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Database: UniProt
Entry: A0A432ZHY7_9GAMM
LinkDB: A0A432ZHY7_9GAMM
Original site: A0A432ZHY7_9GAMM 
ID   A0A432ZHY7_9GAMM        Unreviewed;       336 AA.
AC   A0A432ZHY7;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=Zinc-type alcohol dehydrogenase-like protein {ECO:0000256|RuleBase:RU364000};
GN   ORFNames=CWI81_02820 {ECO:0000313|EMBL:RUO77430.1};
OS   Idiomarina seosinensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Idiomarinaceae; Idiomarina.
OX   NCBI_TaxID=281739 {ECO:0000313|EMBL:RUO77430.1, ECO:0000313|Proteomes:UP000287908};
RN   [1] {ECO:0000313|EMBL:RUO77430.1, ECO:0000313|Proteomes:UP000287908}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CL-SP19 {ECO:0000313|EMBL:RUO77430.1,
RC   ECO:0000313|Proteomes:UP000287908};
RX   PubMed=30364313; DOI=.3389/fmicb.2018.02453;
RA   Liu Y., Lai Q., Shao Z.;
RT   "Genome-Based Analysis Reveals the Taxonomy and Diversity of the Family
RT   Idiomarinaceae.";
RL   Front. Microbiol. 9:2453-2453(2018).
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:RUO77430.1}.
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DR   EMBL; PIQF01000001; RUO77430.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A432ZHY7; -.
DR   OrthoDB; 9785812at2; -.
DR   Proteomes; UP000287908; 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:UP000287908};
KW   Zinc {ECO:0000256|RuleBase:RU364000}.
FT   DOMAIN          11..332
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   336 AA;  36000 MW;  3166CF60EE9F71A6 CRC64;
     MKAVGYQKSL AISEPNALID IELPAPTPGD NDLLVKVTAI AVNPVDTKIR QRVSPEQGYK
     VLGWDAVGEV IDVGQSVSGF KPGDKVWYAG DITRPGCNAQ QQLIDYRIAA KAPSTLQDIQ
     AAAMPLTSIT AWELLFDRLK LNSHSPHSKR CLLVVGAAGG VGSIMVQLAK QLTGATVIAT
     ASRPESQQWV KALGADHVID HNQPLAAQLN DIDAVTDVAL LTHSDQYFDA VVDLIAAQGQ
     IGIIDDPTAP LDITKLKQKS VSLHWEFMYT RSMFQTEDMA TQGQLLAKVA ELIDNNQLRS
     TLGQNFGALN AANLIKAHAA VESGKTIGKI ALTVPE
//
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