putative luciferase-like monooxygenase, FMN-dependent, CE1758 family; This tightly conserved ...
1-357
0e+00
putative luciferase-like monooxygenase, FMN-dependent, CE1758 family; This tightly conserved subfamily of the bacterial luciferase-like monooxygenase (LLM) family, with members showing > 60 % pairwise sequence identity, includes proteins from both species with and species without the ability to make coenzyme F420. Therefore, the like cofactor is FMN rather than F420. The presence of three members in Kineococcus radiotolerans SRS30216 and two in Saccharopolyspora erythraea NRRL 2338 suggest closely related (subfamily) rather than exactly conserved (equivalog) function. Gene neighborhoods around members are not conserved. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 274934 [Multi-domain] Cd Length: 355 Bit Score: 658.37 E-value: 0e+00
Flavin-dependent oxidoreductase, luciferase family (includes alkanesulfonate monooxygenase ...
37-334
6.81e-60
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: 195.54 E-value: 6.81e-60
N5,N10-methylenetetrahydromethanopterin reductase (Mer) catalyzes the reduction of N5, ...
90-273
2.35e-04
N5,N10-methylenetetrahydromethanopterin reductase (Mer) catalyzes the reduction of N5,N10-methylenetetrahydromethanopterin with reduced coenzyme F420 to N5-methyltetrahydromethanopterin and oxidized coenzyme F420.
Pssm-ID: 238530 [Multi-domain] Cd Length: 202 Bit Score: 42.00 E-value: 2.35e-04
putative luciferase-like monooxygenase, FMN-dependent, CE1758 family; This tightly conserved ...
1-357
0e+00
putative luciferase-like monooxygenase, FMN-dependent, CE1758 family; This tightly conserved subfamily of the bacterial luciferase-like monooxygenase (LLM) family, with members showing > 60 % pairwise sequence identity, includes proteins from both species with and species without the ability to make coenzyme F420. Therefore, the like cofactor is FMN rather than F420. The presence of three members in Kineococcus radiotolerans SRS30216 and two in Saccharopolyspora erythraea NRRL 2338 suggest closely related (subfamily) rather than exactly conserved (equivalog) function. Gene neighborhoods around members are not conserved. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 274934 [Multi-domain] Cd Length: 355 Bit Score: 658.37 E-value: 0e+00
Flavin-dependent oxidoreductase, luciferase family (includes alkanesulfonate monooxygenase ...
37-334
6.81e-60
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: 195.54 E-value: 6.81e-60
probable oxidoreductase, LLM family; This model describes a highly conserved, somewhat broadly ...
2-333
6.99e-48
probable oxidoreductase, LLM family; This model describes a highly conserved, somewhat broadly distributed family withing the luciferase-like monooxygenase (LLM) superfamily. Most members are from species incapable of synthesizing coenzyme F420, bound by some members of the LLM superfamily. Members, therefore, are more likely to use FMN as a cofactor.
Pssm-ID: 274817 [Multi-domain] Cd Length: 337 Bit Score: 165.11 E-value: 6.99e-48
luciferase family oxidoreductase, group 1; The Pfam domain family pfam00296 is named for ...
27-255
1.24e-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: 67.90 E-value: 1.24e-12
N5,N10-methylenetetrahydromethanopterin reductase (Mer) catalyzes the reduction of N5, ...
90-273
2.35e-04
N5,N10-methylenetetrahydromethanopterin reductase (Mer) catalyzes the reduction of N5,N10-methylenetetrahydromethanopterin with reduced coenzyme F420 to N5-methyltetrahydromethanopterin and oxidized coenzyme F420.
Pssm-ID: 238530 [Multi-domain] Cd Length: 202 Bit Score: 42.00 E-value: 2.35e-04
Alkanal monooxygenase are flavin monoxygenases. Molecular oxygen is activated by reaction with ...
1-114
6.24e-04
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: 41.21 E-value: 6.24e-04
Alkanesulfonate monoxygenase is the monoxygenase of a two-component system that catalyzes the ...
1-249
4.90e-03
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: 38.03 E-value: 4.90e-03
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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(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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