Acyl-coenzyme A dehydrogenase (Q47146)

Identification
Name:Acyl-coenzyme A dehydrogenase
Synonyms:
  • ACDH
Gene Name:fadE
Enzyme Class:Not Available
Biological Properties
General Function:Involved in acyl-CoA dehydrogenase activity
Specific Function:Catalyzes the dehydrogenation of acyl-CoA
Cellular Location:Not Available
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0FAD + 1.0Octanoyl-CoA ↔ 1.0FADH2 + 1.0(2E)-Octenoyl-CoA
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0FAD + 1.0Palmityl-CoA ↔ 1.0FADH2 + 1.0(2E)-Hexadecenoyl-CoA
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0FAD + 1.0Tetradecanoyl-CoA ↔ 1.0FADH2 + 1.0(2E)-Tetradecenoyl-CoA
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0FAD + 1.0Hexanoyl-CoA ↔ 1.0FADH2 + 1.0trans-2-Hexenoyl-CoA
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Lauroyl-CoA + 1.0FAD ↔ 1.0(2E)-Dodecenoyl-CoA + 1.0FADH2
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Decanoyl-CoA (N-C10:0CoA) + 1.0FAD ↔ 1.0(2E)-Decenoyl-CoA + 1.0FADH2
ReactionCard
1.0Butanoyl-CoA+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Butanoyl-CoA + 1.0FAD ↔ 1.0FADH2 + 1.0Crotonoyl-CoA
ReactionCard
EcoCyc Reactions:
1.0a 2,3,4-saturated fatty acyl CoA+1.0ETF-Oxidized → 1.0a trans-2-enoyl-CoA+1.0ETF-Reduced
1.0a 2,3,4-saturated fatty acyl CoA + 1.0ETF-Oxidized → 1.0a trans-2-enoyl-CoA + 1.0ETF-Reduced
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Butyryl-CoA + 1.0FAD ↔ 1.0Crotonoyl-CoA + 1.0FADH2
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0FAD + 1.0Stearoyl-CoA ↔ 1.0FADH2 + 1.0Trans-Octadec-2-enoyl-CoA
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB03948(2E)-Decenoyl-CoAMetaboCard
ECMDB03712(2E)-Dodecenoyl-CoAMetaboCard
ECMDB03945(2E)-Hexadecenoyl-CoAMetaboCard
ECMDB03949(2E)-Octenoyl-CoAMetaboCard
ECMDB03946(2E)-Tetradecenoyl-CoAMetaboCard
ECMDB01088Butyryl-CoAMetaboCard
ECMDB02009Crotonoyl-CoAMetaboCard
ECMDB06404Decanoyl-CoA (N-C10:0CoA)MetaboCard
ECMDB01248FADMetaboCard
ECMDB01197FADH2MetaboCard
ECMDB02845Hexanoyl-CoAMetaboCard
ECMDB03571Lauroyl-CoAMetaboCard
ECMDB01070Octanoyl-CoAMetaboCard
ECMDB01338Palmityl-CoAMetaboCard
ECMDB21284Stearoyl-CoAMetaboCard
ECMDB01521Tetradecanoyl-CoAMetaboCard
ECMDB03944trans-2-Hexenoyl-CoAMetaboCard
ECMDB21363Trans-Octadec-2-enoyl-CoAMetaboCard
GO Classification:
Function
acyl-CoA dehydrogenase activity
adenyl nucleotide binding
binding
catalytic activity
FAD or FADH2 binding
nucleoside binding
oxidoreductase activity
oxidoreductase activity, acting on the CH-CH group of donors
purine nucleoside binding
Process
carboxylic acid metabolic process
cellular metabolic process
fatty acid beta-oxidation
fatty acid beta-oxidation using acyl-CoA dehydrogenase
fatty acid catabolic process
fatty acid metabolic process
metabolic process
monocarboxylic acid metabolic process
organic acid metabolic process
oxidation reduction
oxoacid metabolic process
Gene Properties
Blattner:b0221
Gene OrientationCounterclockwise
Centisome Percentage:5.19
Left Sequence End240859
Right Sequence End243303
Gene Sequence:
>2445 bp
ATGATGATTTTGAGTATTCTCGCTACGGTTGTCCTGCTCGGCGCGTTGTTCTATCACCGC
GTGAGCTTATTTATCAGCAGTCTGATTTTGCTCGCCTGGACAGCCGCCCTCGGCGTTGCT
GGTCTGTGGTCGGCGTGGGTACTGGTGCCTCTGGCCATTATCCTCGTGCCATTTAACTTT
GCGCCTATGCGTAAGTCGATGATTTCCGCGCCGGTATTTCGCGGTTTCCGTAAGGTGATG
CCGCCGATGTCGCGCACTGAGAAAGAAGCGATTGATGCGGGCACCACCTGGTGGGAGGGC
GACTTGTTCCAGGGCAAGCCGGACTGGAAAAAGCTGCATAACTATCCGCAGCCGCGCCTG
ACCGCCGAAGAGCAAGCGTTTCTCGACGGCCCGGTAGAAGAAGCCTGCCGGATGGCGAAT
GATTTCCAGATCACCCATGAGCTGGCGGATCTGCCGCCGGAGTTGTGGGCGTACCTTAAA
GAGCATCGTTTCTTCGCGATGATCATCAAAAAAGAGTACGGCGGGCTGGAGTTCTCGGCT
TATGCCCAGTCTCGCGTGCTGCAAAAACTCTCCGGCGTGAGCGGGATCCTGGCGATTACC
GTCGGCGTGCCAAACTCATTAGGCCCGGGCGAACTGTTGCAACATTACGGCACTGACGAG
CAGAAAGATCACTATCTGCCGCGTCTGGCGCGTGGTCAGGAGATCCCCTGCTTTGCACTG
ACCAGCCCGGAAGCGGGTTCCGATGCGGGCGCGATTCCGGACACCGGGATTGTCTGCATG
GGCGAATGGCAGGGCCAGCAGGTGCTGGGGATGCGTCTGACCTGGAACAAACGCTACATT
ACGCTGGCACCGATTGCGACCGTGCTTGGGCTGGCGTTTAAACTCTCCGACCCGGAAAAA
TTACTCGGCGGTGCAGAAGATTTAGGCATTACCTGTGCGCTGATCCCAACCACCACGCCG
GGCGTGGAAATTGGTCGTCGCCACTTCCCGCTGAACGTACCGTTCCAGAACGGACCGACG
CGCGGTAAAGATGTCTTCGTGCCGATCGATTACATCATCGGCGGGCCGAAAATGGCCGGG
CAAGGCTGGCGGATGCTGGTGGAGTGCCTCTCGGTAGGCCGCGGCATCACCCTGCCTTCC
AACTCAACCGGCGGCGTGAAATCGGTAGCGCTGGCAACCGGCGCGTATGCTCACATTCGC
CGTCAGTTCAAAATCTCTATTGGTAAGATGGAAGGGATTGAAGAGCCGCTGGCGCGTATT
GCCGGTAATGCCTACGTGATGGATGCTGCGGCATCGCTGATTACCTACGGCATTATGCTC
GGCGAAAAACCTGCCGTGCTGTCGGCTATCGTTAAGTATCACTGTACCCACCGCGGGCAG
CAGTCGATTATTGATGCGATGGATATTACCGGCGGTAAAGGCATTATGCTCGGGCAAAGC
AACTTCCTGGCGCGTGCTTACCAGGGCGCACCGATTGCCATCACCGTTGAAGGGGCTAAC
ATTCTGACCCGCAGCATGATGATCTTCGGACAAGGAGCGATTCGTTGCCATCCGTACGTG
CTGGAAGAGATGGAAGCGGCGAAGAACAATGACGTCAACGCGTTCGATAAACTGTTGTTC
AAACATATCGGTCACGTCGGTAGCAACAAAGTTCGCAGCTTCTGGCTGGGCCTGACGCGC
GGTTTAACCAGCAGCACGCCAACCGGCGATGCCACTAAACGCTACTATCAGCACCTGAAC
CGCCTGAGCGCCAACCTCGCCCTGCTTTCTGATGTCTCGATGGCAGTGCTGGGCGGCAGC
CTGAAACGTCGCGAGCGCATCTCGGCCCGTCTGGGGGATATTTTAAGCCAGCTCTACCTC
GCCTCTGCCGTGCTGAAGCGTTATGACGACGAAGGCCGTAATGAAGCCGACCTGCCGCTG
GTGCACTGGGGCGTACAAGATGCGCTGTATCAGGCTGAACAGGCGATGGATGATTTACTG
CAAAACTTCCCGAACCGCGTGGTTGCCGGGCTGCTGAATGTGGTGATCTTCCCGACCGGA
CGTCATTATCTGGCACCTTCTGACAAGCTGGATCATAAAGTGGCGAAGATTTTACAAGTG
CCGAACGCCACCCGTTCCCGCATTGGTCGCGGTCAGTACCTGACGCCGAGCGAGCATAAT
CCGGTTGGCTTGCTGGAAGAGGCGCTGGTGGATGTGATTGCCGCCGACCCAATTCATCAG
CGGATCTGTAAAGAGCTGGGTAAAAACCTGCCGTTTACCCGTCTGGATGAACTGGCGCAC
AACGCGCTGGTGAAGGGGCTGATTGATAAAGATGAAGCCGCTATTCTGGTGAAAGCTGAA
GAAAGCCGTCTGCGCAGTATTAACGTTGATGACTTTGATCCGGAAGAGCTGGCGACGAAG
CCGGTAAAGTTGCCGGAGAAAGTGCGGAAAGTTGAAGCCGCGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:814
Protein Molecular Weight:89224
Protein Theoretical pI:8
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Acyl-coenzyme A dehydrogenase
MMILSILATVVLLGALFYHRVSLFISSLILLAWTAALGVAGLWSAWVLVPLAIILVPFNF
APMRKSMISAPVFRGFRKVMPPMSRTEKEAIDAGTTWWEGDLFQGKPDWKKLHNYPQPRL
TAEEQAFLDGPVEEACRMANDFQITHELADLPPELWAYLKEHRFFAMIIKKEYGGLEFSA
YAQSRVLQKLSGVSGILAITVGVPNSLGPGELLQHYGTDEQKDHYLPRLARGQEIPCFAL
TSPEAGSDAGAIPDTGIVCMGEWQGQQVLGMRLTWNKRYITLAPIATVLGLAFKLSDPEK
LLGGAEDLGITCALIPTTTPGVEIGRRHFPLNVPFQNGPTRGKDVFVPIDYIIGGPKMAG
QGWRMLVECLSVGRGITLPSNSTGGVKSVALATGAYAHIRRQFKISIGKMEGIEEPLARI
AGNAYVMDAAASLITYGIMLGEKPAVLSAIVKYHCTHRGQQSIIDAMDITGGKGIMLGQS
NFLARAYQGAPIAITVEGANILTRSMMIFGQGAIRCHPYVLEEMEAAKNNDVNAFDKLLF
KHIGHVGSNKVRSFWLGLTRGLTSSTPTGDATKRYYQHLNRLSANLALLSDVSMAVLGGS
LKRRERISARLGDILSQLYLASAVLKRYDDEGRNEADLPLVHWGVQDALYQAEQAMDDLL
QNFPNRVVAGLLNVVIFPTGRHYLAPSDKLDHKVAKILQVPNATRSRIGRGQYLTPSEHN
PVGLLEEALVDVIAADPIHQRICKELGKNLPFTRLDELAHNALVKGLIDKDEAAILVKAE
ESRLRSINVDDFDPEELATKPVKLPEKVRKVEAA
References
External Links:
ResourceLink
Uniprot ID:Q47146
Uniprot Name:FADE_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674387
Ecogene ID:EG13145
Ecocyc:EG13145
ColiBase:b0221
Kegg Gene:b0221
EchoBASE ID:EB2939
CCDB:FADE_ECOLI
BacMap:90111100
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
  • Campbell, J. W., Cronan, J. E. Jr (2002). "The enigmatic Escherichia coli fadE gene is yafH." J Bacteriol 184:3759-3764. Pubmed: 12057976
  • 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