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Database: UniProt/TrEMBL
Entry: A0A1S6QHZ8_9LACO
LinkDB: A0A1S6QHZ8_9LACO
Original site: A0A1S6QHZ8_9LACO 
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
//
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