ID F3G4W1_PSESJ Unreviewed; 559 AA.
AC F3G4W1;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Tryptophan 2-monooxygenase {ECO:0000256|ARBA:ARBA00017871};
DE EC=1.13.12.3 {ECO:0000256|ARBA:ARBA00012535};
GN ORFNames=PSYPI_06715 {ECO:0000313|EMBL:EGH42111.1};
OS Pseudomonas syringae pv. pisi str. 1704B.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX NCBI_TaxID=629263 {ECO:0000313|EMBL:EGH42111.1, ECO:0000313|Proteomes:UP000004986};
RN [1] {ECO:0000313|EMBL:EGH42111.1, ECO:0000313|Proteomes:UP000004986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1704B {ECO:0000313|EMBL:EGH42111.1,
RC ECO:0000313|Proteomes:UP000004986};
RX PubMed=21799664; DOI=10.1371/journal.ppat.1002132;
RA Baltrus D.A., Nishimura M.T., Romanchuk A., Chang J.H., Mukhtar M.S.,
RA Cherkis K., Roach J., Grant S.R., Jones C.D., Dangl J.L.;
RT "Dynamic evolution of pathogenicity revealed by sequencing and comparative
RT genomics of 19 Pseudomonas syringae isolates.";
RL PLoS Pathog. 7:E1002132-e1002132(2011).
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:EGH42111.1}.
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DR EMBL; AEAI01000322; EGH42111.1; -; Genomic_DNA.
DR AlphaFoldDB; F3G4W1; -.
DR SMR; F3G4W1; -.
DR PATRIC; fig|629263.4.peg.1111; -.
DR HOGENOM; CLU_021400_0_0_6; -.
DR BioCyc; PSYR629263:G11X0-1222-MONOMER; -.
DR Proteomes; UP000004986; 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 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, ECO:0000313|EMBL:EGH42111.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023033,
KW ECO:0000313|EMBL:EGH42111.1}.
FT DOMAIN 54..529
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 559 AA; 62296 MW; 8C7ABA6E0981CF66 CRC64;
MKNNRHPANG KKPITMFGPD FPFAFDDWIE HPKGLGSIPV ENHGAEVAII GAGIAGLVAA
YELMKMGLKP VVYEASKMGG RLRSQEFEGA KGIVAELGGM RFPVSSTAFF HYVDKLGLES
RPFPNPLTAA SGSTVIDLEG TTYYAQMLSD LPALFQEVAD AWADALESGS QFGDIQQAIR
DRDVPRLKEL WNKLVPLWDD RTFYDFVATS KAFAKLSFFH REVFGQVGFG TGGWDSDFPN
SMLEIFRVVM TNCDEHQHLI VGGVQQVPVG LWSHVPEHCA HWPKGTSLSS LHRGAPRPGV
KRIARAEDGS FAVTDNWGDT RQYAAVLTTC QSWLLTTQIE CEESLFSQKM WMALDRTRYM
QSSKTFVMVD RPFWKDKDPE TGRDLMSMTL TDRLTRGTYL FDNGDDKPGV ICLSYSWMSD
ALKMLPQPIE KRVKLALDAL KKIYPKVDIA ARIIGDPITV SWEADPHFLG AFKGALPGHY
RYNQRMYAHF MQQDMPSEQR GMFIAGDDVS WTPAWVEGAV QTSLNAVWGI MNHFGGKTHA
ENPGPGDVFH EIGPIALGD
//
