(data stored in ACNUC7421 zone)

SWISSPROT: ETR1_ASHGO

ID   ETR1_ASHGO              Reviewed;         376 AA.
AC   Q757U3;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2013, sequence version 2.
DT   11-DEC-2019, entry version 100.
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=AEL081W;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION, AND SEQUENCE REVISION TO 324.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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}.
DR   EMBL; AE016818; AAS52604.2; -; Genomic_DNA.
DR   RefSeq; NP_984780.2; NM_210134.2.
DR   SMR; Q757U3; -.
DR   STRING; 33169.AAS52604; -.
DR   EnsemblFungi; AAS52604; AAS52604; AGOS_AEL081W.
DR   GeneID; 4620970; -.
DR   KEGG; ago:AGOS_AEL081W; -.
DR   HOGENOM; HOG000294683; -.
DR   InParanoid; Q757U3; -.
DR   KO; K07512; -.
DR   OMA; AFRGFWM; -.
DR   Proteomes; UP000000591; Chromosome V.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0016631; F:enoyl-[acyl-carrier-protein] reductase activity; IEA:EnsemblFungi.
DR   GO; GO:0019166; F:trans-2-enoyl-CoA reductase (NADPH) activity; IBA:GO_Central.
DR   GO; GO:0009060; P:aerobic respiration; IEA:EnsemblFungi.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR   InterPro; IPR013149; ADH_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   3: Inferred from homology;
DR   PRODOM; Q757U3.
DR   SWISS-2DPAGE; Q757U3.
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           ?..376
FT                   /note="Enoyl-[acyl-carrier-protein] reductase,
FT                   mitochondrial"
FT                   /id="PRO_0000000896"
FT   NP_BIND         182..185
FT                   /note="NADP"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WZM3"
FT   NP_BIND         205..207
FT                   /note="NADP"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WZM3"
FT   NP_BIND         280..283
FT                   /note="NADP"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WZM3"
FT   NP_BIND         305..307
FT                   /note="NADP"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WZM3"
FT   ACT_SITE        72
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WZM3"
FT   BINDING         154
FT                   /note="NADP"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WZM3"
FT   BINDING         369
FT                   /note="NADP"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   376 AA;  41439 MW;  A8F107B8CF1CEC7C CRC64;
     MQALNTTKRL MSTKQFPLFK SLLYSSHDPA DCTQVLKVHS YTPKVGADES ILLRTLAFPI
     NPSDINQLQG VYPSVPEKTL DYSTEKPAAI AGNEGVFEVM SVPQGERRLA VGDWVIPLYS
     NTGTWTNYQT CRDAGTLVKV NGLDLYTAAT IAVNGCTAYQ LVNDYVQWDP SGNEWIVQNA
     GTSAVSKIVT QVAQARGVKT LSVIRDRENF AEVAKELEER YGATKVISET QNNDKDFSKD
     ELPVILGPNA RVRLALNSVG GKSSGAIARK LERDGTMLTY GGMSRQPVTV PTTLLIFNGL
     KSLGYWITEN TKRNPQSKID TISALMRMYG DGQLQPPEAD IKKIEWDVQK MNDEQLLEAV
     KNGIQSNGKS VVVLKW
//

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