TR2M_PSESS
ID TR2M_PSESS Reviewed; 557 AA.
AC P06617;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Tryptophan 2-monooxygenase;
DE EC=1.13.12.3;
GN Name=iaaM;
OS Pseudomonas savastanoi (Pseudomonas syringae pv. savastanoi).
OG Plasmid pIAA1.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=29438;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=EW2009;
RX PubMed=16593610; DOI=10.1073/pnas.82.19.6522;
RA Yamada T., Palm C.J., Brooks B., Kosuge T.;
RT "Nucleotide sequences of the Pseudomonas savastanoi indoleacetic acid genes
RT show homology with Agrobacterium tumefaciens T-DNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:6522-6526(1985).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH FAD AND THE
RP SUBSTRATE ANALOG INDOLE-3-ACETAMIDE, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT,
RP IDENTIFICATION BY MASS SPECTROMETRY, AND MUTAGENESIS OF LYS-365 AND
RP TRP-466.
RX PubMed=23521653; DOI=10.1021/bi4001563;
RA Gaweska H.M., Taylor A.B., Hart P.J., Fitzpatrick P.F.;
RT "Structure of the flavoprotein tryptophan 2-monooxygenase, a key enzyme in
RT the formation of galls in plants.";
RL Biochemistry 52:2620-2626(2013).
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:0000269|PubMed:23521653};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000269|PubMed:23521653};
CC Note=Binds 1 FMN per subunit. {ECO:0000269|PubMed:23521653};
CC -!- PATHWAY: Plant hormone metabolism; auxin biosynthesis.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:23521653}.
CC -!- SIMILARITY: Belongs to the tryptophan 2-monooxygenase family.
CC {ECO:0000305}.
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DR EMBL; M11035; AAA25852.1; -; Genomic_DNA.
DR PIR; A25493; A25493.
DR RefSeq; WP_002556046.1; NZ_QUSH01000118.1.
DR PDB; 4IV9; X-ray; 1.95 A; A/B=1-557.
DR PDBsum; 4IV9; -.
DR AlphaFoldDB; P06617; -.
DR SMR; P06617; -.
DR KEGG; ag:AAA25852; -.
DR BioCyc; MetaCyc:MON-7661; -.
DR BRENDA; 1.13.12.3; 5174.
DR SABIO-RK; P06617; -.
DR UniPathway; UPA00151; -.
DR GO; GO:0050361; F:tryptophan 2-monooxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0009851; P:auxin biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR Pfam; PF01593; Amino_oxidase; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Auxin biosynthesis; Flavoprotein; FMN; Monooxygenase;
KW Oxidoreductase; Plasmid.
FT CHAIN 1..557
FT /note="Tryptophan 2-monooxygenase"
FT /id="PRO_0000065590"
FT BINDING 49
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT BINDING 69
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT BINDING 71
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT BINDING 77
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT BINDING 98
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT BINDING 98
FT /ligand="substrate"
FT MUTAGEN 365
FT /note="K->M: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:23521653"
FT MUTAGEN 466
FT /note="W->F: Slightly decreases enzyme activity."
FT /evidence="ECO:0000269|PubMed:23521653"
FT MUTAGEN 466
FT /note="W->M: Abolishes flavin binding."
FT /evidence="ECO:0000269|PubMed:23521653"
FT TURN 10..12
FT /evidence="ECO:0007829|PDB:4IV9"
FT HELIX 16..24
FT /evidence="ECO:0007829|PDB:4IV9"
FT TURN 25..27
FT /evidence="ECO:0007829|PDB:4IV9"
FT STRAND 28..31
FT /evidence="ECO:0007829|PDB:4IV9"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:4IV9"
FT HELIX 48..59
FT /evidence="ECO:0007829|PDB:4IV9"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:4IV9"
FT STRAND 71..75
FT /evidence="ECO:0007829|PDB:4IV9"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:4IV9"
FT STRAND 91..95
FT /evidence="ECO:0007829|PDB:4IV9"
FT HELIX 104..113
FT /evidence="ECO:0007829|PDB:4IV9"
FT STRAND 127..133
FT /evidence="ECO:0007829|PDB:4IV9"
FT STRAND 136..140
FT /evidence="ECO:0007829|PDB:4IV9"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:4IV9"
FT HELIX 151..163
FT /evidence="ECO:0007829|PDB:4IV9"
FT HELIX 175..184
FT /evidence="ECO:0007829|PDB:4IV9"
FT HELIX 187..201
FT /evidence="ECO:0007829|PDB:4IV9"
FT HELIX 206..215
FT /evidence="ECO:0007829|PDB:4IV9"
FT HELIX 229..237
FT /evidence="ECO:0007829|PDB:4IV9"
FT STRAND 239..242
FT /evidence="ECO:0007829|PDB:4IV9"
FT HELIX 245..247
FT /evidence="ECO:0007829|PDB:4IV9"
FT HELIX 252..260
FT /evidence="ECO:0007829|PDB:4IV9"
FT TURN 261..264
FT /evidence="ECO:0007829|PDB:4IV9"
FT HELIX 275..283
FT /evidence="ECO:0007829|PDB:4IV9"
FT HELIX 291..294
FT /evidence="ECO:0007829|PDB:4IV9"
FT STRAND 300..306
FT /evidence="ECO:0007829|PDB:4IV9"
FT STRAND 309..314
FT /evidence="ECO:0007829|PDB:4IV9"
FT STRAND 319..327
FT /evidence="ECO:0007829|PDB:4IV9"
FT HELIX 331..336
FT /evidence="ECO:0007829|PDB:4IV9"
FT STRAND 341..347
FT /evidence="ECO:0007829|PDB:4IV9"
FT HELIX 349..357
FT /evidence="ECO:0007829|PDB:4IV9"
FT STRAND 363..372
FT /evidence="ECO:0007829|PDB:4IV9"
FT HELIX 374..377
FT /evidence="ECO:0007829|PDB:4IV9"
FT STRAND 382..388
FT /evidence="ECO:0007829|PDB:4IV9"
FT STRAND 391..396
FT /evidence="ECO:0007829|PDB:4IV9"
FT STRAND 407..415
FT /evidence="ECO:0007829|PDB:4IV9"
FT HELIX 416..420
FT /evidence="ECO:0007829|PDB:4IV9"
FT HELIX 421..423
FT /evidence="ECO:0007829|PDB:4IV9"
FT HELIX 428..442
FT /evidence="ECO:0007829|PDB:4IV9"
FT HELIX 444..447
FT /evidence="ECO:0007829|PDB:4IV9"
FT HELIX 453..455
FT /evidence="ECO:0007829|PDB:4IV9"
FT TURN 457..459
FT /evidence="ECO:0007829|PDB:4IV9"
FT STRAND 460..466
FT /evidence="ECO:0007829|PDB:4IV9"
FT TURN 470..472
FT /evidence="ECO:0007829|PDB:4IV9"
FT STRAND 473..475
FT /evidence="ECO:0007829|PDB:4IV9"
FT HELIX 484..491
FT /evidence="ECO:0007829|PDB:4IV9"
FT HELIX 493..498
FT /evidence="ECO:0007829|PDB:4IV9"
FT TURN 500..502
FT /evidence="ECO:0007829|PDB:4IV9"
FT STRAND 505..508
FT /evidence="ECO:0007829|PDB:4IV9"
FT HELIX 511..513
FT /evidence="ECO:0007829|PDB:4IV9"
FT STRAND 514..516
FT /evidence="ECO:0007829|PDB:4IV9"
FT HELIX 520..537
FT /evidence="ECO:0007829|PDB:4IV9"
FT HELIX 547..550
FT /evidence="ECO:0007829|PDB:4IV9"
SQ SEQUENCE 557 AA; 61861 MW; A3EA5CF7B4A94289 CRC64;
MYDHFNSPSI DILYDYGPFL KKCEMTGGIG SYSAGTPTPR VAIVGAGISG LVAATELLRA
GVKDVVLYES RDRIGGRVWS QVFDQTRPRY IAEMGAMRFP PSATGLFHYL KKFGISTSTT
FPDPGVVDTE LHYRGKRYHW PAGKKPPELF RRVYEGWQSL LSEGYLLEGG SLVAPLDITA
MLKSGRLEEA AIAWQGWLNV FRDCSFYNAI VCIFTGRHPP GGDRWARPED FELFGSLGIG
SGGFLPVFQA GFTEILRMVI NGYQSDQRLI PDGISSLAAR LADQSFDGKA LRDRVCFSRV
GRISREAEKI IIQTEAGEQR VFDRVIVTSS NRAMQMIHCL TDSESFLSRD VARAVRETHL
TGSSKLFILT RTKFWIKNKL PTTIQSDGLV RGVYCLDYQP DEPEGHGVVL LSYTWEDDAQ
KMLAMPDKKT RCQVLVDDLA AIHPTFASYL LPVDGDYERY VLHHDWLTDP HSAGAFKLNY
PGEDVYSQRL FFQPMTANSP NKDTGLYLAG CSCSFAGGWI EGAVQTALNS ACAVLRSTGG
QLSKGNPLDC INASYRY
