ETR1_YEAST
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 03-AUG-2022, entry version 180.
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; 401.
DR IntAct; P38071; 2.
DR MINT; P38071; -.
DR STRING; 4932.YBR026C; -.
DR SwissLipids; SLP:000001784; -.
DR iPTMnet; P38071; -.
DR MaxQB; P38071; -.
DR PaxDb; P38071; -.
DR PRIDE; P38071; -.
DR EnsemblFungi; YBR026C_mRNA; YBR026C; YBR026C.
DR GeneID; 852314; -.
DR KEGG; sce:YBR026C; -.
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; HQLCRAW; -.
DR BioCyc; MetaCyc:G3O-29006-MON; -.
DR BioCyc; YEAST:G3O-29006-MON; -.
DR BRENDA; 1.3.1.10; 984.
DR Reactome; R-SCE-77346; Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA.
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 InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 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
