ID A0A098UC18_9BURK Unreviewed; 506 AA.
AC A0A098UC18;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Tryptophan halogenase {ECO:0000313|EMBL:KGF81956.1};
GN ORFNames=IA69_08420 {ECO:0000313|EMBL:KGF81956.1};
OS Massilia sp. JS1662.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1519190 {ECO:0000313|EMBL:KGF81956.1, ECO:0000313|Proteomes:UP000029701};
RN [1] {ECO:0000313|EMBL:KGF81956.1, ECO:0000313|Proteomes:UP000029701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS1662 {ECO:0000313|EMBL:KGF81956.1,
RC ECO:0000313|Proteomes:UP000029701};
RA Fida T.T., Spain J.C.;
RT "Identification of Arachidin-3 degrading bacteria in the peanut
RT rhizosphere.";
RL Submitted (JUL-2014) 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:KGF81956.1}.
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DR EMBL; JPQD01000007; KGF81956.1; -; Genomic_DNA.
DR RefSeq; WP_036231510.1; NZ_JPQD01000007.1.
DR AlphaFoldDB; A0A098UC18; -.
DR OrthoDB; 462203at2; -.
DR Proteomes; UP000029701; 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 80
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-1"
FT BINDING 15..18
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 80
FT /ligand="7-chloro-L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:58713"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 335
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 344
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 348
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
SQ SEQUENCE 506 AA; 57076 MW; 101BE3AFA762AE5C CRC64;
MVKNRWIHKV VILGGGTAGW MTAAALSHTF GHAVEIVLVE SDAIGTVGVG EATIPPIRAF
HQMIGVDEAE FMRATGATFK LGIEFRGWRN ESSTYFHPFG VYGVERDIGY FFQYWLRLKE
KGQVADFSEF SLCTLAARSN LFAPASERPG DPLQHLQSAY HFDAGRYAKY LKGVCIARGV
SHKIGDMLTA EHDSENGHIT GLKLKSGELV TGDLFIDCSG MRAMLLGQAL GVDYEDWSHW
LPMNRACAVP CEQKLALTPY TISTARPFGW QWRIPLQHRV GNGVVYSNEF ATDEAAERCL
LDGLEGEPLA PINRIRFTAG RRKTPWHKNV VAIGLASGFL EPLESTSIQF IQSSIQRLIR
YFPEAGFAPV CAQAFNREAT REIENVRDFL ILHYHATERD DSELWRYVKT MQIPDSLQER
IELFRERGQL NLANEELFQS TSWHAVLLGQ GIRPRTYMPT MALQDDAMLA NAYSNLERNF
KKIVSRLPDH AAYIKEHKLT STMENR
//
