2,4-dienoyl-CoA reductase [NADPH]
Details
- Name
- 2,4-dienoyl-CoA reductase [NADPH]
- Synonyms
- 1.3.1.34
- 2,4-dienoyl coenzyme A reductase
- ygjL
- Gene Name
- fadH
- Organism
- Escherichia coli (strain K12)
- Amino acid sequence
>lcl|BSEQ0011413|2,4-dienoyl-CoA reductase [NADPH] MSYPSLFAPLDLGFTTLKNRVLMGSMHTGLEEYPDGAERLAAFYAERARHGVALIVSGGI APDLTGVGMEGGAMLNDASQIPHHRTITEAVHQEGGKIALQILHTGRYSYQPHLVAPSAL QAPINRFVPHELSHEEILQLIDNFARCAQLAREAGYDGVEVMGSEGYLINEFLTLRTNQR SDQWGGDYRNRMRFAVEVVRAVRERVGNDFIIIYRLSMLDLVEDGGTFAETVELAQAIEA AGATIINTGIGWHEARIPTIATPVPRGAFSWVTRKLKGHVSLPLVTTNRINDPQVADDIL SRGDADMVSMARPFLADAELLSKAQSGRADEINTCIGCNQACLDQIFVGKVTSCLVNPRA CHETKMPILPAVQKKNLAVVGAGPAGLAFAINAAARGHQVTLFDAHSEIGGQFNIAKQIP GKEEFYETLRYYRRMIEVTGVTLKLNHTVTADQLQAFDETILASGIVPRTPPIDGIDHPK VLSYLDVLRDKAPVGNKVAIIGCGGIGFDTAMYLSQPGESTSQNIAGFCNEWGIDSSLQQ AGGLSPQGMQIPRSPRQIVMLQRKASKPGQGLGKTTGWIHRTTLLSRGVKMIPGVSYQKI DDDGLHVVINGETQVLAVDNVVICAGQEPNRALAQPLIDSGKTVHLIGGCDVAMELDARR AIAQGTRLALEI
- Number of residues
- 672
- Molecular Weight
- 72677.545
- Theoretical pI
- 6.55
- GO Classification
- Functions2,4-dienoyl-CoA reductase (NADPH) activity / 4 iron, 4 sulfur cluster binding / FAD binding / FMN binding / metal ion binding / NADPH dehydrogenase activityProcessesfatty acid beta-oxidation, unsaturated, even number, reductase/isomerase pathwayComponentsintracellular
- General Function
- Nadph dehydrogenase activity
- Specific Function
- Catalyzes the NADP-dependent reduction of 2,4-dienoyl-CoA to yield trans-2- enoyl-CoA.
- Pfam Domain Function
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0011414|2,4-dienoyl-CoA reductase [NADPH] (fadH) ATGAGCTACCCGTCGCTGTTCGCCCCGCTGGATTTAGGTTTTACCACGTTAAAAAACCGC GTGTTGATGGGCTCAATGCACACCGGGCTGGAGGAATACCCGGACGGTGCCGAGCGGCTG GCAGCGTTTTATGCCGAACGCGCCCGTCACGGCGTGGCGCTGATTGTCAGCGGCGGCATT GCACCAGATTTAACAGGCGTTGGCATGGAAGGTGGCGCAATGCTCAACGACGCCAGCCAG ATCCCACACCATCGCACCATTACCGAAGCGGTACATCAGGAAGGCGGCAAAATAGCCCTG CAAATTTTGCATACCGGGCGCTACAGCTACCAACCGCATCTGGTCGCCCCGTCCGCATTG CAGGCCCCCATCAACCGTTTCGTGCCCCATGAGTTAAGCCATGAAGAGATCCTGCAACTG ATCGACAATTTCGCCCGCTGCGCGCAACTGGCGCGGGAGGCAGGATACGACGGTGTAGAG GTGATGGGTTCCGAAGGGTATTTGATCAACGAATTTCTGACGCTGCGCACCAATCAGCGT AGTGACCAGTGGGGCGGCGATTACCGCAACCGGATGCGATTTGCCGTAGAAGTAGTGCGT GCGGTGCGCGAACGCGTCGGCAACGACTTCATTATTATCTACCGACTGTCGATGCTCGAC CTGGTCGAAGACGGCGGGACTTTTGCCGAAACGGTAGAGCTGGCGCAGGCCATTGAAGCG GCGGGCGCGACCATTATCAACACCGGCATTGGCTGGCATGAAGCACGTATTCCGACCATT GCCACGCCCGTGCCGCGCGGCGCATTTAGCTGGGTCACGCGCAAACTGAAAGGCCACGTC TCGCTGCCGCTGGTAACCACCAACCGGATTAACGATCCGCAGGTTGCCGACGATATTCTC TCGCGCGGCGATGCCGATATGGTATCGATGGCGCGACCGTTTCTTGCTGATGCGGAGCTG CTGTCAAAAGCGCAATCGGGACGAGCCGATGAGATCAACACTTGTATTGGCTGCAATCAG GCCTGTCTCGATCAAATCTTCGTTGGCAAAGTCACCTCGTGCCTGGTGAATCCTCGCGCC TGCCACGAAACCAAAATGCCAATCCTTCCCGCCGTGCAGAAAAAAAATCTGGCGGTGGTC GGTGCGGGACCTGCTGGGCTGGCGTTTGCCATTAACGCGGCGGCGCGTGGGCATCAGGTA ACATTGTTTGACGCTCATAGCGAGATTGGCGGGCAGTTTAATATCGCCAAACAGATCCCC GGCAAAGAGGAGTTTTACGAAACGCTGCGCTATTACCGCCGGATGATCGAAGTGACGGGC GTGACGCTAAAACTCAATCACACCGTGACGGCGGATCAGTTACAGGCTTTCGATGAAACG ATCCTCGCCAGTGGGATCGTGCCGCGCACTCCGCCCATCGACGGGATCGATCATCCGAAG GTATTGAGTTATCTCGATGTACTGCGCGACAAAGCGCCGGTTGGCAACAAAGTTGCCATC ATCGGTTGTGGCGGGATTGGTTTTGATACGGCGATGTATTTAAGTCAGCCGGGCGAATCC ACCAGCCAGAATATCGCCGGGTTCTGTAATGAATGGGGGATCGACAGTAGCCTACAACAG GCTGGTGGCTTAAGCCCGCAGGGAATGCAGATCCCCCGTAGCCCACGGCAGATTGTGATG CTCCAGCGCAAAGCCAGCAAACCAGGACAGGGGTTAGGCAAAACCACCGGCTGGATCCAT CGCACCACCCTGCTCTCGCGGGGTGTGAAAATGATCCCAGGCGTAAGTTATCAGAAGATT GACGATGACGGGCTGCATGTGGTGATCAACGGCGAAACGCAGGTATTAGCAGTGGACAAT GTGGTGATCTGCGCAGGGCAAGAGCCAAACCGCGCGCTGGCGCAACCGCTGATTGATAGC GGGAAAACGGTGCATTTAATTGGCGGCTGCGATGTGGCTATGGAGCTGGACGCACGACGG GCAATTGCCCAGGGAACACGGCTGGCGCTGGAGATTTAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P42593 UniProtKB Entry Name FADH_ECOLI GenBank Protein ID 2584857 GenBank Gene ID U93405 - General References
- He XY, Yang SY, Schulz H: Cloning and expression of the fadH gene and characterization of the gene product 2,4-dienoyl coenzyme A reductase from Escherichia coli. Eur J Biochem. 1997 Sep 1;248(2):516-20. [Article]
- Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
- Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
Drug Relations
- Drug Relations
DrugBank ID Name Drug group Pharmacological action? Actions Details DB03147 Flavin adenine dinucleotide approved unknown Details DB03247 Flavin mononucleotide approved, investigational unknown Details DB03461 Nicotinamide adenine dinucleotide phosphate experimental unknown Details DB03698 5-Mercaptoethanol-2-decenoyl-coenzyme A experimental unknown Details