ID A0A1Q5DBN9_9ACTN Unreviewed; 346 AA.
AC A0A1Q5DBN9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-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=AMK18_31335 {ECO:0000313|EMBL:OKI93282.1};
OS Streptomyces sp. CB01249.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1703929 {ECO:0000313|EMBL:OKI93282.1, ECO:0000313|Proteomes:UP000186839};
RN [1] {ECO:0000313|EMBL:OKI93282.1, ECO:0000313|Proteomes:UP000186839}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB01249 {ECO:0000313|EMBL:OKI93282.1,
RC ECO:0000313|Proteomes:UP000186839};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(2016).
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:OKI93282.1}.
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DR EMBL; LISW01000009; OKI93282.1; -; Genomic_DNA.
DR RefSeq; WP_018102861.1; NZ_LISW01000009.1.
DR AlphaFoldDB; A0A1Q5DBN9; -.
DR OrthoDB; 334894at2; -.
DR Proteomes; UP000186839; 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 Reference proteome {ECO:0000313|Proteomes:UP000186839};
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; 35454 MW; 2D68C909CB946366 CRC64;
MKAVQYREIG AAPEVVTVPD PEPGPGQVLL KVTAAGVCHS DIAVMSWTAD EFPYPLPLTL
GHEGVGTIAA LGDGVSGLET GQSVAVYGPW GCGTCVKCAE GKENYCLRAA ELGINPPGLG
SPGAMAEYMI VDDPRHLVPL GDLDPVRTVP LTDAGLTPYH AIKRSLPKLV PGATAVVIGT
GGLGHVAIQL LRALTSARVI ALDVTEDKLA LARTVGAHET VLSDEHAAAR IRELTGGIGA
QVVLDFVGAP PTVATAGAAA AIDSDVTIVG IGGGALPVGF GALPFNTTVT APYWGSRSEL
AEVLDLARTG AVDVHVETYP LDEAPLAYER LHAGKINGRA VILPQS
//
