ID   A0A061SX52_9RHOB        Unreviewed;       347 AA.
AC   A0A061SX52;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Alcohol dehydrogenase {ECO:0000313|EMBL:KAJ04708.1};
GN   ORFNames=PM02_00345 {ECO:0000313|EMBL:KAJ04708.1};
OS   Sulfitobacter mediterraneus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Sulfitobacter.
OX   NCBI_TaxID=83219 {ECO:0000313|EMBL:KAJ04708.1, ECO:0000313|Proteomes:UP000027337};
RN   [1] {ECO:0000313|EMBL:KAJ04708.1, ECO:0000313|Proteomes:UP000027337}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1FIGIMAR09 {ECO:0000313|EMBL:KAJ04708.1,
RC   ECO:0000313|Proteomes:UP000027337};
RX   PubMed=24855294;
RA   Mas-Llado M., Pina-Villalonga J.M., Brunet-Galmes I., Nogales B., Bosch R.;
RT   "Draft Genome Sequences of Two Isolates of the Roseobacter Group,
RT   Sulfitobacter sp. Strains 3SOLIMAR09 and 1FIGIMAR09, from Harbors of
RT   Mallorca Island (Mediterranean Sea).";
RL   Genome Announc. 2:e00350-14(2014).
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:KAJ04708.1}.
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DR   EMBL; JEMU01000001; KAJ04708.1; -; Genomic_DNA.
DR   RefSeq; WP_037904227.1; NZ_JEMU01000001.1.
DR   AlphaFoldDB; A0A061SX52; -.
DR   STRING; 83219.PM02_00345; -.
DR   eggNOG; COG1064; Bacteria.
DR   Proteomes; UP000027337; Unassembled WGS sequence.
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   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: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:UP000027337};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          10..330
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   347 AA;  35801 MW;  6D2CC21808F9ECF9 CRC64;
     MRAARLTAWR APLEIADLPM PDAPEGGVVL RVLACGVCRS DWHVWTGADP DVSLPHVPGH
     EYCGEVIAVG AGVTRWRTGD RVIAPFILAC GSCPDCAQGH QTICARQALP GFTHAGAFAE
     AIAVPFADAN LTALPKNLDP ALAAALGCRV ITAWHALTGR AAVQAGEWVA VFGTGGVGLS
     AALLARGLGA RVIAVDIAQE KLDHAKALGI DAVVNAAQSD PAAAIREITQ GGADVAIEAL
     GVAQTTVPAL KCLRKLGRMV QVGMPAGDHT TMPIPMDAVY SGQLAVFGTR GMPSWRYPPL
     LDFVMSGRVD LTPLVARRIG LSQATGELAV FDGPAPPGVA VITDFAG
//