| Identification |
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| Name: | Fatty acid oxidation complex subunit alpha |
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| Synonyms: | - Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase
- 3-hydroxyacyl-CoA dehydrogenase
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| Gene Name: | fadB |
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| Enzyme Class: | |
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| Biological Properties |
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| General Function: | Involved in 3-hydroxyacyl-CoA dehydrogenase activity |
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| 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. Involved in the aerobic and anaerobic degradation of long-chain fatty acids |
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| Cellular Location: | Not Available |
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| SMPDB Pathways: | |
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| KEGG Pathways: | - 1,4-Dichlorobenzene degradation ec00627
- Benzoate degradation via hydroxylation ec00362
- Biosynthesis of unsaturated fatty acids ec01040
- Butanoate metabolism ec00650
- Caprolactam degradation ec00930
- Fatty acid elongation in mitochondria ec00062
- Fatty acid metabolism ec00071
- Geraniol degradation ec00281
- Limonene and pinene degradation ec00903
- Lysine degradation ec00310
- Metabolic pathways eco01100
- Microbial metabolism in diverse environments ec01120
- Phenylalanine metabolism ec00360
- Propanoate metabolism ec00640
- Reductive carboxylate cycle (CO2 fixation) ec00720
- Tryptophan metabolism ec00380
- Valine, leucine and isoleucine degradation ec00280
- alpha-Linolenic acid metabolism ec00592
- beta-Alanine metabolism ec00410
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| Transports: | |
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| Transport References: | - Orth, J. D., Conrad, T. M., Na, J., Lerman, J. A., Nam, H., Feist, A. M., Palsson, B. O. (2011). "A comprehensive genome-scale reconstruction of Escherichia coli metabolism--2011." Mol Syst Biol 7:535. Pubmed: 21988831
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| KEGG Reactions: | | | | | | | | | | | | | | | | | | | | | | | | | | | | | | | |
1.0 | ↔ | 1.0 |
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1.0(S)-3-Hydroxyisobutyrate | + | 1.0 | ↔ | 1.0 | + | 1.0 | + | 1.0 |
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1.0(6Z,9Z,12Z,15Z,18Z,21Z)-3-Hydroxytetracosahexa-6,9,12,15,18,21-enoyl-CoA | ↔ | 1.0(2E,6Z,9Z,12Z,15Z,18Z,21Z)-Tetracosahepta-2,6,9,12,15,18,21-enoyl-CoA | + | 1.0 |
| 1.0(6Z,9Z,12Z,15Z,18Z,21Z)-3-Hydroxytetracosahexa-6,9,12,15,18,21-enoyl-CoA ↔ 1.0(2E,6Z,9Z,12Z,15Z,18Z,21Z)-Tetracosahepta-2,6,9,12,15,18,21-enoyl-CoA + 1.0 WaterReactionCard | |
1.0(6Z,9Z,12Z,15Z,18Z)-3-Hydroxytetracosapenta-6,9,12,15,18-enoyl-CoA | ↔ | 1.0(2E,6Z,9Z,12Z,15Z,18Z)-Tetracosahexa-2,6,9,12,15,18-enoyl-CoA | + | 1.0 |
| 1.0(6Z,9Z,12Z,15Z,18Z)-3-Hydroxytetracosapenta-6,9,12,15,18-enoyl-CoA ↔ 1.0(2E,6Z,9Z,12Z,15Z,18Z)-Tetracosahexa-2,6,9,12,15,18-enoyl-CoA + 1.0 WaterReactionCard | | | | | |
1.0(3S)-3-Hydroxyacyl-CoA | ↔ | 1.0 | + | 1.0trans-3-Enoyl-CoA | + | 1.0 |
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1.0(3S)-3-Hydroxyacyl-CoA | + | 1.0 | ↔ | 1.0 | + | 1.0 | + | 1.0 |
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| Complex Reactions: | | | | | | | | | | | |
1.0 | ↔ | 1.0 |
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1.0(S)-3-hydroxyacyl-CoA | + | 1.0 | → | 1.03-oxoacyl-CoA | + | 1.0 |
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1.0(3S)-3-hydroxyacyl-CoA | → | 1.0trans-2(or 3)-enoyl-CoA | + | 1.0 |
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1.0 | → | 1.0(R)-3-hydroxybutanoyl-CoA |
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| Metabolites: | |
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| GO Classification: | | Component |
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| fatty acid beta-oxidation multienzyme complex | | macromolecular complex | | protein complex | | Function |
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| 3-hydroxyacyl-CoA dehydrogenase activity | | 3-hydroxybutyryl-CoA epimerase activity | | binding | | carbon-oxygen lyase activity | | catalytic activity | | coenzyme binding | | cofactor binding | | dodecenoyl-CoA delta-isomerase activity | | enoyl-CoA hydratase activity | | hydro-lyase activity | | intramolecular oxidoreductase activity | | intramolecular oxidoreductase activity, transposing C=C bonds | | isomerase activity | | lyase activity | | 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 |
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| carboxylic acid metabolic process | | cellular metabolic process | | fatty acid catabolic process | | fatty acid metabolic process | | lipid catabolic process | | lipid metabolic process | | metabolic process | | monocarboxylic acid metabolic process | | organic acid metabolic process | | oxidation reduction | | oxoacid metabolic process | | primary metabolic process |
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| Gene Properties |
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| Blattner: | b3846 |
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| Gene Orientation | Counterclockwise |
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| Centisome Percentage: | 86.79 |
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| Left Sequence End | 4026805 |
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| Right Sequence End | 4028994 |
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| Gene Sequence: | >2190 bp
ATGCTTTACAAAGGCGACACCCTGTACCTTGACTGGCTGGAAGATGGCATTGCCGAACTG
GTATTTGATGCCCCAGGTTCAGTTAATAAACTCGACACTGCGACCGTCGCCAGCCTCGGC
GAGGCCATCGGCGTGCTGGAACAGCAATCAGATCTAAAAGGGCTGCTGCTGCGTTCGAAC
AAAGCAGCCTTTATCGTCGGTGCTGATATCACCGAATTTTTGTCCCTGTTCCTCGTTCCT
GAAGAACAGTTAAGTCAGTGGCTGCACTTTGCCAATAGCGTGTTTAATCGCCTGGAAGAT
CTGCCGGTGCCGACCATTGCTGCCGTCAATGGCTATGCGCTGGGCGGTGGCTGCGAATGC
GTGCTGGCGACCGATTATCGTCTGGCGACGCCGGATCTGCGCATCGGTCTGCCGGAAACC
AAACTGGGCATCATGCCTGGCTTTGGCGGTTCTGTACGTATGCCACGTATGCTGGGCGCT
GACAGTGCGCTGGAAATCATTGCCGCCGGTAAAGATGTCGGCGCGGATCAGGCGCTGAAA
ATCGGTCTGGTGGATGGCGTAGTCAAAGCAGAAAAACTGGTTGAAGGCGCAAAGGCGGTT
TTACGCCAGGCCATTAACGGCGACCTCGACTGGAAAGCAAAACGTCAGCCGAAGCTGGAA
CCACTAAAACTGAGCAAGATTGAAGCCACCATGAGCTTCACCATCGCTAAAGGGATGGTC
GCACAAACAGCGGGGAAACATTATCCGGCCCCCATCACCGCAGTAAAAACCATTGAAGCT
GCGGCCCGTTTTGGTCGTGAAGAAGCCTTAAACCTGGAAAACAAAAGTTTTGTCCCGCTG
GCGCATACCAACGAAGCCCGCGCACTGGTCGGCATTTTCCTTAACGATCAATATGTAAAA
GGCAAAGCGAAGAAACTCACCAAAGACGTTGAAACCCCGAAACAGGCCGCGGTGCTGGGT
GCAGGCATTATGGGCGGCGGCATCGCTTACCAGTCTGCGTGGAAAGGCGTGCCGGTTGTC
ATGAAAGATATCAACGACAAGTCGTTAACCCTCGGCATGACCGAAGCCGCGAAACTGCTG
AACAAGCAGCTTGAGCGCGGCAAGATCGATGGTCTGAAACTGGCTGGCGTGATCTCCACA
ATCCACCCAACGCTCGACTACGCCGGATTTGACCGCGTGGATATTGTGGTAGAAGCGGTT
GTTGAAAACCCGAAAGTGAAAAAAGCCGTACTGGCAGAAACCGAACAAAAAGTACGCCAG
GATACCGTGCTGGCGTCTAACACTTCAACCATTCCTATCAGCGAACTGGCCAACGCGCTG
GAACGCCCGGAAAACTTCTGCGGGATGCACTTCTTTAACCCGGTCCACCGAATGCCGTTG
GTAGAAATTATTCGCGGCGAGAAAAGCTCCGACGAAACCATCGCGAAAGTTGTCGCCTGG
GCGAGCAAGATGGGCAAGACGCCGATTGTGGTTAACGACTGCCCCGGCTTCTTTGTTAAC
CGCGTGCTGTTCCCGTATTTCGCCGGTTTCAGCCAGCTGCTGCGCGACGGCGCGGATTTC
CGCAAGATCGACAAAGTGATGGAAAAACAGTTTGGCTGGCCGATGGGCCCGGCATATCTG
CTGGACGTTGTGGGCATTGATACCGCGCATCACGCTCAGGCTGTCATGGCAGCAGGCTTC
CCGCAGCGGATGCAGAAAGATTACCGCGATGCCATCGACGCGCTGTTTGATGCCAACCGC
TTTGGTCAGAAGAACGGCCTCGGTTTCTGGCGTTATAAAGAAGACAGCAAAGGTAAGCCG
AAGAAAGAAGAAGACGCCGCCGTTGAAGACCTGCTGGCAGAAGTGAGCCAGCCGAAGCGC
GATTTCAGCGAAGAAGAGATTATCGCCCGCATGATGATCCCGATGGTCAACGAAGTGGTG
CGCTGTCTGGAGGAAGGCATTATCGCCACTCCGGCGGAAGCGGATATGGCGCTGGTCTAC
GGCCTGGGCTTCCCTCCGTTCCACGGCGGCGCGTTCCGCTGGCTGGACACCCTCGGTAGC
GCAAAATACCTCGATATGGCACAGCAATATCAGCACCTCGGCCCGCTGTATGAAGTGCCG
GAAGGTCTGCGTAATAAAGCGCGTCATAACGAACCGTACTATCCTCCGGTTGAGCCAGCC
CGTCCGGTTGGCGACCTGAAAACGGCTTAA |
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| Protein Properties |
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| Pfam Domain Function: | |
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| Protein Residues: | 729 |
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| Protein Molecular Weight: | 79593 |
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| Protein Theoretical pI: | 6 |
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| Signaling Regions: | |
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| Transmembrane Regions: | |
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| Protein Sequence: | >Fatty acid oxidation complex subunit alpha
MLYKGDTLYLDWLEDGIAELVFDAPGSVNKLDTATVASLGEAIGVLEQQSDLKGLLLRSN
KAAFIVGADITEFLSLFLVPEEQLSQWLHFANSVFNRLEDLPVPTIAAVNGYALGGGCEC
VLATDYRLATPDLRIGLPETKLGIMPGFGGSVRMPRMLGADSALEIIAAGKDVGADQALK
IGLVDGVVKAEKLVEGAKAVLRQAINGDLDWKAKRQPKLEPLKLSKIEATMSFTIAKGMV
AQTAGKHYPAPITAVKTIEAAARFGREEALNLENKSFVPLAHTNEARALVGIFLNDQYVK
GKAKKLTKDVETPKQAAVLGAGIMGGGIAYQSAWKGVPVVMKDINDKSLTLGMTEAAKLL
NKQLERGKIDGLKLAGVISTIHPTLDYAGFDRVDIVVEAVVENPKVKKAVLAETEQKVRQ
DTVLASNTSTIPISELANALERPENFCGMHFFNPVHRMPLVEIIRGEKSSDETIAKVVAW
ASKMGKTPIVVNDCPGFFVNRVLFPYFAGFSQLLRDGADFRKIDKVMEKQFGWPMGPAYL
LDVVGIDTAHHAQAVMAAGFPQRMQKDYRDAIDALFDANRFGQKNGLGFWRYKEDSKGKP
KKEEDAAVEDLLAEVSQPKRDFSEEEIIARMMIPMVNEVVRCLEEGIIATPAEADMALVY
GLGFPPFHGGAFRWLDTLGSAKYLDMAQQYQHLGPLYEVPEGLRNKARHNEPYYPPVEPA
RPVGDLKTA |
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| References |
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| External Links: | |
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| 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
- Daniels, D. L., Plunkett, G. 3rd, Burland, V., Blattner, F. R. (1992). "Analysis of the Escherichia coli genome: DNA sequence of the region from 84.5 to 86.5 minutes." Science 257:771-778. Pubmed: 1379743
- DiRusso, C. C. (1990). "Primary sequence of the Escherichia coli fadBA operon, encoding the fatty acid-oxidizing multienzyme complex, indicates a high degree of homology to eucaryotic enzymes." J Bacteriol 172:6459-6468. Pubmed: 1699931
- 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
- Nakahigashi, K., Inokuchi, H. (1990). "Nucleotide sequence of the fadA and fadB genes from Escherichia coli." Nucleic Acids Res 18:4937. Pubmed: 2204034
- Yang, X. Y., Schulz, H., Elzinga, M., Yang, S. Y. (1991). "Nucleotide sequence of the promoter and fadB gene of the fadBA operon and primary structure of the multifunctional fatty acid oxidation protein from Escherichia coli." Biochemistry 30:6788-6795. Pubmed: 1712230
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