ID   H8H850_HELPX            Unreviewed;       365 AA.
AC   H8H850;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2012, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   SubName: Full=Zinc-dependent alcohol dehydrogenase {ECO:0000313|EMBL:AFF21094.1};
GN   ORFNames=HPELS_07935 {ECO:0000313|EMBL:AFF21094.1};
OS   Helicobacter pylori ELS37.
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=1055527 {ECO:0000313|EMBL:AFF21094.1, ECO:0000313|Proteomes:UP000007885};
RN   [1] {ECO:0000313|EMBL:AFF21094.1, ECO:0000313|Proteomes:UP000007885}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ELS37 {ECO:0000313|EMBL:AFF21094.1,
RC   ECO:0000313|Proteomes:UP000007885};
RA   Bertoli M.T., Kersulyte D., Pascasio M.A., Berg D.E.;
RL   Submitted (JUL-2011) 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; CP002953; AFF21094.1; -; Genomic_DNA.
DR   RefSeq; WP_000282050.1; NC_017063.1.
DR   AlphaFoldDB; H8H850; -.
DR   KEGG; hpe:HPELS_07935; -.
DR   PATRIC; fig|1055527.3.peg.1589; -.
DR   HOGENOM; CLU_026673_20_2_7; -.
DR   Proteomes; UP000007885; Chromosome.
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   Zinc {ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          24..354
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   365 AA;  40620 MW;  5A34748165C1EEA1 CRC64;
     MYNACNCNSQ RVPFKGFAID NKDGKFHEWE HSRHAMGEYD VVIDAHFSGI CHTDIHFAHS
     DWLPGIYPMV PGHEIAGVVS AVGSKVTKFK VGDHAGVGCM VNSCGECHTC KHEHQEQWCE
     NNKTIYTYSW EDSFHNNEPT YSGYSNNIVV SENFVISIPK EAPLDKAAPL LCAGITVYSP
     LKFSKVTKGS KVGIAGFGGL GHMALKYAVA MGAQVSVFAR NDKKKQMAQK LGATNFYTSV
     EECKEKFDLI ISSIPTQYDL LAYTKLLKYG GEVAIVGIPP KDPQRNLDFG DLVLFSGNHK
     VYGSWIGGVK ETQEMMDFSI KHGIYPEIEL VTGQEIDATW DKLLNGQGNF RYVIDMKKSM
     ENFKK
//