ID ETR1_CANTR Reviewed; 386 AA. AC Q8WZM3; DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2002, sequence version 1. DT 22-FEB-2023, entry version 98. DE RecName: Full=Enoyl-[acyl-carrier-protein] reductase 1, mitochondrial {ECO:0000305}; DE EC=1.3.1.104 {ECO:0000305|PubMed:12890667}; DE AltName: Full=2-enoyl thioester reductase 1 {ECO:0000303|PubMed:11509667}; DE Flags: Precursor; GN Name=ETR1; OS Candida tropicalis (Yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida. OX NCBI_TaxID=5482; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 23-29, FUNCTION, RP CATALYTIC ACTIVITY, SUBUNIT, AND SUBCELLULAR LOCATION. RC STRAIN=ATCC 20336 / pK233 / NCYC 997; 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 [2] RP X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) IN COMPLEX WITH NADP, SUBUNIT, RP INDUCTION BY OLEIC ACID, CATALYTIC ACTIVITY, AND FUNCTION. RC STRAIN=ATCC 20336 / pK233 / NCYC 997; RX PubMed=12890667; DOI=10.1074/jbc.m307664200; RA Torkko J.M., Koivuranta K.T., Kastaniotis A.J., Airenne T.T., Glumoff T., RA Ilves M., Hartig A., Gurvitz A., Hiltunen J.K.; RT "Candida tropicalis expresses two mitochondrial 2-enoyl thioester RT reductases that are able to form both homodimers and heterodimers."; RL J. Biol. Chem. 278:41213-41220(2003). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH NADP, MUTAGENESIS OF RP TYR-79, AND FUNCTION. 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 [4] RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS), AND ACTIVE SITE. RX PubMed=25867044; DOI=10.1038/nchembio.1794; RA Rosenthal R.G., Voegeli B., Quade N., Capitani G., Kiefer P., Vorholt J.A., RA Ebert M.O., Erb T.J.; RT "The use of ene adducts to study and engineer enoyl-thioester reductases."; RL Nat. Chem. Biol. 11:398-400(2015). 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 ECO:0000269|PubMed:12890667}. 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:12890667}; 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 and heterodimer with ETR2. CC {ECO:0000269|PubMed:11509667, ECO:0000269|PubMed:12614607, CC ECO:0000269|PubMed:12890667}. CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:11509667}. CC -!- INDUCTION: Up-regulated by growth on oleic acid. CC {ECO:0000269|PubMed:12890667}. 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; U94997; AAL55472.1; -; Genomic_DNA. DR PDB; 1GU7; X-ray; 1.70 A; A/B=23-386. DR PDB; 1GUF; X-ray; 2.25 A; A/B=23-386. DR PDB; 1GYR; X-ray; 2.60 A; A/B/C=23-386. DR PDB; 1N9G; X-ray; 1.98 A; B/D/E=1-386. DR PDB; 4W99; X-ray; 2.00 A; A/B=23-386. DR PDB; 4WAS; X-ray; 1.70 A; A/B/C=23-386. DR PDB; 5LB9; X-ray; 2.10 A; A/B=23-386. DR PDB; 5LBX; X-ray; 2.50 A; A/B=23-386. DR PDBsum; 1GU7; -. DR PDBsum; 1GUF; -. DR PDBsum; 1GYR; -. DR PDBsum; 1N9G; -. DR PDBsum; 4W99; -. DR PDBsum; 4WAS; -. DR PDBsum; 5LB9; -. DR PDBsum; 5LBX; -. DR AlphaFoldDB; Q8WZM3; -. DR SMR; Q8WZM3; -. DR IntAct; Q8WZM3; 1. DR SwissLipids; SLP:000001783; -. DR VEuPathDB; FungiDB:CTMYA2_052270; -. DR VEuPathDB; FungiDB:CTRG_06166; -. DR EvolutionaryTrace; Q8WZM3; -. DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell. DR GO; GO:0019166; F:trans-2-enoyl-CoA reductase (NADPH) activity; IDA:UniProtKB. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0006631; P:fatty acid metabolic process; IDA:UniProtKB. 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; 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 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 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Fatty acid biosynthesis; KW Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism; Mitochondrion; KW NADP; Oxidoreductase; Transit peptide. FT TRANSIT 1..22 FT /note="Mitochondrion" FT /evidence="ECO:0000269|PubMed:11509667" FT CHAIN 23..386 FT /note="Enoyl-[acyl-carrier-protein] reductase 1, FT mitochondrial" FT /id="PRO_0000000898" FT ACT_SITE 79 FT /note="Proton donor" FT /evidence="ECO:0000269|PubMed:25867044" FT BINDING 172 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000269|PubMed:12614607, FT ECO:0000269|PubMed:12890667" FT BINDING 199..202 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000269|PubMed:12614607, FT ECO:0000269|PubMed:12890667" FT BINDING 222..224 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000269|PubMed:12614607, FT ECO:0000269|PubMed:12890667" FT BINDING 296..299 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000269|PubMed:12614607, FT ECO:0000269|PubMed:12890667" FT BINDING 321..323 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000269|PubMed:12614607, FT ECO:0000269|PubMed:12890667" FT BINDING 381 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000269|PubMed:12614607, FT ECO:0000269|PubMed:12890667" FT MUTAGEN 79 FT /note="Y->N: 0.1% of catalytic activity." FT /evidence="ECO:0000269|PubMed:12614607" FT STRAND 24..33 FT /evidence="ECO:0007829|PDB:1GU7" FT HELIX 37..40 FT /evidence="ECO:0007829|PDB:1GU7" FT STRAND 42..48 FT /evidence="ECO:0007829|PDB:1GU7" FT STRAND 57..67 FT /evidence="ECO:0007829|PDB:1GU7" FT HELIX 69..76 FT /evidence="ECO:0007829|PDB:1GU7" FT STRAND 95..97 FT /evidence="ECO:0007829|PDB:1GU7" FT STRAND 103..109 FT /evidence="ECO:0007829|PDB:1GU7" FT STRAND 121..127 FT /evidence="ECO:0007829|PDB:1GU7" FT STRAND 132..139 FT /evidence="ECO:0007829|PDB:1GU7" FT HELIX 140..142 FT /evidence="ECO:0007829|PDB:1GU7" FT STRAND 143..146 FT /evidence="ECO:0007829|PDB:1GU7" FT HELIX 149..154 FT /evidence="ECO:0007829|PDB:1GU7" FT HELIX 163..167 FT /evidence="ECO:0007829|PDB:1GU7" FT STRAND 169..171 FT /evidence="ECO:0007829|PDB:4WAS" FT HELIX 172..181 FT /evidence="ECO:0007829|PDB:1GU7" FT STRAND 182..184 FT /evidence="ECO:0007829|PDB:1GU7" FT TURN 188..190 FT /evidence="ECO:0007829|PDB:1GU7" FT STRAND 192..196 FT /evidence="ECO:0007829|PDB:1GU7" FT HELIX 201..213 FT /evidence="ECO:0007829|PDB:1GU7" FT STRAND 216..221 FT /evidence="ECO:0007829|PDB:1GU7" FT HELIX 227..237 FT /evidence="ECO:0007829|PDB:1GU7" FT STRAND 240..244 FT /evidence="ECO:0007829|PDB:1GU7" FT HELIX 245..249 FT /evidence="ECO:0007829|PDB:1GU7" FT HELIX 251..253 FT /evidence="ECO:0007829|PDB:1GU7" FT HELIX 254..264 FT /evidence="ECO:0007829|PDB:1GU7" FT STRAND 268..275 FT /evidence="ECO:0007829|PDB:1GU7" FT HELIX 277..285 FT /evidence="ECO:0007829|PDB:1GU7" FT STRAND 292..295 FT /evidence="ECO:0007829|PDB:1GU7" FT STRAND 299..301 FT /evidence="ECO:0007829|PDB:1N9G" FT STRAND 304..306 FT /evidence="ECO:0007829|PDB:1GU7" FT HELIX 308..313 FT /evidence="ECO:0007829|PDB:1GU7" FT STRAND 317..320 FT /evidence="ECO:0007829|PDB:1GU7" FT HELIX 323..327 FT /evidence="ECO:0007829|PDB:1GU7" FT HELIX 331..346 FT /evidence="ECO:0007829|PDB:1GU7" FT STRAND 356..359 FT /evidence="ECO:0007829|PDB:1GU7" FT STRAND 362..364 FT /evidence="ECO:0007829|PDB:1GU7" FT HELIX 366..375 FT /evidence="ECO:0007829|PDB:1GU7" FT HELIX 377..379 FT /evidence="ECO:0007829|PDB:1GU7" FT STRAND 382..385 FT /evidence="ECO:0007829|PDB:1GU7" SQ SEQUENCE 386 AA; 42161 MW; FCBC174A240742D8 CRC64; MYSVLKQSIR PRLLATHNQF RTMITAQAVL YTQHGEPKDV LFTQSFEIDD DNLAPNEVIV KTLGSPVNPS DINQIQGVYP SKPAKTTGFG TTEPAAPCGN EGLFEVIKVG SNVSSLEAGD WVIPSHVNFG TWRTHALGND DDFIKLPNPA QSKANGKPNG LTINQGATIS VNPLTAYLML THYVKLTPGK DWFIQNGGTS AVGKYASQIG KLLNFNSISV IRDRPNLDEV VASLKELGAT QVITEDQNNS REFGPTIKEW IKQSGGEAKL ALNCVGGKSS TGIARKLNNN GLMLTYGGMS FQPVTIPTSL YIFKNFTSAG FWVTELLKNN KELKTSTLNQ IIAWYEEGKL TDAKSIETLY DGTKPLHELY QDGVANSKDG KQLITY //