ID MECR2_CAEEL Reviewed; 346 AA. AC Q9XXC8; DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 27-MAR-2024, entry version 146. 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 ORFNames=Y48A6B.9; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae; OC Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bristol N2; RX PubMed=9851916; DOI=10.1126/science.282.5396.2012; RG The C. elegans sequencing consortium; RT "Genome sequence of the nematode C. elegans: a platform for investigating RT biology."; RL Science 282:2012-2018(1998). 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. CC {ECO:0000250|UniProtKB:Q9BV79}. 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:Q9BV79}; CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9BV79}. CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9BV79}. 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; AL023844; CAA19533.1; -; Genomic_DNA. DR PIR; T26986; T26986. DR RefSeq; NP_001255097.1; NM_001268168.1. DR AlphaFoldDB; Q9XXC8; -. DR SMR; Q9XXC8; -. DR BioGRID; 41720; 2. DR DIP; DIP-24981N; -. DR IntAct; Q9XXC8; 2. DR MINT; Q9XXC8; -. DR STRING; 6239.Y48A6B.9a.1; -. DR EPD; Q9XXC8; -. DR PaxDb; 6239-Y48A6B-9a; -. DR PeptideAtlas; Q9XXC8; -. DR EnsemblMetazoa; Y48A6B.9a.1; Y48A6B.9a.1; WBGene00012970. DR GeneID; 176534; -. DR KEGG; cel:CELE_Y48A6B.9; -. DR UCSC; Y48A6B.9; c. elegans. DR AGR; WB:WBGene00012970; -. DR WormBase; Y48A6B.9a; CE19192; WBGene00012970; -. DR eggNOG; KOG0025; Eukaryota. DR HOGENOM; CLU_026673_17_1_1; -. DR InParanoid; Q9XXC8; -. DR OMA; PPTAWIM; -. DR OrthoDB; 6213at2759; -. DR PhylomeDB; Q9XXC8; -. DR BRENDA; 1.3.1.38; 1045. DR PRO; PR:Q9XXC8; -. DR Proteomes; UP000001940; Chromosome III. DR Bgee; WBGene00012970; Expressed in larva and 2 other cell types or tissues. DR ExpressionAtlas; Q9XXC8; baseline and differential. DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central. DR GO; GO:0019166; F:trans-2-enoyl-CoA reductase (NADPH) activity; IBA:GO_Central. 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; 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; PTHR43981; ENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE, MITOCHONDRIAL; 1. DR PANTHER; PTHR43981:SF1; ENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE, MITOCHONDRIAL; 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 Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis; KW Lipid metabolism; Mitochondrion; NADP; Oxidoreductase; Reference proteome; KW Transit peptide. FT TRANSIT 1..22 FT /note="Mitochondrion" FT /evidence="ECO:0000255" FT CHAIN 23..346 FT /note="Enoyl-[acyl-carrier-protein] reductase, FT mitochondrial" FT /id="PRO_0000000893" FT ACT_SITE 59 FT /note="Proton donor" FT /evidence="ECO:0000250|UniProtKB:Q8WZM3" FT BINDING 131 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:Q8WZM3" FT BINDING 157..160 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:Q8WZM3" FT BINDING 180..182 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:Q8WZM3" FT BINDING 249..252 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:Q8WZM3" FT BINDING 274..276 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:Q8WZM3" FT BINDING 332 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:Q8WZM3" SQ SEQUENCE 346 AA; 37944 MW; E14426AADA5FB4A6 CRC64; MQKTIRSQAL IYRKFGDPLK VLQLETVEVP AEPGSGECLV EWLASPINPL DINRIQGNYA VRAELPVIGG SEGVGRVVKA GSGSRFKSGD HVTIFSANTP IWTEFGVVDD DELVKLDNRI PLDLAATLMI NPPTAWIMLK KYVNLQKGDY IIQNSANSGV GRSVIEMCKA LGYKSINIVR NRQNIEALKT DLWRIGADHV FTEEEFKGTS RQFLKSINVR PKLALNGVGG KSALQISSVL ERGGTCVTYG GMSKKAHEFT TSALVFNDIC VRGVAVGMWA RQEEHLDEWN LCVDEVQKLA VAGKITAIPM EKVVLADHKT AIQKSLEGRS IKQLFVINSK ASASHI //