ID   A0A328VEX0_9CHLR        Unreviewed;       363 AA.
AC   A0A328VEX0;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=Enoyl reductase (ER) domain-containing protein {ECO:0000259|SMART:SM00829};
GN   ORFNames=A4R35_03485 {ECO:0000313|EMBL:RAQ94582.1};
OS   Thermogemmatispora tikiterensis.
OC   Bacteria; Chloroflexota; Ktedonobacteria; Thermogemmatisporales;
OC   Thermogemmatisporaceae; Thermogemmatispora.
OX   NCBI_TaxID=1825093 {ECO:0000313|EMBL:RAQ94582.1, ECO:0000313|Proteomes:UP000248706};
RN   [1] {ECO:0000313|EMBL:RAQ94582.1, ECO:0000313|Proteomes:UP000248706}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T81 {ECO:0000313|EMBL:RAQ94582.1,
RC   ECO:0000313|Proteomes:UP000248706};
RA   Tomazini A., Lal S., Stott M., Henrissat B., Polikarpov I., Sparling R.,
RA   Levin D.B.;
RT   "Analysis of Carbohydrate Active Enzymes in Thermogemmatispora T81 Reveals
RT   Carbohydrate Degradation Ability.";
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
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:RAQ94582.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; MCIF01000002; RAQ94582.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A328VEX0; -.
DR   Proteomes; UP000248706; 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   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; L-THREONINE 3-DEHYDROGENASE; 1.
DR   PANTHER; PTHR43401:SF2; 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:UP000248706};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          14..346
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   363 AA;  38732 MW;  6BB1F0E0CFC0525A CRC64;
     MPGQMLAAMF YAPGDVRLEE RPIPEPGPGE LVLQIAAATT CGTDVKTYVR GHPLLFKHPP
     AGFGHEAAGI VAAVGPGVQG WKEGDAVVAA NSAPCDRCFY CRRGRYSLCE DLLLLNGAYA
     EYLLVPARIV QRNLYRLPQG LSFTAAALTE PLACALHGVE ESEIQPGDTV LIIGAGPLGL
     LLAAAARLRG ARVLVSGHGE QRLALARHFG AEQVFETGSL SSEEQCALLR AATPEGRGAD
     VVIEAVGTPE TWELAASLVR RGGLVNFFGG CASGTHISLE TRPLHYDELT LKGVFHHTPT
     YFARALELIA SRQIPVEALI TARFPLTEAV TALHLLLQKQ GVKYALIPPA FARDLPRRAD
     PGE
//