ID A0A101TCP6_9ACTN Unreviewed; 347 AA.
AC A0A101TCP6;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Alcohol dehydrogenase {ECO:0000313|EMBL:KUN89889.1};
GN ORFNames=AQJ66_02130 {ECO:0000313|EMBL:KUN89889.1};
OS Streptomyces bungoensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=285568 {ECO:0000313|EMBL:KUN89889.1, ECO:0000313|Proteomes:UP000053024};
RN [1] {ECO:0000313|EMBL:KUN89889.1, ECO:0000313|Proteomes:UP000053024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 41781 {ECO:0000313|EMBL:KUN89889.1,
RC ECO:0000313|Proteomes:UP000053024};
RA Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT "Draft genome sequence of Streptomyces bungoensis DSM 41781, type strain
RT for the species Streptomyces bungoensis.";
RL Submitted (OCT-2015) 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|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:KUN89889.1}.
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DR EMBL; LMWX01000003; KUN89889.1; -; Genomic_DNA.
DR RefSeq; WP_061915499.1; NZ_KQ948851.1.
DR AlphaFoldDB; A0A101TCP6; -.
DR STRING; 285568.AQJ66_02130; -.
DR OrthoDB; 334894at2; -.
DR Proteomes; UP000053024; 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; PTHR43350; NAD-DEPENDENT ALCOHOL DEHYDROGENASE; 1.
DR PANTHER; PTHR43350:SF17; NAD-DEPENDENT ALCOHOL DEHYDROGENASE; 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:UP000053024};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 2..343
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 347 AA; 36222 MW; A52E65CF15C30D23 CRC64;
MRAFQLVGWR QPPELREVPV PGPGPGQVLV KVAGAGACHS DLHIMQAPGP LPGFTNLPFT
LGHENAGWVE QLGPGVTGFA PGDPVIVYGA WGCGGCANCR EGRENYCQNL GGEGPGLRGG
HDGGMAEYLL VPAARYLIPL GALDPRQAAP LSDAGLTGYH AVKRSLHLLG PGSTAVVIGA
GGLGQMTIQI LRALSAATTV VAVDTDVGKL ETAQRLGAEE ALLPGDEAIA RIRDMTARQG
AQLVLDTVGI DPTLRMAAQV ARMLGHLTIV GLGGGALPVD FSSPPHECSV ASPYWGSLTE
LMEVITLAQQ EKIEVLVEHF PLQRANEAYQ LLHDGRIQGR AVITPHG
//
