MECR2_CAEEL
ID MECR2_CAEEL Reviewed; 346 AA.
AC Q9XXC8;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 139.
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=Y48A6B.9;
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; AL023844; CAA19533.1; -; Genomic_DNA.
DR PIR; T26986; T26986.
DR RefSeq; NP_001255097.1; NM_001268168.1.
DR AlphaFoldDB; Q9XXC8; -.
DR SMR; Q9XXC8; -.
DR BioGRID; 41720; 2.
DR DIP; DIP-24981N; -.
DR IntAct; Q9XXC8; 2.
DR MINT; Q9XXC8; -.
DR STRING; 6239.Y48A6B.9a; -.
DR EPD; Q9XXC8; -.
DR PaxDb; Q9XXC8; -.
DR PeptideAtlas; Q9XXC8; -.
DR EnsemblMetazoa; Y48A6B.9a.1; Y48A6B.9a.1; WBGene00012970.
DR GeneID; 176534; -.
DR KEGG; cel:CELE_Y48A6B.9; -.
DR UCSC; Y48A6B.9; c. elegans.
DR CTD; 176534; -.
DR WormBase; Y48A6B.9a; CE19192; WBGene00012970; -.
DR eggNOG; KOG0025; Eukaryota.
DR HOGENOM; CLU_026673_17_1_1; -.
DR InParanoid; Q9XXC8; -.
DR OMA; PPTAWIM; -.
DR OrthoDB; 1269870at2759; -.
DR PhylomeDB; Q9XXC8; -.
DR BRENDA; 1.3.1.38; 1045.
DR PRO; PR:Q9XXC8; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00012970; Expressed in larva and 2 other tissues.
DR ExpressionAtlas; Q9XXC8; baseline and differential.
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..22
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 23..346
FT /note="Enoyl-[acyl-carrier-protein] reductase,
FT mitochondrial"
FT /id="PRO_0000000893"
FT ACT_SITE 59
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q8WZM3"
FT BINDING 131
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q8WZM3"
FT BINDING 157..160
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q8WZM3"
FT BINDING 180..182
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q8WZM3"
FT BINDING 249..252
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q8WZM3"
FT BINDING 274..276
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q8WZM3"
FT BINDING 332
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q8WZM3"
SQ SEQUENCE 346 AA; 37944 MW; E14426AADA5FB4A6 CRC64;
MQKTIRSQAL IYRKFGDPLK VLQLETVEVP AEPGSGECLV EWLASPINPL DINRIQGNYA
VRAELPVIGG SEGVGRVVKA GSGSRFKSGD HVTIFSANTP IWTEFGVVDD DELVKLDNRI
PLDLAATLMI NPPTAWIMLK KYVNLQKGDY IIQNSANSGV GRSVIEMCKA LGYKSINIVR
NRQNIEALKT DLWRIGADHV FTEEEFKGTS RQFLKSINVR PKLALNGVGG KSALQISSVL
ERGGTCVTYG GMSKKAHEFT TSALVFNDIC VRGVAVGMWA RQEEHLDEWN LCVDEVQKLA
VAGKITAIPM EKVVLADHKT AIQKSLEGRS IKQLFVINSK ASASHI
