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
putative FMN-dependent luciferase-like monooxygenase, KPN_01858 family; This protein family ...
4-329
0e+00
putative FMN-dependent luciferase-like monooxygenase, KPN_01858 family; This protein family consists of luciferase-like monooxygenases (LLM), and include KPN_01858 from Klebsiella pneumoniae as a representative member. Most are from species that lack F420 biosynthesis, so the family is likely to bind FMN as its cofactor. This family is closely associated with a binding protein-dependent ABC transporter, suggesting a role in catabolism. [Unknown function, Enzymes of unknown specificity]
:
Pssm-ID: 274928 Cd Length: 326 Bit Score: 530.42 E-value: 0e+00
putative FMN-dependent luciferase-like monooxygenase, KPN_01858 family; This protein family ...
4-329
0e+00
putative FMN-dependent luciferase-like monooxygenase, KPN_01858 family; This protein family consists of luciferase-like monooxygenases (LLM), and include KPN_01858 from Klebsiella pneumoniae as a representative member. Most are from species that lack F420 biosynthesis, so the family is likely to bind FMN as its cofactor. This family is closely associated with a binding protein-dependent ABC transporter, suggesting a role in catabolism. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 274928 Cd Length: 326 Bit Score: 530.42 E-value: 0e+00
Flavin-dependent oxidoreductase, luciferase family (includes alkanesulfonate monooxygenase ...
32-330
1.34e-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: 183.60 E-value: 1.34e-55
Alkanal monooxygenase are flavin monoxygenases. Molecular oxygen is activated by reaction with ...
33-131
5.77e-12
Alkanal monooxygenase are flavin monoxygenases. Molecular oxygen is activated by reaction with reduced flavin mononucleotide (FMNH2) and reacts with an aldehyde to yield the carboxylic acid, oxidized flavin (FMN) and a blue-green light. Bacterial luciferases are heterodimers made of alpha and beta subunits which are homologous. The single activer center is on the alpha subunit. The alpha subunit has a stretch of 30 amino acid residues that is not present in the beta subunit. The beta subunit does not contain the active site and is required for the formation of the fully active heterodimer. The beta subunit does not contribute anything directly to the active site. Its role is probably to stabilize the high quantum yield conformation of the alpha subunit through interactionbs across the subunit interface.
Pssm-ID: 238529 [Multi-domain] Cd Length: 315 Bit Score: 65.87 E-value: 5.77e-12
putative FMN-dependent luciferase-like monooxygenase, KPN_01858 family; This protein family ...
4-329
0e+00
putative FMN-dependent luciferase-like monooxygenase, KPN_01858 family; This protein family consists of luciferase-like monooxygenases (LLM), and include KPN_01858 from Klebsiella pneumoniae as a representative member. Most are from species that lack F420 biosynthesis, so the family is likely to bind FMN as its cofactor. This family is closely associated with a binding protein-dependent ABC transporter, suggesting a role in catabolism. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 274928 Cd Length: 326 Bit Score: 530.42 E-value: 0e+00
Flavin-dependent oxidoreductase, luciferase family (includes alkanesulfonate monooxygenase ...
32-330
1.34e-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: 183.60 E-value: 1.34e-55
natural product biosynthesis luciferase-like monooxygenase domain; This model describes a ...
15-146
1.60e-22
natural product biosynthesis luciferase-like monooxygenase domain; This model describes a subfamily within the bacterial luciferase-like monooxygenase (LLM) family that regularly occurs within large non-ribosomal protein synthases/polyketide synthases, but also as small proteins. The LLM family includes members that bind either FMN or F420, and FMN is more likely in this case because many members are from species that lack F420 biosynthesis capability. An example member is the MupA protein of mupirocin biosynthesis in Pseudomonas fluorescens NCIMB 10586.
Pssm-ID: 274922 Cd Length: 341 Bit Score: 96.56 E-value: 1.60e-22
probable F420-dependent oxidoreductase, Rv2161c family; Coenzyme F420 has a limited ...
31-185
3.36e-20
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: 88.47 E-value: 3.36e-20
probable F420-dependent oxidoreductase, Rv1855c family; Coenzyme F420 has a limited ...
32-144
7.50e-13
probable F420-dependent oxidoreductase, Rv1855c 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 one such subfamily, exemplified by Rv1855c from Mycobacterium tuberculosis. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 274648 [Multi-domain] Cd Length: 227 Bit Score: 66.96 E-value: 7.50e-13
probable F420-dependent oxidoreductase, MSMEG_2516 family; Coenzyme F420 is produced by ...
32-148
1.07e-12
probable F420-dependent oxidoreductase, MSMEG_2516 family; Coenzyme F420 is produced by methanogenic archaea, a number of the Actinomycetes (including Mycobacterium tuberculosis), and rare members of other lineages. The resulting information-rich phylogenetic profile identifies candidate F420-dependent oxidoreductases within the family of luciferase-like enzymes (pfam00296), where the species range for the subfamily encompasses many F420-positive genomes without straying beyond. This family is uncharacterized, and named for member MSMEG_2516 from Mycobacterium smegmatis. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 200301 [Multi-domain] Cd Length: 295 Bit Score: 67.78 E-value: 1.07e-12
luciferase family oxidoreductase, group 1; The Pfam domain family pfam00296 is named for ...
31-321
1.86e-12
luciferase family oxidoreductase, group 1; The Pfam domain family pfam00296 is named for luciferase-like monooxygenases, but the family also contains several coenzyme F420-dependent enzymes. This protein family represents a well-resolved clade within family pfam00296 and shows no restriction to coenzyme F420-positive species, unlike some other clades within pfam00296. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 274646 [Multi-domain] Cd Length: 323 Bit Score: 67.13 E-value: 1.86e-12
Alkanal monooxygenase are flavin monoxygenases. Molecular oxygen is activated by reaction with ...
33-131
5.77e-12
Alkanal monooxygenase are flavin monoxygenases. Molecular oxygen is activated by reaction with reduced flavin mononucleotide (FMNH2) and reacts with an aldehyde to yield the carboxylic acid, oxidized flavin (FMN) and a blue-green light. Bacterial luciferases are heterodimers made of alpha and beta subunits which are homologous. The single activer center is on the alpha subunit. The alpha subunit has a stretch of 30 amino acid residues that is not present in the beta subunit. The beta subunit does not contain the active site and is required for the formation of the fully active heterodimer. The beta subunit does not contribute anything directly to the active site. Its role is probably to stabilize the high quantum yield conformation of the alpha subunit through interactionbs across the subunit interface.
Pssm-ID: 238529 [Multi-domain] Cd Length: 315 Bit Score: 65.87 E-value: 5.77e-12
Alkanesulfonate monoxygenase is the monoxygenase of a two-component system that catalyzes the ...
32-154
4.34e-05
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: 44.19 E-value: 4.34e-05
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.
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