FMN-dependent oxidoreductase, nitrilotriacetate monooxygenase family; This model represents a ...
22-431
8.47e-130
FMN-dependent oxidoreductase, nitrilotriacetate monooxygenase family; This model represents a distinctive clade, in which all characterized members are FMN-binding, within the larger family of luciferase-like monooxygenases (LLM), among which there are both FMN- and F420-binding enzymes. A well-characterized member is nitrilotriacetate monooxygenase from Aminobacter aminovorans (Chelatobacter heintzii), where nitrilotriacetate is a chelating agent used in detergents. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 274819 [Multi-domain] Cd Length: 422 Bit Score: 381.08 E-value: 8.47e-130
nitrilotriacetate monoxygenase oxidizes nitrilotriacetate utilizing reduced flavin mononucleotide (FMNH2) and oxygen. The FMNH2 is provided by an NADH:flavin mononucleotide (FMN) oxidorductase that uses NADH to reduce FMN to FMNH2.
Pssm-ID: 238528 [Multi-domain] Cd Length: 358 Bit Score: 300.78 E-value: 2.55e-99
Flavin-dependent oxidoreductase, luciferase family (includes alkanesulfonate monooxygenase ...
47-413
1.55e-55
Flavin-dependent oxidoreductase, luciferase family (includes alkanesulfonate monooxygenase SsuD and methylene tetrahydromethanopterin reductase) [Coenzyme transport and metabolism, General function prediction only]; Flavin-dependent oxidoreductase, luciferase family (includes alkanesulfonate monooxygenase SsuD and methylene tetrahydromethanopterin reductase) is part of the Pathway/BioSystem: Pyrimidine degradation
Pssm-ID: 441744 [Multi-domain] Cd Length: 301 Bit Score: 185.91 E-value: 1.55e-55
FMN-dependent oxidoreductase, nitrilotriacetate monooxygenase family; This model represents a ...
22-431
8.47e-130
FMN-dependent oxidoreductase, nitrilotriacetate monooxygenase family; This model represents a distinctive clade, in which all characterized members are FMN-binding, within the larger family of luciferase-like monooxygenases (LLM), among which there are both FMN- and F420-binding enzymes. A well-characterized member is nitrilotriacetate monooxygenase from Aminobacter aminovorans (Chelatobacter heintzii), where nitrilotriacetate is a chelating agent used in detergents. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 274819 [Multi-domain] Cd Length: 422 Bit Score: 381.08 E-value: 8.47e-130
nitrilotriacetate monoxygenase oxidizes nitrilotriacetate utilizing reduced flavin mononucleotide (FMNH2) and oxygen. The FMNH2 is provided by an NADH:flavin mononucleotide (FMN) oxidorductase that uses NADH to reduce FMN to FMNH2.
Pssm-ID: 238528 [Multi-domain] Cd Length: 358 Bit Score: 300.78 E-value: 2.55e-99
Flavin-dependent oxidoreductase, luciferase family (includes alkanesulfonate monooxygenase ...
47-413
1.55e-55
Flavin-dependent oxidoreductase, luciferase family (includes alkanesulfonate monooxygenase SsuD and methylene tetrahydromethanopterin reductase) [Coenzyme transport and metabolism, General function prediction only]; Flavin-dependent oxidoreductase, luciferase family (includes alkanesulfonate monooxygenase SsuD and methylene tetrahydromethanopterin reductase) is part of the Pathway/BioSystem: Pyrimidine degradation
Pssm-ID: 441744 [Multi-domain] Cd Length: 301 Bit Score: 185.91 E-value: 1.55e-55
Alkanesulfonate monoxygenase is the monoxygenase of a two-component system that catalyzes the ...
17-284
7.24e-31
Alkanesulfonate monoxygenase is the monoxygenase of a two-component system that catalyzes the conversion of alkanesulfonates to the corresponding aldehyde and sulfite. Alkanesulfonate monoxygenase (SsuD) has an absolute requirement for reduced flavin mononucleotide (FMNH2), which is provided by the NADPH-dependent FMN oxidoreductase (SsuE).
Pssm-ID: 238527 [Multi-domain] Cd Length: 244 Bit Score: 118.92 E-value: 7.24e-31
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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Functional characterization of the conserved domain architecture found on the query.
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if a domain or superfamily has been annotated with functional sites (conserved features),
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The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
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Concise Display shows only the best scoring domain model, in each hit category listed below except non-specific hits, for each region on the query sequence.
(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
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