ETR1_CANGA
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 03-AUG-2022, entry version 102.
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 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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};
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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; 5478.XP_445158.1; -.
DR EnsemblFungi; CAG58058; CAG58058; CAGL0B04323g.
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 InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR018060; HTH_AraC.
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 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
