ID   A0A2S2C5Y9_9NOCA        Unreviewed;       376 AA.
AC   A0A2S2C5Y9;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Alcohol dehydrogenase {ECO:0000313|EMBL:AWK76233.1};
GN   ORFNames=CBI38_32640 {ECO:0000313|EMBL:AWK76233.1};
OS   Rhodococcus oxybenzonivorans.
OG   Plasmid prb98 {ECO:0000313|Proteomes:UP000245711}.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=1990687 {ECO:0000313|EMBL:AWK76233.1, ECO:0000313|Proteomes:UP000245711};
RN   [1] {ECO:0000313|EMBL:AWK76233.1, ECO:0000313|Proteomes:UP000245711}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S2-17 {ECO:0000313|EMBL:AWK76233.1,
RC   ECO:0000313|Proteomes:UP000245711};
RC   PLASMID=prb98 {ECO:0000313|Proteomes:UP000245711};
RA   Lee Y., Kim K.H., Chun B.H., Jung H.S., Jeon C.O.;
RT   "Isolation of Rhodococcus sp. S2-17 biodegrading of BP-3.";
RL   Submitted (MAY-2017) 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; CP021355; AWK76233.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S2C5Y9; -.
DR   KEGG; roz:CBI38_32640; -.
DR   OrthoDB; 334894at2; -.
DR   Proteomes; UP000245711; Plasmid prb98.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd08278; benzyl_alcohol_DH; 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; 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   Plasmid {ECO:0000313|EMBL:AWK76233.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245711};
KW   Zinc {ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          10..363
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   376 AA;  39211 MW;  529EE90217A0266B CRC64;
     MKTTAAVLRS AQEPLSLEEL DIGELRPREV LVRIVGSGIC HTDLGVIATA EADAAPIVLG
     HEGSGVVTAV GSAVDSVEPG DHVVLSYNFC AECDNCARSL PMHCRDFVPL NLVGARLDGS
     SVLSSGGEQV RGHFFGQSAW ATYAVANEQN CVRVARNLPL ELLAPLGCGI QTGAGAVLNT
     LHPEEGSSIA IFGTGSVGLA ALLGAVVAGC GTIIAVDIQP TRLAKATELG ATHTINSAEE
     DVVDRIREIT GGVGAQYSVD CIGLANVVRS ALECLQSPGV CATVGFQGIP NEISFDQGHL
     LFGRSLIGVI EGDAIPQEFV TRMIDLYQAG KFPFTELIDT FEFDQINEAI DAVHHGKVTK
     AVLTFGDRGV HGDSGE
//