ID   V9XJF7_9NOCA            Unreviewed;       350 AA.
AC   V9XJF7;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   SubName: Full=Dehydrogenase {ECO:0000313|EMBL:AHD21442.1};
GN   ORFNames=Y013_12610 {ECO:0000313|EMBL:AHD21442.1};
OS   Rhodococcus pyridinivorans SB3094.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=1435356 {ECO:0000313|EMBL:AHD21442.1, ECO:0000313|Proteomes:UP000018781};
RN   [1] {ECO:0000313|EMBL:AHD21442.1, ECO:0000313|Proteomes:UP000018781}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SB3094 {ECO:0000313|EMBL:AHD21442.1,
RC   ECO:0000313|Proteomes:UP000018781};
RX   PubMed=24874690;
RA   Dueholm M.S., Albertsen M., D'Imperio S., Tale V.P., Lewis D.,
RA   Nielsen P.H., Nielsen J.L.;
RT   "Complete Genome of Rhodococcus pyridinivorans SB3094, a Methyl-Ethyl-
RT   Ketone-Degrading Bacterium Used for Bioaugmentation.";
RL   Genome Announc. 2:e00525-14(2014).
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; CP006996; AHD21442.1; -; Genomic_DNA.
DR   RefSeq; WP_024102207.1; NC_023150.1.
DR   AlphaFoldDB; V9XJF7; -.
DR   GeneID; 29940798; -.
DR   KEGG; rpy:Y013_12610; -.
DR   PATRIC; fig|1435356.3.peg.2539; -.
DR   eggNOG; COG1063; Bacteria.
DR   HOGENOM; CLU_026673_11_0_11; -.
DR   Proteomes; UP000018781; Chromosome.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd08233; butanediol_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; PTHR43161:SF23; (R,R)-BUTANEDIOL DEHYDROGENASE-RELATED; 1.
DR   PANTHER; PTHR43161; SORBITOL 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|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU361277};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          8..344
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   350 AA;  36837 MW;  3A6E6C6FFECFED65 CRC64;
     MKAAVYYGPN KLEIADVPEP QPGPGTVKVK VGFNGICGTD LHEYYAGPIF VPTEPHPLTG
     RELPLTMGHE FAGTIIEVGA GVTGYVPGDR VAIEPIYRCG RCAPCRAGTY NVCQQIGFHG
     LMSDGGMAEY TIVPVNMLHR LPDNVSLELG ALVEPMAVAY HAAALGDVGP GDTAIIFGAG
     PIGIGLWFAL RGMGLESVFV AEPSPTRRTA IEALGAHTLD PTQVDVSAFV TDVTGGRGAD
     AAFDAAGVKS AIEAATASVG ARRPTISVAI YEKPLTVPLL NLVMNESRIQ GSLCYTSTDF
     EAVIAFMAQG VYDTTGWVTT VRIDDVINEG FEALHAGRKM KVLVDPSDDM
//