ID A0A3R8TWH8_9PSED Unreviewed; 559 AA.
AC A0A3R8TWH8;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE RecName: Full=Tryptophan 2-monooxygenase {ECO:0000256|ARBA:ARBA00017871};
DE EC=1.13.12.3 {ECO:0000256|ARBA:ARBA00012535};
GN ORFNames=EGJ27_20115 {ECO:0000313|EMBL:RRV04787.1};
OS Pseudomonas sp. v388.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=2479849 {ECO:0000313|EMBL:RRV04787.1, ECO:0000313|Proteomes:UP000268166};
RN [1] {ECO:0000313|EMBL:RRV04787.1, ECO:0000313|Proteomes:UP000268166}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=v388 {ECO:0000313|Proteomes:UP000268166};
RA D'Souza A.W., Potter R.F., Wallace M., Shupe A., Patel S., Sun S., Gul D.,
RA Kwon J.H., Andleeb S., Burnham C.-A.D., Dantas G.;
RT "Transmission dynamics of multidrug resistant bacteria on intensive care
RT unit surfaces.";
RL Submitted (OCT-2018) 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}.
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:RRV04787.1}.
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DR EMBL; RHQN01000009; RRV04787.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3R8TWH8; -.
DR OrthoDB; 8845488at2; -.
DR Proteomes; UP000268166; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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 PRINTS; PR00420; RNGMNOXGNASE.
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};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023033};
KW Reference proteome {ECO:0000313|Proteomes:UP000268166}.
FT DOMAIN 54..529
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 559 AA; 62093 MW; 1E5B3E81DAB1FAAB CRC64;
MKTNRHPANG KKPVTIFGPD FPFPFDDWIE HPAGLGSIPK ENLGSEVAII GAGIAGLVAA
YELMKLGLKP VVYEASKMGG RLRSQEFEGA KGIIAELGGM RFPVSSTAFF HYVDKLGLES
RPFPNPLTAA SGSTVIDLEG STHYAQMLSD LPELFQEVAD AWADALEAGA QFSDIQQAIR
DRDVPRLKAL WNTLVPLWDD RTFYDFVATS KAFAKLSFTH REVFGQVGFG TGGWDSDFPN
SMLEIFRVVM TNCDEHQHLI VGGVQQVPVG LWSHVPERCV HWPEGTSLST LHRGAPRPGV
KRIARAADGT LAVTDNWGDT RHYGAVLTTC QSWLLTTQIE CEESLFSQKM WMALDRTRYM
QSSKTFVMVD RPFWKDKDPE TGRDLMSMTL TDRLTRSTYL FDNGDDKPGV ICLSYSWMSD
ALKMLPQPID KRVRLALDAL KKIYPKVDIA ARIIGDPITV SWEADPHFLG AFKGALPGHY
RYNQRMYAHF MQQDMPAEQR GMFIAGDDVS WTPAWVEGAV QTSLNAVWGI MTHFGGKTHA
ENPGPGDVFN DIGPIALAD
//
