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Database: UniProt
Entry: TR2M_AGRT4
LinkDB: TR2M_AGRT4
Original site: 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   27-MAR-2024, entry version 52.
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; Pseudomonadota; 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; 1.10.405.40; -; 1.
DR   Gene3D; 3.90.660.10; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR002937; Amino_oxidase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR006064; Glycosidase.
DR   InterPro; IPR012142; Trp_2-mOase.
DR   PANTHER; PTHR10742:SF342; AMINO_OXIDASE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR10742; FLAVIN MONOAMINE OXIDASE; 1.
DR   Pfam; PF01593; Amino_oxidase; 1.
DR   Pfam; PF02027; RolB_RolC; 1.
DR   PIRSF; PIRSF000319; Trp_2-mono_O2ase; 1.
DR   PRINTS; PR00419; ADXRDTASE.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 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
//
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