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
//