ID   ETR1_CANGA              Reviewed;         385 AA.
AC   Q6FXN7;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 2.
DT   24-JAN-2024, entry version 110.
DE   RecName: Full=Enoyl-[acyl-carrier-protein] reductase, mitochondrial;
DE            EC=1.3.1.104;
DE   AltName: Full=2-enoyl thioester reductase;
DE   Flags: Precursor;
GN   Name=ETR1; OrderedLocusNames=CAGL0B04323g;
OS   Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 /
OS   NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS
RC   138;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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:0000250|UniProtKB:P38071}.
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:0000250|UniProtKB:P38071};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q8WZM3}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000250|UniProtKB:P38071}.
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. Quinone oxidoreductase subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAG58058.1; Type=Erroneous initiation; Evidence={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; CR380948; CAG58058.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; XP_445158.1; XM_445158.1.
DR   AlphaFoldDB; Q6FXN7; -.
DR   SMR; Q6FXN7; -.
DR   STRING; 284593.Q6FXN7; -.
DR   GeneID; 2886666; -.
DR   KEGG; cgr:CAGL0B04323g; -.
DR   eggNOG; KOG0025; Eukaryota.
DR   HOGENOM; CLU_026673_17_0_1; -.
DR   InParanoid; Q6FXN7; -.
DR   Proteomes; UP000002428; Chromosome B.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
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; IPR018060; HTH_AraC.
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   3: Inferred from homology;
KW   Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW   Lipid metabolism; Mitochondrion; NADP; Oxidoreductase; Reference proteome;
KW   Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..385
FT                   /note="Enoyl-[acyl-carrier-protein] reductase,
FT                   mitochondrial"
FT                   /id="PRO_0000000897"
FT   ACT_SITE        78
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WZM3"
FT   BINDING         162
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WZM3"
FT   BINDING         190..193
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WZM3"
FT   BINDING         213..215
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WZM3"
FT   BINDING         288..291
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WZM3"
FT   BINDING         313..315
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WZM3"
FT   BINDING         378
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   385 AA;  42620 MW;  2B2E90144FA5A88C CRC64;
     MSGLRAASVF SPVFKRMASS IPSQFKSIIY NSHSLEDCTG VLSVHNYKPK QDLNKSVVLR
     TLAFPINPSD INQLQGVYPS LPEKTLDYST EKPSAIAGNE GLFEVVSLPE HGDHGELKVG
     DWVIPVQANQ GTWSNYRVFD KASDLIKVNG LDLYSAATVS VNGCTAYQLV NNYVDWNADG
     NEWLIQNAGT SGVSKFVTQI AKARGVKTLS VIRDRDNFEE VAEVLEQKFG ATKVISESQN
     NDKDFGKKEL PKVLGDKARV RLALNSVGGK SSSAIARKLE RDALMLTYGG MSKQPVTIPT
     SLHIFKGLTS KGYWVTENNK RDPTDKVNTI KGFIDLYKQG KIISPEEEIE TMEWDANNGD
     DQQLLELVKR GITEKGKKKM VLLKW
//