ID   C1CZS5_DEIDV            Unreviewed;       347 AA.
AC   C1CZS5;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 80.
DE   SubName: Full=Putative Alcohol dehydrogenase (ADH) {ECO:0000313|EMBL:ACO45177.1};
GN   Name=adh {ECO:0000313|EMBL:ACO45177.1};
GN   OrderedLocusNames=Deide_03550 {ECO:0000313|EMBL:ACO45177.1};
OS   Deinococcus deserti (strain DSM 17065 / CIP 109153 / LMG 22923 / VCD115).
OC   Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=546414 {ECO:0000313|EMBL:ACO45177.1, ECO:0000313|Proteomes:UP000002208};
RN   [1] {ECO:0000313|EMBL:ACO45177.1, ECO:0000313|Proteomes:UP000002208}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17065 / CIP 109153 / LMG 22923 / VCD115
RC   {ECO:0000313|Proteomes:UP000002208};
RX   PubMed=19370165; DOI=10.1371/journal.pgen.1000434;
RA   de Groot A., Dulermo R., Ortet P., Blanchard L., Guerin P., Fernandez B.,
RA   Vacherie B., Dossat C., Jolivet E., Siguier P., Chandler M., Barakat M.,
RA   Dedieu A., Barbe V., Heulin T., Sommer S., Achouak W., Armengaud J.;
RT   "Alliance of proteomics and genomics to unravel the specificities of Sahara
RT   bacterium Deinococcus deserti.";
RL   PLoS Genet. 5:E1000434-E1000434(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|RuleBase:RU361277}.
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DR   EMBL; CP001114; ACO45177.1; -; Genomic_DNA.
DR   RefSeq; WP_012692300.1; NC_012526.1.
DR   AlphaFoldDB; C1CZS5; -.
DR   STRING; 546414.Deide_03550; -.
DR   PaxDb; 546414-Deide_03550; -.
DR   KEGG; ddr:Deide_03550; -.
DR   eggNOG; COG1064; Bacteria.
DR   HOGENOM; CLU_026673_11_2_0; -.
DR   OrthoDB; 9806940at2; -.
DR   Proteomes; UP000002208; 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; cd08260; Zn_ADH6; 1.
DR   Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic 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:SF5; ALCOHOL DEHYDROGENASE-RELATED; 1.
DR   PANTHER; PTHR43401; 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   Reference proteome {ECO:0000313|Proteomes:UP000002208};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          10..343
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   347 AA;  37241 MW;  372BD15E511D6407 CRC64;
     MKAVMVHAFN VRPELVTVSD PTPPEDGVVV QVGATGVCRS DWHGWVGHDP DITLPHVPGH
     ELAGTVVAVG KNIRRWKVGD RVTVPFVSGC GRCHECQSGN QQVCDRQFQP GFTHWGSFAE
     YVALHQAEQN LVALPDDLDF VTAASLGCRF ATSFRAVVHQ GRVRAGEWVA VHGCGGVGLS
     AIMIAKALGA GVVAVDIDEE KLRFAGQLGA DLLINSRATP DVAGAVRDLT GGGVHVSLDA
     LGHPETCANS VANLRTRGRH VQVGLLLAEQ SRPAIPMDRV IARELELYGS HGMAAHAYPE
     MLAMISRGAL RPDQLLGQRV TLEQSIDVLV NMDRFVERGV TVIDRFV
//