Canmetcon
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Identification
NameEnoyl-[acyl-carrier protein] reductase [NADPH, B-specific], mitochondrial
Synonyms
  • Mitochondrial respiratory function protein 1
  • Trans-2-enoyl-CoA reductase
Gene NameETR1
Enzyme Class
Biological Properties
General FunctionInvolved in zinc ion binding
Specific FunctionRequired for respiration and the maintenance of the mitochondrial compartment. May have a role in the mitochondrial synthesis of fatty acids
Cellular LocationMitochondrion matrix
SMPDB Pathways
Biosynthesis of unsaturated fatty acidsPW002403 ThumbThumb?image type=greyscaleThumb?image type=simple
Fatty acid elongation in mitochondriaPW002467 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG Pathways
Biosynthesis of unsaturated fatty acidsec01040 Map01040
Fatty acid elongation in mitochondriaec00062 Map00062
SMPDB Reactions
trans-octadec-2-enoyl-CoA + hydron + NADPHstearoyl-CoA + NADP
(2E)-eicosenoyl-CoA + hydron + NADPHEicosanoyl-CoA + NADP
trans-docos-2-enoyl-CoA + hydron + NADPHDocosanoyl-CoA + NADP
(2E)-lignocerenoyl-CoA + hydron + NADPHNADP + Tetracosanoyl-CoA
(2E)-cerotenoyl-CoA + hydron + NADPHhexacosanoyl-CoA + NADP
KEGG ReactionsNot Available
Metabolites
YMDB IDNameView
YMDB00426NADPHShow
YMDB00427NADPShow
YMDB00470trans-octadec-2-enoyl-CoAShow
YMDB00537hexacosanoyl-CoAShow
YMDB00538stearoyl-CoAShow
YMDB00862hydronShow
YMDB00909Tetracosanoyl-CoA Show
YMDB16181Eicosanoyl-CoAShow
YMDB16242Docosanoyl-CoAShow
YMDB16294(2E)-eicosenoyl-CoAShow
YMDB16296trans-docos-2-enoyl-CoAShow
YMDB16298(2E)-lignocerenoyl-CoAShow
YMDB16300(2E)-cerotenoyl-CoAShow
GO Classification
Component
Not Available
Function
zinc ion binding
catalytic activity
binding
ion binding
cation binding
metal ion binding
transition metal ion binding
oxidoreductase activity
Process
metabolic process
oxidation reduction
Gene Properties
Chromosome Locationchromosome 2
LocusYBR026C
Gene Sequence>1143 bp ATGCTTCCCACATTCAAACGTTACATGTCGTCCTCAGCTCATCAGATTCCCAAGCACTTC AAATCGCTCACCTATTCAACTCATGAAGTTGAGGATTGTACCAAGGTTTTGTCAGTGAAA AATTATACGCCTAAACAAGACTTATCTCAATCAATTGTGTTAAAAACTTTGGCCTTTCCC ATAAACCCTTCGGATATCAATCAGTTGCAAGGAGTATACCCGTCTCGTCCAGAAAAGACA TACGATTACTCCACAGATGAGCCAGCCGCTATCGCCGGTAATGAGGGTGTCTTTGAAGTT GTTTCTTTACCTTCGGGAAGTTCCAAGGGAGATTTGAAATTGGGTGACCGAGTTATCCCA TTGCAGGCAAATCAAGGGACTTGGTCCAATTATAGAGTTTTCTCTAGTAGTTCTGATTTA ATCAAGGTAAATGATTTGGATCTGTTTTCTGCGGCAACTGTATCTGTTAATGGTTGTACC GGTTTCCAATTAGTATCAGACTATATCGACTGGAACAGTAACGGTAATGAATGGATTATC CAAAATGCCGGTACATCTAGTGTATCAAAAATAGTTACGCAAGTAGCAAAAGCTAAAGGG ATCAAAACATTAAGTGTTATACGTGACCGTGATAATTTTGATGAGGTAGCAAAAGTTTTG GAGGATAAGTATGGTGCTACGAAGGTTATTTCCGAATCGCAAAACAACGACAAGACTTTT GCCAAAGAAGTATTGTCCAAGATTTTGGGTGAAAATGCAAGGGTGAGGCTTGCCTTGAAT TCTGTTGGAGGTAAATCCAGTGCATCAATAGCACGTAAGTTGGAAAATAATGCTTTGATG CTCACTTATGGAGGAATGTCAAAACAACCTGTAACTTTACCAACATCTCTACACATTTTC AAAGGCTTGACATCCAAAGGGTACTGGGTGACTGAAAAGAACAAAAAAAACCCCCAAAGC AAGATTGACACCATCAGTGATTTTATCAAAATGTATAATTATGGTCACATTATTTCACCA AGAGATGAAATTGAAACTCTTACCTGGAATACTAACACTACTACTGACGAACAGTTACTA GAACTAGTCAAAAAAGGTATAACTGGGAAGGGGAAGAAAAAAATGGTTGTTTTAGAATGG TAA
Protein Properties
Pfam Domain FunctionNot Available
Protein Residues380
Protein Molecular Weight42066.5
Protein Theoretical pI9.49
Signalling Regions
  • None
Transmembrane Regions
  • None
Protein Sequence>Enoyl-[acyl-carrier protein] reductase [NADPH, B-specific], mitochondrial MLPTFKRYMSSSAHQIPKHFKSLIYSTHEVEDCTKVLSVKNYTPKQDLSQSIVLKTLAFP INPSDINQLQGVYPSRPEKTYDYSTDEPAAIAGNEGVFEVVSLPSGSSKGDLKLGDRVIP LQANQGTWSNYRVFSSSSDLIKVNDLDLFSAATVSVNGCTGFQLVSDYIDWNSNGNEWII QNAGTSSVSKIVTQVAKAKGIKTLSVIRDRDNFDEVAKVLEDKYGATKVISESQNNDKTF AKEVLSKILGENARVRLALNSVGGKSSASIARKLENNALMLTYGGMSKQPVTLPTSLHIF KGLTSKGYWVTEKNKKNPQSKIDTISDFIKMYNYGHIISPRDEIETLTWNTNTTTDEQLL ELVKKGITGKGKKKMVVLEW
References
External Links
ResourceLink
Saccharomyces Genome Database ETR1
Uniprot IDP38071
Uniprot NameETR1_YEAST
GenBank Gene IDAY557872
Genebank Protein ID45269635
General Reference
  • Yamazoe, M., Shirahige, K., Rashid, M. B., Kaneko, Y., Nakayama, T., Ogasawara, N., Yoshikawa, H. (1994). "A protein which binds preferentially to single-stranded core sequence of autonomously replicating sequence is essential for respiratory function in mitochondrial of Saccharomyces cerevisiae." J Biol Chem 269:15244-15252.8195160
  • Smits, P. H., De Haan, M., Maat, C., Grivell, L. A. (1994). "The complete sequence of a 33 kb fragment on the right arm of chromosome II from Saccharomyces cerevisiae reveals 16 open reading frames, including ten new open reading frames, five previously identified genes and a homologue of the SCO1 gene." Yeast 10 Suppl A:S75-S80.8091864
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  • Grandier-Vazeille, X., Bathany, K., Chaignepain, S., Camougrand, N., Manon, S., Schmitter, J. M. (2001). "Yeast mitochondrial dehydrogenases are associated in a supramolecular complex." Biochemistry 40:9758-9769.11502169
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  • Airenne, T. T., Torkko, J. M., Van den plas, S., Sormunen, R. T., Kastaniotis, A. J., Wierenga, R. K., Hiltunen, J. K. (2003). "Structure-function analysis of enoyl thioester reductase involved in mitochondrial maintenance." J Mol Biol 327:47-59.12614607
  • Ghaemmaghami, S., Huh, W. K., Bower, K., Howson, R. W., Belle, A., Dephoure, N., O'Shea, E. K., Weissman, J. S. (2003). "Global analysis of protein expression in yeast." Nature 425:737-741.14562106
  • Sickmann, A., Reinders, J., Wagner, Y., Joppich, C., Zahedi, R., Meyer, H. E., Schonfisch, B., Perschil, I., Chacinska, A., Guiard, B., Rehling, P., Pfanner, N., Meisinger, C. (2003). "The proteome of Saccharomyces cerevisiae mitochondria." Proc Natl Acad Sci U S A 100:13207-13212.14576278
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