molybdenum cofactor biosynthesis protein MoaE serves as the catalytic subunit of the molybdopterin synthase complex, which catalyzes the conversion of precursor Z into molybdopterin
Molybdopterin synthase catalytic subunit MoaE [Coenzyme transport and metabolism]; ...
20-151
1.13e-44
Molybdopterin synthase catalytic subunit MoaE [Coenzyme transport and metabolism]; Molybdopterin synthase catalytic subunit MoaE is part of the Pathway/BioSystem: Molybdopterin biosynthesis
:
Pssm-ID: 440083 [Multi-domain] Cd Length: 143 Bit Score: 143.40 E-value: 1.13e-44
Molybdopterin synthase catalytic subunit MoaE [Coenzyme transport and metabolism]; ...
20-151
1.13e-44
Molybdopterin synthase catalytic subunit MoaE [Coenzyme transport and metabolism]; Molybdopterin synthase catalytic subunit MoaE is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 440083 [Multi-domain] Cd Length: 143 Bit Score: 143.40 E-value: 1.13e-44
MoaE family. Members of this family are involved in biosynthesis of the molybdenum cofactor ...
29-150
2.69e-41
MoaE family. Members of this family are involved in biosynthesis of the molybdenum cofactor (Moco), an essential cofactor for a diverse group of redox enzymes. Moco biosynthesis is an evolutionarily conserved pathway present in eubacteria, archaea and eukaryotes. Moco contains a tricyclic pyranopterin, termed molybdopterin (MPT), which carries the cis-dithiolene group responsible for molybdenum ligation. This dithiolene group is generated by MPT synthase in the second major step in Moco biosynthesis. MPT synthase is a heterotetramer consisting of two large (MoaE) and two small (MoaD) subunits.
Pssm-ID: 238385 [Multi-domain] Cd Length: 124 Bit Score: 134.18 E-value: 2.69e-41
MoaE protein; This family contains the MoaE protein that is involved in biosynthesis of ...
20-133
2.84e-35
MoaE protein; This family contains the MoaE protein that is involved in biosynthesis of molybdopterin. Molybdopterin, the universal component of the pterin molybdenum cofactors, contains a dithiolene group serving to bind Mo. Addition of the dithiolene sulfurs to a molybdopterin precursor requires the activity of the converting factor. Converting factor contains the MoaE and MoaD proteins.
Pssm-ID: 460546 Cd Length: 113 Bit Score: 118.32 E-value: 2.84e-35
Molybdopterin synthase catalytic subunit MoaE [Coenzyme transport and metabolism]; ...
20-151
1.13e-44
Molybdopterin synthase catalytic subunit MoaE [Coenzyme transport and metabolism]; Molybdopterin synthase catalytic subunit MoaE is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 440083 [Multi-domain] Cd Length: 143 Bit Score: 143.40 E-value: 1.13e-44
MoaE family. Members of this family are involved in biosynthesis of the molybdenum cofactor ...
29-150
2.69e-41
MoaE family. Members of this family are involved in biosynthesis of the molybdenum cofactor (Moco), an essential cofactor for a diverse group of redox enzymes. Moco biosynthesis is an evolutionarily conserved pathway present in eubacteria, archaea and eukaryotes. Moco contains a tricyclic pyranopterin, termed molybdopterin (MPT), which carries the cis-dithiolene group responsible for molybdenum ligation. This dithiolene group is generated by MPT synthase in the second major step in Moco biosynthesis. MPT synthase is a heterotetramer consisting of two large (MoaE) and two small (MoaD) subunits.
Pssm-ID: 238385 [Multi-domain] Cd Length: 124 Bit Score: 134.18 E-value: 2.69e-41
MoaE protein; This family contains the MoaE protein that is involved in biosynthesis of ...
20-133
2.84e-35
MoaE protein; This family contains the MoaE protein that is involved in biosynthesis of molybdopterin. Molybdopterin, the universal component of the pterin molybdenum cofactors, contains a dithiolene group serving to bind Mo. Addition of the dithiolene sulfurs to a molybdopterin precursor requires the activity of the converting factor. Converting factor contains the MoaE and MoaD proteins.
Pssm-ID: 460546 Cd Length: 113 Bit Score: 118.32 E-value: 2.84e-35
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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