ID A0A1E7K636_9ACTN Unreviewed; 454 AA.
AC A0A1E7K636;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Dimethylaniline monooxygenase {ECO:0000313|EMBL:OEU99383.1};
GN ORFNames=AN217_17945 {ECO:0000313|EMBL:OEU99383.1};
OS Streptomyces qinglanensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=943816 {ECO:0000313|EMBL:OEU99383.1, ECO:0000313|Proteomes:UP000175829};
RN [1] {ECO:0000313|EMBL:OEU99383.1, ECO:0000313|Proteomes:UP000175829}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCSIO M10379 {ECO:0000313|EMBL:OEU99383.1,
RC ECO:0000313|Proteomes:UP000175829};
RX PubMed=27446038; DOI=10.3389/fmicb.2016.00998;
RA Tian X., Zhang Z., Yang T., Chen M., Li J., Chen F., Yang J., Li W.,
RA Zhang B., Zhang Z., Wu J., Zhang C., Long L., Xiao J.;
RT "Comparative Genomics Analysis of Streptomyces Species Reveals Their
RT Adaptation to the Marine Environment and Their Diversity at the Genomic
RT Level.";
RL Front. Microbiol. 7:998-998(2016).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-dithiol + NADP(+) = [thioredoxin]-disulfide +
CC H(+) + NADPH; Xref=Rhea:RHEA:20345, Rhea:RHEA-COMP:10698, Rhea:RHEA-
CC COMP:10700, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.9;
CC Evidence={ECO:0000256|ARBA:ARBA00000849};
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:OEU99383.1}.
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DR EMBL; LJGV01000022; OEU99383.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E7K636; -.
DR PATRIC; fig|943816.4.peg.3078; -.
DR Proteomes; UP000175829; Unassembled WGS sequence.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR PANTHER; PTHR48105; THIOREDOXIN REDUCTASE 1-RELATED-RELATED; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00469; PNDRDTASEII.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 4: Predicted;
KW Monooxygenase {ECO:0000313|EMBL:OEU99383.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000175829}.
FT DOMAIN 2..206
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT REGION 414..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 454 AA; 48251 MW; 5925FD9BA143AE49 CRC64;
MYDLVVVGAG PYGLSVASHA AAAGLRLRVL GRPMASWRDH MPRGMFLKSE PGASALSDPE
SAHTLTAYCA DRGIEVGHGR PLPLDTFTEY GTWFGSRAAP PAEDLTVTRV APHQSGFRIR
TAEGEQLTTR AVALAVGVLP FAHRPAALRG LPGDLASHST HHRDLSRFRG QDVTVVGAGQ
AALETAALLA EAGAEPRVVA RAPRLNWNTP PKPLDRGRLG GLLDPHSALG TGWPTWVWSR
HPGAVRRLPT ALRLHIARNA LGPAGAWWLR ERFEPVVPTL LGHTITAADR TAGGIRRVGN
GPGSRVRLWL RAADGTARTL ETDHVVAATG FAPELFRLGL LDSTLRETLR RVGESDGPWL
GHDFESSHPG LFFAGLLTAP SFGPAMRFVH GAGFTAPRLV AGVCRHVAAR RAAEATRATG
GTGQSPRVAV PRSATREPAA GETQTPGREV KASR
//
