ID   A0A373DNY5_9MICO        Unreviewed;       370 AA.
AC   A0A373DNY5;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Dehydrogenase {ECO:0000313|EMBL:RGE21070.1};
GN   ORFNames=D1J51_07565 {ECO:0000313|EMBL:RGE21070.1};
OS   Leucobacter sp. wl10.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Leucobacter.
OX   NCBI_TaxID=2304677 {ECO:0000313|EMBL:RGE21070.1, ECO:0000313|Proteomes:UP000263010};
RN   [1] {ECO:0000313|EMBL:RGE21070.1, ECO:0000313|Proteomes:UP000263010}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=wl10 {ECO:0000313|Proteomes:UP000263010};
RA   Liu H.;
RT   "Leucobacter sp. wl 10 isolated from wastewater.";
RL   Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU361277};
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {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:RGE21070.1}.
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DR   EMBL; QWBV01000008; RGE21070.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A373DNY5; -.
DR   OrthoDB; 334894at2; -.
DR   Proteomes; UP000263010; 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; cd08279; Zn_ADH_class_III; 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; PTHR43880; ALCOHOL DEHYDROGENASE; 1.
DR   PANTHER; PTHR43880:SF12; ALCOHOL DEHYDROGENASE CLASS-3; 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; 2.
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:UP000263010};
KW   Zinc {ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          10..369
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   370 AA;  38276 MW;  0E81F4AE222A48FA CRC64;
     MKAVVFRDPE TRVRVVDVDL AAPKAGEVRV RIAAAGVCHS DLHVKRGEWN APAPMVMGHE
     GSGVVTELGE GVTSLAVGDH VVLSWVPPCG ECRYCLQGHE ARCQKVATVV APRGVLFDGT
     SRLSSGGESL HHYLAVSSFA EEVVVPASGA IKVRDDAPLD VIAVVGCAVA TGVGAVLNTA
     AVEPGATVAV IGCGGVGLNV VQGAKLAGAE RIIAIDVVPD KTRMALQFGA TDRIDASEVA
     GSGRDAVERL FELVPDGVDY AFDAIGRTST TEQAIRMLGL GGAAVIVGLP PTGARASFEP
     LVLAEADQRI LGSNYGSVRP SIDIPALVDR YMDGQLKLDP LISGRRPLGE AAEAFDDLEA
     GGVLRTLLIP
//