ID   B8D1K8_HALOH            Unreviewed;       358 AA.
AC   B8D1K8;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 76.
DE   SubName: Full=Zn-dependent alcohol dehydrogenase {ECO:0000313|EMBL:ACL69085.1};
DE            EC=1.1.1.- {ECO:0000313|EMBL:ACL69085.1};
GN   OrderedLocusNames=Hore_03240 {ECO:0000313|EMBL:ACL69085.1};
OS   Halothermothrix orenii (strain H 168 / OCM 544 / DSM 9562).
OC   Bacteria; Bacillota; Clostridia; Halanaerobiales; Halothermotrichaceae;
OC   Halothermothrix.
OX   NCBI_TaxID=373903 {ECO:0000313|EMBL:ACL69085.1, ECO:0000313|Proteomes:UP000000719};
RN   [1] {ECO:0000313|EMBL:ACL69085.1, ECO:0000313|Proteomes:UP000000719}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H 168 / OCM 544 / DSM 9562 {ECO:0000313|Proteomes:UP000000719};
RX   PubMed=19145256; DOI=10.1371/journal.pone.0004192;
RA   Mavromatis K., Ivanova N., Anderson I., Lykidis A., Hooper S.D., Sun H.,
RA   Kunin V., Lapidus A., Hugenholtz P., Patel B., Kyrpides N.C.;
RT   "Genome analysis of the anaerobic thermohalophilic bacterium
RT   Halothermothrix orenii.";
RL   PLoS ONE 4:E4192-E4192(2009).
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|ARBA:ARBA00008072, ECO:0000256|RuleBase:RU361277}.
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DR   EMBL; CP001098; ACL69085.1; -; Genomic_DNA.
DR   RefSeq; WP_012635273.1; NC_011899.1.
DR   AlphaFoldDB; B8D1K8; -.
DR   STRING; 373903.Hore_03240; -.
DR   KEGG; hor:Hore_03240; -.
DR   eggNOG; COG1063; Bacteria.
DR   HOGENOM; CLU_026673_11_0_9; -.
DR   OrthoDB; 9769198at2; -.
DR   Proteomes; UP000000719; Chromosome.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
DR   CDD; cd08256; Zn_ADH2; 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; PTHR43401; L-THREONINE 3-DEHYDROGENASE; 1.
DR   PANTHER; PTHR43401:SF2; L-THREONINE 3-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   ECO:0000313|EMBL:ACL69085.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000719};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          17..356
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   358 AA;  39621 MW;  530D61B670B81D57 CRC64;
     MVNLPEKMKA LVAYAPGDYR FEEVDVPRAG EGEIVVKVEA CGICAGDIKA YHGAPSFWGG
     EGNPPYIKAP MIPGHEFIGE IVEKGAEVSD DFEIGDRVIS EQIVPCWECK FCRTGRYWMC
     QKHDVYGFQN NVNGGMAEYM KFPKEAINYK VPKDIPIEKA ILIEPYACSK HAVDRANISN
     EDVVVLSGAG TLGLGMVGAI KLRNPKSLVV LDLKDDRLEL AKKFGADITM NPKKENVVEK
     ILEMTDGYGC DIYIEATGHP SSVQQGLEAI RKLGTFVEFS VFGDLVTTDW SIISDRKELD
     VLGSHLGPYC YEPVIEWIAN GKLPTEGVVT HKFPLEKWKE AFEKAEKGQD SIKVVLVP
//