ID   S9QPV4_9RHOB            Unreviewed;       362 AA.
AC   S9QPV4;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   SubName: Full=Alcohol dehydrogenase {ECO:0000313|EMBL:EPX81682.1};
DE            EC=1.1.1.1 {ECO:0000313|EMBL:EPX81682.1};
GN   ORFNames=thalar_00238 {ECO:0000313|EMBL:EPX81682.1};
OS   Litoreibacter arenae DSM 19593.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Litoreibacter.
OX   NCBI_TaxID=1123360 {ECO:0000313|EMBL:EPX81682.1, ECO:0000313|Proteomes:UP000015351};
RN   [1] {ECO:0000313|Proteomes:UP000015351}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19593 {ECO:0000313|Proteomes:UP000015351};
RX   PubMed=24501650; DOI=10.4056/sigs.4258318;
RA   Riedel T., Fiebig A., Petersen J., Gronow S., Kyrpides N.C., Goker M.,
RA   Klenk H.P.;
RT   "Genome sequence of the Litoreibacter arenae type strain (DSM 19593(T)), a
RT   member of the Roseobacter clade isolated from sea sand.";
RL   Stand. Genomic Sci. 9:117-127(2013).
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}.
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:EPX81682.1}.
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DR   EMBL; AONI01000005; EPX81682.1; -; Genomic_DNA.
DR   RefSeq; WP_021101181.1; NZ_KE557310.1.
DR   AlphaFoldDB; S9QPV4; -.
DR   STRING; 1123360.thalar_00238; -.
DR   PATRIC; fig|1123360.3.peg.237; -.
DR   eggNOG; COG1062; Bacteria.
DR   HOGENOM; CLU_026673_14_1_5; -.
DR   OrthoDB; 9770544at2; -.
DR   Proteomes; UP000015351; Unassembled WGS sequence.
DR   GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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; PTHR43880; ALCOHOL DEHYDROGENASE; 1.
DR   PANTHER; PTHR43880:SF12; ALCOHOL DEHYDROGENASE CLASS-3; 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; 2.
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   ECO:0000313|EMBL:EPX81682.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015351};
KW   Zinc {ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          13..359
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   362 AA;  37405 MW;  8839798123FCBA49 CRC64;
     MTKIKAAVCH EFGAPLTIED VELRAPQAGE VEVELEACAI CFSDISFMDG GWGGDLPAVY
     GHEAAGRVSA LGEGVSGLQI GDAVLVTLIR SCATCTPCAS GVPTQCATPY DRMAGPLSMP
     DGSALEHGLA CGAFAERAVV DQSQIARIPD DMPMDAASLL SCGVVTGVGA VVNTAKVRPG
     QNVVVIGAGG VGLNAIQGAA ISGAARIIAV DMVPEKLDAA KEFGATDGVL ASDPKPWKQV
     AEITNGRMAD AVMVTVGAIP AFETAPRFLA AGGNMYLVGM PHSGATATYE PVIFGALAQG
     MKGTKMGDVV LKRDIPWLVD LYSQGRLKLD ELVSGRWHLD QINEAIADTR SGAARRNVIV
     FK
//