ID   A0A150WST0_BDEBC        Unreviewed;       348 AA.
AC   A0A150WST0;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Hydroxyacid dehydrogenase {ECO:0000313|EMBL:KYG67551.1};
GN   ORFNames=AZI86_10140 {ECO:0000313|EMBL:KYG67551.1};
OS   Bdellovibrio bacteriovorus.
OC   Bacteria; Bdellovibrionota; Bdellovibrionia; Bdellovibrionales;
OC   Pseudobdellovibrionaceae; Bdellovibrio.
OX   NCBI_TaxID=959 {ECO:0000313|EMBL:KYG67551.1, ECO:0000313|Proteomes:UP000075320};
RN   [1] {ECO:0000313|EMBL:KYG67551.1, ECO:0000313|Proteomes:UP000075320}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R0 {ECO:0000313|EMBL:KYG67551.1,
RC   ECO:0000313|Proteomes:UP000075320};
RA   Ploux O.;
RL   Submitted (MAR-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}.
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:KYG67551.1}.
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DR   EMBL; LUKE01000001; KYG67551.1; -; Genomic_DNA.
DR   RefSeq; WP_061835144.1; NZ_LUKE01000001.1.
DR   AlphaFoldDB; A0A150WST0; -.
DR   Proteomes; UP000075320; Unassembled WGS sequence.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd05283; CAD1; 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; IPR047109; CAD-like.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   PANTHER; PTHR42683; ALDEHYDE REDUCTASE; 1.
DR   PANTHER; PTHR42683:SF85; CINNAMYL ALCOHOL DEHYDROGENASE 6-RELATED; 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:UP000075320};
KW   Zinc {ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          12..342
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   348 AA;  37534 MW;  B26A0E3964FEAB9E CRC64;
     MPTTVQAFAA LKAKEALKPF SFERRDPGAH DVAIDIHYCG VCHSDLHQVR DEWGGSRFPM
     VPGHEIVGKV TAVGSSVKKF KIGDSVGVGC MVDSCQECAS CAEGLEQYCE KGMTGTYNSV
     ERDGKTPTQG GYSTKIVVSE KFVLKIDPKL PLDKAAPLLC AGITTYSPLR HWNIGKGSKV
     AVMGLGGLGH MAVKLAAAMG AEVTVLSSSM KKKEDAIRLG ATNYAVGGDE TFKKYNRYFD
     LIINTVSAGL DLNTYLGMVK LNGTMVLLGI PEAPEPVHPF PLIMGRRSLA GSLIGGIKET
     QEMLDFCAAH NIASDIELIP AQKINEAYER MLKGDVRYRF VIDLASLK
//