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Database: UniProt
Entry: S6HKT1_9GAMM
LinkDB: S6HKT1_9GAMM
Original site: S6HKT1_9GAMM 
ID   S6HKT1_9GAMM            Unreviewed;       373 AA.
AC   S6HKT1;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Tryptophan 2-monooxygenase {ECO:0000256|ARBA:ARBA00017871};
DE            EC=1.13.12.3 {ECO:0000256|ARBA:ARBA00012535};
GN   ORFNames=OFPII_01440 {ECO:0000313|EMBL:EPJ49479.1};
OS   Osedax symbiont Rs1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae.
OX   NCBI_TaxID=1330036 {ECO:0000313|EMBL:EPJ49479.1, ECO:0000313|Proteomes:UP000014822};
RN   [1] {ECO:0000313|EMBL:EPJ49479.1, ECO:0000313|Proteomes:UP000014822}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rs1 {ECO:0000313|Proteomes:UP000014822};
RA   Yi H., Goffredi S.;
RT   "Comparative genomics of two novel heterotrophic symbionts of deep-sea
RT   Osedax worms: functional variation and environmental selection.";
RL   Submitted (MAY-2013) 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; Evidence={ECO:0000256|ARBA:ARBA00000112};
CC   -!- PATHWAY: Plant hormone metabolism; auxin biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004814}.
CC   -!- SIMILARITY: Belongs to the tryptophan 2-monooxygenase family.
CC       {ECO:0000256|ARBA:ARBA00005833}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EPJ49479.1}.
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DR   EMBL; ASZJ01000007; EPJ49479.1; -; Genomic_DNA.
DR   AlphaFoldDB; S6HKT1; -.
DR   Proteomes; UP000014822; Unassembled WGS sequence.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009851; P:auxin biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.660.10; -; 1.
DR   InterPro; IPR002937; Amino_oxidase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
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   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 {ECO:0000256|ARBA:ARBA00023070};
KW   Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023033};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014822}.
FT   DOMAIN          96..326
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
SQ   SEQUENCE   373 AA;  42629 MW;  E3738E4B7189510B CRC64;
     MSYAAVSSRT FAHGFGSDLF LIQGRFVDGT YTPGPHYSDE SMVDTGGSKV KSPRYLGTEI
     FWESMMFETT EFYSVELGGS VSTSMYDLMS TGLGAPLSIW QNNPVTQIQE QLGGKWTIES
     EKFTETNYDH VIITIPSWNF GTETSLVTVN RETAASKWPT SLQTFLKRAH WEPACKVFVS
     LKEPFWENAA LSMPQMFATD TYIRDAYGIK LDVDTNQKGA MLVSYSWWRD ANKLVSYSDS
     DLINLCVRQL DEICQRCINV NGLFSDYVDY SQSYVVHWEM ERFTKGAARL YDQREWNDTQ
     VPMMYNQVYS TTSKLYLAGE SYHVDAGWTE PCMRMAIDSV LRILDNDQDS SITVPNFVFS
     QDYTQYNESF VPV
//
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