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Enoyl-[acyl-carrier-protein] reductase, mitochondrial (EC 1.3.1.104) (2-enoyl thioester reductase) (Mitochondrial respiratory function protein 1)

 ETR1_YEAST              Reviewed;         380 AA.
P38071; D6VQ28; Q6Q5P2;
01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 3.
22-NOV-2017, entry version 154.
RecName: Full=Enoyl-[acyl-carrier-protein] reductase, mitochondrial {ECO:0000305};
EC=1.3.1.104 {ECO:0000305|PubMed:11509667, ECO:0000305|PubMed:12614607};
AltName: Full=2-enoyl thioester reductase {ECO:0000303|PubMed:11509667};
AltName: Full=Mitochondrial respiratory function protein 1 {ECO:0000303|PubMed:8195160};
Flags: Precursor;
Name=ETR1; Synonyms=MRF1, MRF1'; OrderedLocusNames=YBR026C;
ORFNames=YBR0310;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 10-25.
STRAIN=ATCC 26786 / X2180-1A;
PubMed=8195160;
Yamazoe M., Shirahige K., Rashid M.B., Kaneko Y., Nakayama T.,
Ogasawara N., Yoshikawa H.;
"A protein which binds preferentially to single-stranded core sequence
of autonomously replicating sequence is essential for respiratory
function in mitochondrial of Saccharomyces cerevisiae.";
J. Biol. Chem. 269:15244-15252(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=8091864; DOI=10.1002/yea.320100010;
Smits P.H.M., de Haan M., Maat C., Grivell L.A.;
"The complete sequence of a 33 kb fragment on the right arm of
chromosome II from Saccharomyces cerevisiae reveals 16 open reading
frames, including ten new open reading frames, five previously
identified genes and a homologue of the SCO1 gene.";
Yeast 10:S75-S80(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=7813418;
Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J.,
Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C.,
Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M.,
Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L.,
Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J.,
Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T.,
Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A.,
Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B.,
Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I.,
Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M.,
Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A.,
van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I.,
Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H.,
Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.;
"Complete DNA sequence of yeast chromosome II.";
EMBO J. 13:5795-5809(1994).
[4]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=17322287; DOI=10.1101/gr.6037607;
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A.,
Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
Kolodner R.D., LaBaer J.;
"Approaching a complete repository of sequence-verified protein-
encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[6]
SUBCELLULAR LOCATION.
PubMed=11502169; DOI=10.1021/bi010277r;
Grandier-Vazeille X., Bathany K., Chaignepain S., Camougrand N.,
Manon S., Schmitter J.-M.;
"Yeast mitochondrial dehydrogenases are associated in a supramolecular
complex.";
Biochemistry 40:9758-9769(2001).
[7]
FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=11509667; DOI=10.1128/MCB.21.18.6243-6253.2001;
Torkko J.M., Koivuranta K.T., Miinalainen I.J., Yagi A.I., Schmitz W.,
Kastaniotis A.J., Airenne T.T., Gurvitz A., Hiltunen K.J.;
"Candida tropicalis Etr1p and Saccharomyces cerevisiae Ybr026p
(Mrf1'p), 2-enoyl thioester reductases essential for mitochondrial
respiratory competence.";
Mol. Cell. Biol. 21:6243-6253(2001).
[8]
FUNCTION, AND MUTAGENESIS OF TYR-73.
PubMed=12614607; DOI=10.1016/S0022-2836(03)00038-X;
Airenne T.T., Torkko J.M., Van den plas S., Sormunen R.T.,
Kastaniotis A.J., Wierenga R.K., Hiltunen J.K.;
"Structure-function analysis of enoyl thioester reductase involved in
mitochondrial maintenance.";
J. Mol. Biol. 327:47-59(2003).
[9]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[10]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
STRAIN=ATCC 76625 / YPH499;
PubMed=14576278; DOI=10.1073/pnas.2135385100;
Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P.,
Meyer H.E., Schoenfisch B., Perschil I., Chacinska A., Guiard B.,
Rehling P., Pfanner N., Meisinger C.;
"The proteome of Saccharomyces cerevisiae mitochondria.";
Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-339, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
-!- FUNCTION: Catalyzes the NADPH-dependent reduction of trans-2-enoyl
thioesters in mitochondrial fatty acid synthesis (fatty acid
synthesis type II). Fatty acid chain elongation in mitochondria
uses acyl carrier protein (ACP) as an acyl group carrier, but the
enzyme accepts both ACP and CoA thioesters as substrates in vitro.
Required for respiration and the maintenance of the mitochondrial
compartment. {ECO:0000269|PubMed:11509667,
ECO:0000269|PubMed:12614607}.
-!- CATALYTIC ACTIVITY: An acyl-[acyl-carrier protein] + NADP(+) = a
trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH.
{ECO:0000305|PubMed:11509667, ECO:0000305|PubMed:12614607}.
-!- SUBUNIT: Homodimer or in a complex with other proteins
(PubMed:11509667). Interacts with ARS1 (PubMed:8195160).
{ECO:0000269|PubMed:11509667, ECO:0000269|PubMed:8195160}.
-!- SUBCELLULAR LOCATION: Mitochondrion matrix
{ECO:0000269|PubMed:11502169, ECO:0000269|PubMed:11509667,
ECO:0000269|PubMed:14576278}.
-!- MISCELLANEOUS: Present with 1560 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
family. Quinone oxidoreductase subfamily. {ECO:0000305}.
-!- CAUTION: Was originally (PubMed:8195160) thought to be a nuclear
protein involved in transcriptional regulation of genes required
for the functional assembly of mitochondrial respiratory proteins.
This was later proven not to be the case (PubMed:11509667).
{ECO:0000305|PubMed:11509667, ECO:0000305|PubMed:8195160}.
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EMBL; D26606; BAA05651.1; -; Genomic_DNA.
EMBL; Z35895; CAA84968.1; -; Genomic_DNA.
EMBL; X76078; CAA53683.1; -; Genomic_DNA.
EMBL; AY557872; AAS56198.1; -; Genomic_DNA.
EMBL; BK006936; DAA07148.1; -; Genomic_DNA.
RefSeq; NP_009582.1; NM_001178374.1.
ProteinModelPortal; P38071; -.
SMR; P38071; -.
BioGrid; 32729; 391.
IntAct; P38071; 2.
MINT; MINT-2788988; -.
STRING; 4932.YBR026C; -.
SwissLipids; SLP:000001784; -.
iPTMnet; P38071; -.
MaxQB; P38071; -.
PRIDE; P38071; -.
EnsemblFungi; YBR026C; YBR026C; YBR026C.
GeneID; 852314; -.
KEGG; sce:YBR026C; -.
EuPathDB; FungiDB:YBR026C; -.
SGD; S000000230; ETR1.
GeneTree; ENSGT00550000074483; -.
HOGENOM; HOG000294683; -.
InParanoid; P38071; -.
KO; K07512; -.
OMA; AFRGFWM; -.
OrthoDB; EOG092C2NJA; -.
BioCyc; MetaCyc:G3O-29006-MONOMER; -.
BioCyc; YEAST:G3O-29006-MONOMER; -.
BRENDA; 1.3.1.10; 984.
Reactome; R-SCE-6798695; Neutrophil degranulation.
Reactome; R-SCE-6803205; TP53 regulates transcription of several additional cell death genes whose specific roles in p53-dependent apoptosis remain uncertain.
Reactome; R-SCE-77346; Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA.
PRO; PR:P38071; -.
Proteomes; UP000002311; Chromosome II.
GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; IDA:SGD.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0016631; F:enoyl-[acyl-carrier-protein] reductase activity; IDA:SGD.
GO; GO:0009060; P:aerobic respiration; IMP:SGD.
GO; GO:0006633; P:fatty acid biosynthetic process; IMP:SGD.
InterPro; IPR011032; GroES-like_sf.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
SUPFAM; SSF50129; SSF50129; 1.
SUPFAM; SSF51735; SSF51735; 1.
1: Evidence at protein level;
Complete proteome; Direct protein sequencing; DNA-binding;
Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
Lipid metabolism; Mitochondrion; NADP; Oxidoreductase; Phosphoprotein;
Reference proteome; Transit peptide.
TRANSIT 1 9 Mitochondrion.
{ECO:0000269|PubMed:8195160}.
CHAIN 10 380 Enoyl-[acyl-carrier-protein] reductase,
mitochondrial.
/FTId=PRO_0000160924.
NP_BIND 185 188 NADP. {ECO:0000250|UniProtKB:Q8WZM3}.
NP_BIND 208 210 NADP. {ECO:0000250|UniProtKB:Q8WZM3}.
NP_BIND 283 286 NADP. {ECO:0000250|UniProtKB:Q8WZM3}.
NP_BIND 308 310 NADP. {ECO:0000250|UniProtKB:Q8WZM3}.
ACT_SITE 73 73 Proton donor.
{ECO:0000250|UniProtKB:Q8WZM3}.
BINDING 157 157 NADP. {ECO:0000250|UniProtKB:Q8WZM3}.
BINDING 373 373 NADP. {ECO:0000250|UniProtKB:Q8WZM3}.
MOD_RES 339 339 Phosphoserine.
{ECO:0000244|PubMed:18407956}.
MUTAGEN 73 73 Y->N: 0.1% of catalytic activity. No
specific ARS1 binding.
{ECO:0000269|PubMed:12614607}.
CONFLICT 24 24 I -> T (in Ref. 5; AAS56198).
{ECO:0000305}.
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


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