ID   I0L359_9ACTN            Unreviewed;       361 AA.
AC   I0L359;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   SubName: Full=Zinc-dependent alcohol dehydrogenase (Zinc-binding dehydrogenase) {ECO:0000313|EMBL:CCH18256.1};
GN   ORFNames=MILUP08_43161 {ECO:0000313|EMBL:CCH18256.1};
OS   Micromonospora lupini str. Lupac 08.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=1150864 {ECO:0000313|EMBL:CCH18256.1, ECO:0000313|Proteomes:UP000003448};
RN   [1] {ECO:0000313|Proteomes:UP000003448}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lupac 08 {ECO:0000313|Proteomes:UP000003448};
RX   PubMed=22815450; DOI=10.1128/jb.00628-12;
RA   Alonso-Vega P., Normand P., Bacigalupe R., Pujic P., Lajus A., Vallenet D.,
RA   Carro L., Coll P., Trujillo M.E.;
RT   "Genome Sequence of Micromonospora lupini Lupac 08, Isolated from Root
RT   Nodules of Lupinus angustifolius.";
RL   J. Bacteriol. 194:4135-4135(2012).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947,
CC         ECO:0000256|RuleBase:RU361277};
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000256|RuleBase:RU361277}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CCH18256.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CAIE01000025; CCH18256.1; -; Genomic_DNA.
DR   RefSeq; WP_007459489.1; NZ_HF570108.1.
DR   AlphaFoldDB; I0L359; -.
DR   STRING; 1150864.MILUP08_43161; -.
DR   eggNOG; COG1062; Bacteria.
DR   OrthoDB; 334894at2; -.
DR   Proteomes; UP000003448; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd08279; Zn_ADH_class_III; 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; IPR013149; ADH-like_C.
DR   InterPro; IPR013154; ADH-like_N.
DR   InterPro; IPR002328; ADH_Zn_CS.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR017816; MycoS_dep_FDH.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   NCBIfam; TIGR03451; mycoS_dep_FDH; 1.
DR   PANTHER; PTHR43350; NAD-DEPENDENT ALCOHOL DEHYDROGENASE; 1.
DR   PANTHER; PTHR43350:SF19; RIBULOSE-5-PHOSPHATE REDUCTASE; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SUPFAM; SSF50129; GroES-like; 2.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00059; ADH_ZINC; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|RuleBase:RU361277};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003448};
KW   Zinc {ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          14..359
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   361 AA;  37873 MW;  17CAD15FB4F4D00C CRC64;
     MSQEVRGVIS RSKGAPVEVT TIVVPDPGPG EAIVRIQSCG VCHTDLHYRE GGINDDYPFL
     LGHEAAGVVE QVGEGVTDVA PGDFVVLNWR AVCGVCRACR RGRPWYCFNT HNAAQRMTLT
     DGTELAPALG IGAFAEKTLV HAGQCTKVNP AARPAAVGLL GCGVMAGLGA AMNTGNVTRG
     DSVAVIGCGG VGDAAVVGAA LAGATTIVAV DTDSRKLDWA RQFGATHTVN ASETDPVEAI
     RAATGGFGAD VVIDAVGRPE TWKQAFYARD LAGTVVLVGV PTPQMQIELP LLDVFGRGGA
     LKSSWYGDCL PSRDFPMLTD LYLQGRLDLD AFVTEEIALD QVENAFDRMH HGDVLRSVVV
     F
//