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   16-JUN-2009, entry version 51.
DE   RecName: Full=Probable trans-2-enoyl-CoA reductase 1, mitochondrial;
DE            EC=1.3.1.38;
DE   Flags: Precursor;
GN   ORFNames=W09H1.5;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea;
OC   Rhabditidae; Peloderinae; Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   MEDLINE=99069613; 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
RT   investigating biology.";
RL   Science 282:2012-2018(1998).
CC   -!- FUNCTION: Catalyzes the reduction of trans-2-enoyl-CoA to acyl-
CC       CoA. May have a role in the mitochondrial synthesis of fatty acids
CC       (By similarity).
CC   -!- CATALYTIC ACTIVITY: Acyl-CoA + NADP(+) = trans-2,3-dehydroacyl-CoA
CC       + NADPH.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion (By similarity).
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. Quinone oxidoreductase subfamily.
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DR   EMBL; Z82081; CAB04958.1; -; Genomic_DNA.
DR   PIR; T26323; T26323.
DR   RefSeq; NP_496800.1; -.
DR   UniGene; Cel.14175; -.
DR   HSSP; Q8WZM3; 1GU7.
DR   Ensembl; W09H1.5; Caenorhabditis elegans.
DR   GeneID; 174963; -.
DR   KEGG; cel:W09H1.5; -.
DR   NMPDR; fig|6239.3.peg.7945; -.
DR   WormBase; WBGene00012375; W09H1.5.
DR   WormPep; W09H1.5; CE16575.
DR   OMA; O45903; INVVRDX.
DR   BRENDA; 1.3.1.38; 672.
DR   NextBio; 886210; -.
DR   ArrayExpress; O45903; -.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0019166; F:trans-2-enoyl-CoA reductase (NADPH) activity; IEA:EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR013154; ADH_GroES-like.
DR   InterPro; IPR002085; ADH_SF_Zn.
DR   InterPro; IPR013149; ADH_Zn-bd.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   PANTHER; PTHR11695; ADH_Sf_Zn; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
PE   2: Evidence at transcript level;
KW   Complete proteome; Fatty acid biosynthesis; Lipid synthesis;
KW   Mitochondrion; NADP; Oxidoreductase; Transit peptide.
FT   TRANSIT       1     14       Mitochondrion (Potential).
FT   CHAIN        15    344       Probable trans-2-enoyl-CoA reductase 1,
FT                                mitochondrial.
FT                                /FTId=PRO_0000000892.
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
//