ID A0A1M5C773_9RHOB Unreviewed; 548 AA.
AC A0A1M5C773;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Tryptophan 2-monooxygenase {ECO:0000256|ARBA:ARBA00017871};
DE EC=1.13.12.3 {ECO:0000256|ARBA:ARBA00012535};
GN ORFNames=SAMN05444339_10748 {ECO:0000313|EMBL:SHF50624.1};
OS Loktanella atrilutea.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Loktanella.
OX NCBI_TaxID=366533 {ECO:0000313|EMBL:SHF50624.1, ECO:0000313|Proteomes:UP000183987};
RN [1] {ECO:0000313|Proteomes:UP000183987}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 29326 {ECO:0000313|Proteomes:UP000183987};
RA Varghese N., Submissions S.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-tryptophan + O2 = CO2 + H2O + indole-3-acetamide;
CC Xref=Rhea:RHEA:16165, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16031, ChEBI:CHEBI:16526, ChEBI:CHEBI:57912;
CC EC=1.13.12.3; Evidence={ECO:0000256|ARBA:ARBA00000112};
CC -!- PATHWAY: Plant hormone metabolism; auxin biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004814}.
CC -!- SIMILARITY: Belongs to the tryptophan 2-monooxygenase family.
CC {ECO:0000256|ARBA:ARBA00005833}.
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DR EMBL; FQUE01000007; SHF50624.1; -; Genomic_DNA.
DR RefSeq; WP_072857926.1; NZ_FQUE01000007.1.
DR AlphaFoldDB; A0A1M5C773; -.
DR STRING; 366533.SAMN05444339_10748; -.
DR OrthoDB; 337830at2; -.
DR Proteomes; UP000183987; Unassembled WGS sequence.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0009851; P:auxin biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 1.10.405.40; -; 1.
DR Gene3D; 3.90.660.10; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
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 SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW Auxin biosynthesis {ECO:0000256|ARBA:ARBA00023070};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033, ECO:0000313|EMBL:SHF50624.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023033,
KW ECO:0000313|EMBL:SHF50624.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000183987}.
FT DOMAIN 45..519
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 548 AA; 60045 MW; 9E5D6A1E6791DAE3 CRC64;
MSRLTAFGPD FPFAYDDWIA HPDGLGSIPK DAYSTRVAVI GAGAAGITAA FELMKLGLHP
VVYEASRFGG RLRSQAFDGA DGIVAELGGM RFPRSSTAFF HYLDMMGCET RPFPNPLSIA
AGSTVVDLEG ETFFARHLDD LPPLYREIAS AYDAALTDQA AFPDLQAAVR ARDPAAIKAI
WNPLVSQWDE RTFYDFIAGS EAFRGQSFRH REVFGQVGFG TGGWDSDFPN SMLEILRVNL
LGLDDDQHLV VGGVDQVLRR LWKAAPPCAH WPEGTSLASL NGGTTRSRVT AIQRQTDGAL
QVTDQWGNVA SYDAVLATCQ THLLTTAIEV DEDLLAQNLW MALDRTRYMQ SAKTFVMVDR
PFWHDLDPAT DRPVLSMTLT DRHTRGTYLF DNGPDQPAVI CLSYAWMTDA LKVLPLSADK
RVDLALKALA KIYPGVNIAS HIRGTPICVS WEADQNFLGA FKGALPGHYR YNHRIFGHFM
QDRLPDSQRG LFLAGDGVSW TPAWVEGAVQ TGLNAVWGIM TQFGGHSPAS NPGPGDMYAD
WGPVVLPS
//
