ID V4PP63_9CAUL Unreviewed; 507 AA.
AC V4PP63;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=Tryptophan halogenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=ABENE_14915 {ECO:0000313|EMBL:ESQ89074.1};
OS Asticcacaulis benevestitus DSM 16100 = ATCC BAA-896.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Asticcacaulis.
OX NCBI_TaxID=1121022 {ECO:0000313|EMBL:ESQ89074.1, ECO:0000313|Proteomes:UP000017837};
RN [1] {ECO:0000313|EMBL:ESQ89074.1, ECO:0000313|Proteomes:UP000017837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16100 {ECO:0000313|EMBL:ESQ89074.1,
RC ECO:0000313|Proteomes:UP000017837};
RX PubMed=24463524; DOI=10.1038/nature12900;
RA Jiang C., Brown P.J., Ducret A., Brun Y.V.;
RT "Sequential evolution of bacterial morphology by co-option of a
RT developmental regulator.";
RL Nature 506:489-493(2014).
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:ESQ89074.1}.
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DR EMBL; AWGB01000032; ESQ89074.1; -; Genomic_DNA.
DR AlphaFoldDB; V4PP63; -.
DR STRING; 1121022.GCA_000376105_02250; -.
DR PATRIC; fig|1121022.4.peg.3034; -.
DR eggNOG; COG0665; Bacteria.
DR OrthoDB; 7178350at2; -.
DR Proteomes; UP000017837; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:UP000017837};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT ACT_SITE 82
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-1"
FT BINDING 13..16
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 82
FT /ligand="7-chloro-L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:58713"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 190
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 337
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 346
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 350
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
SQ SEQUENCE 507 AA; 56352 MW; E1149CA30530929D CRC64;
MTRSADHFVI LGGGTAGWMA AACLSRLLFR VPGSPKRVTL VESAEIAPIG VGEATIPSIQ
DMLRYLNIDE ADFVSATDAT YKLGIRFRDW RVAGSDFFHG FGELGPTIEN LPLFQHWLSE
KIAGRPVPPL EALSMSAQLA LNNRFAKPKQ DGNSPLFMAG YAYHFDAAKV ATYLRDYAEA
KGVKRIEGHV AEVALAVDGS VNSLRLTDGR DITGDFFIDC SGFKGLIIEK ALGSPFEDWS
HWLPCDRAVA LPSQSIAPLQ PYTQVTARDA GWTWRIPLQS RIGNGYVYAS RFCDAAQAEQ
TLRGALESQP LAEPRQIHFT PGRRREAWVK NCLSLGLASG FLEPLESTSI HLIFANLFRF
FDHFPRDIDS AVLRQTYNDR SVREIEEIRD FLILHYWASA RRDTPFWRYV TAMDIPDSLG
AKLEAFRTQG KILADYYDLF KPASWMAIYD GMGFTPKAPD PLADLVPGDF SRRVLQNVTQ
GIRQAALAAP PHEASLAALL RRPLSPV
//
