ID ETR1_EREGS Reviewed; 376 AA. AC Q757U3; DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot. DT 09-JAN-2013, sequence version 2. DT 24-JAN-2024, entry version 111. DE RecName: Full=Enoyl-[acyl-carrier-protein] reductase, mitochondrial; DE EC=1.3.1.104; DE AltName: Full=2-enoyl thioester reductase; DE Flags: Precursor; GN Name=ETR1; OrderedLocusNames=AEL081W; OS Eremothecium gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL OS Y-1056) (Yeast) (Ashbya gossypii). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Eremothecium. OX NCBI_TaxID=284811; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056; RX PubMed=15001715; DOI=10.1126/science.1095781; RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S., RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A., RA Gaffney T.D., Philippsen P.; RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces RT cerevisiae genome."; RL Science 304:304-307(2004). RN [2] RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 324. RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056; RX PubMed=23749448; DOI=10.1534/g3.112.002881; RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.; RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type RT loci, numerous translocations, lack of transposons, and distinct gene RT duplications."; RL G3 (Bethesda) 3:1225-1239(2013). CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of trans-2-enoyl CC thioesters in mitochondrial fatty acid synthesis (fatty acid synthesis CC type II). Fatty acid chain elongation in mitochondria uses acyl carrier CC protein (ACP) as an acyl group carrier, but the enzyme accepts both ACP CC and CoA thioesters as substrates in vitro. Required for respiration and CC the maintenance of the mitochondrial compartment. CC {ECO:0000250|UniProtKB:P38071}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a 2,3-saturated acyl-[ACP] + NADP(+) = a (2E)-enoyl-[ACP] + CC H(+) + NADPH; Xref=Rhea:RHEA:22564, Rhea:RHEA-COMP:9925, Rhea:RHEA- CC COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, CC ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.104; CC Evidence={ECO:0000250|UniProtKB:P38071}; CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q8WZM3}. CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix CC {ECO:0000250|UniProtKB:P38071}. CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase CC family. Quinone oxidoreductase subfamily. {ECO:0000305}. 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; AE016818; AAS52604.2; -; Genomic_DNA. DR RefSeq; NP_984780.2; NM_210134.2. DR AlphaFoldDB; Q757U3; -. DR SMR; Q757U3; -. DR STRING; 284811.Q757U3; -. DR EnsemblFungi; AAS52604; AAS52604; AGOS_AEL081W. DR GeneID; 4620970; -. DR KEGG; ago:AGOS_AEL081W; -. DR eggNOG; KOG0025; Eukaryota. DR HOGENOM; CLU_026673_17_0_1; -. DR InParanoid; Q757U3; -. DR OMA; YGYTQSK; -. DR OrthoDB; 6213at2759; -. DR Proteomes; UP000000591; Chromosome V. DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central. DR GO; GO:0016631; F:enoyl-[acyl-carrier-protein] reductase activity; IEA:EnsemblFungi. DR GO; GO:0019166; F:trans-2-enoyl-CoA reductase (NADPH) activity; IBA:GO_Central. DR GO; GO:0009060; P:aerobic respiration; IEA:EnsemblFungi. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central. DR CDD; cd08290; ETR; 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; IPR011032; GroES-like_sf. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR InterPro; IPR020843; PKS_ER. DR PANTHER; PTHR43981; ENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE, MITOCHONDRIAL; 1. DR PANTHER; PTHR43981:SF2; ENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE, MITOCHONDRIAL; 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 Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis; KW Lipid metabolism; Mitochondrion; NADP; Oxidoreductase; Reference proteome; KW Transit peptide. FT TRANSIT 1..? FT /note="Mitochondrion" FT /evidence="ECO:0000255" FT CHAIN ?..376 FT /note="Enoyl-[acyl-carrier-protein] reductase, FT mitochondrial" FT /id="PRO_0000000896" FT ACT_SITE 72 FT /note="Proton donor" FT /evidence="ECO:0000250|UniProtKB:Q8WZM3" FT BINDING 154 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:Q8WZM3" FT BINDING 182..185 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:Q8WZM3" FT BINDING 205..207 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:Q8WZM3" FT BINDING 280..283 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:Q8WZM3" FT BINDING 305..307 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:Q8WZM3" FT BINDING 369 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" SQ SEQUENCE 376 AA; 41439 MW; A8F107B8CF1CEC7C CRC64; MQALNTTKRL MSTKQFPLFK SLLYSSHDPA DCTQVLKVHS YTPKVGADES ILLRTLAFPI NPSDINQLQG VYPSVPEKTL DYSTEKPAAI AGNEGVFEVM SVPQGERRLA VGDWVIPLYS NTGTWTNYQT CRDAGTLVKV NGLDLYTAAT IAVNGCTAYQ LVNDYVQWDP SGNEWIVQNA GTSAVSKIVT QVAQARGVKT LSVIRDRENF AEVAKELEER YGATKVISET QNNDKDFSKD ELPVILGPNA RVRLALNSVG GKSSGAIARK LERDGTMLTY GGMSRQPVTV PTTLLIFNGL KSLGYWITEN TKRNPQSKID TISALMRMYG DGQLQPPEAD IKKIEWDVQK MNDEQLLEAV KNGIQSNGKS VVVLKW //