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; similar to Agrobacterium tumefaciens monooxygenase
probable oxidoreductase, LLM family; This model describes a highly conserved, somewhat broadly ...
2-339
0e+00
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.
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Pssm-ID: 274817 [Multi-domain] Cd Length: 337 Bit Score: 620.41 E-value: 0e+00
probable oxidoreductase, LLM family; This model describes a highly conserved, somewhat broadly ...
2-339
0e+00
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: 620.41 E-value: 0e+00
Flavin-dependent oxidoreductase, luciferase family (includes alkanesulfonate monooxygenase ...
37-340
3.66e-82
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: 251.78 E-value: 3.66e-82
Alkanal monooxygenase are flavin monoxygenases. Molecular oxygen is activated by reaction with ...
22-225
3.88e-10
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: 60.09 E-value: 3.88e-10
probable oxidoreductase, LLM family; This model describes a highly conserved, somewhat broadly ...
2-339
0e+00
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: 620.41 E-value: 0e+00
Flavin-dependent oxidoreductase, luciferase family (includes alkanesulfonate monooxygenase ...
37-340
3.66e-82
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: 251.78 E-value: 3.66e-82
putative luciferase-like monooxygenase, FMN-dependent, CE1758 family; This tightly conserved ...
1-344
4.05e-58
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: 191.89 E-value: 4.05e-58
natural product biosynthesis luciferase-like monooxygenase domain; This model describes a ...
19-332
7.39e-31
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: 119.67 E-value: 7.39e-31
probable F420-dependent oxidoreductase, Rv2161c family; Coenzyme F420 has a limited ...
37-232
1.13e-21
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: 92.32 E-value: 1.13e-21
Alkanal monooxygenase are flavin monoxygenases. Molecular oxygen is activated by reaction with ...
22-225
3.88e-10
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: 60.09 E-value: 3.88e-10
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: 41.54 E-value: 5.23e-04
N5,N10-methylenetetrahydromethanopterin reductase (Mer) catalyzes the reduction of N5, ...
95-181
5.21e-03
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: 37.76 E-value: 5.21e-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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