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Database: UniProt
Entry: A0A1E3LWN6_9SPHN
LinkDB: A0A1E3LWN6_9SPHN
Original site: A0A1E3LWN6_9SPHN 
ID   A0A1E3LWN6_9SPHN        Unreviewed;       338 AA.
AC   A0A1E3LWN6;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Zinc-type alcohol dehydrogenase-like protein {ECO:0000256|RuleBase:RU364000};
GN   ORFNames=BFL28_15590 {ECO:0000313|EMBL:ODP38146.1};
OS   Sphingomonas turrisvirgatae.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1888892 {ECO:0000313|EMBL:ODP38146.1, ECO:0000313|Proteomes:UP000094487};
RN   [1] {ECO:0000313|EMBL:ODP38146.1, ECO:0000313|Proteomes:UP000094487}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCT13 {ECO:0000313|EMBL:ODP38146.1,
RC   ECO:0000313|Proteomes:UP000094487};
RA   D'Andrea M.M., Rossolini G.M., Thaller M.C.;
RT   "Draft genome of the agarase producing Sphingomonas sp. MCT13.";
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. Quinone oxidoreductase subfamily.
CC       {ECO:0000256|RuleBase:RU364000}.
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:ODP38146.1}.
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DR   EMBL; MDDS01000019; ODP38146.1; -; Genomic_DNA.
DR   RefSeq; WP_069320193.1; NZ_MDDS01000019.1.
DR   AlphaFoldDB; A0A1E3LWN6; -.
DR   STRING; 1888892.BFL28_15590; -.
DR   OrthoDB; 9785812at2; -.
DR   Proteomes; UP000094487; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd08252; AL_MDR; 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; IPR013154; ADH-like_N.
DR   InterPro; IPR014182; ADH_Zn_typ-1.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   NCBIfam; TIGR02817; adh_fam_1; 1.
DR   PANTHER; PTHR44154; QUINONE OXIDOREDUCTASE; 1.
DR   PANTHER; PTHR44154:SF1; QUINONE OXIDOREDUCTASE; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF13602; ADH_zinc_N_2; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SUPFAM; SSF50129; GroES-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|RuleBase:RU364000};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU364000};
KW   Reference proteome {ECO:0000313|Proteomes:UP000094487};
KW   Zinc {ECO:0000256|RuleBase:RU364000}.
FT   DOMAIN          10..334
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   338 AA;  36299 MW;  5E8AF96EF455F1BD CRC64;
     MRAVAYQQHG TIDRAESLVD IELPDPIVTG RDLLVEVKAV SVNPVDTKVR SGSGPIHGDW
     RVLGWDAAGV VRAVGPDVNG FKAGDEVFYA GSIGRDGTDA ELHLVDERIV GKKPASLDWA
     EAAALPLTAI TAWEALFERL SVRTPVAGAA HALLIVGGAG GVGSMAIQLA RQVPELIVIA
     TASRPETQAW VGELGAHHVI DHRQPLARQV ANLGIGAPAF VFSTTHTDEH IEQIAELIAP
     QGRFALIDDP KTLDVVPFKR KSVSTHWEFM FTRSMFETAD METQGQILSA IASLVDAGEV
     RTTLTERFSP INAANLKRAH QALESTTARG KIVIEGWQ
//
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