ID   M0FNU7_9EURY            Unreviewed;       316 AA.
AC   M0FNU7;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=NADPH:quinone reductase {ECO:0000313|EMBL:ELZ60942.1};
GN   ORFNames=C460_04009 {ECO:0000313|EMBL:ELZ60942.1};
OS   Haloferax sp. ATCC BAA-646.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloferax.
OX   NCBI_TaxID=1227464 {ECO:0000313|EMBL:ELZ60942.1, ECO:0000313|Proteomes:UP000011677};
RN   [1] {ECO:0000313|Proteomes:UP000011677}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-646 {ECO:0000313|Proteomes:UP000011677};
RA   Becker E.A., Seitzer P., Tritt A., Larsen D., Yao A., Wu D., Darling A.,
RA   Eisen J.A., Facciotti M.T.;
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ELZ60942.1, ECO:0000313|Proteomes:UP000011677}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-646 {ECO:0000313|EMBL:ELZ60942.1,
RC   ECO:0000313|Proteomes:UP000011677};
RX   PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA   Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA   Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT   strategies for static and dynamic osmo-response.";
RL   PLoS Genet. 10:E1004784-E1004784(2014).
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ELZ60942.1}.
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DR   EMBL; AOLD01000017; ELZ60942.1; -; Genomic_DNA.
DR   RefSeq; WP_008574184.1; NZ_AOLD01000017.1.
DR   AlphaFoldDB; M0FNU7; -.
DR   PATRIC; fig|1227464.4.peg.779; -.
DR   Proteomes; UP000011677; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; 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   PANTHER; PTHR48106:SF8; QUINONE OXIDOREDUCTASE PIG3; 1.
DR   PANTHER; PTHR48106; QUINONE OXIDOREDUCTASE PIG3-RELATED; 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.
PE   4: Predicted;
FT   DOMAIN          10..306
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   316 AA;  34166 MW;  DF5A47E891503410 CRC64;
     MKAVRIHEYG SPDVLRYEDV DEPEPAADEV RVRVRAAGVN PVDWLTRNGL VERDELPWTV
     GWDAAGVVDA VGSDVHDLEV GDEVYGLVEF EYGGGAYAEA VTAPKDELVR KPASLSFEEA
     AGVPMAALTA WQALEAVDVD AGGRVLIHAA AGGVGHFAVQ FARERDLHVI GTASGSNEEY
     LRELGVDEFV NYREQRFEAV LDPIDGVIDG VGGETFDRSL EILNEGGIID KLPSPPTAEQ
     QELADEHGVE AIMTNVRWNG DWFDDITELL ADGTVSVTLD TVLPLSEARE AHRLSEAKHA
     RGKIILTPGD DESASN
//