acyl-CoA dehydrogenase [Mycobacterium tuberculosis]
Protein Classification
acyl-CoA dehydrogenase family protein( domain architecture ID 11449302)
acyl-CoA dehydrogenase family protein similar to Mycobacterium tuberculosis acyl-CoA dehydrogenase FadE6
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||||
| ACAD_fadE6_17_26 | cd01152 | Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
367-726 | 1.79e-165 | ||||||
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA dehydrogenases (ACAD). Mitochondrial acyl-CoA dehydrogenases (ACAD) catalyze the alpha, beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. The ACD family includes the eukaryotic beta-oxidation, as well as amino acid catabolism enzymes. These enzymes share high sequence similarity, but differ in their substrate specificities. The mitochondrial ACD's are generally homotetramers and have an active site glutamate at a conserved position. : Pssm-ID: 173841 [Multi-domain] Cd Length: 380 Bit Score: 481.46 E-value: 1.79e-165
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| CaiA | COG1960 | Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
1-336 | 1.70e-39 | ||||||
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and metabolism]; Acyl-CoA dehydrogenase related to the alkylation response protein AidB is part of the Pathway/BioSystem: Fatty acid biosynthesis : Pssm-ID: 441563 [Multi-domain] Cd Length: 381 Bit Score: 149.99 E-value: 1.70e-39
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| Name | Accession | Description | Interval | E-value | ||||||
| ACAD_fadE6_17_26 | cd01152 | Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
367-726 | 1.79e-165 | ||||||
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA dehydrogenases (ACAD). Mitochondrial acyl-CoA dehydrogenases (ACAD) catalyze the alpha, beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. The ACD family includes the eukaryotic beta-oxidation, as well as amino acid catabolism enzymes. These enzymes share high sequence similarity, but differ in their substrate specificities. The mitochondrial ACD's are generally homotetramers and have an active site glutamate at a conserved position. Pssm-ID: 173841 [Multi-domain] Cd Length: 380 Bit Score: 481.46 E-value: 1.79e-165
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| CaiA | COG1960 | Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
362-729 | 1.49e-73 | ||||||
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and metabolism]; Acyl-CoA dehydrogenase related to the alkylation response protein AidB is part of the Pathway/BioSystem: Fatty acid biosynthesis Pssm-ID: 441563 [Multi-domain] Cd Length: 381 Bit Score: 243.21 E-value: 1.49e-73
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| pimC_large | TIGR03204 | pimeloyl-CoA dehydrogenase, large subunit; Members of this protein family are the PimC ... |
399-727 | 3.76e-56 | ||||||
pimeloyl-CoA dehydrogenase, large subunit; Members of this protein family are the PimC proteins of species such as Rhodopseudomonas palustris and Bradyrhizobium japonicum. The pimFABCDE operon encodes proteins for the metabolism of straight chain dicarboxylates of seven to fourteen carbons. Especially relevant is pimeloyl-CoA, basis of the gene symbol, as it is a catabolite of benzoyl-CoA degradation, which occurs in Rhodopseudomonas palustris. Pssm-ID: 132248 [Multi-domain] Cd Length: 395 Bit Score: 197.17 E-value: 3.76e-56
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| CaiA | COG1960 | Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
1-336 | 1.70e-39 | ||||||
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and metabolism]; Acyl-CoA dehydrogenase related to the alkylation response protein AidB is part of the Pathway/BioSystem: Fatty acid biosynthesis Pssm-ID: 441563 [Multi-domain] Cd Length: 381 Bit Score: 149.99 E-value: 1.70e-39
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| PRK12341 | PRK12341 | acyl-CoA dehydrogenase; |
444-725 | 2.39e-22 | ||||||
acyl-CoA dehydrogenase; Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 99.80 E-value: 2.39e-22
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| ACAD | cd00567 | Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
7-335 | 4.64e-21 | ||||||
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal acyl-CoA oxidases (AXO) catalyze the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. In contrast, AXO catalyzes a different oxidative half-reaction, in which the reduced FAD is reoxidized by molecular oxygen. The ACAD family includes the eukaryotic beta-oxidation enzymes, short (SCAD), medium (MCAD), long (LCAD) and very-long (VLCAD) chain acyl-CoA dehydrogenases. These enzymes all share high sequence similarity, but differ in their substrate specificities. The ACAD family also includes amino acid catabolism enzymes such as Isovaleryl-CoA dehydrogenase (IVD), short/branched chain acyl-CoA dehydrogenases(SBCAD), Isobutyryl-CoA dehydrogenase (IBDH), glutaryl-CoA deydrogenase (GCD) and Crotonobetainyl-CoA dehydrogenase. The mitochondrial ACAD's are generally homotetramers, except for VLCAD, which is a homodimer. Related enzymes include the SOS adaptive reponse proten aidB, Naphthocyclinone hydroxylase (NcnH), and and Dibenzothiophene (DBT) desulfurization enzyme C (DszC) Pssm-ID: 173838 [Multi-domain] Cd Length: 327 Bit Score: 95.04 E-value: 4.64e-21
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| Acyl-CoA_dh_1 | pfam00441 | Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
217-335 | 5.93e-20 | ||||||
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an all-alpha, four helical up-and-down bundle. Pssm-ID: 395354 [Multi-domain] Cd Length: 149 Bit Score: 86.92 E-value: 5.93e-20
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| Acyl-CoA_dh_M | pfam02770 | Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
469-551 | 1.79e-18 | ||||||
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a beta-barrel fold. Pssm-ID: 460685 [Multi-domain] Cd Length: 95 Bit Score: 80.79 E-value: 1.79e-18
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| PRK12341 | PRK12341 | acyl-CoA dehydrogenase; |
1-323 | 5.46e-12 | ||||||
acyl-CoA dehydrogenase; Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 68.22 E-value: 5.46e-12
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| Name | Accession | Description | Interval | E-value | ||||||
| ACAD_fadE6_17_26 | cd01152 | Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
367-726 | 1.79e-165 | ||||||
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA dehydrogenases (ACAD). Mitochondrial acyl-CoA dehydrogenases (ACAD) catalyze the alpha, beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. The ACD family includes the eukaryotic beta-oxidation, as well as amino acid catabolism enzymes. These enzymes share high sequence similarity, but differ in their substrate specificities. The mitochondrial ACD's are generally homotetramers and have an active site glutamate at a conserved position. Pssm-ID: 173841 [Multi-domain] Cd Length: 380 Bit Score: 481.46 E-value: 1.79e-165
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| CaiA | COG1960 | Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
362-729 | 1.49e-73 | ||||||
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and metabolism]; Acyl-CoA dehydrogenase related to the alkylation response protein AidB is part of the Pathway/BioSystem: Fatty acid biosynthesis Pssm-ID: 441563 [Multi-domain] Cd Length: 381 Bit Score: 243.21 E-value: 1.49e-73
|
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| pimC_large | TIGR03204 | pimeloyl-CoA dehydrogenase, large subunit; Members of this protein family are the PimC ... |
399-727 | 3.76e-56 | ||||||
pimeloyl-CoA dehydrogenase, large subunit; Members of this protein family are the PimC proteins of species such as Rhodopseudomonas palustris and Bradyrhizobium japonicum. The pimFABCDE operon encodes proteins for the metabolism of straight chain dicarboxylates of seven to fourteen carbons. Especially relevant is pimeloyl-CoA, basis of the gene symbol, as it is a catabolite of benzoyl-CoA degradation, which occurs in Rhodopseudomonas palustris. Pssm-ID: 132248 [Multi-domain] Cd Length: 395 Bit Score: 197.17 E-value: 3.76e-56
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| ACAD | cd00567 | Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
445-722 | 9.36e-46 | ||||||
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal acyl-CoA oxidases (AXO) catalyze the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. In contrast, AXO catalyzes a different oxidative half-reaction, in which the reduced FAD is reoxidized by molecular oxygen. The ACAD family includes the eukaryotic beta-oxidation enzymes, short (SCAD), medium (MCAD), long (LCAD) and very-long (VLCAD) chain acyl-CoA dehydrogenases. These enzymes all share high sequence similarity, but differ in their substrate specificities. The ACAD family also includes amino acid catabolism enzymes such as Isovaleryl-CoA dehydrogenase (IVD), short/branched chain acyl-CoA dehydrogenases(SBCAD), Isobutyryl-CoA dehydrogenase (IBDH), glutaryl-CoA deydrogenase (GCD) and Crotonobetainyl-CoA dehydrogenase. The mitochondrial ACAD's are generally homotetramers, except for VLCAD, which is a homodimer. Related enzymes include the SOS adaptive reponse proten aidB, Naphthocyclinone hydroxylase (NcnH), and and Dibenzothiophene (DBT) desulfurization enzyme C (DszC) Pssm-ID: 173838 [Multi-domain] Cd Length: 327 Bit Score: 166.31 E-value: 9.36e-46
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| CaiA | COG1960 | Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
1-336 | 1.70e-39 | ||||||
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and metabolism]; Acyl-CoA dehydrogenase related to the alkylation response protein AidB is part of the Pathway/BioSystem: Fatty acid biosynthesis Pssm-ID: 441563 [Multi-domain] Cd Length: 381 Bit Score: 149.99 E-value: 1.70e-39
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| SCAD_SBCAD | cd01158 | Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
369-726 | 1.85e-36 | ||||||
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA dehydrogenases; Short chain acyl-CoA dehydrogenase (SCAD). SCAD is a mitochondrial beta-oxidation enzyme. It catalyzes the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of SCAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. This subgroup also contains the eukaryotic short/branched chain acyl-CoA dehydrogenase(SBCAD), the bacterial butyryl-CoA dehydorgenase(BCAD) and 2-methylbutyryl-CoA dehydrogenase, which is involved in isoleucine catabolism. These enzymes are homotetramers. Pssm-ID: 173847 [Multi-domain] Cd Length: 373 Bit Score: 141.25 E-value: 1.85e-36
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| LCAD | cd01160 | Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
390-725 | 1.45e-27 | ||||||
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found in the mitochondria of eukaryotes and in some prokaryotes. It catalyzes the alpha, beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of LCAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. LCAD acts as a homodimer. Pssm-ID: 173849 [Multi-domain] Cd Length: 372 Bit Score: 115.29 E-value: 1.45e-27
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| IVD | cd01156 | Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
410-724 | 1.43e-22 | ||||||
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA dehydrogenase, which catalyzes the third step in leucine catabolism, the conversion of isovaleryl-CoA (3-methylbutyryl-CoA) into 3-methylcrotonyl-CoA. IVD is a homotetramer and has the greatest affinity for small branched chain substrates. Pssm-ID: 173845 [Multi-domain] Cd Length: 376 Bit Score: 100.18 E-value: 1.43e-22
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| PRK12341 | PRK12341 | acyl-CoA dehydrogenase; |
444-725 | 2.39e-22 | ||||||
acyl-CoA dehydrogenase; Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 99.80 E-value: 2.39e-22
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| ACAD | cd00567 | Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
7-335 | 4.64e-21 | ||||||
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal acyl-CoA oxidases (AXO) catalyze the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. In contrast, AXO catalyzes a different oxidative half-reaction, in which the reduced FAD is reoxidized by molecular oxygen. The ACAD family includes the eukaryotic beta-oxidation enzymes, short (SCAD), medium (MCAD), long (LCAD) and very-long (VLCAD) chain acyl-CoA dehydrogenases. These enzymes all share high sequence similarity, but differ in their substrate specificities. The ACAD family also includes amino acid catabolism enzymes such as Isovaleryl-CoA dehydrogenase (IVD), short/branched chain acyl-CoA dehydrogenases(SBCAD), Isobutyryl-CoA dehydrogenase (IBDH), glutaryl-CoA deydrogenase (GCD) and Crotonobetainyl-CoA dehydrogenase. The mitochondrial ACAD's are generally homotetramers, except for VLCAD, which is a homodimer. Related enzymes include the SOS adaptive reponse proten aidB, Naphthocyclinone hydroxylase (NcnH), and and Dibenzothiophene (DBT) desulfurization enzyme C (DszC) Pssm-ID: 173838 [Multi-domain] Cd Length: 327 Bit Score: 95.04 E-value: 4.64e-21
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| Acyl-CoA_dh_1 | pfam00441 | Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
217-335 | 5.93e-20 | ||||||
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an all-alpha, four helical up-and-down bundle. Pssm-ID: 395354 [Multi-domain] Cd Length: 149 Bit Score: 86.92 E-value: 5.93e-20
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| SCAD_SBCAD | cd01158 | Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
214-332 | 1.05e-19 | ||||||
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA dehydrogenases; Short chain acyl-CoA dehydrogenase (SCAD). SCAD is a mitochondrial beta-oxidation enzyme. It catalyzes the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of SCAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. This subgroup also contains the eukaryotic short/branched chain acyl-CoA dehydrogenase(SBCAD), the bacterial butyryl-CoA dehydorgenase(BCAD) and 2-methylbutyryl-CoA dehydrogenase, which is involved in isoleucine catabolism. These enzymes are homotetramers. Pssm-ID: 173847 [Multi-domain] Cd Length: 373 Bit Score: 91.56 E-value: 1.05e-19
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| VLCAD | cd01161 | Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
445-595 | 2.84e-19 | ||||||
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is found in the mitochondria of eukaryotes and in some bacteria. It catalyzes the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. VLCAD acts as a homodimer. Pssm-ID: 173850 [Multi-domain] Cd Length: 409 Bit Score: 90.99 E-value: 2.84e-19
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| GCD | cd01151 | Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
401-575 | 9.08e-19 | ||||||
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, which catalyzes the oxidative decarboxylation of glutaryl-CoA to crotonyl-CoA and carbon dioxide in the catabolism of lysine, hydroxylysine, and tryptophan. It uses electron transfer flavoprotein (ETF) as an electron acceptor. GCD is a homotetramer. GCD deficiency leads to a severe neurological disorder in humans. Pssm-ID: 173840 [Multi-domain] Cd Length: 386 Bit Score: 88.95 E-value: 9.08e-19
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| Acyl-CoA_dh_M | pfam02770 | Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
469-551 | 1.79e-18 | ||||||
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a beta-barrel fold. Pssm-ID: 460685 [Multi-domain] Cd Length: 95 Bit Score: 80.79 E-value: 1.79e-18
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| PLN02519 | PLN02519 | isovaleryl-CoA dehydrogenase |
442-590 | 9.42e-18 | ||||||
isovaleryl-CoA dehydrogenase Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 86.08 E-value: 9.42e-18
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| MCAD | cd01157 | Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
441-726 | 1.07e-17 | ||||||
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which catalyze the alpha,beta dehydrogenation of the corresponding medium chain acyl-CoA by FAD, which becomes reduced. The reduced form of MCAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. MCAD is a homotetramer. Pssm-ID: 173846 [Multi-domain] Cd Length: 378 Bit Score: 85.72 E-value: 1.07e-17
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| IBD | cd01162 | Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
437-726 | 5.88e-17 | ||||||
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- dehydrogenation of short branched chain acyl-CoA intermediates in valine catabolism. It is predicted to be a homotetramer. Pssm-ID: 173851 [Multi-domain] Cd Length: 375 Bit Score: 83.26 E-value: 5.88e-17
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| LCAD | cd01160 | Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
7-332 | 2.02e-16 | ||||||
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found in the mitochondria of eukaryotes and in some prokaryotes. It catalyzes the alpha, beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of LCAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. LCAD acts as a homodimer. Pssm-ID: 173849 [Multi-domain] Cd Length: 372 Bit Score: 81.78 E-value: 2.02e-16
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| Acyl-CoA_dh_1 | pfam00441 | Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
575-724 | 1.62e-15 | ||||||
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an all-alpha, four helical up-and-down bundle. Pssm-ID: 395354 [Multi-domain] Cd Length: 149 Bit Score: 74.21 E-value: 1.62e-15
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| PLN02526 | PLN02526 | acyl-coenzyme A oxidase |
365-575 | 6.44e-15 | ||||||
acyl-coenzyme A oxidase Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 77.59 E-value: 6.44e-15
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| PRK03354 | PRK03354 | crotonobetainyl-CoA dehydrogenase; Validated |
449-717 | 2.30e-13 | ||||||
crotonobetainyl-CoA dehydrogenase; Validated Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 72.56 E-value: 2.30e-13
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| ACAD_fadE5 | cd01153 | Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
394-593 | 1.21e-12 | ||||||
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). Mitochondrial acyl-CoA dehydrogenases (ACAD) catalyze the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. The ACD family includes the eukaryotic beta-oxidation, as well as amino acid catabolism enzymes. These enzymes share high sequence similarity, but differ in their substrate specificities. The mitochondrial ACD's are generally homotetramers and have an active site glutamate at a conserved position. Pssm-ID: 173842 [Multi-domain] Cd Length: 407 Bit Score: 70.50 E-value: 1.21e-12
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| PRK12341 | PRK12341 | acyl-CoA dehydrogenase; |
1-323 | 5.46e-12 | ||||||
acyl-CoA dehydrogenase; Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 68.22 E-value: 5.46e-12
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| IVD | cd01156 | Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
213-332 | 1.46e-11 | ||||||
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA dehydrogenase, which catalyzes the third step in leucine catabolism, the conversion of isovaleryl-CoA (3-methylbutyryl-CoA) into 3-methylcrotonyl-CoA. IVD is a homotetramer and has the greatest affinity for small branched chain substrates. Pssm-ID: 173845 [Multi-domain] Cd Length: 376 Bit Score: 66.67 E-value: 1.46e-11
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| ACAD_FadE2 | cd01155 | Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
383-726 | 1.36e-10 | ||||||
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA dehydrogenases (ACAD) catalyze the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. The ACAD family includes the eukaryotic beta-oxidation, as well as amino acid catabolism enzymes. These enzymes share high sequence similarity, but differ in their substrate specificities. ACAD's are generally homotetramers and have an active site glutamate at a conserved position. Pssm-ID: 173844 [Multi-domain] Cd Length: 394 Bit Score: 63.95 E-value: 1.36e-10
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| GCD | cd01151 | Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
126-287 | 1.04e-09 | ||||||
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, which catalyzes the oxidative decarboxylation of glutaryl-CoA to crotonyl-CoA and carbon dioxide in the catabolism of lysine, hydroxylysine, and tryptophan. It uses electron transfer flavoprotein (ETF) as an electron acceptor. GCD is a homotetramer. GCD deficiency leads to a severe neurological disorder in humans. Pssm-ID: 173840 [Multi-domain] Cd Length: 386 Bit Score: 61.22 E-value: 1.04e-09
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| Acyl-CoA_dh_N | pfam02771 | Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
6-81 | 1.45e-09 | ||||||
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is an all-alpha domain. Pssm-ID: 460686 [Multi-domain] Cd Length: 113 Bit Score: 55.93 E-value: 1.45e-09
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| IBD | cd01162 | Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
218-319 | 4.71e-09 | ||||||
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- dehydrogenation of short branched chain acyl-CoA intermediates in valine catabolism. It is predicted to be a homotetramer. Pssm-ID: 173851 [Multi-domain] Cd Length: 375 Bit Score: 58.99 E-value: 4.71e-09
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| PLN02519 | PLN02519 | isovaleryl-CoA dehydrogenase |
211-332 | 9.13e-09 | ||||||
isovaleryl-CoA dehydrogenase Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 58.35 E-value: 9.13e-09
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| PTZ00456 | PTZ00456 | acyl-CoA dehydrogenase; Provisional |
394-534 | 1.50e-08 | ||||||
acyl-CoA dehydrogenase; Provisional Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 57.96 E-value: 1.50e-08
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| PTZ00461 | PTZ00461 | isovaleryl-CoA dehydrogenase; Provisional |
450-592 | 1.88e-08 | ||||||
isovaleryl-CoA dehydrogenase; Provisional Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 57.25 E-value: 1.88e-08
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| PTZ00461 | PTZ00461 | isovaleryl-CoA dehydrogenase; Provisional |
218-335 | 1.42e-07 | ||||||
isovaleryl-CoA dehydrogenase; Provisional Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 54.56 E-value: 1.42e-07
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| fadE | PRK09463 | acyl-CoA dehydrogenase; Reviewed |
213-279 | 2.41e-07 | ||||||
acyl-CoA dehydrogenase; Reviewed Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 54.44 E-value: 2.41e-07
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| PLN02876 | PLN02876 | acyl-CoA dehydrogenase |
445-590 | 3.28e-07 | ||||||
acyl-CoA dehydrogenase Pssm-ID: 215473 [Multi-domain] Cd Length: 822 Bit Score: 54.03 E-value: 3.28e-07
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| VLCAD | cd01161 | Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
218-330 | 1.33e-06 | ||||||
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is found in the mitochondria of eukaryotes and in some bacteria. It catalyzes the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. VLCAD acts as a homodimer. Pssm-ID: 173850 [Multi-domain] Cd Length: 409 Bit Score: 51.31 E-value: 1.33e-06
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| MCAD | cd01157 | Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
218-332 | 2.27e-06 | ||||||
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which catalyze the alpha,beta dehydrogenation of the corresponding medium chain acyl-CoA by FAD, which becomes reduced. The reduced form of MCAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. MCAD is a homotetramer. Pssm-ID: 173846 [Multi-domain] Cd Length: 378 Bit Score: 50.66 E-value: 2.27e-06
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| PRK03354 | PRK03354 | crotonobetainyl-CoA dehydrogenase; Validated |
224-330 | 2.38e-06 | ||||||
crotonobetainyl-CoA dehydrogenase; Validated Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 50.60 E-value: 2.38e-06
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| AidB | cd01154 | Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
222-336 | 3.19e-06 | ||||||
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of several genes involved in the SOS adaptive response to DNA alkylation damage, whose expression is activated by the Ada protein. Its function has not been entirely elucidated; however, it is similar in sequence and function to acyl-CoA dehydrogenases. It has been proposed that aidB directly destroys DNA alkylating agents such as nitrosoguanidines (nitrosated amides) or their reaction intermediates. Pssm-ID: 173843 [Multi-domain] Cd Length: 418 Bit Score: 50.06 E-value: 3.19e-06
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| PRK13026 | PRK13026 | acyl-CoA dehydrogenase; Reviewed |
218-264 | 6.58e-06 | ||||||
acyl-CoA dehydrogenase; Reviewed Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 49.57 E-value: 6.58e-06
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| Acyl-CoA_dh_N | pfam02771 | Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
374-465 | 1.89e-05 | ||||||
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is an all-alpha domain. Pssm-ID: 460686 [Multi-domain] Cd Length: 113 Bit Score: 44.38 E-value: 1.89e-05
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| AidB | cd01154 | Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
442-534 | 1.13e-04 | ||||||
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of several genes involved in the SOS adaptive response to DNA alkylation damage, whose expression is activated by the Ada protein. Its function has not been entirely elucidated; however, it is similar in sequence and function to acyl-CoA dehydrogenases. It has been proposed that aidB directly destroys DNA alkylating agents such as nitrosoguanidines (nitrosated amides) or their reaction intermediates. Pssm-ID: 173843 [Multi-domain] Cd Length: 418 Bit Score: 45.05 E-value: 1.13e-04
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| ACAD_fadE5 | cd01153 | Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
220-332 | 1.14e-04 | ||||||
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). Mitochondrial acyl-CoA dehydrogenases (ACAD) catalyze the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. The ACD family includes the eukaryotic beta-oxidation, as well as amino acid catabolism enzymes. These enzymes share high sequence similarity, but differ in their substrate specificities. The mitochondrial ACD's are generally homotetramers and have an active site glutamate at a conserved position. Pssm-ID: 173842 [Multi-domain] Cd Length: 407 Bit Score: 45.07 E-value: 1.14e-04
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| ACAD_fadE6_17_26 | cd01152 | Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
7-87 | 2.31e-04 | ||||||
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA dehydrogenases (ACAD). Mitochondrial acyl-CoA dehydrogenases (ACAD) catalyze the alpha, beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. The ACD family includes the eukaryotic beta-oxidation, as well as amino acid catabolism enzymes. These enzymes share high sequence similarity, but differ in their substrate specificities. The mitochondrial ACD's are generally homotetramers and have an active site glutamate at a conserved position. Pssm-ID: 173841 [Multi-domain] Cd Length: 380 Bit Score: 44.26 E-value: 2.31e-04
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| PRK13026 | PRK13026 | acyl-CoA dehydrogenase; Reviewed |
448-604 | 4.88e-04 | ||||||
acyl-CoA dehydrogenase; Reviewed Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 43.41 E-value: 4.88e-04
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| NcnH | cd01159 | Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ... |
487-567 | 6.32e-04 | ||||||
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, which is active against Gram-positive bacteria. Polyketides are secondary metabolites, which have important biological functions such as antitumor, immunosupressive or antibiotic activities. NcnH is a hydroxylase involved in the biosynthesis of naphthocyclinone and possibly other polyketides. Pssm-ID: 173848 [Multi-domain] Cd Length: 370 Bit Score: 42.72 E-value: 6.32e-04
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| Acyl-CoA_dh_2 | pfam08028 | Acyl-CoA dehydrogenase, C-terminal domain; |
218-278 | 7.81e-03 | ||||||
Acyl-CoA dehydrogenase, C-terminal domain; Pssm-ID: 429790 [Multi-domain] Cd Length: 133 Bit Score: 37.33 E-value: 7.81e-03
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