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Database: UniProt
Entry: G0LYK9_LACPE
LinkDB: G0LYK9_LACPE
Original site: G0LYK9_LACPE 
ID   G0LYK9_LACPE            Unreviewed;       357 AA.
AC   G0LYK9;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   SubName: Full=Dehydrogenase {ECO:0000313|EMBL:CCC15428.1};
GN   ORFNames=LPENT_00123 {ECO:0000313|EMBL:CCC15428.1};
OS   Lactiplantibacillus pentosus IG1.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactiplantibacillus.
OX   NCBI_TaxID=1042160 {ECO:0000313|EMBL:CCC15428.1};
RN   [1] {ECO:0000313|EMBL:CCC15428.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=IG1 {ECO:0000313|EMBL:CCC15428.1};
RA   Maldonado-Barragan A., Caballero-Guerrero B., Lucena-Padros H.,
RA   Ruiz-Barba J.L.;
RT   "Genome Sequence of Lactobacillus pentosus IG1, a Strain Isolated from
RT   Spanish-Style Green Olive Fermentations.";
RL   J. Bacteriol. 193:5605-5605(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|ARBA:ARBA00008072, ECO:0000256|RuleBase:RU361277}.
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DR   EMBL; FR874849; CCC15428.1; -; Genomic_DNA.
DR   AlphaFoldDB; G0LYK9; -.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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; PTHR43161:SF23; (R,R)-BUTANEDIOL DEHYDROGENASE-RELATED; 1.
DR   PANTHER; PTHR43161; SORBITOL DEHYDROGENASE; 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|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU361277};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          8..353
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   357 AA;  38338 MW;  B0431C129F1922E8 CRC64;
     MKAAVIYGPK DIRFEKRNIP DPAPDEVQIE VAFNGICGSD IHEYLEGMDL ATMPHPLTHM
     QAPLIPGHEF SGTISKIGKQ VSKLRIGDKV AVEPMIACGK CPECLSGHYN WCEHAIGSDQ
     SAGFLGFSAN GGLAEKCNVK STFAHLLPTN FPLDLGALVE PVSVAAQAVM ASRVSPGDDV
     LIQGAGPIGL FTALIAQISG AHHVIINDMS EERLDLANEL GVQYPIRADS QKSLAHAIST
     ITENQGVDVA FDCAGVQPTL TGAIQALKNG GKVTVIALFQ HPPVVDVRAL LKKGGSLLTS
     YGYANIFDRV IKIIDTHRSL FKRVITKKIE LNELVSEGIE SLEKDKKQAK ILVRLHS
//
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