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Database: UniProt
Entry: A9WN45_RENSM
LinkDB: A9WN45_RENSM
Original site: A9WN45_RENSM 
ID   A9WN45_RENSM            Unreviewed;       309 AA.
AC   A9WN45;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   SubName: Full=Quinone oxidoreductase {ECO:0000313|EMBL:ABY23567.1};
DE            EC=1.6.5.5 {ECO:0000313|EMBL:ABY23567.1};
GN   OrderedLocusNames=RSal33209_1834 {ECO:0000313|EMBL:ABY23567.1};
OS   Renibacterium salmoninarum (strain ATCC 33209 / DSM 20767 / JCM 11484 /
OS   NBRC 15589 / NCIMB 2235).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Renibacterium.
OX   NCBI_TaxID=288705 {ECO:0000313|EMBL:ABY23567.1, ECO:0000313|Proteomes:UP000002007};
RN   [1] {ECO:0000313|Proteomes:UP000002007}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33209 / DSM 20767 / JCM 11484 / NBRC 15589 / NCIMB 2235
RC   {ECO:0000313|Proteomes:UP000002007};
RX   PubMed=18723615; DOI=10.1128/JB.00721-08;
RA   Wiens G.D., Rockey D.D., Wu Z., Chang J., Levy R., Crane S., Chen D.S.,
RA   Capri G.R., Burnett J.R., Sudheesh P.S., Schipma M.J., Burd H.,
RA   Bhattacharyya A., Rhodes L.D., Kaul R., Strom M.S.;
RT   "Genome sequence of the fish pathogen Renibacterium salmoninarum suggests
RT   reductive evolution away from an environmental Arthrobacter ancestor.";
RL   J. Bacteriol. 190:6970-6982(2008).
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
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DR   EMBL; CP000910; ABY23567.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9WN45; -.
DR   STRING; 288705.RSal33209_1834; -.
DR   KEGG; rsa:RSal33209_1834; -.
DR   eggNOG; COG0604; Bacteria.
DR   HOGENOM; CLU_026673_3_3_11; -.
DR   Proteomes; UP000002007; Chromosome.
DR   GO; GO:0003960; F:NADPH:quinone reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd05289; MDR_like_2; 1.
DR   Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR013154; ADH-like_N.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   InterPro; IPR002364; Quin_OxRdtase/zeta-crystal_CS.
DR   PANTHER; PTHR44154; QUINONE OXIDOREDUCTASE; 1.
DR   PANTHER; PTHR44154:SF1; QUINONE OXIDOREDUCTASE; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF13602; ADH_zinc_N_2; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SUPFAM; SSF50129; GroES-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS01162; QOR_ZETA_CRYSTAL; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000313|EMBL:ABY23567.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002007};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT   DOMAIN          14..299
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
FT   REGION          283..309
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   309 AA;  32026 MW;  5B5FAF6873584A74 CRC64;
     MLHRMKMMSF AEFGGPEVLQ IIDAEAPDAG PGQVRIAVRS AGVNPVDWRI REGQFLEAHP
     IELPSGVGID AAGVVDQIGE GVEGYKVGDH VFGEGTNTYA EFAVLSAWAP MPEGLAFEEA
     AGYASVVETA LRIIREVGVQ AGQTLLVSGA SGGVGSAVLQ IARDRGIKVI GTAGAANQDY
     LRSLGALGAT YGAGWVERVQ QLGRVDAALD LAGSGVLPEL VELTGDPARV VSIADLSAAE
     FGVRFSGVAG SVPDALIEAS NLISQGKLHI PVEKIYPLES AAEAQRDSQA GHSRGRRVVV
     PSAPAQLTQ
//
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