ID C0ZMZ4_RHOE4 Unreviewed; 666 AA.
AC C0ZMZ4;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE SubName: Full=Putative oxidoreductase {ECO:0000313|EMBL:BAH35402.1};
GN OrderedLocusNames=RER_46940 {ECO:0000313|EMBL:BAH35402.1};
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:BAH35402.1, 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:BAH35402.1, 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).
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
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DR EMBL; AP008957; BAH35402.1; -; Genomic_DNA.
DR AlphaFoldDB; C0ZMZ4; -.
DR KEGG; rer:RER_46940; -.
DR eggNOG; COG0446; Bacteria.
DR eggNOG; COG1902; Bacteria.
DR HOGENOM; CLU_012153_1_2_11; -.
DR Proteomes; UP000002204; Chromosome.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd02803; OYE_like_FMN_family; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR001155; OxRdtase_FMN_N.
DR PANTHER; PTHR42917; 2,4-DIENOYL-COA REDUCTASE; 1.
DR PANTHER; PTHR42917:SF2; 2,4-DIENOYL-COA REDUCTASE [(2E)-ENOYL-COA-PRODUCING]; 1.
DR Pfam; PF00724; Oxidored_FMN; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00419; ADXRDTASE.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
PE 4: Predicted;
FT DOMAIN 25..344
FT /note="NADH:flavin oxidoreductase/NADH oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00724"
FT DOMAIN 391..617
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 666 AA; 70639 MW; 6B5D3795848FEEF4 CRC64;
MSTTEHLLSR EVPGALMKVT APFAEPLDMG SVRLRNRFVS APMERNYCEV DGTMTDEYIA
YLARRAEGGA ALIFTEASYV RADGKGRIRQ MGVDVDERIP GIKKMADAIH AHGALVGVEL
NHGGRTAQGS VSGFVPVAPT PIPCLVVGGE MPEQLDGDDI EHIIECFGEA AARCQQAGVD
VISLHGGHGY LIHQFLSPAY NHRDDEWADP TLFVNKVIAS VHEHAPGITL GLRFSAFEGI
DGGLDAETTR SRIDAIDTDR LDFLDVSAGN YEAGQWIIQP GEWSRGLLAP YSEQYQRDFD
IPVGVAGRIT SPEIAAQIIE SGQANFVSMA RTLHADPDFP NRAVDGGRYR PCIACNYCID
SLAAGPIPCS VNPWVGRELD QPTKPADATV RVAVIGAGPS GMAAARDLAL AGHRVDLYDE
RPSLGGDFAL ASKLHEYPEY GRIVDWYLAE LAELGVQCHT STRADAALLA NSDFDAIVLA
AGGHGPVTDL PGAQTRTVRD VREFLVSGDP APEAITIFGA DREAAAVADD LLQKGTQVVM
IGPQETIAHD VGRRGKIVLL PRLAASENLT TYLSSIVTKV DADRVTISTG GVLSEVDAPG
ELLISQGVEP RSELLAELRS LAPRLGVHAV GDASGDGGSI HAALVTAADV AVAITAAAAA
RQEVHA
//
