asparagine synthetase [glutamine-hydrolyzing] isoform b [Homo sapiens]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||||||
| asnB super family | cl35830 | asparagine synthetase B; Provisional |
2-534 | 0e+00 | |||||||||
asparagine synthetase B; Provisional The actual alignment was detected with superfamily member PRK09431: Pssm-ID: 236513 [Multi-domain] Cd Length: 554 Bit Score: 539.11 E-value: 0e+00
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| Name | Accession | Description | Interval | E-value | |||||||||
| asnB | PRK09431 | asparagine synthetase B; Provisional |
2-534 | 0e+00 | |||||||||
asparagine synthetase B; Provisional Pssm-ID: 236513 [Multi-domain] Cd Length: 554 Bit Score: 539.11 E-value: 0e+00
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| asn_synth_AEB | TIGR01536 | asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing ... |
1-449 | 0e+00 | |||||||||
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing asparagine synthase. A poorly conserved C-terminal extension was removed from the model. Bacterial members of the family tend to have a long, poorly conserved insert lacking from archaeal and eukaryotic sequences. Multiple isozymes have been demonstrated, such as in Bacillus subtilis. Long-branch members of the phylogenetic tree (which typically were also second or third candidate members from their genomes) were removed from the seed alignment and score below trusted cutoff. [Amino acid biosynthesis, Aspartate family] Pssm-ID: 273676 [Multi-domain] Cd Length: 466 Bit Score: 526.90 E-value: 0e+00
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| AsnB | COG0367 | Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
2-517 | 7.06e-122 | |||||||||
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; Asparagine synthetase B (glutamine-hydrolyzing) is part of the Pathway/BioSystem: Asparagine biosynthesis Pssm-ID: 440136 [Multi-domain] Cd Length: 558 Bit Score: 369.55 E-value: 7.06e-122
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| Asn_synthase | pfam00733 | Asparagine synthase; This family is always found associated with pfam00310. Members of this ... |
213-517 | 1.06e-92 | |||||||||
Asparagine synthase; This family is always found associated with pfam00310. Members of this family catalyze the conversion of aspartate to asparagine. Pssm-ID: 395594 [Multi-domain] Cd Length: 279 Bit Score: 284.51 E-value: 1.06e-92
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| Asn_synthase_B_C | cd01991 | C-terminal domain of asparagine synthase B; The C-terminal domain of asparagine synthase (or ... |
228-452 | 2.41e-75 | |||||||||
C-terminal domain of asparagine synthase B; The C-terminal domain of asparagine synthase (or synthetase) B is always associated with an N-terminal amidotransferase domain. Family members that contain this domain catalyze the conversion of aspartate to asparagine. Asparagine synthase B catalyzes the synthesis of asparagine from aspartate, Mg(2+)ATP, and glutamine. The three-dimensional architecture of the N-terminal domain of asparagine synthetase B is similar to that observed for glutamine phosphoribosylpyrophosphate amidotransferase while the molecular motif of the C-domain is reminiscent to that observed for GMP synthetase. Pssm-ID: 467495 [Multi-domain] Cd Length: 224 Bit Score: 237.94 E-value: 2.41e-75
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| Name | Accession | Description | Interval | E-value | |||||||||
| asnB | PRK09431 | asparagine synthetase B; Provisional |
2-534 | 0e+00 | |||||||||
asparagine synthetase B; Provisional Pssm-ID: 236513 [Multi-domain] Cd Length: 554 Bit Score: 539.11 E-value: 0e+00
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| asn_synth_AEB | TIGR01536 | asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing ... |
1-449 | 0e+00 | |||||||||
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing asparagine synthase. A poorly conserved C-terminal extension was removed from the model. Bacterial members of the family tend to have a long, poorly conserved insert lacking from archaeal and eukaryotic sequences. Multiple isozymes have been demonstrated, such as in Bacillus subtilis. Long-branch members of the phylogenetic tree (which typically were also second or third candidate members from their genomes) were removed from the seed alignment and score below trusted cutoff. [Amino acid biosynthesis, Aspartate family] Pssm-ID: 273676 [Multi-domain] Cd Length: 466 Bit Score: 526.90 E-value: 0e+00
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| PLN02549 | PLN02549 | asparagine synthase (glutamine-hydrolyzing) |
5-540 | 2.29e-152 | |||||||||
asparagine synthase (glutamine-hydrolyzing) Pssm-ID: 178164 [Multi-domain] Cd Length: 578 Bit Score: 448.44 E-value: 2.29e-152
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| PTZ00077 | PTZ00077 | asparagine synthetase-like protein; Provisional |
2-539 | 1.77e-149 | |||||||||
asparagine synthetase-like protein; Provisional Pssm-ID: 185431 [Multi-domain] Cd Length: 586 Bit Score: 441.08 E-value: 1.77e-149
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| AsnB | COG0367 | Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
2-517 | 7.06e-122 | |||||||||
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; Asparagine synthetase B (glutamine-hydrolyzing) is part of the Pathway/BioSystem: Asparagine biosynthesis Pssm-ID: 440136 [Multi-domain] Cd Length: 558 Bit Score: 369.55 E-value: 7.06e-122
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| Asn_synthase | pfam00733 | Asparagine synthase; This family is always found associated with pfam00310. Members of this ... |
213-517 | 1.06e-92 | |||||||||
Asparagine synthase; This family is always found associated with pfam00310. Members of this family catalyze the conversion of aspartate to asparagine. Pssm-ID: 395594 [Multi-domain] Cd Length: 279 Bit Score: 284.51 E-value: 1.06e-92
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| Asn_synthase_B_C | cd01991 | C-terminal domain of asparagine synthase B; The C-terminal domain of asparagine synthase (or ... |
228-452 | 2.41e-75 | |||||||||
C-terminal domain of asparagine synthase B; The C-terminal domain of asparagine synthase (or synthetase) B is always associated with an N-terminal amidotransferase domain. Family members that contain this domain catalyze the conversion of aspartate to asparagine. Asparagine synthase B catalyzes the synthesis of asparagine from aspartate, Mg(2+)ATP, and glutamine. The three-dimensional architecture of the N-terminal domain of asparagine synthetase B is similar to that observed for glutamine phosphoribosylpyrophosphate amidotransferase while the molecular motif of the C-domain is reminiscent to that observed for GMP synthetase. Pssm-ID: 467495 [Multi-domain] Cd Length: 224 Bit Score: 237.94 E-value: 2.41e-75
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| AsnB | cd00712 | Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ... |
1-185 | 5.81e-55 | |||||||||
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine synthetase B catalyses the ATP-dependent conversion of aspartate to asparagine. This enzyme is a homodimer, with each monomer composed of a glutaminase domain and a synthetase domain. The N-terminal glutaminase domain hydrolyzes glutamine to glutamic acid and ammonia. Pssm-ID: 238364 [Multi-domain] Cd Length: 220 Bit Score: 184.30 E-value: 5.81e-55
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| Gn_AT_II | cd00352 | Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
1-164 | 9.06e-33 | |||||||||
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide nitrogen transfer from glutamine to the appropriate substrate. In this process, glutamine is hydrolyzed to glutamic acid and ammonia. This domain is related to members of the Ntn (N-terminal nucleophile) hydrolase superfamily and is found at the N-terminus of enzymes such as glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), beta lactam synthetase (beta-LS) and glutamate synthase (GltS). GLMS catalyzes the formation of glucosamine 6-phosphate from fructose 6-phosphate and glutamine in amino sugar synthesis. GPATase catalyzes the first step in purine biosynthesis, an amide transfer from glutamine to PRPP, resulting in phosphoribosylamine, pyrophosphate and glutamate. Asparagine synthetase B synthesizes asparagine from aspartate and glutamine. Beta-LS catalyzes the formation of the beta-lactam ring in the beta-lactamase inhibitor clavulanic acid. GltS synthesizes L-glutamate from 2-oxoglutarate and L-glutamine. These enzymes are generally dimers, but GPATase also exists as a homotetramer. Pssm-ID: 238212 [Multi-domain] Cd Length: 220 Bit Score: 124.87 E-value: 9.06e-33
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| GATase_7 | pfam13537 | Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
28-143 | 7.70e-31 | |||||||||
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain found in a variety of enzymes such as asparagine synthetase and glutamine-fructose-6-phosphate transaminase. Pssm-ID: 433289 [Multi-domain] Cd Length: 123 Bit Score: 116.08 E-value: 7.70e-31
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| GATase_6 | pfam13522 | Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
8-134 | 2.20e-17 | |||||||||
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain found in a variety of enzymes, such as asparagine synthetase and glutamine--fructose-6-phosphate transaminase. Pssm-ID: 433279 [Multi-domain] Cd Length: 130 Bit Score: 78.50 E-value: 2.20e-17
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| Gn_AT_II_novel | cd03766 | Gn_AT_II_novel. This asparagine synthase-related domain is present in eukaryotes but its ... |
3-158 | 1.81e-13 | |||||||||
Gn_AT_II_novel. This asparagine synthase-related domain is present in eukaryotes but its function has not yet been determined. The glutaminase domain catalyzes an amide nitrogen transfer from glutamine to the appropriate substrate. In this process, glutamine is hydrolyzed to glutamic acid and ammonia. This domain is related to members of the Ntn (N-terminal nucleophile) hydrolase superfamily and is found at the N-terminus of enzymes such as glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), beta lactam synthetase (beta-LS) and glutamate synthase (GltS). GLMS catalyzes the formation of glucosamine 6-phosphate from fructose 6-phosphate and glutamine in amino sugar synthesis. GPATase catalyzes the first step in purine biosynthesis, an amide transfer from glutamine to PRPP, resulting in phosphoribosylamine, pyrophosphate and glutamate. Asparagine synthetase B synthesizes asparagine from aspartate and glutamine. Beta-LS catalyzes the formation of the beta-lactam ring in the beta-lactamase inhibitor clavulanic acid. GltS synthesizes L-glutamate from 2-oxoglutarate and L-glutamine. These enzymes are generally dimers, but GPATase also exists as a homotetramer. Pssm-ID: 239735 [Multi-domain] Cd Length: 181 Bit Score: 68.85 E-value: 1.81e-13
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| PRK05793 | PRK05793 | amidophosphoribosyltransferase; Provisional |
35-146 | 7.71e-08 | |||||||||
amidophosphoribosyltransferase; Provisional Pssm-ID: 235611 [Multi-domain] Cd Length: 469 Bit Score: 54.65 E-value: 7.71e-08
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| PurF | COG0034 | Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ... |
39-139 | 4.00e-07 | |||||||||
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; Glutamine phosphoribosylpyrophosphate amidotransferase is part of the Pathway/BioSystem: Purine biosynthesis Pssm-ID: 439804 [Multi-domain] Cd Length: 464 Bit Score: 52.72 E-value: 4.00e-07
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| DUF3700 | pfam12481 | Aluminium induced protein; This domain family is found in eukaryotes, and is approximately 120 ... |
90-153 | 6.06e-05 | |||||||||
Aluminium induced protein; This domain family is found in eukaryotes, and is approximately 120 amino acids in length. There are two conserved sequence motifs: YGL and LRDR. This family is related to GATase enzyme domains. Pssm-ID: 403619 [Multi-domain] Cd Length: 228 Bit Score: 44.66 E-value: 6.06e-05
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| GPATase_N | cd00715 | Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ... |
39-139 | 8.44e-05 | |||||||||
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the N-terminus of glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase) . The glutaminase domain catalyzes amide nitrogen transfer from glutamine to the appropriate substrate. In this process, glutamine is hydrolyzed to glutamic acid and ammonia. GPATase catalyzes the first step in purine biosynthesis, an amide transfer from glutamine to PRPP, resulting in phosphoribosylamine, pyrophosphate and glutamate. GPATase crystalizes as a homotetramer, but can also exist as a homdimer. Pssm-ID: 238367 [Multi-domain] Cd Length: 252 Bit Score: 44.37 E-value: 8.44e-05
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| Wali7 | cd01910 | This domain is present in Wali7, a protein of unknown function, expressed in wheat and induced ... |
90-140 | 9.21e-05 | |||||||||
This domain is present in Wali7, a protein of unknown function, expressed in wheat and induced by aluminum. Wali7 has a single domain similar to the glutamine amidotransferase domain of glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), beta lactam synthetase (beta-LS) and glutamate synthase (GltS). The Wali7 domain is also somewhat similar to the Ntn hydrolase fold of the proteasomal alph and beta subunits. Pssm-ID: 238891 [Multi-domain] Cd Length: 224 Bit Score: 43.84 E-value: 9.21e-05
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| MnmA_TRMU-like | cd01998 | MnmA/TRMU family 2-thiouridylases and similar proteins; This family is composed of bacterial ... |
231-297 | 1.23e-04 | |||||||||
MnmA/TRMU family 2-thiouridylases and similar proteins; This family is composed of bacterial tRNA-specific 2-thiouridylase MnmA (EC 2.8.1.13) and mitochondrial tRNA-specific 2-thiouridylase 1 (TRMU or MTU1, EC 2.8.1.14). MnmA catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34. TRMU/MTU1 catalyzes the 2-thiolation of uridine at the wobble position (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln); this is required for the formation of 5-taurinomethyl-2-thiouridine (tm5s2U) of mitochondrial tRNA(Lys), tRNA(Glu), and tRNA(Gln) at the wobble position. This family belongs to the adenine nucleotide alpha hydrolase (AANH) superfamily that also includes other N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group. Pssm-ID: 467502 [Multi-domain] Cd Length: 349 Bit Score: 44.42 E-value: 1.23e-04
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| QueC | pfam06508 | Queuosine biosynthesis protein QueC; This family of proteins participate in the biosynthesis ... |
234-292 | 2.94e-04 | |||||||||
Queuosine biosynthesis protein QueC; This family of proteins participate in the biosynthesis of 7-carboxy-7-deazaguanine. They catalyze the conversion of 7-deaza-7-carboxyguanine to preQ0. Pssm-ID: 428982 [Multi-domain] Cd Length: 210 Bit Score: 42.22 E-value: 2.94e-04
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| tRNA_Me_trans | pfam03054 | tRNA methyl transferase HUP domain; This family represents the N-terminal HUP domain in tRNA ... |
230-294 | 1.22e-03 | |||||||||
tRNA methyl transferase HUP domain; This family represents the N-terminal HUP domain in tRNA(5-methylaminomethyl-2-thiouridine)-methyltransferase which is involved in the biosynthesis of the modified nucleoside 5-methylaminomethyl-2-thiouridine present in the wobble position of some tRNAs. Pssm-ID: 460787 [Multi-domain] Cd Length: 202 Bit Score: 40.31 E-value: 1.22e-03
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| NAD_synthase | cd00553 | NAD(+) synthase; NAD(+) synthase (EC 6.3.5.1), a homodimer, catalyzes the final step in the de ... |
236-292 | 1.72e-03 | |||||||||
NAD(+) synthase; NAD(+) synthase (EC 6.3.5.1), a homodimer, catalyzes the final step in the de novo nicotinamide adenine dinucleotide (NAD(+)) biosynthesis, an amide transfer from either ammonia or glutamine to nicotinic acid adenine dinucleotide (NaAD). The conversion of NaAD to NAD(+) occurs via a NAD-adenylate intermediate and requires ATP and Mg(2+). The intermediate is subsequently cleaved into NAD(+) and AMP. In many prokaryotes, such as Escherichia coli, NAD synthase consists of a single domain and is strictly ammonia dependent. In contrast, eukaryotes and other prokaryotes have an additional N-terminal amidohydrolase domain that prefer glutamine. Interestingly, NAD(+) synthases in these prokaryotes, can also utilize ammonia as an amide source. Pssm-ID: 467484 [Multi-domain] Cd Length: 248 Bit Score: 40.23 E-value: 1.72e-03
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| QueC | COG0603 | 7-cyano-7-deazaguanine synthase (queuosine biosynthesis) [Translation, ribosomal structure and ... |
234-292 | 6.53e-03 | |||||||||
7-cyano-7-deazaguanine synthase (queuosine biosynthesis) [Translation, ribosomal structure and biogenesis]; 7-cyano-7-deazaguanine synthase (queuosine biosynthesis) is part of the Pathway/BioSystem: tRNA modification Pssm-ID: 440368 [Multi-domain] Cd Length: 223 Bit Score: 38.22 E-value: 6.53e-03
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| NadE | COG0171 | NH3-dependent NAD+ synthetase [Coenzyme transport and metabolism]; NH3-dependent NAD+ ... |
236-326 | 8.35e-03 | |||||||||
NH3-dependent NAD+ synthetase [Coenzyme transport and metabolism]; NH3-dependent NAD+ synthetase is part of the Pathway/BioSystem: NAD biosynthesis Pssm-ID: 439941 [Multi-domain] Cd Length: 542 Bit Score: 38.67 E-value: 8.35e-03
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