2,4-dienoyl-CoA reductase [NADPH] (P42593)

Identification
Name:2,4-dienoyl-CoA reductase [NADPH]
Synonyms:
  • 2,4-dienoyl coenzyme A reductase
Gene Name:fadH
Enzyme Class:
Biological Properties
General Function:Involved in catalytic activity
Specific Function:Catalyzes the NADP-dependent reduction of 2,4-dienoyl- CoA to yield trans-2- enoyl-CoA
Cellular Location:Not Available
SMPDB Pathways:
  • Collection of Reactions without pathways PW001891
KEGG Pathways:Not Available
KEGG Reactions:
1.0Thumb+1.0Thumb ↔ 1.0trans,trans-2,3,4,5-Tetradehydroacyl-CoA+1.0Thumb+1.0Thumb
1.0trans-2,3-Dehydroacyl-CoA + 1.0NADP ↔ 1.0trans,trans-2,3,4,5-Tetradehydroacyl-CoA + 1.0NADPH + 1.0Hydrogen ion
ReactionCard
SMPDB Reactions:
1.0trans-Delta2, cis-delta4-decadienoyl-CoA+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0trans-Delta2, cis-delta4-decadienoyl-CoA + 1.0NADPH + 1.0Hydrogen ion → 1.0(2E)-Decenoyl-CoA + 1.0NADP
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0(2E)-Decenoyl-CoA + 1.0NADP ↔ 1.0Hydrogen ion + 1.0trans-Delta2, cis-delta4-decadienoyl-CoA + 1.0NADPH
ReactionCard
Complex Reactions:
1.0Trans-2,3-didehydroacyl-CoA+1.0Thumb → 1.0trans,trans-2,3,4,5-tetradehydroacyl-CoA+1.0Thumb
1.0Trans-2,3-didehydroacyl-CoA + 1.0NADP → 1.0trans,trans-2,3,4,5-tetradehydroacyl-CoA + 1.0NADPH
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB03948(2E)-Decenoyl-CoAMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB00217NADPMetaboCard
ECMDB04111NADPHMetaboCard
ECMDB20611trans-Delta2, cis-delta4-decadienoyl-CoAMetaboCard
GO Classification:
Function
binding
catalytic activity
FMN binding
nucleotide binding
oxidoreductase activity
Process
metabolic process
Gene Properties
Blattner:b3081
Gene OrientationClockwise
Centisome Percentage:69.61
Left Sequence End3229687
Right Sequence End3231705
Gene Sequence:
>2019 bp
ATGGATGCCCTGCAATTATTAACCTGGTCGCTGATTCTCTATCTGTTTGCTAGTCTGGCT
TCGCTGTTTTTACTCGGTCTGGACAGACTGGCTATTAAGCTTTCCGGCATCACATCGCTG
GTGGGCGGCGTGATTGGCATCATCAGCGGAATTACGCAATTACATGCTGGTGTAACTTTA
GTCGCCCGTTTTGCCCCCCCTTTTGAATTTGCCGATTTAACCCTGCGAATGGATAGCCTC
TCGGCATTTATGGTGCTGGTTATCTCCTTGCTGGTGGTGGTTTGTTCTCTCTATTCATTG
ACTTATATGCGCGAATACGAGGGCAAAGGCGCGGCGGCGATGGGCTTCTTTATGAATATT
TTCATCGCATCGATGGTTGCCCTGCTGGTGATGGACAACGCTTTTTGGTTCATCGTGCTG
TTTGAAATGATGTCGCTGTCTTCCTGGTTTCTGGTCATTGCCAGGCAGGATAAAACGTCG
ATCAACGCTGGCATGCTCTACTTTTTTATCGCCCACGCCGGATCGGTGCTGATAATGATC
GCCTTCTTGCTGATGGGGCGCGAAAGCGGCAGCCTCGATTTTGCCAGTTTCCGCACGCTT
TCACTTTCTCCGGGGCTGGCGTCGGCGGTGTTCCTGCTGGCCTTTTTCGGTTTTGGCGCG
AAAGCCGGGATGATGCCGTTGCACAGCTGGTTGCCGCGCGCTCACCCTGCCGCACCATCG
CACGCTTCGGCGTTGATGTCTGGCGTAATGGTCAAAATAGGTATTTTCGGCATCCTGAAA
GTAGCGATGGATCTGCTGGCGCAAACGGGTTTGCCTCTGTGGTGGGGCATTCTGGTGATG
GCGATCGGCGCAATCTCCGCGCTCCTGGGCGTGCTATATGCGCTGGCGGAACAGGATATC
AAACGGCTGCTGGCCTGGAGTACCGTCGAAAACGTCGGCATTATTTTGCTGGCAGTCGGT
GTGGCGATGGTCGGTCTGTCACTGCACGACCCGCTGCTCACCGTGGTTGGACTGCTCGGC
GCACTGTTTCATCTGCTCAACCATGCGCTGTTCAAAGGGCTGCTATTTCTCGGCGCGGGA
GCGATTATTTCGCGTTTGCATACCCACGACATGGAAAAAATGGGGGCACTAGCGAAACGG
ATGCCGTGGACAGCCGCAGCATGCCTGATTGGTTGCCTCGCGATATCAGCCATTCCTCCG
CTGAATGGTTTTATCAGCGAATGGTACACCTGGCAGTCGCTGTTCTCACTAAGTCGTGTG
GAAGCCGTAGCGCTACAACTTGCGGGTCCTATTGCTATGGTAATGCTGGCAGTCACTGGT
GGGCTGGCAGTAATGTGCTTCGTAAAAATGTACGGTATTACTTTCTGTGGTGCGCCGCGC
AGTACACACGCTGAAGAGGCACAGGAAGTGCCAAATACGATGATCGTCGCCATGCTACTG
CTCGCGGCACTCTGCGTATTAATTGCGCTTAGTGCCAGTTGGCTGGCACCGAAGATAATG
CATATTGCCCATGCGTTTACCAATACCCCTCCCGCCACTGTCGCCAGCGGAATAGCACTT
GTACCCGGCACGTTTCATACACAGGTCACCCCCTCATTACTGTTGCTGTTACTACTGGCG
ATGCCTTTGCTGCCTGGCCTTTACTGGCTGTGGTGTCGTTCGCGCCGCGCAGCGTTTCGT
CGCACAGGAGATGCCTGGGCATGCGGCTACGGCTGGGAAAATGCGATGGCCCCGTCAGGC
AATGGCGTGATGCAGCCGCTGCGTGTGGTCTTTTCTGCGCTATTTCGTCTACGACAACAG
CTCGACCCTACGCTGAGGCTAAATAAAGGTCTTGCGCACGTCACCGCCAGGGCTCAGAGC
ACAGAACCCTTCTGGGATGAGCGGGTGATCCGCCCCATCGTGAGCGCCACCCAACGGCTG
GCCAAAGAAATACAGCATCTGCAAAGCGGCGACTTTCGTCTCTATTGCCTGTATGTGGTC
GCCGCACTGGTTGTGCTGCTAATCGCTATTGCCGTCTAA
Protein Properties
Pfam Domain Function:
Protein Residues:672
Protein Molecular Weight:72678
Protein Theoretical pI:7
PDB File:1PS9
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>2,4-dienoyl-CoA reductase [NADPH]
MSYPSLFAPLDLGFTTLKNRVLMGSMHTGLEEYPDGAERLAAFYAERARHGVALIVSGGI
APDLTGVGMEGGAMLNDASQIPHHRTITEAVHQEGGKIALQILHTGRYSYQPHLVAPSAL
QAPINRFVPHELSHEEILQLIDNFARCAQLAREAGYDGVEVMGSEGYLINEFLTLRTNQR
SDQWGGDYRNRMRFAVEVVRAVRERVGNDFIIIYRLSMLDLVEDGGTFAETVELAQAIEA
AGATIINTGIGWHEARIPTIATPVPRGAFSWVTRKLKGHVSLPLVTTNRINDPQVADDIL
SRGDADMVSMARPFLADAELLSKAQSGRADEINTCIGCNQACLDQIFVGKVTSCLVNPRA
CHETKMPILPAVQKKNLAVVGAGPAGLAFAINAAARGHQVTLFDAHSEIGGQFNIAKQIP
GKEEFYETLRYYRRMIEVTGVTLKLNHTVTADQLQAFDETILASGIVPRTPPIDGIDHPK
VLSYLDVLRDKAPVGNKVAIIGCGGIGFDTAMYLSQPGESTSQNIAGFCNEWGIDSSLQQ
AGGLSPQGMQIPRSPRQIVMLQRKASKPGQGLGKTTGWIHRTTLLSRGVKMIPGVSYQKI
DDDGLHVVINGETQVLAVDNVVICAGQEPNRALAQPLIDSGKTVHLIGGCDVAMELDARR
AIAQGTRLALEI
References
External Links:
ResourceLink
Uniprot ID:P42593
Uniprot Name:FADH_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:1799910
PDB ID:1PS9
Ecogene ID:EG12723
Ecocyc:EG12723
ColiBase:b3081
Kegg Gene:b3081
EchoBASE ID:EB2582
CCDB:FADH_ECOLI
BacMap:16130976
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • He, X. Y., Yang, S. Y., Schulz, H. (1997). "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 248:516-520. Pubmed: 9346310