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 16-JUN-2009, entry version 54. DE RecName: Full=Probable trans-2-enoyl-CoA reductase, mitochondrial; DE EC=1.3.1.38; DE Flags: Precursor; GN ORFNames=CG16935; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7227; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley; RX MEDLINE=20196006; 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., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA 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., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA 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., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., RA Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP GENOME REANNOTATION. RX MEDLINE=22426069; PubMed=12537572; 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., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). 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. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE013599; AAF58322.2; -; Genomic_DNA. DR RefSeq; NP_610914.2; -. DR UniGene; Dm.30974; -. DR HSSP; Q8WZM4; 1H0K. DR IntAct; Q9V6U9; 2. DR Ensembl; FBgn0033883; Drosophila melanogaster. DR GeneID; 36540; -. DR KEGG; dme:Dmel_CG16935; -. DR NMPDR; fig|7227.3.peg.5127; -. DR FlyBase; FBgn0033883; CG16935. DR HOGENOM; Q9V6U9; -. DR OMA; Q9V6U9; AYLMLTH. DR BRENDA; 1.3.1.38; 48. DR NextBio; 799088; -. DR ArrayExpress; Q9V6U9; -. DR GermOnline; CG16935; Drosophila melanogaster. DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB. DR GO; GO:0019166; F:trans-2-enoyl-CoA reductase (NADPH) activity; ISS:UniProtKB. 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 19 Mitochondrion (Potential). FT CHAIN 20 357 Probable trans-2-enoyl-CoA reductase, FT mitochondrial. FT /FTId=PRO_0000000894. 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 //