TR2M2_AGRVI
ID TR2M2_AGRVI Reviewed; 755 AA.
AC P25017;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Tryptophan 2-monooxygenase;
DE EC=1.13.12.3;
GN Name=iaaM;
OS Agrobacterium vitis (Rhizobium vitis).
OG Plasmid pTiTM4.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium.
OX NCBI_TaxID=373;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=TM4;
RX PubMed=1868204; DOI=10.1007/bf00023438;
RA Bonnard G., Vincent F., Otten L.;
RT "Sequence of Agrobacterium tumefaciens biotype III auxin genes.";
RL Plant Mol. Biol. 16:733-738(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CG474;
RA Otten L., de Ruffray P.;
RL Submitted (FEB-1997) 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;
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 -!- CAUTION: The plasmid pTiTM4 carries two T-regions, the TA and TB
CC region, both of which have a functional iaaM gene, with low homology
CC between them. {ECO:0000305}.
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DR EMBL; X56185; CAA39646.1; -; Genomic_DNA.
DR EMBL; U83987; AAB41874.1; -; Genomic_DNA.
DR AlphaFoldDB; P25017; -.
DR SMR; P25017; -.
DR PRIDE; P25017; -.
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 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.
FT CHAIN 1..755
FT /note="Tryptophan 2-monooxygenase"
FT /id="PRO_0000065591"
FT BINDING 247
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 267
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 275
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 295
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 295
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 755 AA; 83973 MW; 6FA63E502343136F CRC64;
MSASSLLDKQ CDHFSTKIVD LIMVDKADEL DRRVAAAFSE REASRERRIS QISGECNAGL
ACKRLADGRF PEISAGQRVA VLSAYIYVGE EILRWILEPE ASVRTRVSGL VAIDLAPSCM
DISRAQLLQT MNLLSGKRCA PSDLSHFVAI SISETARSRT LQMAPYEEGS LKSVTGFTVI
IEEAVPFDMV AYGRNLMLKA SAGSFPTIDL LYDYRLFLDK CSDSGRIGFF PEDVPRPKVA
VIGAGISGLV VASELLHAGV DDVTIYEAGD RVGGKLWSHA FKDAPGVVAE MGAMRFPPAA
SCLFFFLERY GLSSMRPFPN PGTVDTDLVY EGCRYMWKAG QQPPKLFHRV YSGWHAFLKD
GFLEGDIVLA SPDAITEALK SGDIRRAHDS WQIWLNRFGR ESFSSAIERI FLGTHPPGGE
TWSFPHDWDL FKLMGIGSGG FGPVFESGFT EILRLVINGY EENQRMCSEG ISELPRRIAS
QVVNGVSVSQ RIRHVQVRAI EKEKTKIKIR LKSGISELYD KVVVTSGLAN IQLRHCLTCD
TTIFRAPVNQ AVDNSHMTGS SKLFLLTERK FWFDHMLPSC VLMDGFAKAV YCLDYEPQDP
NGKGLVLISY TWEDDSHKLL AVPDKKERLC LLRDAISKSF PVFAQHLVPA CADYDQNVVQ
HDWLTDENAG GRFKLNRRGE DFYSEELFFQ ALDTTNDTGV YLAGCSCSFT GGWVEGAIQT
ACNAVCAIIH NCGGILAKDN PLKHPWKRYN YRNRN