ID Q0SK30_RHOJR Unreviewed; 454 AA.
AC Q0SK30;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 110.
DE SubName: Full=Probable dibenzothiophene desulfurziation enzyme {ECO:0000313|EMBL:ABG92106.1};
GN OrderedLocusNames=RHA1_ro00270 {ECO:0000313|EMBL:ABG92106.1};
OS Rhodococcus jostii (strain RHA1).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=101510 {ECO:0000313|EMBL:ABG92106.1, 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; ABG92106.1; -; Genomic_DNA.
DR RefSeq; WP_011593559.1; NC_008268.1.
DR AlphaFoldDB; Q0SK30; -.
DR KEGG; rha:RHA1_ro00270; -.
DR PATRIC; fig|101510.16.peg.298; -.
DR eggNOG; COG2141; Bacteria.
DR HOGENOM; CLU_022256_1_2_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 Reference proteome {ECO:0000313|Proteomes:UP000008710}.
FT DOMAIN 16..386
FT /note="Luciferase-like"
FT /evidence="ECO:0000259|Pfam:PF00296"
FT BINDING 56
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000337-1"
FT BINDING 103
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000337-1"
FT BINDING 157
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"
SQ SEQUENCE 454 AA; 50096 MW; 2BF5B24C1E9AEAA1 CRC64;
MSPSRMHLAA FVTAGPGRPG GWRYPGSVPG WLSAGYYQNI ARTLEDARFD LVFFADILSV
PDRFGGSPDS QLRNGALGSM RLDPLHVLSS MGAVTSHLGL AATVSTTYAQ PFTVARSFAT
LDHLTEGRAA WNVVTSFQES EARNFNRDEQ FPRDQRYERA DEFLEVAGKL WDSWEDDALV
LDTEQPLFAD PDRVHPIRHK GDWFTVQGPL NVPRPPQGYP VVIQAGASAK GKDFAARWSD
VIFCSHASLE SAQDFYKEIK ERAAAHGRDP ESVKILPSIA PVVGATTAIA QQTFEELFDL
VPPLGGLSTL AYHLDVDLST FPLDERLPDV EVPGVEGHYQ EVREMTEREG LTLRELGKRY
GGRVEGGFIG TATEVADGLG EWFGQGACDG FMVQAPYQPG GFEDFTRHVV PELQKRGLFR
KEYEGSNLRE NLGLPRVQSG EWANRVRRGA EAAL
//
