ID A0A0B5E1H0_9RHOB Unreviewed; 569 AA.
AC A0A0B5E1H0;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Tryptophan 2-monooxygenase {ECO:0000256|ARBA:ARBA00017871};
DE EC=1.13.12.3 {ECO:0000256|ARBA:ARBA00012535};
GN ORFNames=P73_2156 {ECO:0000313|EMBL:AJE46871.1};
OS Celeribacter indicus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Celeribacter.
OX NCBI_TaxID=1208324 {ECO:0000313|EMBL:AJE46871.1, ECO:0000313|Proteomes:UP000031521};
RN [1] {ECO:0000313|EMBL:AJE46871.1, ECO:0000313|Proteomes:UP000031521}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P73 {ECO:0000313|EMBL:AJE46871.1};
RX PubMed=25256706; DOI=10.1099/ijs.0.069039-0;
RA Lai Q., Cao J., Yuan J., Li F., Shao Z.;
RT "Celeribacter indicus sp. nov., a polycyclic aromatic hydrocarbon-degrading
RT bacterium from deep-sea sediment and reclassification of Huaishuia
RT halophila as Celeribacter halophilus comb. nov.";
RL Int. J. Syst. Evol. Microbiol. 64:4160-4167(2014).
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; CP004393; AJE46871.1; -; Genomic_DNA.
DR RefSeq; WP_052453190.1; NZ_FNNW01000007.1.
DR AlphaFoldDB; A0A0B5E1H0; -.
DR STRING; 1208324.P73_2156; -.
DR KEGG; cid:P73_2156; -.
DR HOGENOM; CLU_021400_0_0_5; -.
DR OrthoDB; 337830at2; -.
DR Proteomes; UP000031521; Chromosome.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0009851; P:auxin biosynthetic process; IEA:UniProtKB-KW.
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 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:UP000031521}.
FT DOMAIN 47..520
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 569 AA; 61993 MW; 9061A07ED9DBCE7F CRC64;
MTARPLTAFG PDFPFAHDDW LAHPAGLGAV PRDMLGTPVA VIGAGAAGVV AAYELMKIGL
KPVVYEASRF GGRLRSEPFD GTANVVAELG AMRFPASAAC FNHYLDLTGL KTAPFPNPLT
PAAGSTVIDL EGETVFARDI SELPKVYRDI AAAYARALDE GAAFRDLRQA IRDKDAARVR
ALWSPLVAAW DERTFYDFVT TSDAFRTLSF RHRELFGQVG FGTGGWDSDF PNSMLEILRV
NLLGFDEDQR LVIGGAEAVL RRLWQAAPDC AHWPAGTSLA SLNGGATRSR VCEISRPGGA
GPLRVTDRWG NEDRFEAVLV TCQSHLLTTA MDVDEDLLSQ PLWMALDRTR YMQAAKTFVM
VDRPFWTDPH PQTGRPLMSM TLTDRITRGT YLFDNGADRP AVICLSYAWM TDALKILPLA
DEKRVDLALK ALRRIYPDVD IAAHIRGAPK CVSWEADENF LGAFKGALPG HYRYNHRVYG
HFMQADLPEA QRGLFLAGDS VSWTPAWVEG AVQTALNAVW GVVAHLGGAA HPANPGPGDR
YPEAGPVALT DQGGHCPETG QECPESGRM
//
