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Identification
HMDB Protein ID HMDBP01040
Secondary Accession Numbers
  • 6329
Name 2,4-dienoyl-CoA reductase, mitochondrial
Synonyms
  1. 2,4-dienoyl-CoA reductase [NADPH]
  2. 4-enoyl-CoA reductase [NADPH]
Gene Name DECR1
Protein Type Enzyme
Biological Properties
General Function Involved in oxidoreductase activity
Specific Function Auxiliary enzyme of beta-oxidation. It participates in the metabolism of unsaturated fatty enoyl-CoA esters having double bonds in both even- and odd-numbered positions. Catalyzes the NADP-dependent reduction of 2,4-dienoyl-CoA to yield trans-3-enoyl-CoA.
Pathways Not Available
Reactions
Trans-2,3-didehydroacyl-CoA + NADP → trans,trans-2,3,4,5-tetradehydroacyl-CoA + NADPH details
GO Classification
Biological Process
protein homotetramerization
fatty acid beta-oxidation
Cellular Component
mitochondrial matrix
nucleus
Function
binding
catalytic activity
oxidoreductase activity
Molecular Function
2,4-dienoyl-CoA reductase (NADPH) activity
oxidoreductase activity, acting on NADH or NADPH
NADPH binding
Process
metabolic process
oxidation reduction
Cellular Location
  1. Mitochondrion
Gene Properties
Chromosome Location 8
Locus 8q21.3
SNPs DECR1
Gene Sequence
>1008 bp
ATGAAGCTACCGGCCAGGGTTTTCTTTACTCTGGGGTCCCGGCTGCCCTGTGGCCTCGCT
CCTCGGAGGTTTTTCAGTTATGGGACAAAAATATTATATCAAAACACTGAAGCTTTGCAA
TCTAAATTCTTTTCACCTCTTCAAAAAGCGATGCTACCACCTAATAGTTTTCAAGGAAAA
GTGGCATTCATTACTGGGGGAGGTACTGGCCTTGGTAAAGGAATGACAACTCTTCTGTCC
AGCCTAGGTGCTCAGTGCGTGATAGCCAGCCGGAAGATGGATGTTTTGAAAGCTACCGCA
GAACAAATTTCTTCTCAAACTGGAAATAAGGTTCATGCAATTCAGTGTGATGTGAGGGAT
CCTGATATGGTTCAAAACACTGTGTCAGAACTGATCAAAGTTGCAGGACATCCTAATATT
GTGATAAACAATGCAGCAGGGAATTTTATTTCTCCTACTGAAAGACTTTCTCCTAATGCT
TGGAAAACCATAACTGACATAGTTCTAAATGGCACAGCCTTCGTGACACTAGAAATTGGA
AAACAACTAATTAAAGCACAGAAAGGAGCAGCATTTCTTTCTATTACTACTATCTATGCT
GAGACTGGTTCAGGTTTTGTAGTACCAAGTGCTTCTGCCAAAGCAGGTGTGGAAGCCATG
AGCAAGTCTCTTGCAGCTGAATGGGGTAAATATGGAATGCGATTCAATGTGATTCAACCA
GGGCCTATAAAAACCAAAGGTGCCTTTAGCCGTCTGGACCCAACTGGAACATTTGAGAAA
GAAATGATTGGCAGAATTCCCTGTGGTCGCCTGGGGACTGTAGAAGAACTCGCAAATCTT
GCTGCTTTCCTTTGTAGTGATTATGCTTCTTGGATTAATGGAGCAGTCATTAAATTTGAC
GGTGGAGAGGAAGTACTTATTTCAGGGGAATTCAACGACCTGAGAAAGGTCACCAAGGAG
CAGTGGGACACCATAGAAGAACTCATCAGGAAGACAAAAGGTTCCTAA
Protein Properties
Number of Residues 335
Molecular Weight 36067.4
Theoretical pI 9.274
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>2,4-dienoyl-CoA reductase, mitochondrial
MKLPARVFFTLGSRLPCGLAPRRFFSYGTKILYQNTEALQSKFFSPLQKAMLPPNSFQGK
VAFITGGGTGLGKGMTTLLSSLGAQCVIASRKMDVLKATAEQISSQTGNKVHAIQCDVRD
PDMVQNTVSELIKVAGHPNIVINNAAGNFISPTERLSPNAWKTITDIVLNGTAFVTLEIG
KQLIKAQKGAAFLSITTIYAETGSGFVVPSASAKAGVEAMSKSLAAEWGKYGMRFNVIQP
GPIKTKGAFSRLDPTGTFEKEMIGRIPCGRLGTVEELANLAAFLCSDYASWINGAVIKFD
GGEEVLISGEFNDLRKVTKEQWDTIEELIRKTKGS
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID Q16698
UniProtKB/Swiss-Prot Entry Name DECR_HUMAN
PDB IDs
GenBank Gene ID L26050
GeneCard ID DECR1
GenAtlas ID DECR1
HGNC ID HGNC:2753
References
General References
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  2. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. doi: 10.1126/science.1175371. Epub 2009 Jul 16. [PubMed:19608861 ]
  3. Nusbaum C, Mikkelsen TS, Zody MC, Asakawa S, Taudien S, Garber M, Kodira CD, Schueler MG, Shimizu A, Whittaker CA, Chang JL, Cuomo CA, Dewar K, FitzGerald MG, Yang X, Allen NR, Anderson S, Asakawa T, Blechschmidt K, Bloom T, Borowsky ML, Butler J, Cook A, Corum B, DeArellano K, DeCaprio D, Dooley KT, Dorris L 3rd, Engels R, Glockner G, Hafez N, Hagopian DS, Hall JL, Ishikawa SK, Jaffe DB, Kamat A, Kudoh J, Lehmann R, Lokitsang T, Macdonald P, Major JE, Matthews CD, Mauceli E, Menzel U, Mihalev AH, Minoshima S, Murayama Y, Naylor JW, Nicol R, Nguyen C, O'Leary SB, O'Neill K, Parker SC, Polley A, Raymond CK, Reichwald K, Rodriguez J, Sasaki T, Schilhabel M, Siddiqui R, Smith CL, Sneddon TP, Talamas JA, Tenzin P, Topham K, Venkataraman V, Wen G, Yamazaki S, Young SK, Zeng Q, Zimmer AR, Rosenthal A, Birren BW, Platzer M, Shimizu N, Lander ES: DNA sequence and analysis of human chromosome 8. Nature. 2006 Jan 19;439(7074):331-5. [PubMed:16421571 ]
  4. Koivuranta KT, Hakkola EH, Hiltunen JK: Isolation and characterization of cDNA for human 120 kDa mitochondrial 2,4-dienoyl-coenzyme A reductase. Biochem J. 1994 Dec 15;304 ( Pt 3):787-92. [PubMed:7818482 ]
  5. Helander HM, Koivuranta KT, Horelli-Kuitunen N, Palvimo JJ, Palotie A, Hiltunen JK: Molecular cloning and characterization of the human mitochondrial 2,4-dienoyl-CoA reductase gene (DECR). Genomics. 1997 Nov 15;46(1):112-9. [PubMed:9403065 ]
  6. Alphey MS, Yu W, Byres E, Li D, Hunter WN: Structure and reactivity of human mitochondrial 2,4-dienoyl-CoA reductase: enzyme-ligand interactions in a distinctive short-chain reductase active site. J Biol Chem. 2005 Jan 28;280(4):3068-77. Epub 2004 Nov 6. [PubMed:15531764 ]