ID C0ZMV1_RHOE4 Unreviewed; 328 AA.
AC C0ZMV1;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE SubName: Full=Putative oxidoreductase {ECO:0000313|EMBL:BAH35359.1};
GN OrderedLocusNames=RER_46510 {ECO:0000313|EMBL:BAH35359.1};
OS Rhodococcus erythropolis (strain PR4 / NBRC 100887).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus; Rhodococcus erythropolis group.
OX NCBI_TaxID=234621 {ECO:0000313|EMBL:BAH35359.1, ECO:0000313|Proteomes:UP000002204};
RN [1] {ECO:0000313|Proteomes:UP000002204}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204};
RA Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT "Comparison of the complete genome sequences of Rhodococcus erythropolis
RT PR4 and Rhodococcus opacus B4.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:BAH35359.1, ECO:0000313|Proteomes:UP000002204}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204};
RX PubMed=16423019; DOI=10.1111/j.1462-2920.2005.00899.x;
RA Sekine M., Tanikawa S., Omata S., Saito M., Fujisawa T., Tsukatani N.,
RA Tajima T., Sekigawa T., Kosugi H., Matsuo Y., Nishiko R., Imamura K.,
RA Ito M., Narita H., Tago S., Fujita N., Harayama S.;
RT "Sequence analysis of three plasmids harboured in Rhodococcus erythropolis
RT strain PR4.";
RL Environ. Microbiol. 8:334-346(2006).
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DR EMBL; AP008957; BAH35359.1; -; Genomic_DNA.
DR RefSeq; WP_020908810.1; NC_012490.1.
DR AlphaFoldDB; C0ZMV1; -.
DR KEGG; rer:RER_46510; -.
DR PATRIC; fig|234621.6.peg.5204; -.
DR eggNOG; COG2141; Bacteria.
DR HOGENOM; CLU_027853_6_2_11; -.
DR Proteomes; UP000002204; Chromosome.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR Gene3D; 3.20.20.30; Luciferase-like domain; 1.
DR InterPro; IPR019952; F420_OxRdatse_Rv1855c_pred.
DR InterPro; IPR011251; Luciferase-like_dom.
DR InterPro; IPR036661; Luciferase-like_sf.
DR NCBIfam; TIGR03560; F420_Rv1855c; 1.
DR PANTHER; PTHR42847; ALKANESULFONATE MONOOXYGENASE; 1.
DR PANTHER; PTHR42847:SF8; CONSERVED PROTEIN; 1.
DR Pfam; PF00296; Bac_luciferase; 1.
DR SUPFAM; SSF51679; Bacterial luciferase-like; 1.
PE 4: Predicted;
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW FMN {ECO:0000256|ARBA:ARBA00022643};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 1..299
FT /note="Luciferase-like"
FT /evidence="ECO:0000259|Pfam:PF00296"
SQ SEQUENCE 328 AA; 35893 MW; E5B7E4D9817F49C8 CRC64;
MRFGLFVPQG WRLDLVGIDP AKQWEVMRDF TLRAEAGPWE SVWVYDHFHT VPQPTEEATH
EAWTLMAALG ASTSRIRLGQ MCTAMSYRNP AYLAKVAATT DLITGGRVEM GIGGGWYEQE
WRAYGYGFPS AGERLGRLDE GIQIMQQAWS TGSSTLDGKY YQVDGALCRP LPLQEGGIPI
WVAGGGEKVT LKIAAKYAQY TNFDGTPAGF AHKSEILKKH CDTVGTDFDA IVRSANYNVA
IGATESEVAQ RLETLKDRLT PLVGEAAADA SLDAFRGMPA VGTPEQIIEN LSALKAQGLE
YAIFYFPEAA YDTSGIEMFE KEVLPALA
//
