ID   A0A0W1R705_9EURY        Unreviewed;       336 AA.
AC   A0A0W1R705;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Alcohol dehydrogenase {ECO:0000313|EMBL:KTG09161.1};
GN   ORFNames=AUR64_15310 {ECO:0000313|EMBL:KTG09161.1};
OS   Haloprofundus marisrubri.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloprofundus.
OX   NCBI_TaxID=1514971 {ECO:0000313|EMBL:KTG09161.1, ECO:0000313|Proteomes:UP000054387};
RN   [1] {ECO:0000313|EMBL:KTG09161.1, ECO:0000313|Proteomes:UP000054387}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SB9 {ECO:0000313|EMBL:KTG09161.1,
RC   ECO:0000313|Proteomes:UP000054387};
RA   Zhang G., Stingl U., Rashid M.;
RT   "Haloprofundus marisrubri gen. nov., sp. nov., an extremely halophilic
RT   archaeon isolated from the Discovery deep brine-seawater interface in the
RT   Red Sea.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947,
CC         ECO:0000256|RuleBase:RU361277};
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000256|ARBA:ARBA00008072, ECO:0000256|RuleBase:RU361277}.
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:KTG09161.1}.
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DR   EMBL; LOPU01000029; KTG09161.1; -; Genomic_DNA.
DR   RefSeq; WP_058582314.1; NZ_LOPU01000029.1.
DR   AlphaFoldDB; A0A0W1R705; -.
DR   STRING; 1514971.AUR64_15310; -.
DR   OrthoDB; 75495at2157; -.
DR   Proteomes; UP000054387; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd08296; CAD_like; 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; IPR013149; ADH-like_C.
DR   InterPro; IPR013154; ADH-like_N.
DR   InterPro; IPR002328; ADH_Zn_CS.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   PANTHER; PTHR42940; ALCOHOL DEHYDROGENASE 1-RELATED; 1.
DR   PANTHER; PTHR42940:SF7; ALCOHOL DEHYDROGENASE N-TERMINAL DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 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; PS00059; ADH_ZINC; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|RuleBase:RU361277};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Zinc {ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          10..332
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   336 AA;  35538 MW;  9FB669AD5CF84621 CRC64;
     MKAVQVTEPG EPFEVVDRDV PDPAADEVRV EVDACGICHS DVFVKEGQWP GVEYPRIPGH
     EVAGRIDAVG DDVEAWEVGD RVGVGWHGGH CFTCDACRRG NFINCENAKV TGISYDGGYA
     EYMTAPQEAL ARMPEDLDSV DAAPLLCAGI TTFNALRNTD ARAGDLVAVQ GVGGLGHLAI
     QYAHAAGFET VAISRSPDKE DLAYDLGADH FLDASEVDPA EELQSMGGAR VVLGTAPSAD
     AMESVAGGLG VDGELVAVAV PGGPVSVPVQ QFVTSRNAVS GWPSGDARDS QDTLEFSDLR
     DITPEIEMYA LEDAEEAYDA MLDNEVRFRA VLVPGE
//