ID   W7CPL3_9LIST            Unreviewed;       349 AA.
AC   W7CPL3;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   SubName: Full=Zinc-dependent dehydrogenase {ECO:0000313|EMBL:EUJ37641.1};
GN   ORFNames=BCAMP_09775 {ECO:0000313|EMBL:EUJ37641.1};
OS   Brochothrix campestris FSL F6-1037.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Brochothrix.
OX   NCBI_TaxID=1265861 {ECO:0000313|EMBL:EUJ37641.1, ECO:0000313|Proteomes:UP000019243};
RN   [1] {ECO:0000313|EMBL:EUJ37641.1, ECO:0000313|Proteomes:UP000019243}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSL F6-1037 {ECO:0000313|EMBL:EUJ37641.1,
RC   ECO:0000313|Proteomes:UP000019243};
RA   den Bakker H.C., Allred A., Warchocki S., Wright E.M., Burrell A.,
RA   Nightingale K.K., Kephart D., Wiedmann M.;
RT   "Novel taxa of Listeriaceae from agricultural environments in the United
RT   States.";
RL   Submitted (DEC-2012) 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}.
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:EUJ37641.1}.
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DR   EMBL; AODH01000040; EUJ37641.1; -; Genomic_DNA.
DR   RefSeq; WP_035315119.1; NZ_AODH01000040.1.
DR   AlphaFoldDB; W7CPL3; -.
DR   STRING; 1265861.BCAMP_09775; -.
DR   PATRIC; fig|1265861.3.peg.1916; -.
DR   OrthoDB; 9770238at2; -.
DR   Proteomes; UP000019243; 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; 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   Reference proteome {ECO:0000313|Proteomes:UP000019243};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          8..343
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   349 AA;  37187 MW;  CC7A07E07848B71F CRC64;
     MKAAVWYGEK DIRIEERELK ALKTDEVTVR VAWAGICGSD LHEYQEGPVF VPVNEPDQFT
     GEVAPLIMGH EFAGVIEKVG SEVTRFKVGD RVAINPTLTH GIKPEALDTY DGFSFIGLHG
     DGGFTTFANA PEKQVYKLPE TMTLQDGALV EPMAVAVQAI KESELLFGDT VAVFGAGPIG
     LLTVIAAKAA GASKIIVLDL SANRLEKALE LGATHAINSG EVDGIQAIRD IVPGGVDVTF
     EVAGVAPTFK AAIDATRARG TMVIVSIFAR PIEWNPLHLT NTGVKITSSI AYTPTTFQQT
     VDLMGTGQLK PQGIVTSQIV LDDIVSNGFE ALTNDKTQAK ILVELSGEK
//