ID D1AD57_THECD Unreviewed; 485 AA.
AC D1AD57;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=FAD-dependent pyridine nucleotide-disulphide oxidoreductase {ECO:0000313|EMBL:ACY99366.1};
GN OrderedLocusNames=Tcur_3835 {ECO:0000313|EMBL:ACY99366.1};
OS Thermomonospora curvata (strain ATCC 19995 / DSM 43183 / JCM 3096 / KCTC
OS 9072 / NBRC 15933 / NCIMB 10081 / Henssen B9).
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Thermomonosporaceae; Thermomonospora.
OX NCBI_TaxID=471852 {ECO:0000313|EMBL:ACY99366.1, ECO:0000313|Proteomes:UP000001918};
RN [1] {ECO:0000313|EMBL:ACY99366.1, ECO:0000313|Proteomes:UP000001918}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19995 / DSM 43183 / JCM 3096 / KCTC 9072 / NBRC 15933 /
RC NCIMB 10081 / Henssen B9 {ECO:0000313|Proteomes:UP000001918};
RX PubMed=21475583; DOI=10.4056/sigs.1453580;
RA Chertkov O., Sikorski J., Nolan M., Lapidus A., Lucas S., Del Rio T.G.,
RA Tice H., Cheng J.F., Goodwin L., Pitluck S., Liolios K., Ivanova N.,
RA Mavromatis K., Mikhailova N., Ovchinnikova G., Pati A., Chen A.,
RA Palaniappan K., Djao O.D., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA Brettin T., Han C., Detter J.C., Rohde M., Goker M., Woyke T., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Thermomonospora curvata type strain (B9).";
RL Stand. Genomic Sci. 1:13-22(2011).
CC -!- SIMILARITY: Belongs to the FAD-binding monooxygenase family.
CC {ECO:0000256|ARBA:ARBA00010139}.
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DR EMBL; CP001738; ACY99366.1; -; Genomic_DNA.
DR RefSeq; WP_012854150.1; NC_013510.1.
DR AlphaFoldDB; D1AD57; -.
DR STRING; 471852.Tcur_3835; -.
DR KEGG; tcu:Tcur_3835; -.
DR eggNOG; COG2072; Bacteria.
DR HOGENOM; CLU_006937_7_1_11; -.
DR OrthoDB; 5168853at2; -.
DR Proteomes; UP000001918; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0004499; F:N,N-dimethylaniline monooxygenase activity; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR020946; Flavin_mOase-like.
DR PANTHER; PTHR42877; -; 1.
DR PANTHER; PTHR42877:SF4; FAD_NAD(P)-BINDING DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR Pfam; PF00743; FMO-like; 1.
DR PRINTS; PR00419; ADXRDTASE.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000001918}.
SQ SEQUENCE 485 AA; 55160 MW; 6EB756A13D4F9D1B CRC64;
MSENPSVVIV GSGFAGLGMA IQLIKAGFHD FVILEKDKEL GGTWRDNTYP GCACDVPSHM
YSYSFELNPR WSRLFAPQQE IWDYMRDVAA KYGLEKYLRY DSRVDALEYD DQARRWDVIV
ADGRRYRPRA VIYGIGALHV PSYPDLPGLP KFQGKTFHSA EWDHDYDLTG KRVAVIGTGA
SAIQFVPQVA KKASQLYVFQ RTAPWIQPKP DVAIPKSAQW LFEHVPGTAR VFRDALFWIL
EGRALGFALD PRLMAPLEHS ARSHLKRQIP DPELRRKLTP NYRIGCKRIL LSNDYYPTFN
LPHVELVTEG IGEVTENAIV TGDGRELEVD CIIYGTGFKV VETLASQHIV GRNGLKIQEA
WADGAEAYHG VTIPGFPNFF MLMGPNTGLG HHSMIFMMEA QFQHILGCLR LIQRQGGDTI
EVTRRALRRY NDRMHRRLRK GVWNEGGCQS WYLDENGVNR TLWPGFAFEY WAGTRRVKAS
DYVVS
//
