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Database: UniProt/TrEMBL
Entry: A0A168EM58_9MICO
LinkDB: A0A168EM58_9MICO
Original site: A0A168EM58_9MICO 
ID   A0A168EM58_9MICO        Unreviewed;       342 AA.
AC   A0A168EM58;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=alcohol dehydrogenase {ECO:0000256|ARBA:ARBA00013190};
DE            EC=1.1.1.1 {ECO:0000256|ARBA:ARBA00013190};
GN   Name=adh_1 {ECO:0000313|EMBL:ANC30208.1};
GN   ORFNames=I598_0628 {ECO:0000313|EMBL:ANC30208.1};
OS   Isoptericola dokdonensis DS-3.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC   Promicromonosporaceae; Isoptericola.
OX   NCBI_TaxID=1300344 {ECO:0000313|EMBL:ANC30208.1, ECO:0000313|Proteomes:UP000076794};
RN   [1] {ECO:0000313|EMBL:ANC30208.1, ECO:0000313|Proteomes:UP000076794}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS-3 {ECO:0000313|EMBL:ANC30208.1,
RC   ECO:0000313|Proteomes:UP000076794};
RA   Kwon S.-K., Kim J.F.;
RT   "Complete genome sequence of a soil Actinobacterium, Isoptericola
RT   dokdonensis DS-3.";
RL   Submitted (JAN-2016) 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}.
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DR   EMBL; CP014209; ANC30208.1; -; Genomic_DNA.
DR   RefSeq; WP_068201197.1; NZ_CP014209.1.
DR   AlphaFoldDB; A0A168EM58; -.
DR   STRING; 1300344.I598_0628; -.
DR   KEGG; ido:I598_0628; -.
DR   PATRIC; fig|1300344.3.peg.631; -.
DR   OrthoDB; 3567264at2; -.
DR   Proteomes; UP000076794; Chromosome.
DR   GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd08297; CAD3; 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   ECO:0000313|EMBL:ANC30208.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076794};
KW   Zinc {ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          6..338
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   342 AA;  35923 MW;  D4A3AD4C35616DE3 CRC64;
     MTMKAAVVRE FRAPLDVTDA ELPTPGPGQA LVKVLYSGVC HTDLHAAHGD WPVKPTPPFI
     PGHEGVGEVV AVADDVTRLH VGDTVGNAWL WSACGECEYC ETGRETLCPN QLNGGYSVDG
     SFGQYMLVDA TYAPIVPAGV DLAAAAPILC AGVTVYKGLK ESEVKPGQWV LISGIGGLGH
     IAVQYAHAMG MRVVAVDVSD DKLALARRHG AEATVNARTT DDVVARIHEV TGGGAHGGLV
     TAVNGKAFPQ AVGGLRRGGT VSLVGLPPEE FGLDIFSTVL FGLTVRGSIV GTRKDMTEAL
     DFFARGLIEP TYTVRPLADI NDIFDEMLHG AIDGRVVMDM QA
//
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