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TR2M_AGRVS
ID   TR2M_AGRVS              Reviewed;         723 AA.
AC   Q04564; B9K454;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Tryptophan 2-monooxygenase;
DE            EC=1.13.12.3;
GN   Name=iaaM; Synonyms=tms1; OrderedLocusNames=Avi_8288;
OS   Agrobacterium vitis (strain S4 / ATCC BAA-846) (Rhizobium vitis (strain
OS   S4)).
OG   Plasmid pTiS4.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium.
OX   NCBI_TaxID=311402;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1465104; DOI=10.1007/bf00279373;
RA   Canaday J., Gerard J.-C., Crouzet P., Otten L.;
RT   "Organization and functional analysis of three T-DNAs from the vitopine Ti
RT   plasmid pTiS4.";
RL   Mol. Gen. Genet. 235:292-303(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S4 / ATCC BAA-846;
RX   PubMed=19251847; DOI=10.1128/jb.01779-08;
RA   Slater S.C., Goldman B.S., Goodner B., Setubal J.C., Farrand S.K.,
RA   Nester E.W., Burr T.J., Banta L., Dickerman A.W., Paulsen I., Otten L.,
RA   Suen G., Welch R., Almeida N.F., Arnold F., Burton O.T., Du Z., Ewing A.,
RA   Godsy E., Heisel S., Houmiel K.L., Jhaveri J., Lu J., Miller N.M.,
RA   Norton S., Chen Q., Phoolcharoen W., Ohlin V., Ondrusek D., Pride N.,
RA   Stricklin S.L., Sun J., Wheeler C., Wilson L., Zhu H., Wood D.W.;
RT   "Genome sequences of three Agrobacterium biovars help elucidate the
RT   evolution of multichromosome genomes in bacteria.";
RL   J. Bacteriol. 191:2501-2511(2009).
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;
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250};
CC       Note=Binds 1 FMN per subunit. {ECO:0000250};
CC   -!- PATHWAY: Plant hormone metabolism; auxin biosynthesis.
CC   -!- SIMILARITY: Belongs to the tryptophan 2-monooxygenase family.
CC       {ECO:0000305}.
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DR   EMBL; M91609; AAA98149.1; -; Genomic_DNA.
DR   EMBL; CP000637; ACM39708.1; -; Genomic_DNA.
DR   PIR; S30105; S30105.
DR   RefSeq; WP_012649067.1; NC_011982.1.
DR   AlphaFoldDB; Q04564; -.
DR   SMR; Q04564; -.
DR   EnsemblBacteria; ACM39708; ACM39708; Avi_8288.
DR   KEGG; avi:Avi_8288; -.
DR   HOGENOM; CLU_021400_0_0_5; -.
DR   OMA; YCLDYEP; -.
DR   OrthoDB; 1442136at2; -.
DR   UniPathway; UPA00151; -.
DR   Proteomes; UP000001596; Plasmid pTiS4.
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   InterPro; IPR006064; Glycosidase.
DR   InterPro; IPR012142; Trp_2-mOase.
DR   Pfam; PF01593; Amino_oxidase; 1.
DR   Pfam; PF02027; RolB_RolC; 1.
DR   PIRSF; PIRSF000319; Trp_2-mono_O2ase; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   3: Inferred from homology;
KW   Auxin biosynthesis; Crown gall tumor; Flavoprotein; FMN; Monooxygenase;
KW   Oxidoreductase; Plasmid; Reference proteome.
FT   CHAIN           1..723
FT                   /note="Tryptophan 2-monooxygenase"
FT                   /id="PRO_0000065588"
FT   BINDING         218
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         238
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         246
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         266
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         266
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   723 AA;  80803 MW;  ABA9CEA94B6B4E36 CRC64;
     MANFFYSRIT NRSYSTKNLL NIEDKGRLKD ELEKTRQTNI CEICLHPRGH RASVCRQILM
     GFAYTSKTVL EGLLSTMPHD DAPLGKIFVT DLPPYDEQVP QVLLMQAAAL VTSYEYSFED
     LAYFLVLPLQ MALMQKSPSL GKDFPVISGY SITKDSVHSP VAFGRNLMPR GVSCEFPQID
     VLYDYRGFLE GGAFSEGVTS FPKETKKPKV AVIGAGISGL VSATLLLRNG IDDVTIFEAK
     NVVGGRAHTH FFKGEPSVCA ELGAMRFPRS QACLFYLLEY LGINAMTKFP NPGTVDTGLY
     YRGRSYNWKA HSLPPAIFNR VHKGWRTFLH AGFVDGVAAF ASPFTLTECL RLRNYEFASS
     LWQKWLDAFS SETFSSGIER IFRGAHPPGG EKWTRDVDME LFKELGVGSG GFGPVFGCGF
     IEILRLIVNG YEDNVMLLLD GIEEIPRRLS QQKVGSYSIR DRIIHKEVKE IIRTESGISL
     AIGEGMHATF DRVIVTSGFT NIQLRHLLTN DDSFFSYDVN QAIENSHMTG SSKLFVLTQN
     KFWKAEELPS CILTTGVAKA VYCLDYEPDK PSGKGLVLLS YTWEDDSHKL LTFDKGERFQ
     ILKRDLAKSY PRFADLLEPA DGDYDNNIIQ HDWILDPYAG GAFKLNRRCE DVYSKRLFFQ
     PLRLNGEPDG RVCLAGCSCS FSGGWVEGAI QTACNAAMAT IRDAGGLISG DNPLTNEFVN
     YHY
 
 
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