ID Q085A0_SHEFN Unreviewed; 525 AA.
AC Q085A0;
DT 31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE SubName: Full=Tryptophan halogenase {ECO:0000313|EMBL:ABI71165.1};
GN OrderedLocusNames=Sfri_1312 {ECO:0000313|EMBL:ABI71165.1};
OS Shewanella frigidimarina (strain NCIMB 400).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=318167 {ECO:0000313|EMBL:ABI71165.1, ECO:0000313|Proteomes:UP000000684};
RN [1] {ECO:0000313|EMBL:ABI71165.1, ECO:0000313|Proteomes:UP000000684}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCIMB 400 {ECO:0000313|EMBL:ABI71165.1,
RC ECO:0000313|Proteomes:UP000000684};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Fredrickson J.K., Kolker E., McCuel L.A., DiChristina T., Nealson K.H.,
RA Newman D., Tiedje J.M., Zhou J., Romine M.F., Culley D.E., Serres M.,
RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.;
RT "Complete sequence of Shewanella frigidimarina NCIMB 400.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0007829|PDB:2PYX}
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS).
RG Joint Center for Structural Genomics (JCSG);
RT "Crystal structure of tryptophan halogenase (YP_750003.1) from Shewanella
RT frigidimarina NCIMB 400 at 1.50 A resolution.";
RL Submitted (MAY-2007) to the PDB data bank.
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DR EMBL; CP000447; ABI71165.1; -; Genomic_DNA.
DR PDB; 2PYX; X-ray; 1.50 A; A/B=1-525.
DR PDBsum; 2PYX; -.
DR AlphaFoldDB; Q085A0; -.
DR SMR; Q085A0; -.
DR STRING; 318167.Sfri_1312; -.
DR KEGG; sfr:Sfri_1312; -.
DR eggNOG; COG0665; Bacteria.
DR HOGENOM; CLU_022247_0_0_6; -.
DR EvolutionaryTrace; Q085A0; -.
DR Proteomes; UP000000684; 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 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:2PYX}; 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:UP000000684}.
FT ACT_SITE 88
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 88
FT /ligand="7-chloro-L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:58713"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 197
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 360
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
SQ SEQUENCE 525 AA; 58873 MW; AFA081D5B5029C2F CRC64;
MMQKPITEII IVGGGTAGWI TAGLLAAEHN VDKGVLAHSP KLNITLIESP DVATIGVGEG
TWPSMRSTLS KIGIDENDFI RQCDASFKQG SRFINWCKDP QSNVADSYLH PFSLPHGHQE
LDLCPYWLPH AEQVSFAEAV CSQQVLTQLG LAPKSIVTAQ YHFQNNYGYH LNAAKFSQLL
TEHCTQKLGV THIRDHVSQI INNQHGDIEK LITKQNGEIS GQLFIDCTGA KSLLLGEHLQ
VPFLSQKSVL FNDRALAIQV PYSDANSPIA SCTHSTAQPN GWIWDIGLPT RKGVGYVYSS
SHTNDIDAQK TLFNYLGVDG AAADKLEPRQ LAINPGYRAK CWQNNCIAIG MAAGFIEPLE
ASALALIEWT ASTLAQQLPP NRMVMDTISA RVNERYQQHW QQIIDFLKLH YVISQRQEDR
YWRDHRESNS IPDSLQAMLE LWRYQTPSQQ DISYKEALFP AASFQYVLYG MSFNTQLPTH
VKPSMQQLAQ RLFNDNQQRT QALSKNLPTN RELLDKVAQY GFPKL
//
