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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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