ID   S3T5M5_9GAMM            Unreviewed;       331 AA.
AC   S3T5M5;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Enoyl reductase (ER) domain-containing protein {ECO:0000259|SMART:SM00829};
GN   ORFNames=F907_02725 {ECO:0000313|EMBL:EPG36188.1};
OS   Acinetobacter colistiniresistens.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=280145 {ECO:0000313|EMBL:EPG36188.1, ECO:0000313|Proteomes:UP000014559};
RN   [1] {ECO:0000313|EMBL:EPG36188.1, ECO:0000313|Proteomes:UP000014559}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIPH 2036 {ECO:0000313|EMBL:EPG36188.1,
RC   ECO:0000313|Proteomes:UP000014559};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA   Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA   Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA   Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A., Gujja S.,
RA   Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Acinetobacter sp. NIPH 2036.";
RL   Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
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:EPG36188.1}.
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DR   EMBL; ATGK01000014; EPG36188.1; -; Genomic_DNA.
DR   RefSeq; WP_005206914.1; NZ_UEGJ01000007.1.
DR   AlphaFoldDB; S3T5M5; -.
DR   GeneID; 45417078; -.
DR   PATRIC; fig|1217696.3.peg.2678; -.
DR   HOGENOM; CLU_026673_3_3_6; -.
DR   Proteomes; UP000014559; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd08272; MDR6; 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; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   InterPro; IPR002364; Quin_OxRdtase/zeta-crystal_CS.
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.
DR   PROSITE; PS01162; QOR_ZETA_CRYSTAL; 1.
PE   4: Predicted;
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT   DOMAIN          14..328
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   331 AA;  35085 MW;  57D5BAC7A24BC338 CRC64;
     MNKMMNALIL ENFGDHEFTR VELPIPQPEA GQVLVRIHAS GVNPIDYKIR LGEAPYAMPE
     LPAVLGTDMA GVVTAVGEGV THFNVGDEVY GLIGGVRGLQ GSLAEYVVAD ADLIALKPRN
     ISMREAAVLP LTFLTAWEGL VDNAKVQPGQ TVLVQGGAGG VGYMVVQLAK ALDANVWATG
     RTADQSLISE LGATPLDYTT ASSDDIIAAS PEGQGFNIVY DTVGGPVLEA SLSMTTHYGH
     ITSCAAFGNH NLASSSLRCA TVSGVFVLMP MLTGNRRAHH GDILKIATRL VEEGKLRPIV
     DPRHFTLDQA IEAHDAVQDR SANIKVVIDV I
//