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Database: UniProt
Entry: G0M465_LACPE
LinkDB: G0M465_LACPE
Original site: G0M465_LACPE 
ID   G0M465_LACPE            Unreviewed;       341 AA.
AC   G0M465;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   13-SEP-2023, entry version 33.
DE   RecName: Full=Zinc-type alcohol dehydrogenase-like protein {ECO:0000256|RuleBase:RU364000};
GN   ORFNames=LPENT_01667 {ECO:0000313|EMBL:CCC16971.1};
OS   Lactiplantibacillus pentosus IG1.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactiplantibacillus.
OX   NCBI_TaxID=1042160 {ECO:0000313|EMBL:CCC16971.1};
RN   [1] {ECO:0000313|EMBL:CCC16971.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=IG1 {ECO:0000313|EMBL:CCC16971.1};
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   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. Quinone oxidoreductase subfamily.
CC       {ECO:0000256|RuleBase:RU364000}.
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DR   EMBL; FR874854; CCC16971.1; -; Genomic_DNA.
DR   AlphaFoldDB; G0M465; -.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd08252; AL_MDR; 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; IPR013154; ADH-like_N.
DR   InterPro; IPR014182; ADH_Zn_typ-1.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   InterPro; IPR002364; Quin_OxRdtase/zeta-crystal_CS.
DR   NCBIfam; TIGR02817; adh_fam_1; 1.
DR   PANTHER; PTHR43482; PROTEIN AST1-RELATED; 1.
DR   PANTHER; PTHR43482:SF1; PROTEIN AST1-RELATED; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF13602; ADH_zinc_N_2; 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; PS01162; QOR_ZETA_CRYSTAL; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|RuleBase:RU364000};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU364000,
KW   ECO:0000313|EMBL:CCC16971.1}; Zinc {ECO:0000256|RuleBase:RU364000}.
FT   DOMAIN          16..337
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   341 AA;  37218 MW;  0476C51997E9DF5F CRC64;
     MKAVGFYAPL PIESQDSLQD VTLPVPVVSG HDLLVQVAAV SVNPVDVGVR HAKRRPLSAP
     KIIGWDAYGT VTAVGDQTSL FKVGDKVYYA GSFKRPGSDS QYQLVDERIV GLAPKSIRPE
     EIAAMPLTAL TAYEALFEQL QIPLTAPSQS QPSKTILIIN GAGGVGSIAT QLAKLAGLTV
     ISTASRPESI AWTKAHGADF VVNHRNDLVH EVHQLGLKYV DYILGLNDLD GHWNEMCDLI
     KPSGHIASIT ENHRPINLKK LTKKRGTFAW EWMYAKSYYG TDDLQSQHDI LNQIAAWLDQ
     GLISSTLTKA LTPINAANLR LAHQLVESHH MIGKVVVRGW D
//
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