ID ETR1_YEAST Reviewed; 380 AA. AC P38071; D6VQ28; Q6Q5P2; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 3. DT 27-MAR-2024, entry version 188. DE RecName: Full=Enoyl-[acyl-carrier-protein] reductase, mitochondrial {ECO:0000305}; DE EC=1.3.1.104 {ECO:0000305|PubMed:11509667, ECO:0000305|PubMed:12614607}; DE AltName: Full=2-enoyl thioester reductase {ECO:0000303|PubMed:11509667}; DE AltName: Full=Mitochondrial respiratory function protein 1 {ECO:0000303|PubMed:8195160}; DE Flags: Precursor; GN Name=ETR1; Synonyms=MRF1, MRF1'; OrderedLocusNames=YBR026C; GN ORFNames=YBR0310; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 10-25. RC STRAIN=ATCC 26786 / X2180-1A; RX PubMed=8195160; DOI=10.1016/s0021-9258(17)36598-5; RA Yamazoe M., Shirahige K., Rashid M.B., Kaneko Y., Nakayama T., RA Ogasawara N., Yoshikawa H.; RT "A protein which binds preferentially to single-stranded core sequence of RT autonomously replicating sequence is essential for respiratory function in RT mitochondrial of Saccharomyces cerevisiae."; RL J. Biol. Chem. 269:15244-15252(1994). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=8091864; DOI=10.1002/yea.320100010; RA Smits P.H.M., de Haan M., Maat C., Grivell L.A.; RT "The complete sequence of a 33 kb fragment on the right arm of chromosome RT II from Saccharomyces cerevisiae reveals 16 open reading frames, including RT ten new open reading frames, five previously identified genes and a RT homologue of the SCO1 gene."; RL Yeast 10:S75-S80(1994). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x; RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H., RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., RA Mewes H.-W., Kleine K.; RT "Complete DNA sequence of yeast chromosome II."; RL EMBO J. 13:5795-5809(1994). RN [4] RP GENOME REANNOTATION. RC STRAIN=ATCC 204508 / S288c; RX PubMed=24374639; DOI=10.1534/g3.113.008995; RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now."; RL G3 (Bethesda) 4:389-398(2014). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=17322287; DOI=10.1101/gr.6037607; RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J., RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., RA LaBaer J.; RT "Approaching a complete repository of sequence-verified protein-encoding RT clones for Saccharomyces cerevisiae."; RL Genome Res. 17:536-543(2007). RN [6] RP SUBCELLULAR LOCATION. RX PubMed=11502169; DOI=10.1021/bi010277r; RA Grandier-Vazeille X., Bathany K., Chaignepain S., Camougrand N., Manon S., RA Schmitter J.-M.; RT "Yeast mitochondrial dehydrogenases are associated in a supramolecular RT complex."; RL Biochemistry 40:9758-9769(2001). RN [7] RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND SUBCELLULAR LOCATION. RX PubMed=11509667; DOI=10.1128/mcb.21.18.6243-6253.2001; RA Torkko J.M., Koivuranta K.T., Miinalainen I.J., Yagi A.I., Schmitz W., RA Kastaniotis A.J., Airenne T.T., Gurvitz A., Hiltunen K.J.; RT "Candida tropicalis Etr1p and Saccharomyces cerevisiae Ybr026p (Mrf1'p), 2- RT enoyl thioester reductases essential for mitochondrial respiratory RT competence."; RL Mol. Cell. Biol. 21:6243-6253(2001). RN [8] RP FUNCTION, AND MUTAGENESIS OF TYR-73. RX PubMed=12614607; DOI=10.1016/s0022-2836(03)00038-x; RA Airenne T.T., Torkko J.M., Van den plas S., Sormunen R.T., RA Kastaniotis A.J., Wierenga R.K., Hiltunen J.K.; RT "Structure-function analysis of enoyl thioester reductase involved in RT mitochondrial maintenance."; RL J. Mol. Biol. 327:47-59(2003). RN [9] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., RA O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [10] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RC STRAIN=ATCC 76625 / YPH499; RX PubMed=14576278; DOI=10.1073/pnas.2135385100; RA Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E., RA Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P., RA Pfanner N., Meisinger C.; RT "The proteome of Saccharomyces cerevisiae mitochondria."; RL Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-339, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200; RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; RT "A multidimensional chromatography technology for in-depth phosphoproteome RT analysis."; RL Mol. Cell. Proteomics 7:1389-1396(2008). RN [12] RP INDUCTION. RX PubMed=26711224; DOI=10.1111/mmi.13298; RA Singh N., Yadav K.K., Rajasekharan R.; RT "ZAP1-mediated modulation of triacylglycerol levels in yeast by RT transcriptional control of mitochondrial fatty acid biosynthesis."; RL Mol. Microbiol. 100:55-75(2016). 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:0000269|PubMed:11509667, ECO:0000269|PubMed:12614607}. 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:0000305|PubMed:11509667, ECO:0000305|PubMed:12614607}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(2E,4E)-hexadienoyl-CoA + H(+) + NADPH = (4E)-hexenoyl-CoA + CC NADP(+); Xref=Rhea:RHEA:54908, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, CC ChEBI:CHEBI:58349, ChEBI:CHEBI:84788, ChEBI:CHEBI:138404; CC Evidence={ECO:0000269|PubMed:11509667}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54909; CC Evidence={ECO:0000305|PubMed:11509667}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(2E)-hexenoyl-CoA + H(+) + NADPH = hexanoyl-CoA + NADP(+); CC Xref=Rhea:RHEA:44956, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, CC ChEBI:CHEBI:58349, ChEBI:CHEBI:62077, ChEBI:CHEBI:62620; CC Evidence={ECO:0000269|PubMed:11509667}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44957; CC Evidence={ECO:0000305|PubMed:11509667}; CC -!- SUBUNIT: Homodimer or in a complex with other proteins CC (PubMed:11509667). Interacts with ARS1 (PubMed:8195160). CC {ECO:0000269|PubMed:11509667, ECO:0000269|PubMed:8195160}. CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix CC {ECO:0000269|PubMed:11502169, ECO:0000269|PubMed:11509667, CC ECO:0000269|PubMed:14576278}. CC -!- INDUCTION: Positively regulated by the zinc-responsive transcriptional CC regulator ZAP1. {ECO:0000269|PubMed:26711224}. CC -!- MISCELLANEOUS: Present with 1560 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase CC family. Quinone oxidoreductase subfamily. {ECO:0000305}. CC -!- CAUTION: Was originally (PubMed:8195160) thought to be a nuclear CC protein involved in transcriptional regulation of genes required for CC the functional assembly of mitochondrial respiratory proteins. This was CC later proven not to be the case (PubMed:11509667). CC {ECO:0000305|PubMed:11509667, ECO:0000305|PubMed:8195160}. 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; D26606; BAA05651.1; -; Genomic_DNA. DR EMBL; Z35895; CAA84968.1; -; Genomic_DNA. DR EMBL; X76078; CAA53683.1; -; Genomic_DNA. DR EMBL; AY557872; AAS56198.1; -; Genomic_DNA. DR EMBL; BK006936; DAA07148.1; -; Genomic_DNA. DR RefSeq; NP_009582.1; NM_001178374.1. DR AlphaFoldDB; P38071; -. DR SMR; P38071; -. DR BioGRID; 32729; 414. DR IntAct; P38071; 2. DR MINT; P38071; -. DR STRING; 4932.YBR026C; -. DR SwissLipids; SLP:000001784; -. DR iPTMnet; P38071; -. DR MaxQB; P38071; -. DR PaxDb; 4932-YBR026C; -. DR PeptideAtlas; P38071; -. DR EnsemblFungi; YBR026C_mRNA; YBR026C; YBR026C. DR GeneID; 852314; -. DR KEGG; sce:YBR026C; -. DR AGR; SGD:S000000230; -. DR SGD; S000000230; ETR1. DR VEuPathDB; FungiDB:YBR026C; -. DR eggNOG; KOG0025; Eukaryota. DR GeneTree; ENSGT00940000156592; -. DR HOGENOM; CLU_026673_17_0_1; -. DR InParanoid; P38071; -. DR OMA; YGYTQSK; -. DR OrthoDB; 6213at2759; -. DR BioCyc; MetaCyc:G3O-29006-MONOMER; -. DR BioCyc; YEAST:G3O-29006-MONOMER; -. DR BRENDA; 1.3.1.10; 984. DR Reactome; R-SCE-77346; Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA. DR BioGRID-ORCS; 852314; 0 hits in 10 CRISPR screens. DR PRO; PR:P38071; -. DR Proteomes; UP000002311; Chromosome II. DR RNAct; P38071; Protein. DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; IDA:SGD. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0016631; F:enoyl-[acyl-carrier-protein] reductase activity; IDA:SGD. DR GO; GO:0019166; F:trans-2-enoyl-CoA reductase (NADPH) activity; IBA:GO_Central. DR GO; GO:0009060; P:aerobic respiration; IMP:SGD. DR GO; GO:0006633; P:fatty acid biosynthetic process; IMP:SGD. 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 PANTHER; PTHR43981; ENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE, MITOCHONDRIAL; 1. DR PANTHER; PTHR43981:SF2; ENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE, MITOCHONDRIAL; 1. DR SUPFAM; SSF50129; GroES-like; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. PE 1: Evidence at protein level; KW Direct protein sequencing; DNA-binding; Fatty acid biosynthesis; KW Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism; Mitochondrion; KW NADP; Oxidoreductase; Phosphoprotein; Reference proteome; Transit peptide. FT TRANSIT 1..9 FT /note="Mitochondrion" FT /evidence="ECO:0000269|PubMed:8195160" FT CHAIN 10..380 FT /note="Enoyl-[acyl-carrier-protein] reductase, FT mitochondrial" FT /id="PRO_0000160924" FT ACT_SITE 73 FT /note="Proton donor" FT /evidence="ECO:0000250|UniProtKB:Q8WZM3" FT BINDING 157 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:Q8WZM3" FT BINDING 185..188 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:Q8WZM3" FT BINDING 208..210 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:Q8WZM3" FT BINDING 283..286 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:Q8WZM3" FT BINDING 308..310 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:Q8WZM3" FT BINDING 373 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:Q8WZM3" FT MOD_RES 339 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18407956" FT MUTAGEN 73 FT /note="Y->N: 0.1% of catalytic activity. No specific ARS1 FT binding." FT /evidence="ECO:0000269|PubMed:12614607" FT CONFLICT 24 FT /note="I -> T (in Ref. 5; AAS56198)" FT /evidence="ECO:0000305" SQ SEQUENCE 380 AA; 42067 MW; 9795013283C3E9F8 CRC64; MLPTFKRYMS SSAHQIPKHF KSLIYSTHEV EDCTKVLSVK NYTPKQDLSQ SIVLKTLAFP INPSDINQLQ GVYPSRPEKT YDYSTDEPAA IAGNEGVFEV VSLPSGSSKG DLKLGDRVIP LQANQGTWSN YRVFSSSSDL IKVNDLDLFS AATVSVNGCT GFQLVSDYID WNSNGNEWII QNAGTSSVSK IVTQVAKAKG IKTLSVIRDR DNFDEVAKVL EDKYGATKVI SESQNNDKTF AKEVLSKILG ENARVRLALN SVGGKSSASI ARKLENNALM LTYGGMSKQP VTLPTSLHIF KGLTSKGYWV TEKNKKNPQS KIDTISDFIK MYNYGHIISP RDEIETLTWN TNTTTDEQLL ELVKKGITGK GKKKMVVLEW //