ID Q0SDG6_RHOJR Unreviewed; 452 AA.
AC Q0SDG6;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 109.
DE SubName: Full=Probable dibenzothiophene desulfurization enzyme {ECO:0000313|EMBL:ABG94420.1};
DE EC=1.14.13.- {ECO:0000313|EMBL:ABG94420.1};
GN OrderedLocusNames=RHA1_ro02615 {ECO:0000313|EMBL:ABG94420.1};
OS Rhodococcus jostii (strain RHA1).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=101510 {ECO:0000313|EMBL:ABG94420.1, ECO:0000313|Proteomes:UP000008710};
RN [1] {ECO:0000313|Proteomes:UP000008710}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RHA1 {ECO:0000313|Proteomes:UP000008710};
RX PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C.,
RA Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H.,
RA Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H.,
RA Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R.,
RA Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W.,
RA Eltis L.D.;
RT "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT catabolic powerhouse.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
CC -!- SIMILARITY: Belongs to the NtaA/SnaA/DszA monooxygenase family.
CC {ECO:0000256|ARBA:ARBA00033748}.
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DR EMBL; CP000431; ABG94420.1; -; Genomic_DNA.
DR RefSeq; WP_011595323.1; NC_008268.1.
DR AlphaFoldDB; Q0SDG6; -.
DR KEGG; rha:RHA1_ro02615; -.
DR PATRIC; fig|101510.16.peg.2649; -.
DR eggNOG; COG2141; Bacteria.
DR HOGENOM; CLU_022256_0_1_11; -.
DR OrthoDB; 9135350at2; -.
DR Proteomes; UP000008710; Chromosome.
DR GO; GO:0004497; F:monooxygenase activity; IEA:InterPro.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR CDD; cd01095; Nitrilotriacetate_monoxgenase; 1.
DR Gene3D; 3.20.20.30; Luciferase-like domain; 1.
DR InterPro; IPR011251; Luciferase-like_dom.
DR InterPro; IPR036661; Luciferase-like_sf.
DR InterPro; IPR016215; NTA_MOA.
DR NCBIfam; TIGR03860; FMN_nitrolo; 1.
DR PANTHER; PTHR30011; ALKANESULFONATE MONOOXYGENASE-RELATED; 1.
DR PANTHER; PTHR30011:SF16; C2H2 FINGER DOMAIN TRANSCRIPTION FACTOR (EUROFUNG)-RELATED; 1.
DR Pfam; PF00296; Bac_luciferase; 1.
DR PIRSF; PIRSF000337; NTA_MOA; 1.
DR SUPFAM; SSF51679; Bacterial luciferase-like; 1.
PE 3: Inferred from homology;
KW Flavoprotein {ECO:0000256|PIRSR:PIRSR000337-1};
KW FMN {ECO:0000256|PIRSR:PIRSR000337-1};
KW Oxidoreductase {ECO:0000313|EMBL:ABG94420.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008710}.
FT DOMAIN 23..383
FT /note="Luciferase-like"
FT /evidence="ECO:0000259|Pfam:PF00296"
FT BINDING 57
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000337-1"
FT BINDING 104
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000337-1"
FT BINDING 154
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000337-1"
FT BINDING 158
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000337-1"
FT BINDING 228
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000337-1"
FT BINDING 229
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000337-1"
SQ SEQUENCE 452 AA; 49668 MW; CF01C22CE474ABA6 CRC64;
MSRELHLAGF LIASHVTHSH AAWRHPASET DYLGPDYYRR VAQTLERGKF DFLFFADLLA
TPVRYGNDIR VPLSSGTQAS ATIDPSLVAA GLANVTEKIG LAITKSTTYF HPYEVARIFA
TLDHLSRGRA GWNVVTSLNQ AEAQNFGIEN HLGHDERYDR AQEFLEVAFK LWGSWDRDAL
VRDKASGVFA DPDKVRTVDH EGEWFKTRGP LTVPQSPQSR PVIIQAGSSS VGKDFAARWA
EAIFEIDPTS EGRKAYYDDV KSRASNFGRN PEDIKIFPSF VPFVGETESI AREKQAFHNE
LADPISGLIT MSVHTDHDFS QYDLDAPIED VVVPGTQGLF DVARRLSVKD NLTLRDIGKL
YAQGVLLPQF VGTASQIADQ IEEGFLGGEA DGYILSAAQA PGTFDDFVDL VVPELQRRGL
FRTDYTGSTL RDHLGLGGAS LTPAPRGVAV GA
//
