ID G1Y0E6_9PROT Unreviewed; 554 AA.
AC G1Y0E6;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=Tryptophan halogenase {ECO:0000313|EMBL:EGY01011.1};
GN ORFNames=AZA_24523 {ECO:0000313|EMBL:EGY01011.1};
OS Nitrospirillum amazonense Y2.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Nitrospirillum.
OX NCBI_TaxID=1003237 {ECO:0000313|EMBL:EGY01011.1, ECO:0000313|Proteomes:UP000018435};
RN [1] {ECO:0000313|EMBL:EGY01011.1, ECO:0000313|Proteomes:UP000018435}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y2 (ATCC 35120) {ECO:0000313|Proteomes:UP000018435};
RX PubMed=21838888; DOI=10.1186/1471-2164-12-409;
RA Sant'anna F.H., Almeida L.G., Cecagno R., Reolon L.A., Siqueira F.M.,
RA Machado M.R., Vasconcelos A.T., Schrank I.S.;
RT "Genomic insights into the versatility of the plant growth-promoting
RT bacterium Azospirillum amazonense.";
RL BMC Genomics 12:409-409(2011).
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:EGY01011.1}.
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DR EMBL; AFBX01000492; EGY01011.1; -; Genomic_DNA.
DR AlphaFoldDB; G1Y0E6; -.
DR PATRIC; fig|1003237.3.peg.2911; -.
DR Proteomes; UP000018435; Unassembled WGS sequence.
DR GO; GO:0004497; F:monooxygenase activity; IEA:InterPro.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR006905; Flavin_halogenase.
DR InterPro; IPR033856; Trp_halogen.
DR PANTHER; PTHR43747; FAD-BINDING PROTEIN; 1.
DR PANTHER; PTHR43747:SF4; FLAVIN-DEPENDENT TRYPTOPHAN HALOGENASE; 1.
DR Pfam; PF04820; Trp_halogenase; 1.
DR PIRSF; PIRSF011396; Trp_halogenase; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 4: Predicted;
KW FAD {ECO:0000256|PIRSR:PIRSR011396-2};
KW Flavoprotein {ECO:0000256|PIRSR:PIRSR011396-2};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR011396-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000018435}.
FT REGION 532..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 92
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-1"
FT BINDING 23..26
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 92
FT /ligand="7-chloro-L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:58713"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 207
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 358
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 367
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 371
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
SQ SEQUENCE 554 AA; 60756 MW; F5C2FDECC18299F2 CRC64;
MEAPTDGARA KGAPVKNVLI VGGGTAGWLA AAYLARTLSI GQPGGARITL VESADIGILG
VGEGTFPNIQ RTLRRIGIDE SVFMRESEAT FKQGIRFDHW QHAPGPSATG AGQRDHYFHP
FQSAIGPQDL DLIPYWLLGA AGDGVPLDTA LTMQKRVADA ALAPKRSGDA DYAAPLNYAY
HFDAVKFARL LRVVATDLGV RHVIDTVDAV PLDETGAVAG VVTRENGTLT ADLYIDCTGF
RAQLIGQALK SPYQSCRKWL FCDRAVALQV PYDQPDAPIP SYTISTAHEA GWTWDIGLET
RRGIGHVYSS DHTDDARAEQ VLRDYIGPAA ADKTARTFRF EAGYRPEPWV RNCVAIGLSS
GFFEPLESTG IVLIEVASVL LTSLFPWAGD MATAARQFNR IMRQRYERAL DFLKLHYCLT
RRTDTAFWRD NADAATVPDT LHDLLDRWRH RPPEGLDFDL NLDTFSEASW QFVLYGMGYR
TDLSAQAGAF RHMDEARQQF AAIRAGTEQA LAALPRHRDL ITQIYRHGLR PRTPLAGAPS
GRATLSSGMA GLSR
//
