ID A0A1M7N007_9BURK Unreviewed; 499 AA.
AC A0A1M7N007;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Tryptophan halogenase {ECO:0000313|EMBL:SHM96842.1};
GN ORFNames=SAMN05192549_103409 {ECO:0000313|EMBL:SHM96842.1};
OS Duganella sacchari.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Duganella.
OX NCBI_TaxID=551987 {ECO:0000313|EMBL:SHM96842.1, ECO:0000313|Proteomes:UP000184339};
RN [1] {ECO:0000313|EMBL:SHM96842.1, ECO:0000313|Proteomes:UP000184339}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sac-22 {ECO:0000313|EMBL:SHM96842.1,
RC ECO:0000313|Proteomes:UP000184339};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FRCX01000003; SHM96842.1; -; Genomic_DNA.
DR RefSeq; WP_072783455.1; NZ_FRCX01000003.1.
DR AlphaFoldDB; A0A1M7N007; -.
DR STRING; 551987.SAMN05192549_103409; -.
DR OrthoDB; 8868802at2; -.
DR Proteomes; UP000184339; 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 77
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-1"
FT BINDING 12..15
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 77
FT /ligand="7-chloro-L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:58713"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 185
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 333
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 342
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 346
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
SQ SEQUENCE 499 AA; 55822 MW; A8FD6DB3E2F04CD3 CRC64;
MENIKQVVIV GGGTAGWMTA AALARVLGDK IKLTLIESDD IGTVGVGEST IPMIKLFNSV
LGIDEDEFMR ATQATFKLGI EFKDWGRIGD SYMHGFGIFG QDLATLPFYQ YWLRMQHAGK
APDIEHYSIN RMAAKAGKFM RADRSHGNSP LADIVHAFHI DAGLYARYLR HYAEAKGVRR
IEGKVVDALT RASDGHVDAV RMENGELIGG ELFIDCSGFR GLLIEQALHT GFEDWSHWLP
CDRAYAVPCE LGNELLPYTR ATARPAGWQW RIGLQHRTGN GHVYCSKFMS DDEAAGILMS
SLDGRALAEP KQLRFTAGKR KQVWNRNVVA VGLSSGFMEP LESTSIHLIQ STIARLIAFF
PDQGFSAADV AEFNRQCDFE VERIRDFLIL HYHATERNDT PFWDHVRTMD VPQTLRDKMA
LWRTRGRIVR VDNELFAEAG WLQVLQGQRV PVEGYHPLAD LMDESEVAGY LRDIASVIGQ
CVSQMPSHAA YIKARCAAK
//
