ID A0A1S6QHZ8_9LACO Unreviewed; 345 AA.
AC A0A1S6QHZ8;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Alcohol dehydrogenase {ECO:0000256|ARBA:ARBA00016352};
DE EC=1.1.1.1 {ECO:0000256|ARBA:ARBA00013190};
GN ORFNames=PL11_004480 {ECO:0000313|EMBL:AQW21232.1};
OS Lentilactobacillus curieae.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lentilactobacillus.
OX NCBI_TaxID=1138822 {ECO:0000313|EMBL:AQW21232.1, ECO:0000313|Proteomes:UP000030361};
RN [1] {ECO:0000313|EMBL:AQW21232.1, ECO:0000313|Proteomes:UP000030361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCTCC M 2011381 {ECO:0000313|EMBL:AQW21232.1,
RC ECO:0000313|Proteomes:UP000030361};
RX PubMed=26021929;
RA Wang Y., Wang Y., Lang C., Wei D., Xu P., Xie J.;
RT "Genome Sequence of Lactobacillus curieae CCTCC M 2011381T, a Novel
RT Producer of Gamma-aminobutyric Acid.";
RL Genome Announc. 3:0-0(2015).
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; CP018906; AQW21232.1; -; Genomic_DNA.
DR RefSeq; WP_035166641.1; NZ_CP018906.1.
DR AlphaFoldDB; A0A1S6QHZ8; -.
DR KEGG; lcu:PL11_004480; -.
DR eggNOG; COG1064; Bacteria.
DR OrthoDB; 9806940at2; -.
DR Proteomes; UP000030361; Chromosome.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; 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; IPR002328; ADH_Zn_CS.
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.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000030361}.
FT DOMAIN 22..340
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 345 AA; 37541 MW; 6FFE110B6166A99E CRC64;
MKYQIPETMR AWQITTPGKI DGSKSPLELV TKPVPQPQRG EVLVRVLTCG VCHTDLHVTE
GDLPVHKDHL TPGHEIVGEV VKQGPESSRF KLGDRIGIPW LRWTCGVCQY CRSGKENLCP
NSLYTGWDHD GGYAEYATVP EGFAYRIPDR FDSQTAAPLL CAGIIGYRAF LRANIPAGGK
LGLYGFGGSA HITAQLAIDQ GMEVHVLTRG EDAKKFALKL GAKSVNGAYD LPPVKLDSSI
IFAPVGDIVP KALEGLKPGG TLALAGIHMT DVPQISYQEH IFHEKNLTSV ESNTRSDGEH
FLTLADRLGI EPKTTPYPFE KADEALRYVS KGDIKGACVL KIGEK
//