FAD synthase-like isoform X2 [Limulus polyphemus]
List of domain hits
Name | Accession | Description | Interval | E-value | ||||
FAD_synthase | cd23948 | FAD synthase; FAD synthase (FMN:ATP adenylyl transferase (FMNAT); FAD pyrophosphorylase; ... |
296-476 | 3.01e-99 | ||||
FAD synthase; FAD synthase (FMN:ATP adenylyl transferase (FMNAT); FAD pyrophosphorylase; Flavin adenine dinucleotide synthase (FADS); EC 2.7.7.2) is involved in the biochemical pathway for converting riboflavin into FAD. By sequence comparison, bacterial and eukaryotic FMNAT enzymes belong to two different protein superfamilies and apparently utilize different sets of active-site residues to accomplish the same chemistry. This subfamily includes eukaryotic FMNATs, which are members of the 3'-phosphoadenosine 5'-phosphosulfate (PAPS) reductase-like family belonging to the adenine nucleotide alpha hydrolase superfamily, which has conserved motifs different from those of nucleotidylyl transferases. : Pssm-ID: 467513 [Multi-domain] Cd Length: 179 Bit Score: 296.35 E-value: 3.01e-99
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cinA | cd00885 | Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon ... |
12-186 | 1.01e-48 | ||||
Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon and is thought to be specifically required at some stage in the process of transformation. This domain is closely related to a domain, found in a variety of proteins involved in biosynthesis of molybdopterin cofactor, where the domain is presumed to bind molybdopterin. : Pssm-ID: 238450 [Multi-domain] Cd Length: 170 Bit Score: 165.35 E-value: 1.01e-48
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Name | Accession | Description | Interval | E-value | |||||
FAD_synthase | cd23948 | FAD synthase; FAD synthase (FMN:ATP adenylyl transferase (FMNAT); FAD pyrophosphorylase; ... |
296-476 | 3.01e-99 | |||||
FAD synthase; FAD synthase (FMN:ATP adenylyl transferase (FMNAT); FAD pyrophosphorylase; Flavin adenine dinucleotide synthase (FADS); EC 2.7.7.2) is involved in the biochemical pathway for converting riboflavin into FAD. By sequence comparison, bacterial and eukaryotic FMNAT enzymes belong to two different protein superfamilies and apparently utilize different sets of active-site residues to accomplish the same chemistry. This subfamily includes eukaryotic FMNATs, which are members of the 3'-phosphoadenosine 5'-phosphosulfate (PAPS) reductase-like family belonging to the adenine nucleotide alpha hydrolase superfamily, which has conserved motifs different from those of nucleotidylyl transferases. Pssm-ID: 467513 [Multi-domain] Cd Length: 179 Bit Score: 296.35 E-value: 3.01e-99
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cinA | cd00885 | Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon ... |
12-186 | 1.01e-48 | |||||
Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon and is thought to be specifically required at some stage in the process of transformation. This domain is closely related to a domain, found in a variety of proteins involved in biosynthesis of molybdopterin cofactor, where the domain is presumed to bind molybdopterin. Pssm-ID: 238450 [Multi-domain] Cd Length: 170 Bit Score: 165.35 E-value: 1.01e-48
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CinA | COG1058 | ADP-ribose pyrophosphatase domain of DNA damage- and competence-inducible protein CinA ... |
12-254 | 5.33e-47 | |||||
ADP-ribose pyrophosphatase domain of DNA damage- and competence-inducible protein CinA [Replication, recombination and repair]; Pssm-ID: 440678 Cd Length: 249 Bit Score: 163.36 E-value: 5.33e-47
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PAPS_reduct | pfam01507 | Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine ... |
317-474 | 5.19e-32 | |||||
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine phosphosulfate (PAPS) reductase enzymes or PAPS sulfotransferase. PAPS reductase is part of the adenine nucleotide alpha hydrolases superfamily also including N type ATP PPases and ATP sulphurylases. The enzyme uses thioredoxin as an electron donor for the reduction of PAPS to phospho-adenosine-phosphate (PAP). It is also found in NodP nodulation protein P from Rhizobium which has ATP sulfurylase activity (sulfate adenylate transferase). Pssm-ID: 396201 [Multi-domain] Cd Length: 173 Bit Score: 120.86 E-value: 5.19e-32
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MoCF_biosynth | pfam00994 | Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
15-173 | 7.95e-27 | |||||
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: 105.41 E-value: 7.95e-27
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MoCF_biosynth | smart00852 | Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
15-164 | 1.04e-22 | |||||
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: 93.81 E-value: 1.04e-22
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PRK01215 | PRK01215 | nicotinamide mononucleotide deamidase-related protein; |
8-254 | 2.11e-22 | |||||
nicotinamide mononucleotide deamidase-related protein; Pssm-ID: 179250 [Multi-domain] Cd Length: 264 Bit Score: 96.62 E-value: 2.11e-22
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CysD | COG0175 | 3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ... |
293-474 | 1.31e-20 | |||||
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or related enzyme [Amino acid transport and metabolism, Coenzyme transport and metabolism]; 3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or related enzyme is part of the Pathway/BioSystem: Cysteine biosynthesis Pssm-ID: 439945 [Multi-domain] Cd Length: 232 Bit Score: 90.68 E-value: 1.31e-20
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molyb_syn | TIGR00177 | molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ... |
12-99 | 4.38e-15 | |||||
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: 72.35 E-value: 4.38e-15
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PRK02090 | PRK02090 | phosphoadenylyl-sulfate reductase; |
327-474 | 1.19e-12 | |||||
phosphoadenylyl-sulfate reductase; Pssm-ID: 234997 Cd Length: 241 Bit Score: 67.56 E-value: 1.19e-12
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cysH | TIGR00434 | phosophoadenylyl-sulfate reductase (thioredoxin); This enzyme, involved in the assimilation of ... |
327-504 | 1.16e-11 | |||||
phosophoadenylyl-sulfate reductase (thioredoxin); This enzyme, involved in the assimilation of inorganic sulfate, is designated cysH in Bacteria and MET16 in Saccharomyces cerevisiae. Synonyms include phosphoadenosine phosphosulfate reductase, PAPS reductase, and PAPS reductase, thioredoxin-dependent. In a reaction requiring reduced thioredoxin and NADPH, it converts 3(prime)-phosphoadenylylsulfate (PAPS) to sulfite and adenosine 3(prime),5(prime) diphosphate (PAP). A related family of plant enzymes, scoring below the trusted cutoff, differs in having a thioredoxin-like C-terminal domain, not requiring thioredoxin, and in having a preference for 5(prime)-adenylylsulfate (APS) over PAPS. [Central intermediary metabolism, Sulfur metabolism] Pssm-ID: 129526 Cd Length: 212 Bit Score: 64.04 E-value: 1.16e-11
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Name | Accession | Description | Interval | E-value | |||||
FAD_synthase | cd23948 | FAD synthase; FAD synthase (FMN:ATP adenylyl transferase (FMNAT); FAD pyrophosphorylase; ... |
296-476 | 3.01e-99 | |||||
FAD synthase; FAD synthase (FMN:ATP adenylyl transferase (FMNAT); FAD pyrophosphorylase; Flavin adenine dinucleotide synthase (FADS); EC 2.7.7.2) is involved in the biochemical pathway for converting riboflavin into FAD. By sequence comparison, bacterial and eukaryotic FMNAT enzymes belong to two different protein superfamilies and apparently utilize different sets of active-site residues to accomplish the same chemistry. This subfamily includes eukaryotic FMNATs, which are members of the 3'-phosphoadenosine 5'-phosphosulfate (PAPS) reductase-like family belonging to the adenine nucleotide alpha hydrolase superfamily, which has conserved motifs different from those of nucleotidylyl transferases. Pssm-ID: 467513 [Multi-domain] Cd Length: 179 Bit Score: 296.35 E-value: 3.01e-99
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cinA | cd00885 | Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon ... |
12-186 | 1.01e-48 | |||||
Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon and is thought to be specifically required at some stage in the process of transformation. This domain is closely related to a domain, found in a variety of proteins involved in biosynthesis of molybdopterin cofactor, where the domain is presumed to bind molybdopterin. Pssm-ID: 238450 [Multi-domain] Cd Length: 170 Bit Score: 165.35 E-value: 1.01e-48
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CinA | COG1058 | ADP-ribose pyrophosphatase domain of DNA damage- and competence-inducible protein CinA ... |
12-254 | 5.33e-47 | |||||
ADP-ribose pyrophosphatase domain of DNA damage- and competence-inducible protein CinA [Replication, recombination and repair]; Pssm-ID: 440678 Cd Length: 249 Bit Score: 163.36 E-value: 5.33e-47
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PAPS_reduct | pfam01507 | Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine ... |
317-474 | 5.19e-32 | |||||
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine phosphosulfate (PAPS) reductase enzymes or PAPS sulfotransferase. PAPS reductase is part of the adenine nucleotide alpha hydrolases superfamily also including N type ATP PPases and ATP sulphurylases. The enzyme uses thioredoxin as an electron donor for the reduction of PAPS to phospho-adenosine-phosphate (PAP). It is also found in NodP nodulation protein P from Rhizobium which has ATP sulfurylase activity (sulfate adenylate transferase). Pssm-ID: 396201 [Multi-domain] Cd Length: 173 Bit Score: 120.86 E-value: 5.19e-32
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MoCF_biosynth | pfam00994 | Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
15-173 | 7.95e-27 | |||||
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: 105.41 E-value: 7.95e-27
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MoCF_biosynth | smart00852 | Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
15-164 | 1.04e-22 | |||||
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: 93.81 E-value: 1.04e-22
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PRK01215 | PRK01215 | nicotinamide mononucleotide deamidase-related protein; |
8-254 | 2.11e-22 | |||||
nicotinamide mononucleotide deamidase-related protein; Pssm-ID: 179250 [Multi-domain] Cd Length: 264 Bit Score: 96.62 E-value: 2.11e-22
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CysD | COG0175 | 3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ... |
293-474 | 1.31e-20 | |||||
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or related enzyme [Amino acid transport and metabolism, Coenzyme transport and metabolism]; 3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or related enzyme is part of the Pathway/BioSystem: Cysteine biosynthesis Pssm-ID: 439945 [Multi-domain] Cd Length: 232 Bit Score: 90.68 E-value: 1.31e-20
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PRK03670 | PRK03670 | competence damage-inducible protein A; Provisional |
13-250 | 1.73e-20 | |||||
competence damage-inducible protein A; Provisional Pssm-ID: 167581 Cd Length: 252 Bit Score: 90.63 E-value: 1.73e-20
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PAPS_reductase | cd23945 | Phosphoadenylyl-sulfate reductase (thioredoxin); Phosphoadenosine phosphosulfate (PAPS) ... |
313-467 | 3.60e-16 | |||||
Phosphoadenylyl-sulfate reductase (thioredoxin); Phosphoadenosine phosphosulfate (PAPS) reductase (or PAPS sulfotransferase EC 1.8.4.8) is part of the adenine nucleotide alpha hydrolase superfamily that also includes N-type ATP PPases and ATP sulfurylases. A highly modified version of the P loop, the fingerprint peptide of mononucleotide-binding proteins, is present in the active site of the protein, which appears to be a positively charged cleft containing a number of conserved arginine and lysine residues. Although PAPS reductase has no ATPase activity, it shows a striking similarity to the structure of the ATP pyrophosphatase (ATP PPase) domain of GMP synthetase, indicating that both enzyme families have evolved from a common ancestral nucleotide-binding fold. The enzyme uses thioredoxin as an electron donor for the reduction of PAPS to phospho-adenosine-phosphate (PAP). Pssm-ID: 467510 [Multi-domain] Cd Length: 183 Bit Score: 76.48 E-value: 3.60e-16
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molyb_syn | TIGR00177 | molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ... |
12-99 | 4.38e-15 | |||||
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: 72.35 E-value: 4.38e-15
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PRK00549 | PRK00549 | competence damage-inducible protein A; Provisional |
13-163 | 4.01e-14 | |||||
competence damage-inducible protein A; Provisional Pssm-ID: 234789 [Multi-domain] Cd Length: 414 Bit Score: 74.05 E-value: 4.01e-14
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cinA_nterm | TIGR00200 | competence/damage-inducible protein CinA N-terminal domain; cinA is a DNA damage- or ... |
13-180 | 9.33e-13 | |||||
competence/damage-inducible protein CinA N-terminal domain; cinA is a DNA damage- or competence-inducible protein that is polycistronic with recA in a number of species [DNA metabolism, DNA replication, recombination, and repair] Pssm-ID: 161761 [Multi-domain] Cd Length: 413 Bit Score: 69.94 E-value: 9.33e-13
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PRK02090 | PRK02090 | phosphoadenylyl-sulfate reductase; |
327-474 | 1.19e-12 | |||||
phosphoadenylyl-sulfate reductase; Pssm-ID: 234997 Cd Length: 241 Bit Score: 67.56 E-value: 1.19e-12
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PAPS_reductase-like_YbdN | cd23947 | uncharacterized phosphoadenosine phosphosulfate reductase-like proteins, similar to ... |
299-467 | 2.31e-12 | |||||
uncharacterized phosphoadenosine phosphosulfate reductase-like proteins, similar to Escherichia coli YbdN; This subgroup contains Escherichia coli YbdN and other phosphoadenosine phosphosulfate (PAPS) reductase (or PAPS sulfotransferase EC 1.8.4.8)-like proteins. PAPS reductase is part of the adenine nucleotide alpha hydrolases superfamily also including N-type ATP PPases and ATP sulfurylases. A highly modified version of the P loop, the fingerprint peptide of mononucleotide-binding proteins, is present in the active site of the protein, which appears to be a positively charged cleft containing a number of conserved arginine and lysine residues. Although PAPS reductase has no ATPase activity, it shows a striking similarity to the structure of the ATP pyrophosphatase (ATP PPase) domain of GMP synthetase, indicating that both enzyme families have evolved from a common ancestral nucleotide-binding fold. The enzyme uses thioredoxin as an electron donor for the reduction of PAPS to phospho-adenosine-phosphate (PAP). Pssm-ID: 467512 [Multi-domain] Cd Length: 206 Bit Score: 65.87 E-value: 2.31e-12
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cysH | TIGR00434 | phosophoadenylyl-sulfate reductase (thioredoxin); This enzyme, involved in the assimilation of ... |
327-504 | 1.16e-11 | |||||
phosophoadenylyl-sulfate reductase (thioredoxin); This enzyme, involved in the assimilation of inorganic sulfate, is designated cysH in Bacteria and MET16 in Saccharomyces cerevisiae. Synonyms include phosphoadenosine phosphosulfate reductase, PAPS reductase, and PAPS reductase, thioredoxin-dependent. In a reaction requiring reduced thioredoxin and NADPH, it converts 3(prime)-phosphoadenylylsulfate (PAPS) to sulfite and adenosine 3(prime),5(prime) diphosphate (PAP). A related family of plant enzymes, scoring below the trusted cutoff, differs in having a thioredoxin-like C-terminal domain, not requiring thioredoxin, and in having a preference for 5(prime)-adenylylsulfate (APS) over PAPS. [Central intermediary metabolism, Sulfur metabolism] Pssm-ID: 129526 Cd Length: 212 Bit Score: 64.04 E-value: 1.16e-11
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MoCF_BD | cd00758 | MoCF_BD: molybdenum cofactor (MoCF) binding domain (BD). This domain is found a variety of ... |
15-100 | 2.86e-10 | |||||
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: 58.12 E-value: 2.86e-10
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PRK08557 | PRK08557 | hypothetical protein; Provisional |
295-467 | 4.85e-08 | |||||
hypothetical protein; Provisional Pssm-ID: 181465 [Multi-domain] Cd Length: 417 Bit Score: 55.15 E-value: 4.85e-08
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PLN02309 | PLN02309 | 5'-adenylylsulfate reductase |
406-474 | 1.74e-07 | |||||
5'-adenylylsulfate reductase Pssm-ID: 215175 [Multi-domain] Cd Length: 457 Bit Score: 53.64 E-value: 1.74e-07
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MoeA | COG0303 | Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ... |
15-79 | 3.83e-07 | |||||
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: 52.40 E-value: 3.83e-07
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Sulfate_adenylyltransferase_2 | cd23946 | Sulfate adenylyltransferase subunit 2; Sulfate adenylyltransferase subunits 1 and 2 form ATP ... |
295-459 | 3.96e-07 | |||||
Sulfate adenylyltransferase subunit 2; Sulfate adenylyltransferase subunits 1 and 2 form ATP sulfurylase (ATPS) that catalyzes the adenylation of sulfate producing adenosine 5'-phosphosulfate (APS) and diphosphate, the first enzymatic step in the sulfur assimilation pathway. APS synthesis involves the formation of a high-energy phosphoric-sulfuric acid anhydride bond driven by GTP hydrolysis by CysN, coupled to ATP hydrolysis by CysD. CysD belongs to the ATP pyrophosphatase (ATP PPase) family of proteins, members of which include PAPS reductase, GMP synthetase, asparagine synthetase, and NAD(+) synthetase. This subunit is responsible for directly forming APS under control of the G protein. A modified version of the P loop (PP-loop), the fingerprint peptide of mononucleotide-binding proteins, is present in the active site of the protein, which appears to be a positively charged cleft containing a number of conserved arginine and lysine residues. Pssm-ID: 467511 Cd Length: 214 Bit Score: 50.96 E-value: 3.96e-07
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MogA_MoaB | cd00886 | MogA_MoaB family. Members of this family are involved in biosynthesis of the molybdenum ... |
12-99 | 4.25e-07 | |||||
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: 49.40 E-value: 4.25e-07
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PRK03673 | PRK03673 | nicotinamide mononucleotide deamidase-related protein YfaY; |
19-100 | 8.81e-07 | |||||
nicotinamide mononucleotide deamidase-related protein YfaY; Pssm-ID: 179629 [Multi-domain] Cd Length: 396 Bit Score: 51.24 E-value: 8.81e-07
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MoaB | COG0521 | Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]; Molybdopterin ... |
1-88 | 1.19e-06 | |||||
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: 48.57 E-value: 1.19e-06
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APS_reduc | TIGR00424 | 5'-adenylylsulfate reductase, thioredoxin-independent; This enzyme, involved in the ... |
406-474 | 1.39e-06 | |||||
5'-adenylylsulfate reductase, thioredoxin-independent; This enzyme, involved in the assimilation of inorganic sulfate, is closely related to the thioredoxin-dependent PAPS reductase of Bacteria (CysH) and Saccharomyces cerevisiae. However, it has its own C-terminal thioredoxin-like domain and is not thioredoxin-dependent. Also, it has a substrate preference for 5'-adenylylsulfate (APS) over 3'-phosphoadenylylsulfate (PAPS) so the pathway does not require an APS kinase (CysC) to convert APS to PAPS. Arabidopsis thaliana appears to have three isozymes, all able to complement E. coli CysH mutants (even in backgrounds lacking thioredoxin or APS kinase) but likely localized to different compartments in Arabidopsis. [Central intermediary metabolism, Sulfur metabolism] Pssm-ID: 273072 [Multi-domain] Cd Length: 463 Bit Score: 50.78 E-value: 1.39e-06
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MoeA | cd00887 | MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ... |
15-79 | 2.27e-05 | |||||
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: 46.72 E-value: 2.27e-05
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moaC | PRK03604 | bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional |
13-87 | 1.46e-04 | |||||
bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional Pssm-ID: 235138 [Multi-domain] Cd Length: 312 Bit Score: 43.78 E-value: 1.46e-04
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AANH-like | cd01986 | adenine nucleotide alpha hydrolase (AANH)-like proteins; This group of adenine nucleotide ... |
315-380 | 1.12e-03 | |||||
adenine nucleotide alpha hydrolase (AANH)-like proteins; This group of adenine nucleotide alpha hydrolase (AANH)-like proteins includes N-type ATP PPases and ATP sulfurylases. The domain forms an alpha/beta/alpha fold which binds to adenosine nucleotide. Pssm-ID: 467490 [Multi-domain] Cd Length: 74 Bit Score: 37.82 E-value: 1.12e-03
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PRK12563 | PRK12563 | sulfate adenylyltransferase subunit CysD; |
319-459 | 1.63e-03 | |||||
sulfate adenylyltransferase subunit CysD; Pssm-ID: 237138 Cd Length: 312 Bit Score: 40.54 E-value: 1.63e-03
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PRK13794 | PRK13794 | hypothetical protein; Provisional |
236-396 | 3.98e-03 | |||||
hypothetical protein; Provisional Pssm-ID: 237509 [Multi-domain] Cd Length: 479 Bit Score: 39.65 E-value: 3.98e-03
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Blast search parameters | ||||
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