ID C6XNJ5_HIRBI Unreviewed; 502 AA.
AC C6XNJ5;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Tryptophan halogenase {ECO:0000313|EMBL:ACT60139.1};
GN OrderedLocusNames=Hbal_2461 {ECO:0000313|EMBL:ACT60139.1};
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:ACT60139.1, 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; ACT60139.1; -; Genomic_DNA.
DR RefSeq; WP_015828289.1; NC_012982.1.
DR AlphaFoldDB; C6XNJ5; -.
DR STRING; 582402.Hbal_2461; -.
DR KEGG; hba:Hbal_2461; -.
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 186
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 334
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 343
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 347
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
SQ SEQUENCE 502 AA; 56754 MW; E270D8BF75A7BEC2 CRC64;
MSNTQIQKIV IVGGGTAGWI SAAALAKLLP PSISVTLIES DSIATVGVGE ATIPQIRRLN
GMLGLNENTF LKATKGTIKL GIEFSNWGKI GESYLHTFGD VGLNLSNLQF HHYWKRAQEE
GKQSSLWDYS LHHKVAYSNK FDRLERIGKT GMTGLSYAFH FDAGLYARFL RNFAETSGVT
RIEGFVKQTV LNPHTGFIDH VKLENGTQIE GDLFIDCSGF RGLLIDKALG VSYQDWTHWL
PCNRAIAVPS QSTRPLVPYT KSIAHTAGWQ WCIPLQHRTG NGHVYSDQFM QDETALEVLL
SNLDSTPIAE PNHIRFTTGR REKFWHKNCI SIGLSSGFLE PLESTSIHLI QSNISRLIEL
LPTKKMEPAN SNEYNRQVSK EYELIRDFII LHYHCTQRED SDFWRYCKNM DIPDSLKQKL
ELFSATGRIH KEPEDLFREA SWVQVMIGQG LIPQSYHAMA DRLSTDQLEK FLADIDAIIA
QAEAQLPSHE DFLTRNCQLD LQ
//
