L-lysine epsilon-oxidase from Marinomonas mediterranea and similar proteins; L-lysine ...
4-669
0e+00
L-lysine epsilon-oxidase from Marinomonas mediterranea and similar proteins; L-lysine epsilon-oxidase is responsible for oxidative deamination of L-lysine, producing L-2-aminoadipate-6-semialdehyde. Hydrogen peroxide is a side-product of this enzymatic reaction, which requires the cofactor CTQ (cysteine tryptophylquinone). CTQ most likely forms a Schiff base with the free amino acid substrate. The protein is also called marinocine, for its broad-spectrum antibacterial activity; the latter is most likely caused by hydrogen peroxide synthesis. The dimerization interface observed in the available 3D structure does not seem to be conserved. Homologs of LodA have been detected in various gram-negative bacteria, and they appear to be associated with the formation of biofilms.
:
Pssm-ID: 269832 [Multi-domain] Cd Length: 639 Bit Score: 861.25 E-value: 0e+00
L-lysine epsilon-oxidase from Marinomonas mediterranea and similar proteins; L-lysine ...
4-669
0e+00
L-lysine epsilon-oxidase from Marinomonas mediterranea and similar proteins; L-lysine epsilon-oxidase is responsible for oxidative deamination of L-lysine, producing L-2-aminoadipate-6-semialdehyde. Hydrogen peroxide is a side-product of this enzymatic reaction, which requires the cofactor CTQ (cysteine tryptophylquinone). CTQ most likely forms a Schiff base with the free amino acid substrate. The protein is also called marinocine, for its broad-spectrum antibacterial activity; the latter is most likely caused by hydrogen peroxide synthesis. The dimerization interface observed in the available 3D structure does not seem to be conserved. Homologs of LodA have been detected in various gram-negative bacteria, and they appear to be associated with the formation of biofilms.
Pssm-ID: 269832 [Multi-domain] Cd Length: 639 Bit Score: 861.25 E-value: 0e+00
L-Lysine epsilon oxidase N-terminal; This is the N-terminal domain found in antimicrobial ...
9-312
1.75e-67
L-Lysine epsilon oxidase N-terminal; This is the N-terminal domain found in antimicrobial protein (LodA) with lysine-epsilon oxidase activity (EC 1.4.3.20) which is produced by gram-negative marine bacteria such as Marinomonas mediterranea. The enzyme, previously named marinocine, catalyzes the oxidative deamination of l-lysine into 6-semialdehyde 2-aminoadipic acid, ammonia, and hydrogen peroxide (H2O2). Orthologous proteins have been detected in other bacterial genera, where they participate in biofilm development and dispersal. It has been shown that M. mediterranea LodA and its homologs induce cell death in the microcolonies formed in the process of biofilm development due to the hydrogen peroxide generated by their enzymatic activity. Moreover, cells dispersed from the biofilm by means of this mechanism show a phenotypic variation in growth and biofilm formation. The active form of LodA containing the quinonic cofactor is generated intracellularly only in the presence of LodB, suggesting that the latter protein is involved in this process.
Pssm-ID: 436192 Cd Length: 215 Bit Score: 220.55 E-value: 1.75e-67
L-lysine epsilon-oxidase from Marinomonas mediterranea and similar proteins; L-lysine ...
4-669
0e+00
L-lysine epsilon-oxidase from Marinomonas mediterranea and similar proteins; L-lysine epsilon-oxidase is responsible for oxidative deamination of L-lysine, producing L-2-aminoadipate-6-semialdehyde. Hydrogen peroxide is a side-product of this enzymatic reaction, which requires the cofactor CTQ (cysteine tryptophylquinone). CTQ most likely forms a Schiff base with the free amino acid substrate. The protein is also called marinocine, for its broad-spectrum antibacterial activity; the latter is most likely caused by hydrogen peroxide synthesis. The dimerization interface observed in the available 3D structure does not seem to be conserved. Homologs of LodA have been detected in various gram-negative bacteria, and they appear to be associated with the formation of biofilms.
Pssm-ID: 269832 [Multi-domain] Cd Length: 639 Bit Score: 861.25 E-value: 0e+00
L-lysine epsilon-oxidase from Marinomonas mediterranea and similar proteins; L-lysine ...
6-666
4.37e-99
L-lysine epsilon-oxidase from Marinomonas mediterranea and similar proteins; L-lysine epsilon-oxidase is responsible for oxidative deamination of L-lysine, producing L-2-aminoadipate-6-semialdehyde. Hydrogen peroxide is a side-product of this enzymatic reaction, which requires the cofactor CTQ (cysteine tryptophylquinone). CTQ most likely forms a Schiff base with the free amino acid substrate. The protein is also called marinocine, for its broad-spectrum antibacterial activity; the latter is most likely caused by hydrogen peroxide synthesis. Homologs of LodA have been detected in various gram-negative bacteria, and they appear to be associated with the formation of biofilms.
Pssm-ID: 269830 [Multi-domain] Cd Length: 509 Bit Score: 313.53 E-value: 4.37e-99
Uncharacterized proteins similar to L-lysine epsilon-oxidase from Marinomonas mediterranea; ...
6-668
1.02e-82
Uncharacterized proteins similar to L-lysine epsilon-oxidase from Marinomonas mediterranea; L-lysine epsilon-oxidase is responsible for oxidative deamination of L-lysine, producing L-2-aminoadipate-6-semialdehyde. Hydrogen peroxide is a side-product of this enzymatic reaction, which requires the cofactor CTQ (cysteine tryptophylquinone). CTQ most likely forms a Schiff base with the free amino acid substrate. The protein is known for its broad-spectrum antibacterial activity; the latter is most likely caused by hydrogen peroxide synthesis. Although members of this related family share features of the active site, their functions are not known. Homologs of LodA have been detected in various gram-negative bacteria, and they appear to be associated with the formation of biofilms.
Pssm-ID: 269831 [Multi-domain] Cd Length: 587 Bit Score: 272.95 E-value: 1.02e-82
L-Lysine epsilon oxidase N-terminal; This is the N-terminal domain found in antimicrobial ...
9-312
1.75e-67
L-Lysine epsilon oxidase N-terminal; This is the N-terminal domain found in antimicrobial protein (LodA) with lysine-epsilon oxidase activity (EC 1.4.3.20) which is produced by gram-negative marine bacteria such as Marinomonas mediterranea. The enzyme, previously named marinocine, catalyzes the oxidative deamination of l-lysine into 6-semialdehyde 2-aminoadipic acid, ammonia, and hydrogen peroxide (H2O2). Orthologous proteins have been detected in other bacterial genera, where they participate in biofilm development and dispersal. It has been shown that M. mediterranea LodA and its homologs induce cell death in the microcolonies formed in the process of biofilm development due to the hydrogen peroxide generated by their enzymatic activity. Moreover, cells dispersed from the biofilm by means of this mechanism show a phenotypic variation in growth and biofilm formation. The active form of LodA containing the quinonic cofactor is generated intracellularly only in the presence of LodB, suggesting that the latter protein is involved in this process.
Pssm-ID: 436192 Cd Length: 215 Bit Score: 220.55 E-value: 1.75e-67
L-lysine epsilon oxidase C-terminal domain; This is the C-terminal domain of L-Lysine ...
427-573
1.48e-39
L-lysine epsilon oxidase C-terminal domain; This is the C-terminal domain of L-Lysine epsilon-oxidase (LodA, EC 1.4.3.20), an enzyme which catalyzes the oxidative deamination of free L-lysine into L-2-aminoadipate 6-semialdehyde, ammonia and hydrogen peroxide.
Pssm-ID: 436486 [Multi-domain] Cd Length: 144 Bit Score: 142.22 E-value: 1.48e-39
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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