TR2M_AGRT4
ID TR2M_AGRT4 Reviewed; 755 AA.
AC P0A3V2; P04029;
DT 23-OCT-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-1986, sequence version 1.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=Tryptophan 2-monooxygenase;
DE EC=1.13.12.3;
GN Name=tms1;
OS Agrobacterium tumefaciens (strain Ach5).
OG Plasmid pTiAch5.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC Agrobacterium tumefaciens complex.
OX NCBI_TaxID=176298;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6327292; DOI=10.1002/j.1460-2075.1984.tb01894.x;
RA Gielen J., de Beuckeleer M., Seurinck J., Deboeck F., de Greve H.,
RA Lemmers M., van Montagu M., Schell J.;
RT "The complete nucleotide sequence of the TL-DNA of the Agrobacterium
RT tumefaciens plasmid pTiAch5.";
RL EMBO J. 3:835-846(1984).
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 PIR; A04497; QQAG4T.
DR AlphaFoldDB; P0A3V2; -.
DR SMR; P0A3V2; -.
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_0000065586"
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; 83947 MW; 9FD2B83FEA001A4D CRC64;
MSASPLLDNQ CDHLPTKMVD LTMVDKADEL DRRVSDAFLE REASRGRRIT QISTECSAGL
ACKRLADGRF PEISAGGKVA VLSAYIYIGK EILGRILESK PWARATVSGL VAIDLAPFCM
DFSEAQLIQA LFLLSGKRCA PIDLSHFVAI SISKTAGFRT LPMPLYENGT MKCVTGFTIT
LEGAVPFDMV AYGRNLMLKG SAGSFPTIDL LYDYRPFFDQ CSDSGRIGFF PEDVPKPKVA
VIGAGISGLV VANELLHAGV DDVTIYEASD RVGGKLWSHA FRDAPSVVAE MGAMRFPPAA
FCLFFFLERY GLSSMRPFPN PGTVDTYLVY QGVQYMWKAG QLPPKLFHRV YNGWRAFLKD
GFYERDIVLA SPVAITQALK SGDIRWAHDS WQIWLNRFGR ESFSSGIERI FLGTHPPGGE
TWSFPHDWDL FKLMGIGSGG FGPVFESGFI EILRLVINGY EENQRMCPEG ISELPRRIAS
EVVNGVSVSQ RICHVQVRAI QKEKTKIKIR LKSGISELYD KVVVTSGLAN IQLRHCLTCD
TNIFQAPVNQ AVDNSHMTGS SKLFLMTERK FWLDHILPSC VLMDGIAKAV YCLDYEPQDP
NGKGLVLISY TWEDDSHKLL AVPDKKERLC LLRDAISRSF PAFAQHLFPA CADYDQNVIQ
HDWLTDENAG GAFKLNRRGE DFYSEELFFQ ALDTANDTGV YLAGCSCSFT GGWVEGANRT
PCNAVCAIIH NCGGILAKGN PLEHSWKRYN YRTRN