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Database: UniProt/TrEMBL
Entry: A0A1B2J0Y6_9LACO
LinkDB: A0A1B2J0Y6_9LACO
Original site: A0A1B2J0Y6_9LACO 
ID   A0A1B2J0Y6_9LACO        Unreviewed;       348 AA.
AC   A0A1B2J0Y6;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=alcohol dehydrogenase {ECO:0000256|ARBA:ARBA00013190};
DE            EC=1.1.1.1 {ECO:0000256|ARBA:ARBA00013190};
GN   ORFNames=AYR63_12920 {ECO:0000313|EMBL:ANZ67952.1};
OS   Secundilactobacillus paracollinoides.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Secundilactobacillus.
OX   NCBI_TaxID=240427 {ECO:0000313|EMBL:ANZ67952.1, ECO:0000313|Proteomes:UP000093267};
RN   [1] {ECO:0000313|EMBL:ANZ67952.1, ECO:0000313|Proteomes:UP000093267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TMW 1.1995 {ECO:0000313|EMBL:ANZ67952.1,
RC   ECO:0000313|Proteomes:UP000093267};
RA   Behr J., Geissler A.J., Vogel R.F.;
RT   "Pediococcus and Lactobacillus from brewery environment - whole genome
RT   sequencing and assembly.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a secondary alcohol + NAD(+) = a ketone + H(+) + NADH;
CC         Xref=Rhea:RHEA:10740, ChEBI:CHEBI:15378, ChEBI:CHEBI:17087,
CC         ChEBI:CHEBI:35681, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00000781};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000256|ARBA:ARBA00008072}.
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DR   EMBL; CP014924; ANZ67952.1; -; Genomic_DNA.
DR   RefSeq; WP_056987966.1; NZ_CP014924.1.
DR   AlphaFoldDB; A0A1B2J0Y6; -.
DR   STRING; 240427.AYR62_06015; -.
DR   KEGG; lpd:AYR62_06015; -.
DR   Proteomes; UP000093267; Chromosome.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   CDD; cd08298; CAD2; 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; IPR014187; ADH_Zn_typ-2.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   NCBIfam; TIGR02822; adh_fam_2; 1.
DR   PANTHER; PTHR42940; ALCOHOL DEHYDROGENASE 1-RELATED; 1.
DR   PANTHER; PTHR42940:SF8; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 11; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SUPFAM; SSF50129; GroES-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
FT   DOMAIN          26..344
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   348 AA;  37700 MW;  CF02A0A72B607177 CRC64;
     MTTTQIQNLP TEMKAWQVTT PGPIDGAESP LAFVTKPVPT PERGEVLVKV LACGVCHTDL
     HVTEGDLPVH HEHVTPGHEI VGEVVATGPE TSRFQLGDRI GIPWLRWTCG VCEFCRSGRE
     NLCPNSLYTG WDHDGGYAEY VTAPEGFSYR IPDQFDNITA APLLCAGIIG YRAYHRANLP
     AGGRLGLYGF GGSAHITAQI ALDQGMEVHV LTRGTDARKF ALELGAKSAQ GPYDLPPVKL
     DSSIIFAPVG DIVPKALEGL APGGTLALAG IHLTDIPSLN YQDHIFHEKN LTSVESNTRR
     DGEEFLTLAD RLNIHPETTP YAFDKADEAL RYVKKGDIRG ACVLKISD
//
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