLYAYAHL LAESKRRSPG
     PDVMSILLAQ QGEDRLSVDE FENMFWLFAV AGNETIRNGL PGAMIALLEH PAEMARLRRD
     PDLFDTAVDE LLRWWTPVMV FRRTATTDTA VAGVPVRAGD KVVVSFASAN RDERVFADPD
     RLDLARHPNP HLVFGHGPHF CLGAHLARCQ LRALFEALLA NTASITYAGP PAYLRSNFQR
     GVKRLPIHWR RR
//
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