ID   U1LS82_9MICO            Unreviewed;       355 AA.
AC   U1LS82;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Enoyl reductase (ER) domain-containing protein {ECO:0000259|SMART:SM00829};
GN   ORFNames=L332_10975 {ECO:0000313|EMBL:ERG64962.1};
OS   Agrococcus pavilionensis RW1.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Agrococcus.
OX   NCBI_TaxID=1330458 {ECO:0000313|EMBL:ERG64962.1, ECO:0000313|Proteomes:UP000016462};
RN   [1] {ECO:0000313|EMBL:ERG64962.1, ECO:0000313|Proteomes:UP000016462}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RW1 {ECO:0000313|EMBL:ERG64962.1,
RC   ECO:0000313|Proteomes:UP000016462};
RX   PubMed=23814108;
RA   White R.A.III., Grassa C.J., Suttle C.A.;
RT   "First draft genome sequence from a member of the genus agrococcus,
RT   isolated from modern microbialites.";
RL   Genome Announc. 1:e00391-13(2013).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000256|ARBA:ARBA00008072}.
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:ERG64962.1}.
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DR   EMBL; ASHR01000014; ERG64962.1; -; Genomic_DNA.
DR   RefSeq; WP_021009981.1; NZ_ASHR01000014.1.
DR   AlphaFoldDB; U1LS82; -.
DR   OrthoDB; 9797931at2; -.
DR   Proteomes; UP000016462; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd08232; idonate-5-DH; 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; IPR013149; ADH-like_C.
DR   InterPro; IPR013154; ADH-like_N.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   PANTHER; PTHR43161; SORBITOL DEHYDROGENASE; 1.
DR   PANTHER; PTHR43161:SF9; SORBITOL 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.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016462};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          15..345
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   355 AA;  36412 MW;  3E528D85AC7C90C9 CRC64;
     MSDDRMADNL GLVAHAKEDV RVEALPEPVP AADEAVVEIA FGGICGSDLH YWLHGAAGQS
     ILREPMLLGH EIVGTVLEPA ADGTGPAAGT RVAVHPATPI DDGSAPFPAD RPNLSPAGTY
     LGSAARMPHT AGAFARRVAL PARMLRPLPA GLDLRLASLA EPAAVAWHGV GQAGDVEGQR
     VLVIGTGPIG ALAIAVARRH GAAEVVATDL HEHPRALAER LGARAMDARD AEGIAALHAD
     VVIESSGTVP GLAAAISGAR RGGTVVMLGL QRAGEIAVPM ASAITRELTL VGSFRFNDEI
     DDVLEALADG SLDAAPVISH ELPIERGLDA LELARDASVS SKVLLTFGEH EGVDA
//