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Database: UniProt
Entry: A0A1Q5N8D1_9ACTN
LinkDB: A0A1Q5N8D1_9ACTN
Original site: A0A1Q5N8D1_9ACTN 
ID   A0A1Q5N8D1_9ACTN        Unreviewed;       750 AA.
AC   A0A1Q5N8D1;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=Salicylyl-CoA 5-hydroxylase {ECO:0000313|EMBL:OKK22699.1};
GN   ORFNames=AMK16_06410 {ECO:0000313|EMBL:OKK22699.1};
OS   Streptomyces sp. CB00455.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1703927 {ECO:0000313|EMBL:OKK22699.1, ECO:0000313|Proteomes:UP000185643};
RN   [1] {ECO:0000313|EMBL:OKK22699.1, ECO:0000313|Proteomes:UP000185643}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CB00455 {ECO:0000313|EMBL:OKK22699.1,
RC   ECO:0000313|Proteomes:UP000185643};
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   -!- 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:OKK22699.1}.
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DR   EMBL; LIVQ01000001; OKK22699.1; -; Genomic_DNA.
DR   RefSeq; WP_073909615.1; NZ_LIVQ01000001.1.
DR   AlphaFoldDB; A0A1Q5N8D1; -.
DR   STRING; 1703927.AMK16_06410; -.
DR   OrthoDB; 3169239at2; -.
DR   Proteomes; UP000185643; Unassembled WGS sequence.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0003959; F:NADPH dehydrogenase activity; IEA:InterPro.
DR   CDD; cd02932; OYE_YqiM_FMN; 1.
DR   Gene3D; 3.30.9.20; -; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR002938; FAD-bd.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR001155; OxRdtase_FMN_N.
DR   InterPro; IPR044152; YqjM-like.
DR   PANTHER; PTHR43303:SF3; BLR3436 PROTEIN; 1.
DR   PANTHER; PTHR43303; NADPH DEHYDROGENASE C23G7.10C-RELATED; 1.
DR   Pfam; PF01494; FAD_binding_3; 1.
DR   Pfam; PF00724; Oxidored_FMN; 1.
DR   PRINTS; PR00420; RNGMNOXGNASE.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000185643}.
FT   DOMAIN          7..321
FT                   /note="FAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01494"
FT   DOMAIN          387..722
FT                   /note="NADH:flavin oxidoreductase/NADH oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00724"
SQ   SEQUENCE   750 AA;  80311 MW;  DC69EBDD81EE6B0F CRC64;
     MSAGALRVAV VGGGPGGLYA AALLARQGHG VEVWERGAPD ETFGFGVVLS DETLGGIEQA
     DTVVHAALSS QFVRWDDVDI VHRGRLLTSG GHGFAALGRR RLLEILHERC AGLGVRLRFR
     TGPVDAAALA GSHDLVVAAD GVHSATRQAG AAHFGPTVTS GRCRYIWLAA DFAFDAFRFE
     IAETGHGVMQ LHAYPYAADA STVIVEMREE VWRRAGFDLC DETESADRCA KIFSEALRGR
     PLHGNRSAWN RFHTVVNSRW SHGNVVLLGD AAHTAHFSIG SGTKLAVEDA LALAGALAGQ
     DGVPRALAAY EAARRPAVAS TQRAAAASMR WFEEVAGYAG QPARQFAFNL LTRSRRVTHE
     NLRLRDERFA RAVERDFGCP DEDTPPMFTP FTLRGLTLRN RVVVSPMDVY SAREGVPGDF
     HLVHLGARAL GGAGLVMTEM VCVSAEGRIT PGCTGLYTRE QAAAWQRITD FVHTSAPGTA
     LGVQLGHSGR KGSTRVMWEG MDEPLPDGNW PLTAASELPY LPGVSAVPRA LTEADMAKVR
     SDFAAAAVRA ADCGFDLLEL HCAHGYLLSG FLSPLTNRRS DAYGGSLENR LRFPLEVFDA
     VRAVWPGDRP MTVRLSATDW APGGTSPQEA VRIAAAFAAR GADAIDVSTG QVVADETPEY
     GRSYQTPYAD RIRNALGIPV IAVGAISSWD DVNSLLLAGR ADLCAVGRPH LFDPHWTLHA
     AADQAYEGPA APWPLPYRAG SRRPPTGRGA
//
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