LLM (luciferase-like monooxygenase) class flavin-dependent oxidoreductase transfers one oxygen atom of an oxygen molecule to a substrate while reducing the other oxygen atom to water
FMN-dependent oxidoreductase, nitrilotriacetate monooxygenase family; This model represents a ...
9-429
0e+00
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: 665.36 E-value: 0e+00
FMN-dependent oxidoreductase, nitrilotriacetate monooxygenase family; This model represents a ...
9-429
0e+00
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: 665.36 E-value: 0e+00
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: 475.66 E-value: 7.91e-168
Flavin-dependent oxidoreductase, luciferase family (includes alkanesulfonate monooxygenase ...
47-413
1.99e-73
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: 232.52 E-value: 1.99e-73
FMN-dependent oxidoreductase, nitrilotriacetate monooxygenase family; This model represents a ...
9-429
0e+00
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: 665.36 E-value: 0e+00
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: 475.66 E-value: 7.91e-168
Flavin-dependent oxidoreductase, luciferase family (includes alkanesulfonate monooxygenase ...
47-413
1.99e-73
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: 232.52 E-value: 1.99e-73
Alkanesulfonate monoxygenase is the monoxygenase of a two-component system that catalyzes the ...
18-293
6.47e-38
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: 137.79 E-value: 6.47e-38
probable F420-dependent oxidoreductase, Rv2161c family; Coenzyme F420 has a limited ...
40-299
1.59e-16
probable F420-dependent oxidoreductase, Rv2161c family; Coenzyme F420 has a limited phylogenetic distribution, including methanogenic archaea, Mycobacterium tuberculosis and related species, Colwellia psychrerythraea 34H, Rhodopseudomonas palustris HaA2, and others. Partial phylogenetic profiling identifies protein subfamilies, within the larger family called luciferase-like monooxygenanases (pfam00296), that appear only in F420-positive genomes and are likely to be F420-dependent. This model describes a domain found in a distinctive subset of bacterial luciferase homologs, found only in F420-biosynthesizing members of the Actinobacteria. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 274680 [Multi-domain] Cd Length: 246 Bit Score: 78.84 E-value: 1.59e-16
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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(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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