Identification
Name:Fatty acid oxidation complex subunit alpha_
Synonyms:
  • Enoyl-CoA hydratase/3-hydroxybutyryl-CoA epimerase
  • 3-hydroxyacyl-CoA dehydrogenase
Gene Name:fadJ
Enzyme Class:
Biological Properties
General Function:Involved in 3-hydroxyacyl-CoA dehydrogenase activity
Specific Function:Catalyzes the formation of an hydroxyacyl-CoA by addition of water on enoyl-CoA. Also exhibits 3-hydroxyacyl-CoA epimerase and 3-hydroxyacyl-CoA dehydrogenase activities. Strongly involved in the anaerobic degradation of long and medium-chain fatty acids in the presence of nitrate and weakly involved in the aerobic degradation of long-chain fatty acids
Cellular Location:Cytoplasm
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
ThumbThumb+Thumb
ThumbThumb+Thumb
Thumb+Thumb+ThumbThumb+Thumb
ThumbThumb+Thumb
Thumb+Thumb+ThumbThumb+Thumb
ThumbThumb+Thumb
ThumbThumb+Thumb
Thumb+Thumb+ThumbThumb+Thumb
ThumbThumb+Thumb
Thumb+Thumb+ThumbThumb+Thumb
Thumb+Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb
Thumb+ThumbThumb+Thumb+Thumb
Thumb+ThumbThumb+Thumb+Thumb
ThumbThumb+Thumb
ThumbThumb
ThumbThumb+Thumb
ThumbThumb+Thumb
Thumb+ThumbThumb
Thumb+ThumbThumb+Thumb+Thumb
ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb+Thumb
ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb+Thumb
ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb+Thumb
ThumbThumb+Thumb
(S)-3-Hydroxyisobutyrate+ThumbThumb+Thumb+Thumb
Thumb+ThumbThumb+Thumb+Thumb
Thumb+ThumbThumb
(6Z,9Z,12Z,15Z,18Z)-3-Hydroxytetracosapenta-6,9,12,15,18-enoyl-CoA(2E,6Z,9Z,12Z,15Z,18Z)-Tetracosahexa-2,6,9,12,15,18-enoyl-CoA+Thumb
(6Z,9Z,12Z,15Z,18Z)-3-Hydroxytetracosapenta-6,9,12,15,18-enoyl-CoA ↔ (2E,6Z,9Z,12Z,15Z,18Z)-Tetracosahexa-2,6,9,12,15,18-enoyl-CoA + Water
ReactionCard
Thumb+ThumbThumb
Thumb+ThumbThumb+Thumb+Thumb
(3S)-3-Hydroxyacyl-CoAThumb+trans-3-Enoyl-CoA+Thumb
(3S)-3-Hydroxyacyl-CoA ↔ trans-2,3-Dehydroacyl-CoA + trans-3-Enoyl-CoA + Water
ReactionCard
(3S)-3-Hydroxyacyl-CoA+ThumbThumb+Thumb+Thumb
(3S)-3-Hydroxyacyl-CoA + NAD3-Oxoacyl-CoA + NADH + Hydrogen ion
ReactionCard
SMPDB Reactions:
a cis-3-enoyl-CoA a trans-2-enoyl-CoA 
a cis-3-enoyl-CoA  → a trans-2-enoyl-CoA 
ReactionCard
3-Hydroxybutyryl-CoA+ThumbThumb
ThumbThumb
ThumbThumb
ThumbThumb
ThumbThumb
(S)-Hydroxyoctanoyl-CoA+ThumbThumb
ThumbThumb
Thumbtrans-Octadec-2-enoyl-CoA+Thumb
Complex Reactions:
ThumbThumb+Thumb
Thumb+Thumb+ThumbThumb+Thumb
Thumb+Thumb+ThumbThumb+Thumb
ThumbThumb+Thumb
Thumb+Thumb+ThumbThumb+Thumb
(3S)-3-hydroxyacyl-CoAtrans-2(or 3)-enoyl-CoA+Thumb
(3S)-3-hydroxyacyl-CoA → trans-2(or 3)-enoyl-CoA + Water
ReactionCard
(S)-3-hydroxyacyl-CoA+Thumb3-oxoacyl-CoA+Thumb
(S)-3-hydroxyacyl-CoA + NAD → 3-oxoacyl-CoA + NADH
ReactionCard
Thumb(R)-3-hydroxybutanoyl-CoA
3-Hydroxybutyryl-CoA → (R)-3-hydroxybutanoyl-CoA
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB20008(2E)-5-Methylhexa-2,4-dienoyl-CoAMetaboCard
ECMDB03948(2E)-Decenoyl-CoAMetaboCard
ECMDB03712(2E)-Dodecenoyl-CoAMetaboCard
ECMDB03945(2E)-Hexadecenoyl-CoAMetaboCard
ECMDB03949(2E)-Octenoyl-CoAMetaboCard
ECMDB03946(2E)-Tetradecenoyl-CoAMetaboCard
ECMDB20010(3S)-3-Hydroxyadipyl-CoAMetaboCard
ECMDB23150(3Z)-Dodec-3-enoyl-CoAMetaboCard
ECMDB21642(S)-3-Hydroxybutanoyl-CoAMetaboCard
ECMDB03936(S)-3-Hydroxydodecanoyl-CoAMetaboCard
ECMDB03932(S)-3-Hydroxyhexadecanoyl-CoAMetaboCard
ECMDB01052(S)-3-Hydroxyisobutyryl-CoAMetaboCard
ECMDB21101(S)-3-Hydroxyoctadecanoyl-CoAMetaboCard
ECMDB03934(S)-3-Hydroxytetradecanoyl-CoAMetaboCard
ECMDB03938(S)-Hydroxydecanoyl-CoAMetaboCard
ECMDB03942(S)-Hydroxyhexanoyl-CoAMetaboCard
ECMDB03940(S)-Hydroxyoctanoyl-CoAMetaboCard
ECMDB02217(S)-Methylmalonic acid semialdehydeMetaboCard
ECMDB011572-Methylacetoacetyl-CoAMetaboCard
ECMDB200713-Hydroxy-5-methylhex-4-enoyl-CoAMetaboCard
ECMDB011663-Hydroxybutyryl-CoAMetaboCard
ECMDB068703-Hydroxyisovaleryl-CoAMetaboCard
ECMDB014933-Methylcrotonyl-CoAMetaboCard
ECMDB200773-Oxoadipyl-CoAMetaboCard
ECMDB039393-Oxodecanoyl-CoAMetaboCard
ECMDB039373-Oxododecanoyl-CoAMetaboCard
ECMDB064023-Oxohexadecanoyl-CoAMetaboCard
ECMDB039433-Oxohexanoyl-CoAMetaboCard
ECMDB211703-Oxooctadecanoyl-CoAMetaboCard
ECMDB039413-Oxooctanoyl-CoAMetaboCard
ECMDB039353-Oxotetradecanoyl-CoAMetaboCard
ECMDB201015-Carboxy-2-pentenoyl-CoAMetaboCard
ECMDB201045-Methyl-3-oxo-4-hexenoyl-CoAMetaboCard
ECMDB01484Acetoacetyl-CoAMetaboCard
ECMDB02307Acrylyl-CoAMetaboCard
ECMDB02009Crotonoyl-CoAMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB01011Methacrylyl-CoAMetaboCard
ECMDB00902NADMetaboCard
ECMDB01487NADHMetaboCard
ECMDB02054Tiglyl-CoAMetaboCard
ECMDB03944trans-2-Hexenoyl-CoAMetaboCard
ECMDB21363Trans-Octadec-2-enoyl-CoAMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Component
fatty acid beta-oxidation multienzyme complex
macromolecular complex
protein complex
Function
3-hydroxyacyl-CoA dehydrogenase activity
3-hydroxybutyryl-CoA epimerase activity
binding
carbon-oxygen lyase activity
catalytic activity
coenzyme binding
cofactor binding
enoyl-CoA hydratase activity
hydro-lyase activity
isomerase activity
lyase activity
NAD or NADH binding
nucleotide binding
oxidoreductase activity
oxidoreductase activity, acting on CH-OH group of donors
oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
racemase and epimerase activity
racemase and epimerase activity, acting on hydroxy acids and derivatives
Process
carboxylic acid metabolic process
cellular metabolic process
fatty acid beta-oxidation
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:b2341
Gene OrientationCounterclockwise
Centisome Percentage:52.91
Left Sequence End2455037
Right Sequence End2457181
Gene Sequence:
>2145 bp
GTGTCCCGTATTATTATGCTGATCCCTACCGGAACCAGCGTCGGTCTGACCAGCGTCAGC
CTTGGCGTGATCCGTGCAATGGAACGCAAAGGCGTTCGTCTGAGCGTTTTCAAACCTATC
GCTCAGCCGCGTACCGGTGGCGATGCGCCCGATCAGACTACGACTATCGTGCGTGCGAAC
TCTTCCACCACGACGGCCGCTGAACCGCTGAAAATGAGCTACGTTGAAGGTCTGCTTTCC
AGCAATCAGAAAGATGTGCTGATGGAAGAGATCGTCGCAAACTACCACGCTAACACCAAA
GACGCTGAAGTCGTTCTGGTTGAAGGTCTGGTCCCGACACGTAAGCACCAGTTTGCCCAG
TCTCTGAACTACGAAATCGCTAAAACGCTGAATGCGGAAATCGTCTTCGTTATGTCTCAG
GGCACTGACACCCCGGAACAGCTGAAAGAGCGTATCGAACTGACCCGCAACAGCTTCGGC
GGTGCCAAAAACACCAACATCACCGGCGTTATCGTTAACAAACTGAACGCACCGGTTGAT
GAACAGGGTCGTACTCGCCCGGATCTGTCCGAGATTTTCGACGACTCTTCCAAAGCTAAA
GTAAACAATGTTGATCCGGCGAAGCTGCAAGAATCCAGCCCGCTGCCGGTTCTCGGCGCT
GTGCCGTGGAGCTTTGACCTGATCGCGACTCGTGCGATCGATATGGCTCGCCACCTGAAT
GCGACCATCATCAACGAAGGCGACATCAATACTCGCCGCGTTAAATCCGTCACTTTCTGC
GCACGCAGCATTCCGCACATGCTGGAGCACTTCCGTGCCGGTTCTCTGCTGGTGACTTCC
GCAGACCGTCCTGACGTGCTGGTGGCCGCTTGCCTGGCAGCCATGAACGGCGTAGAAATC
GGTGCCCTGCTGCTGACTGGCGGTTACGAAATGGACGCGCGCATTTCTAAACTGTGCGAA
CGTGCTTTCGCTACCGGCCTGCCGGTATTTATGGTGAACACCAACACCTGGCAGACCTCT
CTGAGCCTGCAGAGCTTCAACCTGGAAGTTCCGGTTGACGATCACGAACGTATCGAGAAA
GTTCAGGAATACGTTGCTAACTACATCAACGCTGACTGGATCGAATCTCTGACTGCCACT
TCTGAGCGCAGCCGTCGTCTGTCTCCGCCTGCGTTCCGTTATCAGCTGACTGAACTTGCG
CGCAAAGCGGGCAAACGTATCGTACTGCCGGAAGGTGACGAACCGCGTACCGTTAAAGCA
GCCGCTATCTGTGCTGAACGTGGTATCGCAACTTGCGTACTGCTGGGTAATCCGGCAGAG
ATCAACCGTGTTGCAGCGTCTCAGGGTGTAGAACTGGGTGCAGGGATTGAAATCGTTGAT
CCAGAAGTGGTTCGCGAAAGCTATGTTGGTCGTCTGGTCGAACTGCGTAAGAACAAAGGC
ATGACCGAAACCGTTGCCCGCGAACAGCTGGAAGACAACGTGGTGCTCGGTACGCTGATG
CTGGAACAGGATGAAGTTGATGGTCTGGTTTCCGGTGCTGTTCACACTACCGCAAACACC
ATCCGTCCGCCGCTGCAGCTGATCAAAACTGCACCGGGCAGCTCCCTGGTATCTTCCGTG
TTCTTCATGCTGCTGCCGGAACAGGTTTACGTTTACGGTGACTGTGCGATCAACCCGGAT
CCGACCGCTGAACAGCTGGCAGAAATCGCGATTCAGTCCGCTGATTCCGCTGCGGCCTTC
GGTATCGAACCGCGCGTTGCTATGCTCTCCTACTCCACCGGTACTTCTGGTGCAGGTAGC
GACGTAGAAAAAGTTCGCGAAGCAACTCGTCTGGCGCAGGAAAAACGTCCTGACCTGATG
ATCGACGGTCCGCTGCAGTACGACGCTGCGGTAATGGCTGACGTTGCGAAATCCAAAGCG
CCGAACTCTCCGGTTGCAGGTCGCGCTACCGTGTTCATCTTCCCGGATCTGAACACCGGT
AACACCACCTACAAAGCGGTACAGCGTTCTGCCGACCTGATCTCCATCGGGCCGATGCTG
CAGGGTATGCGCAAGCCGGTTAACGACCTGTCCCGTGGCGCACTGGTTGACGATATCGTC
TACACCATCGCGCTGACTGCGATTCAGTCTGCACAGCAGCAGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:714
Protein Molecular Weight:77072
Protein Theoretical pI:9
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Fatty acid oxidation complex subunit alpha
MEMTSAFTLNVRLDNIAVITIDVPGEKMNTLKAEFASQVRAIIKQLRENKELRGVVFVSA
KPDNFIAGADINMIGNCKTAQEAEALARQGQQLMAEIHALPIQVIAAIHGACLGGGLELA
LACHGRVCTDDPKTVLGLPEVQLGLLPGSGGTQRLPRLIGVSTALEMILTGKQLRAKQAL
KLGLVDDVVPHSILLEAAVELAKKERPSSRPLPVRERILAGPLGRALLFKMVGKKTEHKT
QGNYPATERILEVVETGLAQGTSSGYDAEARAFGELAMTPQSQALRSIFFASTDVKKDPG
SDAPPAPLNSVGILGGGLMGGGIAYVTACKAGIPVRIKDINPQGINHALKYSWDQLEGKV
RRRHLKASERDKQLALISGTTDYRGFAHRDLIIEAVFENLELKQQMVAEVEQNCAAHTIF
ASNTSSLPIGDIAAHATRPEQVIGLHFFSPVEKMPLVEIIPHAGTSAQTIATTVKLAKKQ
GKTPIVVRDKAGFYVNRILAPYINEAIRMLTQGERVEHIDAALVKFGFPVGPIQLLDEVG
IDTGTKIIPVLEAAYGERFSAPANVVSSILNDDRKGRKNGRGFYLYGQKGRKSKKQVDPA
IYPLIGTQGQGRISAPQVAERCVMLMLNEAVRCVDEQVIRSVRDGDIGAVFGIGFPPFLG
GPFRYIDSLGAGEVVAIMQRLATQYGSRFTPCERLVEMGARGESFWKTTATDLQ
References
External Links:
ResourceLink
Uniprot ID:P77399
Uniprot Name:FADJ_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85675350
Ecogene ID:EG14127
Ecocyc:EG14127
ColiBase:b2341
Kegg Gene:b2341
EchoBASE ID:EB3879
CCDB:FADJ_ECOLI
BacMap:16130274
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., Morgan-Kiss, R. M., Cronan, J. E. Jr (2003). "A new Escherichia coli metabolic competency: growth on fatty acids by a novel anaerobic beta-oxidation pathway." Mol Microbiol 47:793-805. Pubmed: 12535077
  • 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
  • Snell, K. D., Feng, F., Zhong, L., Martin, D., Madison, L. L. (2002). "YfcX enables medium-chain-length poly(3-hydroxyalkanoate) formation from fatty acids in recombinant Escherichia coli fadB strains." J Bacteriol 184:5696-5705. Pubmed: 12270828
  • Yamamoto, Y., Aiba, H., Baba, T., Hayashi, K., Inada, T., Isono, K., Itoh, T., Kimura, S., Kitagawa, M., Makino, K., Miki, T., Mitsuhashi, N., Mizobuchi, K., Mori, H., Nakade, S., Nakamura, Y., Nashimoto, H., Oshima, T., Oyama, S., Saito, N., Sampei, G., Satoh, Y., Sivasundaram, S., Tagami, H., Horiuchi, T., et, a. l. .. (1997). "Construction of a contiguous 874-kb sequence of the Escherichia coli -K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features." DNA Res 4:91-113. Pubmed: 9205837