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
Functions
2,4-dienoyl-CoA reductase (NADPH) activity / 4 iron, 4 sulfur cluster binding / FAD binding / FMN binding / metal ion binding / NADPH dehydrogenase activity
Processes
fatty acid beta-oxidation, unsaturated, even number, reductase/isomerase pathway
Components
intracellular
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
ResourceLink
UniProtKB IDP42593
UniProtKB Entry NameFADH_ECOLI
GenBank Protein ID2584857
GenBank Gene IDU93405
General References
  1. 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]
  2. 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]
  3. 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 IDNameDrug groupPharmacological action?ActionsDetails
DB03147Flavin adenine dinucleotideapprovedunknownDetails
DB03247Flavin mononucleotideapproved, investigationalunknownDetails
DB03461Nicotinamide adenine dinucleotide phosphateexperimentalunknownDetails
DB036985-Mercaptoethanol-2-decenoyl-coenzyme AexperimentalunknownDetails