ID A0A0Q5PSY4_9SPHN Unreviewed; 515 AA.
AC A0A0Q5PSY4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Tryptophan halogenase {ECO:0000313|EMBL:KQR84179.1};
GN ORFNames=ASG07_06205 {ECO:0000313|EMBL:KQR84179.1};
OS Sphingomonas sp. Leaf343.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1736345 {ECO:0000313|EMBL:KQR84179.1, ECO:0000313|Proteomes:UP000051323};
RN [1] {ECO:0000313|EMBL:KQR84179.1, ECO:0000313|Proteomes:UP000051323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf343 {ECO:0000313|EMBL:KQR84179.1,
RC ECO:0000313|Proteomes:UP000051323};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQR84179.1, ECO:0000313|Proteomes:UP000051323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf343 {ECO:0000313|EMBL:KQR84179.1,
RC ECO:0000313|Proteomes:UP000051323};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQR84179.1}.
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DR EMBL; LMPG01000010; KQR84179.1; -; Genomic_DNA.
DR RefSeq; WP_055843769.1; NZ_LMPG01000010.1.
DR AlphaFoldDB; A0A0Q5PSY4; -.
DR STRING; 1736345.ASG07_06205; -.
DR OrthoDB; 7178350at2; -.
DR Proteomes; UP000051323; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:UP000051323}.
FT ACT_SITE 85
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-1"
FT BINDING 17..20
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 85
FT /ligand="7-chloro-L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:58713"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 189
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 340
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 349
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
SQ SEQUENCE 515 AA; 55977 MW; 9C0FAF8806F12E21 CRC64;
MGGKSAATVN TVIVVGGGSA GWLAACRLAA QAKRTGSGVS VTLVESDRIP TIGVGEGTWP
TMRNTLAKIG ISETEFIRSC DAALKQGARF VGWTDGQPGD AYYHPLNPPA GASEIDLAPY
WLGRSTDFAD CVDYQAALCE AGLAPKTITS AEYAGHANYA YHLDAGKFAT MLREHATGAL
GVTHVIGDVA RANQADNGDI LDVEMADGRR IAGDLFVDCT GFAALLIGGV YGVPFESCRD
VLFADRAIAM QVPHASDDDP IACHTISTAQ DAGWIWDIGL WTRRGVGHVY SSAHTSDDAA
EAALRRYVGP AGDDLSVRTI RIDGGHRERF WQNNCVAVGL SAGFIEPLEA SALMLIEASM
DAIAERLPRT RSAMNLAARQ FNATFRHHWM RIIEFLKLHY VITQRTDTDF WQDNVAASSI
PDGLEERLEF WRHHSPAPQD FPHAREVFSW PSYQYVLHGM RFASRYPPVG TATPEAAMAA
GLITRNERIR GDLIARAPAH RDLLRAVRNY GLQRV
//