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Database: UniProt/TrEMBL
Entry: A0A1W6SP15_9PROT
LinkDB: A0A1W6SP15_9PROT
Original site: A0A1W6SP15_9PROT 
ID   A0A1W6SP15_9PROT        Unreviewed;       336 AA.
AC   A0A1W6SP15;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=alcohol dehydrogenase {ECO:0000256|ARBA:ARBA00013190};
DE            EC=1.1.1.1 {ECO:0000256|ARBA:ARBA00013190};
GN   ORFNames=EBAPG3_007040 {ECO:0000313|EMBL:ARO87544.1};
OS   Nitrosospira lacus.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosospira.
OX   NCBI_TaxID=1288494 {ECO:0000313|EMBL:ARO87544.1, ECO:0000313|Proteomes:UP000012179};
RN   [1] {ECO:0000313|EMBL:ARO87544.1, ECO:0000313|Proteomes:UP000012179}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APG3 {ECO:0000313|EMBL:ARO87544.1,
RC   ECO:0000313|Proteomes:UP000012179};
RX   PubMed=25336720; DOI=10.1099/ijs.0.070789-0;
RA   Urakawa H., Garcia J.C., Nielsen J.L., Le V.Q., Kozlowski J.A., Stein L.Y.,
RA   Lim C.K., Pommerening-Roser A., Martens-Habbena W., Stahl D.A., Klotz M.G.;
RT   "Nitrosospira lacus sp. nov., a psychrotolerant, ammonia-oxidizing
RT   bacterium from sandy lake sediment.";
RL   Int. J. Syst. Evol. Microbiol. 65:242-250(2015).
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; CP021106; ARO87544.1; -; Genomic_DNA.
DR   RefSeq; WP_004180025.1; NZ_CP021106.3.
DR   AlphaFoldDB; A0A1W6SP15; -.
DR   KEGG; nlc:EBAPG3_007040; -.
DR   eggNOG; COG1064; Bacteria.
DR   Proteomes; UP000012179; 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:UP000012179}.
FT   DOMAIN          17..332
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   336 AA;  36343 MW;  6AEC01669C2AB546 CRC64;
     MSELNYSMQA MVLDEPGQTV HMRCLPRPLP NPDQLLVRVA ACAVCRTDLH IVDGELPNPK
     LPIIPGHEIV GRVVSCGTNV PNFSIGERVG IPWLGWTCGH CRYCRNGHEN LCEDAKFTGY
     QIDGGYAEYA VADARYCFRI PEIYSDVEAA PLLCAGLIGY RALKMAGSAD RVGIYGFGAA
     AHIVAQILRY QGRKLFAFTR PGDVTAQDFA DKMGAAWVGG SDRMPPEELD AAIIFAPDGT
     LVPAALRAIR PGGIVICGGI HMSDIPAFPY SILWREKQLV SVANLTRQDA EEFLALAPKV
     PVRVTTESLP LSQAGTALMR LREGKLTGAA VLVPDL
//
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