ID A0A0Q4FRM3_9SPHN Unreviewed; 526 AA.
AC A0A0Q4FRM3;
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:KQM67813.1};
GN ORFNames=ASE75_02640 {ECO:0000313|EMBL:KQM67813.1};
OS Sphingomonas sp. Leaf17.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1735683 {ECO:0000313|EMBL:KQM67813.1, ECO:0000313|Proteomes:UP000051777};
RN [1] {ECO:0000313|EMBL:KQM67813.1, ECO:0000313|Proteomes:UP000051777}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf17 {ECO:0000313|EMBL:KQM67813.1,
RC ECO:0000313|Proteomes:UP000051777};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQM67813.1, ECO:0000313|Proteomes:UP000051777}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf17 {ECO:0000313|EMBL:KQM67813.1,
RC ECO:0000313|Proteomes:UP000051777};
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:KQM67813.1}.
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DR EMBL; LMKL01000001; KQM67813.1; -; Genomic_DNA.
DR RefSeq; WP_055928300.1; NZ_LMKL01000001.1.
DR AlphaFoldDB; A0A0Q4FRM3; -.
DR STRING; 1735683.ASE75_02640; -.
DR OrthoDB; 7178350at2; -.
DR Proteomes; UP000051777; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR011396-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000051777};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT ACT_SITE 87
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-1"
FT BINDING 18..21
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 87
FT /ligand="7-chloro-L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:58713"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 195
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
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"
FT BINDING 357
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 361
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
SQ SEQUENCE 526 AA; 57576 MW; 1411BF9820F43A94 CRC64;
MTTDTGDRPV QHIVVVGGGT AGWLSACLIA ARADPRVRRP ITVTLVESPD VATIGVGEGT
WPTMRGTLER IGISETAFLL ACDGAFKQGS RFDGWRTGAA DDRYFHPFTA PIEGDPRDIV
AAWADQPTHD GAGFAHRVGA QADMCARDLA PRQRAMPDYA GTLNYAYHLD AGKLAALLMR
QATETLGVRH VRDHVVGIDT TGDGDIAAVR TRDNGAIAGD LFLDCTGQPA LLIGGHYGVG
TVDRGGELFN DRALAVQIPV APDSAIASQT NATAHAAGWI WDIGLPTRRG VGCVYSSAHC
SDDAAADTLA RYCRRVAPDM AVPSFRQLTF QSRHRQRFWE RNCLAIGLSA GFLEPLEASA
IVLIELSLEA LLDNFPVTRA AMDIHAARFN TLFRYRWDRI VEFLKLHYVL SRRKEPYWRD
HRDPASIPDR LAELLRLWQH QPPSRADFPM IDEIFPAASY QYVLYGMGFS PPTSGPIASG
SRTRAQILLG QMEQRKRQLA AGLPTNRAYL DALRRESGMP VLEPVA
//
