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Database: UniProt
Entry: A0A086N7R1_9ACTN
LinkDB: A0A086N7R1_9ACTN
Original site: A0A086N7R1_9ACTN 
ID   A0A086N7R1_9ACTN        Unreviewed;       346 AA.
AC   A0A086N7R1;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=alcohol dehydrogenase {ECO:0000256|ARBA:ARBA00013190};
DE            EC=1.1.1.1 {ECO:0000256|ARBA:ARBA00013190};
GN   ORFNames=FM21_14345 {ECO:0000313|EMBL:KFG77179.1};
OS   Streptomyces mutabilis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=67332 {ECO:0000313|EMBL:KFG77179.1, ECO:0000313|Proteomes:UP000029095};
RN   [1] {ECO:0000313|EMBL:KFG77179.1, ECO:0000313|Proteomes:UP000029095}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TRM45540 {ECO:0000313|EMBL:KFG77179.1,
RC   ECO:0000313|Proteomes:UP000029095};
RA   Luo X., Zhang L.;
RT   "Complete genome sequence of the Streptomyces mutabilis TRM45540.";
RL   Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00008072, 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:KFG77179.1}.
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DR   EMBL; JNFQ01000001; KFG77179.1; -; Genomic_DNA.
DR   RefSeq; WP_043376263.1; NZ_KN039946.1.
DR   AlphaFoldDB; A0A086N7R1; -.
DR   STRING; 1915400.FM21_14345; -.
DR   HOGENOM; CLU_026673_11_2_11; -.
DR   Proteomes; UP000029095; 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; cd05284; arabinose_DH_like; 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; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
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   Pfam; PF00107; ADH_zinc_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   Metal-binding {ECO:0000256|RuleBase:RU361277};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Zinc {ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          10..342
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   346 AA;  35349 MW;  8550B2108728AB87 CRC64;
     MKALQYRTIG APPEVVTVRD PEPGPGQVLL KVTAAGVCHS DIAVMGWPAE GFPYELPLTL
     GHEGVGTVAA LGDGVTGLNE GDAVAVYGPW GCGTCAKCAE GKENYCLRAG ELGIHPPGLG
     RPGSMAEYLL VDDPRHLVPL DGLDPVAAVP LTDAGLTPYH AVKRSLPKLV PGSTAVVIGA
     GGLGHVAIQL LRALTSARVV ALDVSEDKLR LAREVGAHEA VLSDEKAADA VRELTGGLGA
     EAVFDFVGAA PTVRTAGAVA AVEGDVTLVG IGGGSIPVGF GLLPFEVSVS APYWGSRGEL
     IEVLNLARSG AVSVHTETYS LDDAPLAYER LHGGKVNGRA VILPHG
//
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