MULTISPECIES: bifunctional molybdenum cofactor biosynthesis protein MoaC/MoaB [Acinetobacter]
bifunctional molybdenum cofactor biosynthesis protein MoaC/MoaB( domain architecture ID 11480000)
bifunctional molybdenum cofactor biosynthesis protein MoaC/MoaB catalyzes the conversion of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP)
List of domain hits
Name | Accession | Description | Interval | E-value | |||||
moaC | PRK03604 | bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional |
1-303 | 3.76e-159 | |||||
bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional : Pssm-ID: 235138 [Multi-domain] Cd Length: 312 Bit Score: 446.31 E-value: 3.76e-159
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Name | Accession | Description | Interval | E-value | |||||
moaC | PRK03604 | bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional |
1-303 | 3.76e-159 | |||||
bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional Pssm-ID: 235138 [Multi-domain] Cd Length: 312 Bit Score: 446.31 E-value: 3.76e-159
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MoaB | COG0521 | Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]; Molybdopterin ... |
145-303 | 4.85e-58 | |||||
Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]; Molybdopterin biosynthesis enzyme MoaB/MogA is part of the Pathway/BioSystem: Molybdopterin biosynthesis Pssm-ID: 440287 [Multi-domain] Cd Length: 169 Bit Score: 183.78 E-value: 4.85e-58
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MoaC | pfam01967 | MoaC family; Members of this family are involved in molybdenum cofactor biosynthesis. However ... |
1-116 | 1.82e-56 | |||||
MoaC family; Members of this family are involved in molybdenum cofactor biosynthesis. However their molecular function is not known. Pssm-ID: 460399 Cd Length: 136 Bit Score: 178.69 E-value: 1.82e-56
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MogA_MoaB | cd00886 | MogA_MoaB family. Members of this family are involved in biosynthesis of the molybdenum ... |
148-295 | 2.42e-55 | |||||
MogA_MoaB family. Members of this family are involved in biosynthesis of the molybdenum cofactor (MoCF) an essential cofactor of a diverse group of redox enzymes. MoCF biosynthesis is an evolutionarily conserved pathway present in eubacteria, archaea, and eukaryotes. MoCF contains a tricyclic pyranopterin, termed molybdopterin (MPT). MogA, together with MoeA, is responsible for the metal incorporation into MPT, the third step in MoCF biosynthesis. The plant homolog Cnx1 is a MoeA-MogA fusion protein. The mammalian homolog gephyrin is a MogA-MoeA fusion protein, that plays a critical role in postsynaptic anchoring of inhibitory glycine receptors and major GABAa receptor subtypes. In contrast, MoaB shows high similarity to MogA, but little is known about its physiological role. All well studied members of this family form highly stable trimers. Pssm-ID: 238451 [Multi-domain] Cd Length: 152 Bit Score: 176.51 E-value: 2.42e-55
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moaC | TIGR00581 | molybdenum cofactor biosynthesis protein MoaC; MoaC catalyzes an early step in molybdenum ... |
1-115 | 2.14e-40 | |||||
molybdenum cofactor biosynthesis protein MoaC; MoaC catalyzes an early step in molybdenum cofactor biosynthesis in E. coli. The Arabidopsis homolog Cnx3 complements MoaC deficiency in E. coli. Eukarotic members of this family branch within the bacterial branch, with the archaeal members as an apparent outgroup. This protein is absent in a number of the pathogens with smaller genomes, including Mycoplasmas, Chlamydias, and spirochetes, but is found in most other complete genomes to date. The homolog form Synechocystis sp. is fused to a MobA-homologous region and is an outlier to all other bacterial forms by both neighbor-joining and UPGMA analyses. Members of this family are well-conserved. The seed for this model excludes both archaeal sequences and the most divergent bacterial sequences, but still finds all candidate MoaC sequences easily between trusted and noise cutoffs. We suggest that sequences branching outside the set that contains all seed members be regarded only as putative functional equivalents of MoaC unless and until a member of the archaeal outgroup is shown to have equivalent function. [Biosynthesis of cofactors, prosthetic groups, and carriers, Molybdopterin] Pssm-ID: 129670 Cd Length: 147 Bit Score: 137.95 E-value: 2.14e-40
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MoCF_biosynth | smart00852 | Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
151-286 | 4.16e-26 | |||||
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in biosynthesis of molybdopterin cofactor. The domain is presumed to bind molybdopterin. The structure of this domain is known, and it forms an alpha/beta structure. In the known structure of Gephyrin this domain mediates trimerisation. Pssm-ID: 214856 [Multi-domain] Cd Length: 138 Bit Score: 100.36 E-value: 4.16e-26
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Name | Accession | Description | Interval | E-value | |||||
moaC | PRK03604 | bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional |
1-303 | 3.76e-159 | |||||
bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional Pssm-ID: 235138 [Multi-domain] Cd Length: 312 Bit Score: 446.31 E-value: 3.76e-159
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MoaB | COG0521 | Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]; Molybdopterin ... |
145-303 | 4.85e-58 | |||||
Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]; Molybdopterin biosynthesis enzyme MoaB/MogA is part of the Pathway/BioSystem: Molybdopterin biosynthesis Pssm-ID: 440287 [Multi-domain] Cd Length: 169 Bit Score: 183.78 E-value: 4.85e-58
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MoaC | pfam01967 | MoaC family; Members of this family are involved in molybdenum cofactor biosynthesis. However ... |
1-116 | 1.82e-56 | |||||
MoaC family; Members of this family are involved in molybdenum cofactor biosynthesis. However their molecular function is not known. Pssm-ID: 460399 Cd Length: 136 Bit Score: 178.69 E-value: 1.82e-56
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MogA_MoaB | cd00886 | MogA_MoaB family. Members of this family are involved in biosynthesis of the molybdenum ... |
148-295 | 2.42e-55 | |||||
MogA_MoaB family. Members of this family are involved in biosynthesis of the molybdenum cofactor (MoCF) an essential cofactor of a diverse group of redox enzymes. MoCF biosynthesis is an evolutionarily conserved pathway present in eubacteria, archaea, and eukaryotes. MoCF contains a tricyclic pyranopterin, termed molybdopterin (MPT). MogA, together with MoeA, is responsible for the metal incorporation into MPT, the third step in MoCF biosynthesis. The plant homolog Cnx1 is a MoeA-MogA fusion protein. The mammalian homolog gephyrin is a MogA-MoeA fusion protein, that plays a critical role in postsynaptic anchoring of inhibitory glycine receptors and major GABAa receptor subtypes. In contrast, MoaB shows high similarity to MogA, but little is known about its physiological role. All well studied members of this family form highly stable trimers. Pssm-ID: 238451 [Multi-domain] Cd Length: 152 Bit Score: 176.51 E-value: 2.42e-55
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MoaC | COG0315 | Molybdenum cofactor biosynthesis enzyme MoaC [Coenzyme transport and metabolism]; Molybdenum ... |
1-115 | 4.05e-54 | |||||
Molybdenum cofactor biosynthesis enzyme MoaC [Coenzyme transport and metabolism]; Molybdenum cofactor biosynthesis enzyme MoaC is part of the Pathway/BioSystem: Molybdopterin biosynthesis Pssm-ID: 440084 Cd Length: 153 Bit Score: 173.32 E-value: 4.05e-54
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moaC | PRK09364 | cyclic pyranopterin monophosphate synthase MoaC; |
1-115 | 2.28e-49 | |||||
cyclic pyranopterin monophosphate synthase MoaC; Pssm-ID: 236483 Cd Length: 159 Bit Score: 161.51 E-value: 2.28e-49
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MoaC | cd00528 | MoaC family. Members of this family are involved in molybdenum cofactor (Moco) biosynthesis, ... |
1-115 | 1.35e-46 | |||||
MoaC family. Members of this family are involved in molybdenum cofactor (Moco) biosynthesis, an essential cofactor of a diverse group of redox enzymes. MoaC, a small hexameric protein, converts, together with MoaA, a guanosine derivative to the precursor Z by inserting the carbon-8 of the purine between the 2' and 3' ribose carbon atoms, which is the first of three phases of Moco biosynthesis. Pssm-ID: 238293 Cd Length: 136 Bit Score: 153.44 E-value: 1.35e-46
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MoaC_PE | cd01420 | MoaC family, prokaryotic and eukaryotic. Members of this family are involved in molybdenum ... |
1-115 | 2.28e-46 | |||||
MoaC family, prokaryotic and eukaryotic. Members of this family are involved in molybdenum cofactor (Moco) biosynthesis, an essential cofactor of a diverse group of redox enzymes. MoaC, a small hexameric protein, converts, together with MoaA, a guanosine derivative to the precursor Z by inserting the carbon-8 of the purine between the 2' and 3' ribose carbon atoms, which is the first of three phases of Moco biosynthesis. Pssm-ID: 238708 Cd Length: 140 Bit Score: 153.09 E-value: 2.28e-46
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PRK12343 | PRK12343 | cyclic pyranopterin monophosphate synthase MoaC; |
1-115 | 2.39e-41 | |||||
cyclic pyranopterin monophosphate synthase MoaC; Pssm-ID: 237067 Cd Length: 151 Bit Score: 140.43 E-value: 2.39e-41
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moaC | TIGR00581 | molybdenum cofactor biosynthesis protein MoaC; MoaC catalyzes an early step in molybdenum ... |
1-115 | 2.14e-40 | |||||
molybdenum cofactor biosynthesis protein MoaC; MoaC catalyzes an early step in molybdenum cofactor biosynthesis in E. coli. The Arabidopsis homolog Cnx3 complements MoaC deficiency in E. coli. Eukarotic members of this family branch within the bacterial branch, with the archaeal members as an apparent outgroup. This protein is absent in a number of the pathogens with smaller genomes, including Mycoplasmas, Chlamydias, and spirochetes, but is found in most other complete genomes to date. The homolog form Synechocystis sp. is fused to a MobA-homologous region and is an outlier to all other bacterial forms by both neighbor-joining and UPGMA analyses. Members of this family are well-conserved. The seed for this model excludes both archaeal sequences and the most divergent bacterial sequences, but still finds all candidate MoaC sequences easily between trusted and noise cutoffs. We suggest that sequences branching outside the set that contains all seed members be regarded only as putative functional equivalents of MoaC unless and until a member of the archaeal outgroup is shown to have equivalent function. [Biosynthesis of cofactors, prosthetic groups, and carriers, Molybdopterin] Pssm-ID: 129670 Cd Length: 147 Bit Score: 137.95 E-value: 2.14e-40
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MoaC_A | cd01419 | MoaC family, archaeal. Members of this family are involved in molybdenum cofactor (Moco) ... |
1-115 | 2.64e-39 | |||||
MoaC family, archaeal. Members of this family are involved in molybdenum cofactor (Moco) biosynthesis, an essential cofactor of a diverse group of redox enzymes. MoaC, a small hexameric protein, converts, together with MoaA, a guanosine derivative to the precursor Z by inserting the carbon-8 of the purine between the 2' and 3' ribose carbon atoms, which is the first of three phases of Moco biosynthesis. Pssm-ID: 238707 Cd Length: 141 Bit Score: 134.80 E-value: 2.64e-39
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PRK14499 | PRK14499 | cyclic pyranopterin monophosphate synthase MoaC/MOSC-domain-containing protein; |
1-115 | 1.69e-31 | |||||
cyclic pyranopterin monophosphate synthase MoaC/MOSC-domain-containing protein; Pssm-ID: 237733 [Multi-domain] Cd Length: 308 Bit Score: 119.58 E-value: 1.69e-31
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MoCF_biosynth | pfam00994 | Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
151-292 | 7.74e-29 | |||||
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in biosynthesis of molybdopterin cofactor. The domain is presumed to bind molybdopterin. The structure of this domain is known, and it forms an alpha/beta structure. In the known structure of Gephyrin this domain mediates trimerization. Pssm-ID: 425979 [Multi-domain] Cd Length: 143 Bit Score: 107.72 E-value: 7.74e-29
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MoCF_biosynth | smart00852 | Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
151-286 | 4.16e-26 | |||||
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in biosynthesis of molybdopterin cofactor. The domain is presumed to bind molybdopterin. The structure of this domain is known, and it forms an alpha/beta structure. In the known structure of Gephyrin this domain mediates trimerisation. Pssm-ID: 214856 [Multi-domain] Cd Length: 138 Bit Score: 100.36 E-value: 4.16e-26
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MoCF_BD | cd00758 | MoCF_BD: molybdenum cofactor (MoCF) binding domain (BD). This domain is found a variety of ... |
150-290 | 1.02e-25 | |||||
MoCF_BD: molybdenum cofactor (MoCF) binding domain (BD). This domain is found a variety of proteins involved in biosynthesis of molybdopterin cofactor, like MoaB, MogA, and MoeA. The domain is presumed to bind molybdopterin. Pssm-ID: 238387 [Multi-domain] Cd Length: 133 Bit Score: 99.34 E-value: 1.02e-25
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molyb_syn | TIGR00177 | molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ... |
148-287 | 6.94e-24 | |||||
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein cnx1, and rat protein gephyrin each have one domain like MoeA and one like MoaB and Mog. These domains are, however, distantly related to each other, as captured by this model. Gephyrin is unusual in that it seems to be a tubulin-binding neuroprotein involved in the clustering of both blycine receptors and GABA receptors, rather than a protein of molybdenum cofactor biosynthesis. Pssm-ID: 272944 [Multi-domain] Cd Length: 148 Bit Score: 94.69 E-value: 6.94e-24
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PRK14500 | PRK14500 | putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MoaC/MobA; ... |
1-117 | 4.18e-22 | |||||
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MoaC/MobA; Provisional Pssm-ID: 237734 [Multi-domain] Cd Length: 346 Bit Score: 94.58 E-value: 4.18e-22
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PLN02699 | PLN02699 | Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase |
148-292 | 1.85e-20 | |||||
Bifunctional molybdopterin adenylyltransferase/molybdopterin molybdenumtransferase Pssm-ID: 215376 [Multi-domain] Cd Length: 659 Bit Score: 91.41 E-value: 1.85e-20
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mogA | PRK09417 | molybdenum cofactor biosynthesis protein MogA; Provisional |
151-274 | 1.56e-17 | |||||
molybdenum cofactor biosynthesis protein MogA; Provisional Pssm-ID: 181837 [Multi-domain] Cd Length: 193 Bit Score: 78.84 E-value: 1.56e-17
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PLN02375 | PLN02375 | molybderin biosynthesis protein CNX3 |
1-115 | 5.34e-17 | |||||
molybderin biosynthesis protein CNX3 Pssm-ID: 178003 [Multi-domain] Cd Length: 270 Bit Score: 79.03 E-value: 5.34e-17
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MoeA | COG0303 | Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ... |
176-274 | 1.75e-06 | |||||
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; Molybdopterin Mo-transferase (molybdopterin biosynthesis) is part of the Pathway/BioSystem: Molybdopterin biosynthesis Pssm-ID: 440072 [Multi-domain] Cd Length: 401 Bit Score: 48.93 E-value: 1.75e-06
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MoeA | cd00887 | MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ... |
142-231 | 2.78e-06 | |||||
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor (MoCF), an essential cofactor of a diverse group of redox enzymes. MoCF biosynthesis is an evolutionarily conserved pathway present in eubacteria, archaea and eukaryotes. MoCF contains a tricyclic pyranopterin, termed molybdopterin (MPT). MoeA, together with MoaB, is responsible for the metal incorporation into MPT, the third step in MoCF biosynthesis. The plant homolog Cnx1 is a MoeA-MogA fusion protein. The mammalian homolog gephyrin is a MogA-MoeA fusion protein, that plays a critical role in postsynaptic anchoring of inhibitory glycine receptors and major GABAa receptor subtypes. Pssm-ID: 238452 [Multi-domain] Cd Length: 394 Bit Score: 48.26 E-value: 2.78e-06
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PRK14498 | PRK14498 | putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing ... |
176-274 | 5.08e-04 | |||||
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing protein; Provisional Pssm-ID: 237732 [Multi-domain] Cd Length: 633 Bit Score: 41.35 E-value: 5.08e-04
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Blast search parameters | ||||
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