F420-dependent oxidoreductase, CPS_4043 family; This model represents a family of putative ...
2-330
0e+00
F420-dependent oxidoreductase, CPS_4043 family; This model represents a family of putative F420-dependent oxidoreductases, fairly closely related to 5,10-methylenetetrahydromethanopterin reductase (mer, TIGR03555), both within the bacterial luciferase-like monoxygenase (LLM) family. A fairly deep split (to about 40 % sequence identity) in the present family separates a strictly Actinobacterial clade from an alpha/beta/gamma-proteobacterial clade, in which the member is often the only apparent F420-dependent LLM family member. The specific function, and whether Actinobacterial and Proteobacterial clades differ in function, are unknown. [Unknown function, Enzymes of unknown specificity]
:
Pssm-ID: 163554 Cd Length: 330 Bit Score: 647.16 E-value: 0e+00
F420-dependent oxidoreductase, CPS_4043 family; This model represents a family of putative ...
2-330
0e+00
F420-dependent oxidoreductase, CPS_4043 family; This model represents a family of putative F420-dependent oxidoreductases, fairly closely related to 5,10-methylenetetrahydromethanopterin reductase (mer, TIGR03555), both within the bacterial luciferase-like monoxygenase (LLM) family. A fairly deep split (to about 40 % sequence identity) in the present family separates a strictly Actinobacterial clade from an alpha/beta/gamma-proteobacterial clade, in which the member is often the only apparent F420-dependent LLM family member. The specific function, and whether Actinobacterial and Proteobacterial clades differ in function, are unknown. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 163554 Cd Length: 330 Bit Score: 647.16 E-value: 0e+00
Flavin-dependent oxidoreductase, luciferase family (includes alkanesulfonate monooxygenase ...
23-330
6.26e-48
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: 163.57 E-value: 6.26e-48
N5,N10-methylenetetrahydromethanopterin reductase (Mer) catalyzes the reduction of N5, ...
1-218
1.98e-18
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: 82.06 E-value: 1.98e-18
F420-dependent oxidoreductase, CPS_4043 family; This model represents a family of putative ...
2-330
0e+00
F420-dependent oxidoreductase, CPS_4043 family; This model represents a family of putative F420-dependent oxidoreductases, fairly closely related to 5,10-methylenetetrahydromethanopterin reductase (mer, TIGR03555), both within the bacterial luciferase-like monoxygenase (LLM) family. A fairly deep split (to about 40 % sequence identity) in the present family separates a strictly Actinobacterial clade from an alpha/beta/gamma-proteobacterial clade, in which the member is often the only apparent F420-dependent LLM family member. The specific function, and whether Actinobacterial and Proteobacterial clades differ in function, are unknown. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 163554 Cd Length: 330 Bit Score: 647.16 E-value: 0e+00
Flavin-dependent oxidoreductase, luciferase family (includes alkanesulfonate monooxygenase ...
23-330
6.26e-48
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: 163.57 E-value: 6.26e-48
N5,N10-methylenetetrahydromethanopterin reductase (Mer) catalyzes the reduction of N5, ...
1-218
1.98e-18
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: 82.06 E-value: 1.98e-18
probable F420-dependent oxidoreductase, Rv2161c family; Coenzyme F420 has a limited ...
17-222
8.16e-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: 75.76 E-value: 8.16e-16
probable F420-dependent oxidoreductase, Rv3093c family; This model describes a small family of ...
5-304
2.61e-15
probable F420-dependent oxidoreductase, Rv3093c family; This model describes a small family of enzymes in the bacterial luciferase-like monooxygenase family, which includes F420-dependent enzymes such as N5,N10-methylenetetrahydromethanopterin reductase as well as FMN-dependent enzymes. All members of this family are from species that produce coenzyme F420; SIMBAL analysis suggests that members of this family bind F420 rather than FMN. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 274812 Cd Length: 301 Bit Score: 75.24 E-value: 2.61e-15
Alkanesulfonate monoxygenase is the monoxygenase of a two-component system that catalyzes the ...
17-196
3.71e-07
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: 50.35 E-value: 3.71e-07
Alkanal monooxygenase are flavin monoxygenases. Molecular oxygen is activated by reaction with ...
1-120
4.35e-03
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: 38.52 E-value: 4.35e-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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Functional characterization of the conserved domain architecture found on the query.
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