ID C6XQH0_HIRBI Unreviewed; 493 AA.
AC C6XQH0;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Tryptophan halogenase {ECO:0000313|EMBL:ACT60469.1};
GN OrderedLocusNames=Hbal_2796 {ECO:0000313|EMBL:ACT60469.1};
OS Hirschia baltica (strain ATCC 49814 / DSM 5838 / IFAM 1418).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomonadales;
OC Hyphomonadaceae; Hirschia.
OX NCBI_TaxID=582402 {ECO:0000313|EMBL:ACT60469.1, ECO:0000313|Proteomes:UP000002745};
RN [1] {ECO:0000313|Proteomes:UP000002745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49814 / DSM 5838 / IFAM 1418
RC {ECO:0000313|Proteomes:UP000002745};
RX PubMed=21705585; DOI=10.1128/JB.05453-11;
RG US DOE Joint Genome Institute;
RA Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.;
RT "Genome sequences of eight morphologically diverse alphaproteobacteria.";
RL J. Bacteriol. 193:4567-4568(2011).
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DR EMBL; CP001678; ACT60469.1; -; Genomic_DNA.
DR RefSeq; WP_015828619.1; NC_012982.1.
DR AlphaFoldDB; C6XQH0; -.
DR STRING; 582402.Hbal_2796; -.
DR KEGG; hba:Hbal_2796; -.
DR eggNOG; COG0665; Bacteria.
DR HOGENOM; CLU_022247_1_0_5; -.
DR OrthoDB; 462203at2; -.
DR Proteomes; UP000002745; Chromosome.
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:UP000002745}.
FT ACT_SITE 79
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-1"
FT BINDING 14..17
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 79
FT /ligand="7-chloro-L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:58713"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 329
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 338
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 342
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
SQ SEQUENCE 493 AA; 55766 MW; B7EAF133A97066D8 CRC64;
MERQTINRVV IAGGGTAGWV TAASLSHNLG PALDITLVES EAIGTIGVGE ATIPTHTSFH
AMLGINEAEF MRATHATFKL GIQFEGWKDK GESYIHSFGQ VGKHTWMAPF HHLWLHARDL
GIEGDFEDYC LELKAAKADK FFTSDKQKPL NYAYHLDAVA YAKYLRGFSE KKGVKRVEGK
IQNVLQYAES GNIKAVELEN GALIEGDLFI DCTGFNGLLI EKTLKTGYDD WRHWLPMDSA
YAVQTQKTGP AIPYTRAIAH ENGWRWRIPL QHRVGNGFVF TSEKLSNDDA REQFENALEG
EALTEPRLIR FITGRRKKVW NKNCVALGLS SGFLEPLEST SIHLFQRGVT ELVKHFPYHG
ITPALADLYN DKISKEVEQI RDFLILHYKV TQRDDSEFWR ERQAMDIPDT LAARLSLFEE
NAHAYNGCDE LFLLDSWIQV MFGQGIEPKG YHAIGQLFPK DRLENALKSQ REKVASTLAQ
LPSHQEFIDQ YCS
//
