ID   MECR_DROME              Reviewed;         357 AA.
AC   Q9V6U9;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 2.
DT   27-MAR-2024, entry version 149.
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   ORFNames=CG16935;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
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.
CC       {ECO:0000250|UniProtKB:Q9BV79}.
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:Q9BV79};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9BV79}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9BV79}.
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; AE013599; AAF58322.2; -; Genomic_DNA.
DR   RefSeq; NP_001286396.1; NM_001299467.1.
DR   RefSeq; NP_610914.2; NM_137070.2.
DR   AlphaFoldDB; Q9V6U9; -.
DR   SMR; Q9V6U9; -.
DR   BioGRID; 62294; 3.
DR   IntAct; Q9V6U9; 2.
DR   STRING; 7227.FBpp0086748; -.
DR   PaxDb; 7227-FBpp0086748; -.
DR   EnsemblMetazoa; FBtr0087622; FBpp0086748; FBgn0033883.
DR   EnsemblMetazoa; FBtr0339954; FBpp0308976; FBgn0033883.
DR   GeneID; 36540; -.
DR   KEGG; dme:Dmel_CG16935; -.
DR   UCSC; CG16935-RA; d. melanogaster.
DR   AGR; FB:FBgn0033883; -.
DR   FlyBase; FBgn0033883; CG16935.
DR   VEuPathDB; VectorBase:FBgn0033883; -.
DR   eggNOG; KOG0025; Eukaryota.
DR   GeneTree; ENSGT00940000156592; -.
DR   HOGENOM; CLU_026673_17_1_1; -.
DR   InParanoid; Q9V6U9; -.
DR   OMA; YGYTQSK; -.
DR   OrthoDB; 6213at2759; -.
DR   PhylomeDB; Q9V6U9; -.
DR   Reactome; R-DME-77346; Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA.
DR   BioGRID-ORCS; 36540; 1 hit in 1 CRISPR screen.
DR   GenomeRNAi; 36540; -.
DR   PRO; PR:Q9V6U9; -.
DR   Proteomes; UP000000803; Chromosome 2R.
DR   Bgee; FBgn0033883; Expressed in adult hindgut (Drosophila) and 26 other cell types or tissues.
DR   ExpressionAtlas; Q9V6U9; baseline and differential.
DR   GO; GO:0005739; C:mitochondrion; IDA:FlyBase.
DR   GO; GO:0016631; F:enoyl-[acyl-carrier-protein] reductase activity; ISS:UniProtKB.
DR   GO; GO:0019166; F:trans-2-enoyl-CoA reductase (NADPH) activity; IBA:GO_Central.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006631; P:fatty acid metabolic process; ISS: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; IPR013154; ADH-like_N.
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; PF08240; ADH_N; 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.
DR   Genevisible; Q9V6U9; DM.
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..19
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..357
FT                   /note="Enoyl-[acyl-carrier-protein] reductase,
FT                   mitochondrial"
FT                   /id="PRO_0000000894"
FT   ACT_SITE        74
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WZM3"
FT   BINDING         147
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WZM3"
FT   BINDING         173..176
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WZM3"
FT   BINDING         196..198
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WZM3"
FT   BINDING         264..267
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WZM3"
FT   BINDING         289..291
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WZM3"
FT   BINDING         349
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         350
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WZM3"
SQ   SEQUENCE   357 AA;  39111 MW;  7E5F0D1EF9C70693 CRC64;
     MLRRGFLSRI NAAQWSRQMS VVAKSLKYTQ HGEPQEVLQL VEDKLPDPKD NQVLVKILAA
     PINPADINTI QGKYPVKPKF PAVGGNECVA EVICVGDKVK GFEAGQHVIP LASGLGTWTT
     HAVYKEDQLL IVSKKVGLAE AATSTVNPTT AYRMLKDFVQ LCPGDTVIQN GANSAVGQAV
     HQLCRAWGIN SVGIVRDRPE IAELKQMLQC LGATEVLTEA EIRTSDIFKS GKLKKPRLAF
     NCVGGKSATE VSRHLDNGGV LVTYGGMSRE PVTVATGPLI FKDIAFRGFW MTRWSKENYS
     SPERSKMFKE IFELMEQGKF VAPNHEMVPL AKFKDAAAAA LSFKGFTGKK YILDMSI
//