ID A0A0C9MTJ3_SPHPI Unreviewed; 494 AA.
AC A0A0C9MTJ3;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=DNA, contig: SP630 {ECO:0000313|EMBL:GAN14046.1};
GN ORFNames=SP6_30_01870 {ECO:0000313|EMBL:GAN14046.1};
OS Sphingomonas paucimobilis NBRC 13935.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1219050 {ECO:0000313|EMBL:GAN14046.1, ECO:0000313|Proteomes:UP000032025};
RN [1] {ECO:0000313|EMBL:GAN14046.1, ECO:0000313|Proteomes:UP000032025}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 13935 {ECO:0000313|EMBL:GAN14046.1,
RC ECO:0000313|Proteomes:UP000032025};
RA Hosoyama A., Hashimoto M., Hosoyama Y., Noguchi M., Uohara A., Ohji S.,
RA Katano-Makiyama Y., Ichikawa N., Kimura A., Yamazoe A., Fujita N.;
RT "Whole genome shotgun sequence of Sphingomonas paucimobilis NBRC 13935.";
RL Submitted (AUG-2014) 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:GAN14046.1}.
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DR EMBL; BBJS01000030; GAN14046.1; -; Genomic_DNA.
DR RefSeq; WP_007404945.1; NZ_BBJS01000030.1.
DR AlphaFoldDB; A0A0C9MTJ3; -.
DR GeneID; 78528788; -.
DR Proteomes; UP000032025; 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.
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 80
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 80
FT /ligand="7-chloro-L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:58713"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 187
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 335
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR011396-2"
FT BINDING 344
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
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"
SQ SEQUENCE 494 AA; 53711 MW; 2A5EFD302764FEF3 CRC64;
MTDNRIRRIV ILGGGTAGWM TAAALSRAVA GQGVTITLIE SDAIGTIGVG EATIPTIHWF
NQIIGLDERQ FMAETKATVK LGIEFVGWNG AGSRYFHPFG TFGPPGDGAM FLHRLIRGRA
DGDAAPTEAY SLTAQAAKAG RFARPVADRR SLLSTLGYAY HFDAGLYARY LRGLAERSGV
TRIEGIVASV GQEGESGFIA SLTLEDGRTV AGDLFIDCSG LRALLIGETL GVGYDDWSHW
LPCDRAWAAP SAAETSLTPF TRATAAEAGW RWRIPLQHRV GNGYVFASRF QDEDAARASL
LAGMDGPPLA DPRLIRFTPG MRREAWRANV VAIGLSSGFL EPLESTSIHL IQSGIAKLLS
LFPAADCSPL LARQFNRVFG QEMHDVRDFL ILHYHATAGR DEPMWRERQA MTIPDSLAER
IAHFRHSGRI VLSSDELFRD ASWFAVLDGQ GERAEDHNPL IEAVGRDDNL RHLATLRAEI
AKVAASLPPL PARG
//
