ID   MECR_DANRE              Reviewed;         377 AA.
AC   Q6GQN8;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 2.
DT   03-AUG-2022, entry version 111.
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=mecr; ORFNames=zgc:110153;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
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   -!- SEQUENCE CAUTION:
CC       Sequence=AAH72704.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BC072704; AAH72704.1; ALT_INIT; mRNA.
DR   AlphaFoldDB; Q6GQN8; -.
DR   SMR; Q6GQN8; -.
DR   STRING; 7955.ENSDARP00000038801; -.
DR   PaxDb; Q6GQN8; -.
DR   Ensembl; ENSDART00000039054; ENSDARP00000038801; ENSDARG00000032326.
DR   ZFIN; ZDB-GENE-050417-399; mecr.
DR   eggNOG; KOG0025; Eukaryota.
DR   GeneTree; ENSGT00940000156592; -.
DR   HOGENOM; CLU_026673_17_1_1; -.
DR   InParanoid; Q6GQN8; -.
DR   OMA; HQLCRAW; -.
DR   PhylomeDB; Q6GQN8; -.
DR   TreeFam; TF312886; -.
DR   Reactome; R-DRE-77346; Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA.
DR   PRO; PR:Q6GQN8; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 16.
DR   Bgee; ENSDARG00000032326; Expressed in testis and 27 other tissues.
DR   ExpressionAtlas; Q6GQN8; baseline.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
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; IBA:GO_Central.
DR   InterPro; IPR013149; ADH-like_C.
DR   InterPro; IPR013154; ADH_N.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SUPFAM; SSF50129; SSF50129; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   2: Evidence at transcript level;
KW   Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW   Lipid metabolism; Mitochondrion; NADP; Oxidoreductase; Reference proteome;
KW   Transit peptide.
FT   TRANSIT         1..52
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           53..377
FT                   /note="Enoyl-[acyl-carrier-protein] reductase,
FT                   mitochondrial"
FT                   /id="PRO_0000000891"
FT   ACT_SITE        96
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WZM3"
FT   BINDING         169
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WZM3"
FT   BINDING         195..198
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WZM3"
FT   BINDING         218..220
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WZM3"
FT   BINDING         287..290
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WZM3"
FT   BINDING         312..314
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WZM3"
FT   BINDING         372
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WZM3"
SQ   SEQUENCE   377 AA;  41079 MW;  3FB9E922C6A0EDB2 CRC64;
     MKLPSVASLL IRVYRTTGPV SHIQRIRHGA VLNKNYSSVS AVKNCTALLY RNHGEPSQVV
     QLESLDLPQV GAECVLVKML AAPINPSDLN MLQGTYAILP ELPAVGGNEG VAQVMEVGDK
     VKTLKVGDWV IPKDAGIGTW RTAAVLKADD LVTLPKDIPV LSAATLGVNP CTAYRMLTDF
     EELKAGDTVI QNAANSGVGQ AVIQIAAAKG IHTINVIRDR PDLRQLSDRL TAMGATHVIT
     EETLRRPEMK ELFKSCPRPK LALNGVGGKS ATELLRHLQS GGSLVTYGGM AKQPVTVPVS
     ALIFKDVRVR GFWVTQWKRD NRHDDEALRH MLDELCILIR AGKLSAPICT QVQLQDFRKA
     LENAMKPYVS TKQVFVM