ID J2Q9W5_9CAUL Unreviewed; 513 AA.
AC J2Q9W5;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE SubName: Full=Tryptophan halogenase {ECO:0000313|EMBL:EJL36862.1};
GN ORFNames=PMI01_00874 {ECO:0000313|EMBL:EJL36862.1};
OS Caulobacter sp. AP07.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=1144304 {ECO:0000313|EMBL:EJL36862.1, ECO:0000313|Proteomes:UP000007300};
RN [1] {ECO:0000313|EMBL:EJL36862.1, ECO:0000313|Proteomes:UP000007300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP07 {ECO:0000313|EMBL:EJL36862.1,
RC ECO:0000313|Proteomes:UP000007300};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(2012).
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:EJL36862.1}.
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DR EMBL; AKKF01000049; EJL36862.1; -; Genomic_DNA.
DR RefSeq; WP_007663452.1; NZ_AKKF01000049.1.
DR AlphaFoldDB; J2Q9W5; -.
DR PATRIC; fig|1144304.3.peg.838; -.
DR Proteomes; UP000007300; 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}.
FT ACT_SITE 80
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-1"
FT BINDING 11..14
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 80
FT /ligand="7-chloro-L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:58713"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 191
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 343
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 352
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 356
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
SQ SEQUENCE 513 AA; 56357 MW; 0877D2951369C56E CRC64;
MAGNRIVIVG GGTAGWLTAA YLAKQLGADR PGGARITLIE SPEIGIIGVG EGTFPTIRST
LATLGVSEAR FMRESSATFK QGVRFVDWER RSADGKSSEY FHPFNLPLRP EGRDLSPYWL
LDHQAGAPLA FADAVTTQGK IIEAGLAPKR LEDADFQGPM NYAYHFDAAR FADFLRGVAK
ELGVIHLAAK VETVQLDAET GDIASVTAGE LGVIEGNLFI DCSGFRALLI GEALGAPFRR
CDDVLFNDRA LAVQVPYPAP DAPIAPYTLA TAHEAGWTWD IGLDGRRGVG YVFSSRHTDE
ARAEQVLRAY VGPEADHLPV RLLKFQTGYR ERQWIGNCVA VGLSAGFFEP LESTGIMLIE
VAATMIAEVF PLRDRAAMDS AARTFNGLMA GRFERIVSFL KLHYCLSKRD EPYWRDNADP
ASWPQGLRDL MAQWKHRPVS RFDFLVDLET FLPASYQYIL YGMNAATDFA PVEGRYADGA
MARQAFAKVA GAATEALKHL PPHRTLVEAY YRR
//
