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Database: UniProt
Entry: A0A1B1EIQ7_VIBNA
LinkDB: A0A1B1EIQ7_VIBNA
Original site: A0A1B1EIQ7_VIBNA 
ID   A0A1B1EIQ7_VIBNA        Unreviewed;       527 AA.
AC   A0A1B1EIQ7;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, 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=BA894_19670 {ECO:0000313|EMBL:ANQ28633.1};
OS   Vibrio natriegens.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=691 {ECO:0000313|EMBL:ANQ28633.1, ECO:0000313|Proteomes:UP000092577};
RN   [1] {ECO:0000313|EMBL:ANQ28633.1, ECO:0000313|Proteomes:UP000092577}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCUG 16374 {ECO:0000313|EMBL:ANQ28633.1,
RC   ECO:0000313|Proteomes:UP000092577};
RA   Weinstock M.T., Hesek E.D., Wilson C.M., Gibson D.G.;
RT   "Developing Vibrio natriegens as a novel, fast-growing host for
RT   biotechnology.";
RL   Submitted (JUL-2016) 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}.
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DR   EMBL; CP016352; ANQ28633.1; -; Genomic_DNA.
DR   RefSeq; WP_065298185.1; NZ_CP016352.1.
DR   AlphaFoldDB; A0A1B1EIQ7; -.
DR   OrthoDB; 337830at2; -.
DR   Proteomes; UP000092577; Chromosome 2.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 1.20.1440.240; -; 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; IPR006311; TAT_signal.
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.
DR   PROSITE; PS51318; TAT; 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}.
FT   DOMAIN          61..513
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
SQ   SEQUENCE   527 AA;  58357 MW;  A9DFDB0E79ADB0E7 CRC64;
     MDNMGKSRRE FIQKVMAIGG AGAALATINA LSIPSAFASD LPPKMKANGN GKKVLILGGG
     LAGMTSAYEL AQKGYDVQII EARSFAGGRC QTARKGMVIE ELGGTKQICD FDKGQYLNLG
     PMRIPAHHRS TLYYTQKFKI PLETYINYNE DAWVYNDKQK SLPPQRMREV LADMHGYVNE
     MMAKSLSSDS LDKTISDKDK ELLLAYLIRE GHLDQADLSY KGYGGRGYKL DPGALLQAGD
     PTTPNDLESL LESELWNVAS SVSSHTQPKT VFQPVGGMDM IAKGFEEHTK QYISYNTEVQ
     KIRQKDGKVI VDVMNLDTKK PRTLTGDFCI CTIPLSVLKQ IDSDFSPRFK EAMEAVAYTP
     TCKLGIQTAT RFWETKDLIF GGHSVLTAGS PKTGNITYPS HDMFQEKGVL LSAYNFNSDA
     AQFSALSPQE RFELSVRVGQ LVHGDDYKNN AEKAVSISWH LQKYNLGGWA SWTDEARDQH
     YPILCEPEGN IYLAGEHMSY MNGWMAGAIE SAWDQIAKLD QAVLKAA
//
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