ID   F3Z5D6_9ACTN            Unreviewed;       358 AA.
AC   F3Z5D6;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   SubName: Full=Putative alcohol dehydrogenase {ECO:0000313|EMBL:EGJ78423.1};
GN   ORFNames=STTU_5634 {ECO:0000313|EMBL:EGJ78423.1};
OS   Streptomyces sp. Tu6071.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=355249 {ECO:0000313|EMBL:EGJ78423.1};
RN   [1] {ECO:0000313|EMBL:EGJ78423.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Tu6071 {ECO:0000313|EMBL:EGJ78423.1};
RA   Erxleben A., Wunsch-Palasis J., Gruening B.A., Luzhetska M., Bechthold A.,
RA   Gunther S.;
RT   "Genome sequence of Streptomyces sp. Tu6071.";
RL   Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU361277};
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000256|RuleBase:RU361277}.
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DR   EMBL; CM001165; EGJ78423.1; -; Genomic_DNA.
DR   RefSeq; WP_007828865.1; NZ_CM001165.1.
DR   AlphaFoldDB; F3Z5D6; -.
DR   HOGENOM; CLU_026673_11_2_11; -.
DR   Proteomes; UP000003955; Chromosome.
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; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   PANTHER; PTHR43880; ALCOHOL DEHYDROGENASE; 1.
DR   PANTHER; PTHR43880:SF12; ALCOHOL DEHYDROGENASE CLASS-3; 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   Zinc {ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          11..357
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   358 AA;  36511 MW;  BCF9F480C37BF99D CRC64;
     MVRAAVQSAV GAPLEIARID LPEPGPGQVR VRLAAAGVCH SDLSLSDGTL RVPLPAVLGH
     EGSGTVVSIG EGVRSVRPGD PVVLNWAPSC GTCAACGRGE VWLCENALTG AGAEYARTED
     GRTLHPGLNV AAFAEETVVS EACLLPAPEG VALDEAALLG CAVLTGYGAV HHAARVREGE
     SVVVFGAGGV GLAALQAARI AGAGSILAVD TSPAKEELAR RAGATDFVLA SGTTAKEVRR
     LTGGGADVAI ECVGRAVTIR TAWESTRRGG RTTVVGIGPV TEEVRFNARE LFHWGRTLSG
     CVYGNSDPAA DVPVLGEHVR AGRLDLSALV TERVPLDAIP DAFAAMRAGK GARALVVF
//