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Database: UniProt
Entry: A0A120I877_PSEAA
LinkDB: A0A120I877_PSEAA
Original site: A0A120I877_PSEAA 
ID   A0A120I877_PSEAA        Unreviewed;       560 AA.
AC   A0A120I877;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, 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=AWM79_00630 {ECO:0000313|EMBL:AMB83893.1};
OS   Pseudomonas agarici.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=46677 {ECO:0000313|EMBL:AMB83893.1, ECO:0000313|Proteomes:UP000063229};
RN   [1] {ECO:0000313|EMBL:AMB83893.1, ECO:0000313|Proteomes:UP000063229}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCPPB 2472 {ECO:0000313|EMBL:AMB83893.1,
RC   ECO:0000313|Proteomes:UP000063229};
RA   McClelland M., Jain A., Saraogi P., Mendelson R., Westerman R.,
RA   SanMiguel P., Csonka L.;
RL   Submitted (JAN-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; CP014135; AMB83893.1; -; Genomic_DNA.
DR   RefSeq; WP_060781915.1; NZ_CP014135.1.
DR   AlphaFoldDB; A0A120I877; -.
DR   STRING; 46677.AWM79_00630; -.
DR   Proteomes; UP000063229; Chromosome.
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   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:UP000063229}.
FT   DOMAIN          55..530
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
SQ   SEQUENCE   560 AA;  62109 MW;  C9C81EF5E1C72840 CRC64;
     MNQNSRHPAD GKKPITLFGP DFPFAFDDWI EHPAGLGSIP AHNHGAEVAI VGAGIAGLVA
     AYELMKLGLK PVVYEASKMG GRLRSQAFEG AEGIIAELGG MRFPASSTAF YHYVDKLGLH
     TKPFPNPLTP ASGSTVIDLE GQTHYAQKLS DLPALFQEVA DAWADALEEG SRFGDIQQAI
     RDRNVPRLKE LWNTLVPLWD DRTFYDFIAT SKAFAKLSFR HREVFGQVGF GTGGWDSDFP
     NSMLEIFRVV MTNCDDHQHL VVGGVEQVPL GIWRHVPPRC AHWPAGTSLS SLHHGAPRTG
     VKRIDRAADG QFAVTDNWGD TRHYAAVLTT CQSWLLTTQI ECEESLFSQK MWMALDRTRY
     MQSSKTFVMV DRPFWKDKDP QTGRDLMSMT LTDRLTRGTY LFDNGDDQPG VICLSYSWMS
     DALKMLPQPI DKRVKLALDA LKKIYPKVDI AARIIGEPIT VSWEADPHFL GAFKGALPGH
     YRYNQRMYAH FMQADMLAEQ RGIFIAGDDV SWTPAWVEGA VQTSLNAVWG IMNHFGGSSH
     AENPGPGDVF AEIGPIALAD
//
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