ID I3IFM3_9GAMM Unreviewed; 503 AA.
AC I3IFM3;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=Tryptophan halogenase {ECO:0000313|EMBL:EIK46858.1};
GN ORFNames=O59_000879 {ECO:0000313|EMBL:EIK46858.1};
OS Cellvibrio sp. BR.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Cellvibrio.
OX NCBI_TaxID=1134474 {ECO:0000313|EMBL:EIK46858.1, ECO:0000313|Proteomes:UP000003395};
RN [1] {ECO:0000313|EMBL:EIK46858.1, ECO:0000313|Proteomes:UP000003395}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BR {ECO:0000313|EMBL:EIK46858.1,
RC ECO:0000313|Proteomes:UP000003395};
RA Peng Y.Y., Li N.Z., Xia T., Qiu R.R.;
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
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:EIK46858.1}.
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DR EMBL; AICM01000001; EIK46858.1; -; Genomic_DNA.
DR RefSeq; WP_007639763.1; NZ_JH668200.1.
DR AlphaFoldDB; I3IFM3; -.
DR STRING; 1134474.O59_000879; -.
DR PATRIC; fig|1134474.3.peg.863; -.
DR eggNOG; COG0665; Bacteria.
DR HOGENOM; CLU_022247_1_0_6; -.
DR OrthoDB; 6278312at2; -.
DR Proteomes; UP000003395; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR011396-2};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT ACT_SITE 83
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-1"
FT BINDING 17..20
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 83
FT /ligand="7-chloro-L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:58713"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 338
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 347
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 351
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
SQ SEQUENCE 503 AA; 56373 MW; 34A812820F8A99B4 CRC64;
MNDNAKRRIK KIIIVGGGTA GWMTAAAFSK VLGTSCYDIV LIESDDIGTV GVGEATIPLI
TSFNQILGLD ESQFMKKTQA TFKLGIEFVN WGNIDDRYIH PFGVYGKGIG SLAFYNFLLK
QQKIKPDTDV GDYSINIQAA RHNKFMRAPN LPNSPLADIR YAYHFDAGLY ALYLRNYAEQ
QGAIRVQGEI TNVSLDDDSG CITSVTLKDG QTHSADFFID CSGFRGLLIE QALKTGYEDW
SHLLLSDTAV TVPSEVIHPL PSFTRSTAHS AGWQWCIPLQ HRTGNGHVFS SRFMSEDEAT
SLLLQHLPTP ALAGPRTVKF KTGIRRKLWN KNCVAIGLSS GFIEPLESTS IHLIHSAIHK
LLTFFPTGAL SQVDIDKYND VMRTDIEFIR DFILLHYKAT SRTDSAFWNH CRTMDVPDGL
RKKMELYIKS GRLYRDNNEL FTEDSWFAVM EGQGVKVEDY HPLVDSVEQV KFDAMLGDIA
RAIRESTDVI PSHAEYIARY CKA
//
