MECR1_CAEEL
ID MECR1_CAEEL Reviewed; 344 AA.
AC O45903;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 128.
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=W09H1.5;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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}.
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DR EMBL; Z82081; CAB04958.1; -; Genomic_DNA.
DR PIR; T26323; T26323.
DR RefSeq; NP_496800.1; NM_064399.3.
DR AlphaFoldDB; O45903; -.
DR SMR; O45903; -.
DR BioGRID; 40259; 6.
DR STRING; 6239.W09H1.5; -.
DR EPD; O45903; -.
DR PaxDb; O45903; -.
DR PeptideAtlas; O45903; -.
DR EnsemblMetazoa; W09H1.5.1; W09H1.5.1; WBGene00012375.
DR GeneID; 174963; -.
DR KEGG; cel:CELE_W09H1.5; -.
DR UCSC; W09H1.5; c. elegans.
DR CTD; 174963; -.
DR WormBase; W09H1.5; CE16575; WBGene00012375; mecr-1.
DR eggNOG; KOG0025; Eukaryota.
DR GeneTree; ENSGT00940000156592; -.
DR HOGENOM; CLU_026673_17_1_1; -.
DR InParanoid; O45903; -.
DR OMA; RNSKHTE; -.
DR OrthoDB; 1269870at2759; -.
DR PhylomeDB; O45903; -.
DR BRENDA; 1.3.1.38; 1045.
DR Reactome; R-CEL-77346; Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA.
DR PRO; PR:O45903; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00012375; Expressed in germ line (C elegans) and 4 other tissues.
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 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..14
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 15..344
FT /note="Enoyl-[acyl-carrier-protein] reductase,
FT mitochondrial"
FT /id="PRO_0000000892"
FT ACT_SITE 69
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q8WZM3"
FT BINDING 142
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q8WZM3"
FT BINDING 168..171
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q8WZM3"
FT BINDING 191..193
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q8WZM3"
FT BINDING 255..258
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q8WZM3"
FT BINDING 280..282
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q8WZM3"
FT BINDING 338
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
SQ SEQUENCE 344 AA; 38195 MW; F1E47BB2C89D5268 CRC64;
MLKVLSLRSA LQRAASTRQL VYEGYRNPPE AIQLKTVTIA DKPSADQVLV QWIAAPINPA
DLNQIQGVYP VKPALPAVGG NEGFGKVISV GSNVSSIKVG DHVIPDRSGL GTWRELGLHQ
ENDLFPIDNT LSMEYAATFQ VNPPTAYRML KDFIDLKKGD TVAQNGANSA VGKHVIQICR
ILGIKTVNVV RSRDNLEELV KELKDLGADE VITQEELYSR KKKFPGVKLA LNCVGGRSSL
FLASLLDHGG CMVTYGGMSK QPVDCPTGPL IFKDISLRGF WMSRWYDIQK SPEKRHEMYQ
ELAGWMKSGE IKKQEIVKNR LEDHAKALDT ALSKFDKKQF FVLE
