ID A0A0Q0H7Y5_9GAMM Unreviewed; 514 AA.
AC A0A0Q0H7Y5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Flavin-dependent tryptophan halogenase RebH {ECO:0000313|EMBL:KPZ69030.1};
DE EC=1.14.19.9 {ECO:0000313|EMBL:KPZ69030.1};
GN Name=rebH_5 {ECO:0000313|EMBL:KPZ69030.1};
GN ORFNames=AN944_03243 {ECO:0000313|EMBL:KPZ69030.1};
OS Shewanella sp. P1-14-1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=1723761 {ECO:0000313|EMBL:KPZ69030.1, ECO:0000313|Proteomes:UP000050414};
RN [1] {ECO:0000313|EMBL:KPZ69030.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P1-14-1 {ECO:0000313|EMBL:KPZ69030.1};
RA Gilbert D.G.;
RL Submitted (OCT-2015) 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:KPZ69030.1}.
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DR EMBL; LKTL01000022; KPZ69030.1; -; Genomic_DNA.
DR RefSeq; WP_055025646.1; NZ_LKTL01000022.1.
DR AlphaFoldDB; A0A0Q0H7Y5; -.
DR PATRIC; fig|1723761.3.peg.3328; -.
DR Proteomes; UP000050414; 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 Oxidoreductase {ECO:0000313|EMBL:KPZ69030.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000050414}.
FT ACT_SITE 78
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 78
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 341
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 350
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 354
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
SQ SEQUENCE 514 AA; 57669 MW; 1305A50F5BFFBAA0 CRC64;
MKVQRIVIVG GGTAGWLAAN HIGKAAQHLA DVSVTLIESP DIPTIGVGEG TVPAIKQSLQ
SFGISETEFI RECDVSFKQS IKFCNWLDKD IHGANNSYHH LFDVPSPLGE NLTDYWLQQT
KQQATNQQSF SATVSPQHFI CDAFKAPKLI TTPEYGGKVS YAYHLNAARF AQLLAKNATT
KFNVTHLKAN VLDANIDEKG NLTCLKTDSL GELAFDFYVD ASGFESILLA KKLKVGFIDK
SKQLFVNKAI VAQVPTTEEQ VIPPYTIATA HQAGWVWDIA LPQRRGTGFV YSDNHMTSAQ
AEETFDRYLG GKLASLASRE IPMKVGYREK FWAKNCVSLG LAQGFLEPIE ATSILLTDFA
AAYLSKRLPH ALSQMPALAE RFNHTMGYAW ERVVEFAKLH YCISDRQDSD FWRDNRCPDS
IPNPLKQKMA LWQNFSPLTD DLFSRYEVFN VDNYLYVLYG MKYATQVNQC DKQYLLAAQQ
QTEQIRRIGQ GLAAELPEHR VLLNKIKQYG LKTI
//
