ID M0LSP3_9EURY Unreviewed; 334 AA.
AC M0LSP3;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Zinc-binding dehydrogenase family oxidoreductase {ECO:0000313|EMBL:EMA36562.1};
GN ORFNames=C447_14931 {ECO:0000313|EMBL:EMA36562.1};
OS Halococcus hamelinensis 100A6.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halococcaceae; Halococcus.
OX NCBI_TaxID=1132509 {ECO:0000313|EMBL:EMA36562.1, ECO:0000313|Proteomes:UP000011566};
RN [1] {ECO:0000313|EMBL:EMA36562.1, ECO:0000313|Proteomes:UP000011566}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=100A6 {ECO:0000313|EMBL:EMA36562.1,
RC ECO:0000313|Proteomes:UP000011566};
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 -!- 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:EMA36562.1}.
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DR EMBL; AOMB01000041; EMA36562.1; -; Genomic_DNA.
DR RefSeq; WP_007695280.1; NZ_AOMB01000041.1.
DR AlphaFoldDB; M0LSP3; -.
DR PATRIC; fig|1132509.6.peg.3477; -.
DR eggNOG; arCOG01455; Archaea.
DR OrthoDB; 8709at2157; -.
DR Proteomes; UP000011566; 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 Reference proteome {ECO:0000313|Proteomes:UP000011566};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 11..332
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 334 AA; 35150 MW; 172EFDD69BA50FC4 CRC64;
MRAVQVPEPE GDFEVVEVDV PEPGPEEVRV SVDACGVCHS DAFLKEGQWP GVEYPRTPGH
EVVGHVDAVG ERVETFEAGD RVGVGWHGGH CFTCEPCRRG DFIACENGDV TGFDHDGGYA
EYLTAPQETL ARVPDDLDAT AAAPLLCAGV TTFNSLRNSE AEPGDLVAVQ GVGGLGHLGV
QYASAFGFET VAVSRGTEKR DLAFDLGADH YVDSEAEDPA EALTELGGAS VVLATAPHVD
AMESVVGGLG VEGTLLTVGV PGEPLSVPVQ PLVTSRQSVA GWPSGDARDS QDTLEFSSLR
DVASMVETYS LEEADAAYES MMNSEARFRA VIEP
//
