ID A0A154R6E7_9GAMM Unreviewed; 533 AA.
AC A0A154R6E7;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=Tryptophan halogenase {ECO:0000313|EMBL:KZC33577.1};
GN ORFNames=RhoFW510R10_07650 {ECO:0000313|EMBL:KZC33577.1};
OS Rhodanobacter sp. FW510-R10.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Rhodanobacter.
OX NCBI_TaxID=1524462 {ECO:0000313|EMBL:KZC33577.1, ECO:0000313|Proteomes:UP000076310};
RN [1] {ECO:0000313|EMBL:KZC33577.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FW510-R10 {ECO:0000313|EMBL:KZC33577.1};
RX PubMed=27048805; DOI=10.1128/mBio.02234-15;
RA Hemme C.L., Green S.J., Rishishwar L., Prakash O., Pettenato A.,
RA Chakraborty R., Deutschbauer A.M., Van Nostrand J.D., Wu L., He Z.,
RA Jordan I.K., Hazen T.C., Arkin A.P., Kostka J.E., Zhou J.;
RT "Lateral Gene Transfer in a Heavy Metal-Contaminated-Groundwater Microbial
RT Community.";
RL MBio 7:e02234-e02215(2016).
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:KZC33577.1}.
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DR EMBL; LVJU01000007; KZC33577.1; -; Genomic_DNA.
DR RefSeq; WP_068096645.1; NZ_LVJU01000007.1.
DR AlphaFoldDB; A0A154R6E7; -.
DR OrthoDB; 462203at2; -.
DR Proteomes; UP000076310; 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; 2.
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; 2.
DR PIRSF; PIRSF011396; Trp_halogenase; 2.
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 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 217
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 365
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 374
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 378
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
SQ SEQUENCE 533 AA; 58687 MW; DAD2A091EC15C930 CRC64;
MNDSRIRQVV IVGGGTAGWM AAALLAQALG AGVAMRLVES AEIGTVGVGE ATIPQIRHIN
RFLGIDEDEL LRFVHGTYKL GVQLNGFTRL GDSYLHAFGD LGLPLGLTPF HHYWLRAVQG
RTSAASAGDG RDAGDRAMPG AIAECAGAAG RADAPDLWAY SLNAAAAAEN RFAPLEKIPD
SPLGGLRYAY HFDATRYAQY LRERIAPGAV QRIEGKVTEV RLREGDGFIE SLRLDSGEIV
EGDFFIDCSG FRGLLIEGAL NTGYENWQHW LPCDRALAVA SAPGGPMRPY TQASARTAGW
QWRIPLRHRT GNGHVYCSRF ISDDEAAAQL LANLETEPLG DPRPLRFVTG MRRLAWNRNC
LALGLAAGFM EPLESTSIHL VQSGISRLLA MFPDRHCDSA LVDEYNRQTR FEYEHVRDFL
ILHYKATERT DTPFWRQCGA MEIPPSLARR IELFRRTGMV FREGEELFAE TGWVQVLLGQ
RIEPEHHHPL ADALSDAQLE GFLADIRTLV GRAKNTLPPH HAFVARAAGS LVT
//
