ID   D7LBY2_ARALL            Unreviewed;       375 AA.
AC   D7LBY2;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   RecName: Full=Enoyl reductase (ER) domain-containing protein {ECO:0000259|SMART:SM00829};
GN   ORFNames=ARALYDRAFT_320022 {ECO:0000313|EMBL:EFH54829.1};
OS   Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN   [1] {ECO:0000313|Proteomes:UP000008694}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX   PubMed=21478890; DOI=10.1038/ng.807;
RA   Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA   Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA   Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA   Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA   Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA   Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT   "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT   change.";
RL   Nat. Genet. 43:476-481(2011).
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|RuleBase:RU361277}.
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DR   EMBL; GL348716; EFH54829.1; -; Genomic_DNA.
DR   RefSeq; XP_002878570.1; XM_002878524.1.
DR   AlphaFoldDB; D7LBY2; -.
DR   STRING; 81972.D7LBY2; -.
DR   EnsemblPlants; fgenesh1_pm.C_scaffold_4000079; fgenesh1_pm.C_scaffold_4000079; fgenesh1_pm.C_scaffold_4000079.
DR   GeneID; 9316464; -.
DR   Gramene; fgenesh1_pm.C_scaffold_4000079; fgenesh1_pm.C_scaffold_4000079; fgenesh1_pm.C_scaffold_4000079.
DR   KEGG; aly:9316464; -.
DR   eggNOG; KOG0023; Eukaryota.
DR   HOGENOM; CLU_026673_20_2_1; -.
DR   OrthoDB; 1550at2759; -.
DR   Proteomes; UP000008694; Unassembled WGS sequence.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0009809; P:lignin biosynthetic process; IEA:UniProt.
DR   CDD; cd05283; CAD1; 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; IPR047109; CAD-like.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   PANTHER; PTHR42683; ALDEHYDE REDUCTASE; 1.
DR   PANTHER; PTHR42683:SF44; CINNAMYL ALCOHOL DEHYDROGENASE 2-RELATED; 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:UP000008694};
KW   Zinc {ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          17..346
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   375 AA;  40835 MW;  D53D5BDA8AFB8783 CRC64;
     MVDRNKAFGW AANDESGVLS PFHFSRRENC ENDVTVKIFF CGVCHSDLHT IKNHWGISRY
     PVVPGHEIVG IATKVGKNVT KFKEGDRVGV GVIIGSCESC ESCNQDLENY CPEVVFTYNS
     RSSDGTRNQG GYSDVIVVDH RFVLSIPDGL PSDAGAPLLC AGITVYSPMK YYGMAEESGK
     HLGVNGLGGL GHIAVKIGKA FGLRVTVMSR SSEKEREAID RLGADSFLVT TDSQKMKDAT
     GTIDFIIDTV SAEHALLPLF SLLKVSGKLV ALGLPEKPLE LPIFPLVLGR NMVGGSQIGG
     MKETQEMLEF CAKHNIVSDI ELIKMSDINS AMDRLAKSDV RYRFVIDVAN SLVTDSSAEN
     LEDHVDHEVS ITSRF
//