ETR1_CANTR
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 03-AUG-2022, entry version 96.
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}.
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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 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 Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 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
