ID M1QUG4_BACTU Unreviewed; 487 AA.
AC M1QUG4;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Tryptophan 2-monooxygenase {ECO:0000313|EMBL:AGG00710.1};
DE EC=1.13.12.3 {ECO:0000313|EMBL:AGG00710.1};
GN ORFNames=H175_ch1997 {ECO:0000313|EMBL:AGG00710.1};
OS Bacillus thuringiensis serovar thuringiensis str. IS5056.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1286404 {ECO:0000313|EMBL:AGG00710.1};
RN [1] {ECO:0000313|EMBL:AGG00710.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IS5056 {ECO:0000313|EMBL:AGG00710.1};
RX PubMed=23516221;
RA Murawska E., Fiedoruk K., Bideshi D.K., Swiecicka I.;
RT "Complete genome sequence of Bacillus thuringiensis subsp. thuringiensis
RT strain IS5056, an isolate highly toxic to Trichoplusia ni.";
RL Genome Announc. 1:E0010813-E0010813(2013).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP004123; AGG00710.1; -; Genomic_DNA.
DR RefSeq; WP_001168110.1; NC_020376.1.
DR AlphaFoldDB; M1QUG4; -.
DR SMR; M1QUG4; -.
DR GeneID; 67466433; -.
DR KEGG; btht:H175_ch1997; -.
DR PATRIC; fig|1286404.3.peg.2021; -.
DR HOGENOM; CLU_004498_8_3_9; -.
DR Proteomes; UP000011719; Chromosome.
DR GO; GO:0050361; F:tryptophan 2-monooxygenase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.90.660.10; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 1.10.405.10; Guanine Nucleotide Dissociation Inhibitor, domain 1; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR001613; Flavin_amine_oxidase.
DR PANTHER; PTHR10742:SF342; AMINO_OXIDASE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR10742; FLAVIN MONOAMINE OXIDASE; 1.
DR Pfam; PF01593; Amino_oxidase; 1.
DR PRINTS; PR00757; AMINEOXDASEF.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 4: Predicted;
KW Monooxygenase {ECO:0000313|EMBL:AGG00710.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:AGG00710.1}.
FT DOMAIN 38..485
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 487 AA; 55473 MW; A9E36EA3693F8E74 CRC64;
MQKDIMYNTE MDEALKVIDK GLKKTINPKQ IIVVGAGMAG LVSASLLKAA GHDVKIFEAN
NRVGGRIETV RMEDTGLYLD VGAMRIPYSH TLTMAYIRKF GLQVGPFINR NETDIIYVNG
RKTTLKQYEK DPNILRYPVE MNEVGKTSEE LLLLAVQPII NFIKRNPEKN WDVVVKDFGR
YSTGQFLKYH PYQYNTYFSP VTIEMIGVLL DLEGFLERSF VETLRFLYIM QEESGFCEIV
GGNDRLPKSF LPQLEENIIY NQKLMKLHQH DNGVTAFYRN EETFEYSSIT GDLVIVTIPF
STMRFVEVDP FDSISHEKWK AIRELHYMPA TKIGIQFKSR FWEEQGQLGG RIITDLPIRY
GYYPSYGIGE KGPAMMLGSY TWSYDALLWD GLSKGDRIYY ALHNLATILG GQVYDEFISG
ISKSWTLDPY ALGGFALFQA GQESELQPAI VKPEGRIFFA GDHTTLYHGW IQGAIESGIR
VAAEVNE
//
