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Database: UniProt
Entry: A0A0L0GKB8_9ENTR
LinkDB: A0A0L0GKB8_9ENTR
Original site: A0A0L0GKB8_9ENTR 
ID   A0A0L0GKB8_9ENTR        Unreviewed;       333 AA.
AC   A0A0L0GKB8;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Zinc-type alcohol dehydrogenase-like protein {ECO:0000256|RuleBase:RU364000};
GN   ORFNames=GM31_11770 {ECO:0000313|EMBL:KNC88152.1};
OS   Trabulsiella odontotermitis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Trabulsiella.
OX   NCBI_TaxID=379893 {ECO:0000313|EMBL:KNC88152.1, ECO:0000313|Proteomes:UP000037393};
RN   [1] {ECO:0000313|EMBL:KNC88152.1, ECO:0000313|Proteomes:UP000037393}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12 {ECO:0000313|EMBL:KNC88152.1,
RC   ECO:0000313|Proteomes:UP000037393};
RX   PubMed=26162887;
RA   Sapountzis P., Gruntjes T., Otani S., Estevez J., da Costa R.R.,
RA   Plunkett G.3rd., Perna N.T., Poulsen M.;
RT   "The Enterobacterium Trabulsiella odontotermitis Presents Novel Adaptations
RT   Related to Its Association with Fungus-Growing Termites.";
RL   Appl. Environ. Microbiol. 81:6577-6588(2015).
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:KNC88152.1}.
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DR   EMBL; JNGI01000185; KNC88152.1; -; Genomic_DNA.
DR   RefSeq; WP_049849761.1; NZ_JNGI01000185.1.
DR   AlphaFoldDB; A0A0L0GKB8; -.
DR   PATRIC; fig|379893.3.peg.1878; -.
DR   OrthoDB; 9785812at2; -.
DR   Proteomes; UP000037393; 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   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU364000};
KW   Zinc {ECO:0000256|RuleBase:RU364000}.
FT   DOMAIN          14..331
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   333 AA;  35838 MW;  59353A177E2A80F7 CRC64;
     MSVKAIAVNP ENPSTFIEIN LPLPAPGEHD LLVEVKAVSV NPVDTKVHAG IAKSGIQTPR
     ILGWDASGIV TAVGSAVTGF KPGDEVWYAG DITRPGSNTT HQLIDARIVG HKPASLDWAA
     SAALPLTALT AWEGLFERLN IQDAGSEKTL LIIGGAGGVG SLAIPFAKHN SKVKIVATAS
     RKDSAQWCRD RGADLVVNYR DLKGELAKQG ISFVDYIFIL NDTDGHWDAV SELIAPQGHI
     CSIVENQHPL NQDKLKSKSA ALHWEFMYTR SMYQTEDMAR QGEILNDVAK LVDDGVVESS
     LSETLHGLSV ESITEAHRKV LDGHMRGKVV VAF
//
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