GMP synthase [glutamine-hydrolyzing] [Homo sapiens]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||||||||
| guaA super family | cl35057 | GMP synthase; Reviewed |
28-693 | 0e+00 | ||||||||||
GMP synthase; Reviewed The actual alignment was detected with superfamily member PRK00074: Pssm-ID: 234614 [Multi-domain] Cd Length: 511 Bit Score: 525.00 E-value: 0e+00
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| Name | Accession | Description | Interval | E-value | ||||||||||
| guaA | PRK00074 | GMP synthase; Reviewed |
28-693 | 0e+00 | ||||||||||
GMP synthase; Reviewed Pssm-ID: 234614 [Multi-domain] Cd Length: 511 Bit Score: 525.00 E-value: 0e+00
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| GuaA2 | COG0519 | GMP synthase, PP-ATPase domain/subunit [Nucleotide transport and metabolism]; GMP synthase, ... |
28-693 | 7.22e-156 | ||||||||||
GMP synthase, PP-ATPase domain/subunit [Nucleotide transport and metabolism]; GMP synthase, PP-ATPase domain/subunit is part of the Pathway/BioSystem: Purine biosynthesis Pssm-ID: 440285 [Multi-domain] Cd Length: 512 Bit Score: 460.45 E-value: 7.22e-156
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| GMP_synthase_C | cd01997 | C-terminal domain of GMP synthetase (glutamine-hydrolyzing); The C-terminal domain of GMP ... |
230-693 | 4.68e-155 | ||||||||||
C-terminal domain of GMP synthetase (glutamine-hydrolyzing); The C-terminal domain of GMP synthetase (glutamine-hydrolyzing, EC 6.3.5.2) contains two subdomains: the ATP pyrophosphatase domain at the N-terminal and the dimerization domain at the C-terminal end. The ATP-PPase domain is a twisted, five-stranded parallel beta-sheet sandwiched between helical layers. It has a signature nucleotide-binding motif, or PP-loop, at the end of the first-beta strand. GMP synthetase is a homodimer, but in some archaea, it is a heterodimer made up of ATP pyrophosphatase (ATP-PPase) and a GATase subunit. In eukaryotes and bacteria, the two catalytic units are encoded by a single gene producing a two-domain-type GMP with a GATase domain in the N-terminus and an ATP-PPase domain in the C-terminus. Pssm-ID: 467501 [Multi-domain] Cd Length: 311 Bit Score: 450.45 E-value: 4.68e-155
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| guaA_Cterm | TIGR00884 | GMP synthase (glutamine-hydrolyzing), C-terminal domain or B subunit; This protein of purine ... |
225-693 | 9.87e-70 | ||||||||||
GMP synthase (glutamine-hydrolyzing), C-terminal domain or B subunit; This protein of purine de novo biosynthesis is well-conserved. However, it appears to split into two separate polypeptide chains in most of the Archaea. This C-terminal region would be the larger subunit [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis] Pssm-ID: 273321 [Multi-domain] Cd Length: 311 Bit Score: 229.92 E-value: 9.87e-70
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| GATase | pfam00117 | Glutamine amidotransferase class-I; |
29-210 | 9.57e-51 | ||||||||||
Glutamine amidotransferase class-I; Pssm-ID: 395067 [Multi-domain] Cd Length: 188 Bit Score: 174.73 E-value: 9.57e-51
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| Name | Accession | Description | Interval | E-value | ||||||||||
| guaA | PRK00074 | GMP synthase; Reviewed |
28-693 | 0e+00 | ||||||||||
GMP synthase; Reviewed Pssm-ID: 234614 [Multi-domain] Cd Length: 511 Bit Score: 525.00 E-value: 0e+00
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| GuaA2 | COG0519 | GMP synthase, PP-ATPase domain/subunit [Nucleotide transport and metabolism]; GMP synthase, ... |
28-693 | 7.22e-156 | ||||||||||
GMP synthase, PP-ATPase domain/subunit [Nucleotide transport and metabolism]; GMP synthase, PP-ATPase domain/subunit is part of the Pathway/BioSystem: Purine biosynthesis Pssm-ID: 440285 [Multi-domain] Cd Length: 512 Bit Score: 460.45 E-value: 7.22e-156
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| GMP_synthase_C | cd01997 | C-terminal domain of GMP synthetase (glutamine-hydrolyzing); The C-terminal domain of GMP ... |
230-693 | 4.68e-155 | ||||||||||
C-terminal domain of GMP synthetase (glutamine-hydrolyzing); The C-terminal domain of GMP synthetase (glutamine-hydrolyzing, EC 6.3.5.2) contains two subdomains: the ATP pyrophosphatase domain at the N-terminal and the dimerization domain at the C-terminal end. The ATP-PPase domain is a twisted, five-stranded parallel beta-sheet sandwiched between helical layers. It has a signature nucleotide-binding motif, or PP-loop, at the end of the first-beta strand. GMP synthetase is a homodimer, but in some archaea, it is a heterodimer made up of ATP pyrophosphatase (ATP-PPase) and a GATase subunit. In eukaryotes and bacteria, the two catalytic units are encoded by a single gene producing a two-domain-type GMP with a GATase domain in the N-terminus and an ATP-PPase domain in the C-terminus. Pssm-ID: 467501 [Multi-domain] Cd Length: 311 Bit Score: 450.45 E-value: 4.68e-155
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| PLN02347 | PLN02347 | GMP synthetase |
19-562 | 4.24e-127 | ||||||||||
GMP synthetase Pssm-ID: 215197 [Multi-domain] Cd Length: 536 Bit Score: 387.50 E-value: 4.24e-127
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| GATase1_GMP_Synthase | cd01742 | Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ... |
28-207 | 7.36e-98 | ||||||||||
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase. GMP synthetase is a glutamine amidotransferase from the de novo purine biosynthetic pathway. Glutamine amidotransferase (GATase) activity catalyse the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. GMP synthetase catalyses the amination of the nucleotide precursor xanthosine 5'-monophosphate to form GMP. GMP synthetase belongs to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site. Pssm-ID: 153213 [Multi-domain] Cd Length: 181 Bit Score: 298.68 E-value: 7.36e-98
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| guaA_Cterm | TIGR00884 | GMP synthase (glutamine-hydrolyzing), C-terminal domain or B subunit; This protein of purine ... |
225-693 | 9.87e-70 | ||||||||||
GMP synthase (glutamine-hydrolyzing), C-terminal domain or B subunit; This protein of purine de novo biosynthesis is well-conserved. However, it appears to split into two separate polypeptide chains in most of the Archaea. This C-terminal region would be the larger subunit [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis] Pssm-ID: 273321 [Multi-domain] Cd Length: 311 Bit Score: 229.92 E-value: 9.87e-70
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| guaA_Nterm | TIGR00888 | GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ... |
28-213 | 1.05e-68 | ||||||||||
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine de novo biosynthesis is well-conserved. However, it appears to split into two separate polypeptide chains in most of the Archaea. This N-terminal region would be the smaller subunit. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis] Pssm-ID: 129966 [Multi-domain] Cd Length: 188 Bit Score: 222.96 E-value: 1.05e-68
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| GATase | pfam00117 | Glutamine amidotransferase class-I; |
29-210 | 9.57e-51 | ||||||||||
Glutamine amidotransferase class-I; Pssm-ID: 395067 [Multi-domain] Cd Length: 188 Bit Score: 174.73 E-value: 9.57e-51
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| GuaA1 | COG0518 | GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ... |
28-210 | 1.87e-46 | ||||||||||
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP synthase, glutamine amidotransferase domain is part of the Pathway/BioSystem: Purine biosynthesis Pssm-ID: 440284 [Multi-domain] Cd Length: 225 Bit Score: 164.35 E-value: 1.87e-46
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| PRK00758 | PRK00758 | GMP synthase subunit A; Validated |
28-207 | 1.76e-36 | ||||||||||
GMP synthase subunit A; Validated Pssm-ID: 179112 [Multi-domain] Cd Length: 184 Bit Score: 134.98 E-value: 1.76e-36
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| GATase1_1 | cd01741 | Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ... |
21-207 | 5.97e-25 | ||||||||||
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group contains a subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain. GATase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. Glutamine amidotransferases (GATase) includes the triad family of amidotransferases which have a conserved Cys-His-Glu catalytic triad in the glutaminase active site. In this subgroup this triad is conserved. GATase activity can be found in a range of biosynthetic enzymes, including: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase , anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. Glutamine amidotransferase (GATase) domains can occur either as single polypeptides, as in glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase. Pssm-ID: 153212 [Multi-domain] Cd Length: 188 Bit Score: 102.32 E-value: 5.97e-25
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| GATase1_Anthranilate_Synthase | cd01743 | Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ... |
58-207 | 1.23e-19 | ||||||||||
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase (ASase). This group contains proteins similar to para-aminobenzoate (PABA) synthase and ASase. These enzymes catalyze similar reactions and produce similar products, PABA and ortho-aminobenzoate (anthranilate). Each enzyme is composed of non-identical subunits: a glutamine amidotransferase subunit (component II) and a subunit that produces an aminobenzoate products (component I). ASase catalyses the synthesis of anthranilate from chorismate and glutamine and is a tetrameric protein comprising two copies each of components I and II. Component II of ASase belongs to the family of triad GTases which hydrolyze glutamine and transfer nascent ammonia between the active sites. In some bacteria, such as Escherichia coli, component II can be much larger than in other organisms, due to the presence of phosphoribosyl-anthranilate transferase (PRTase) activity. PRTase catalyses the second step in tryptophan biosynthesis and results in the addition of 5-phosphoribosyl-1-pyrophosphate to anthranilate to create N-5'-phosphoribosyl-anthranilate. In E.coli, the first step in the conversion of chorismate to PABA involves two proteins: PabA and PabB which co-operate to transfer the amide nitrogen of glutamine to chorismate forming 4-amino-4 deoxychorismate (ADC). PabA acts as a glutamine amidotransferase, supplying an amino group to PabB, which carries out the amination reaction. A third protein PabC then mediates elimination of pyruvate and aromatization to give PABA. Several organisms have bipartite proteins containing fused domains homologous to PabA and PabB commonly called PABA synthases. These hybrid PABA synthases may produce ADC and not PABA. Pssm-ID: 153214 [Multi-domain] Cd Length: 184 Bit Score: 87.20 E-value: 1.23e-19
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| PabA | COG0512 | Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ... |
64-207 | 3.07e-19 | ||||||||||
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis Pssm-ID: 440278 [Multi-domain] Cd Length: 189 Bit Score: 85.86 E-value: 3.07e-19
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| PRK05670 | PRK05670 | anthranilate synthase component II; Provisional |
71-207 | 1.30e-17 | ||||||||||
anthranilate synthase component II; Provisional Pssm-ID: 235552 [Multi-domain] Cd Length: 189 Bit Score: 81.33 E-value: 1.30e-17
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| Peptidase_C26 | pfam07722 | Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ... |
71-192 | 3.66e-15 | ||||||||||
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze the cleavage of the gamma-glutamyl bond in poly-gamma-glutamyl substrates. They are structurally related to pfam00117, but contain extensions in four loops and at the C terminus. Pssm-ID: 429620 [Multi-domain] Cd Length: 219 Bit Score: 74.99 E-value: 3.66e-15
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| PuuD | COG2071 | Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ... |
71-192 | 8.49e-15 | ||||||||||
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains GATase1-like domain [Amino acid transport and metabolism]; Pssm-ID: 441674 [Multi-domain] Cd Length: 231 Bit Score: 74.43 E-value: 8.49e-15
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| GATase1_2 | cd01745 | Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ... |
32-192 | 5.73e-14 | ||||||||||
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group contains a subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain. GATase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. Glutamine amidotransferases (GATase) includes the triad family of amidotransferases which have a conserved Cys-His-Glu catalytic triad in the glutaminase active site. In this subgroup this triad is conserved. GATase activity can be found in a range of biosynthetic enzymes, including: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase , anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. Glutamine amidotransferase (GATase) domains can occur either as single polypeptides, as in glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase. Pssm-ID: 153216 [Multi-domain] Cd Length: 189 Bit Score: 70.68 E-value: 5.73e-14
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| GMP_synt_C | pfam00958 | GMP synthase C terminal domain; GMP synthetase is a glutamine amidotransferase from the de ... |
599-692 | 2.04e-13 | ||||||||||
GMP synthase C terminal domain; GMP synthetase is a glutamine amidotransferase from the de novo purine biosynthetic pathway. This family is the C-terminal domain specific to the GMP synthases EC:6.3.5.2. In prokaryotes this domain mediates dimerization. Eukaryotic GMP synthases are monomers. This domain in eukaryotes includes several large insertions that may form globular domains. Pssm-ID: 425963 [Multi-domain] Cd Length: 92 Bit Score: 66.28 E-value: 2.04e-13
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| PRK09065 | PRK09065 | glutamine amidotransferase; Provisional |
56-192 | 8.64e-12 | ||||||||||
glutamine amidotransferase; Provisional Pssm-ID: 181635 [Multi-domain] Cd Length: 237 Bit Score: 65.37 E-value: 8.64e-12
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| PRK08007 | PRK08007 | aminodeoxychorismate synthase component 2; |
99-207 | 1.10e-11 | ||||||||||
aminodeoxychorismate synthase component 2; Pssm-ID: 181194 [Multi-domain] Cd Length: 187 Bit Score: 64.17 E-value: 1.10e-11
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| PRK14607 | PRK14607 | bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase; |
71-208 | 1.27e-11 | ||||||||||
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase; Pssm-ID: 237764 [Multi-domain] Cd Length: 534 Bit Score: 67.43 E-value: 1.27e-11
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| PRK06895 | PRK06895 | anthranilate synthase component II; |
69-207 | 2.90e-11 | ||||||||||
anthranilate synthase component II; Pssm-ID: 235882 [Multi-domain] Cd Length: 190 Bit Score: 62.83 E-value: 2.90e-11
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| trpG | CHL00101 | anthranilate synthase component 2 |
64-207 | 5.05e-11 | ||||||||||
anthranilate synthase component 2 Pssm-ID: 214365 [Multi-domain] Cd Length: 190 Bit Score: 62.44 E-value: 5.05e-11
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| GATase1_CPSase | cd01744 | Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ... |
28-192 | 6.76e-11 | ||||||||||
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This group of sequences represents the small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II. CPSase II catalyzes the production of carbomyl phosphate (CP) from bicarbonate, glutamine and two molecules of MgATP. The reaction is believed to proceed by a series of four biochemical reactions involving a minimum of three discrete highly reactive intermediates. The synthesis of CP is critical for the initiation of two separate biosynthetic pathways. In one CP is coupled to aspartate, its carbon and nitrogen nuclei ultimately incorporated into the aromatic moieties of pyrimidine nucleotides. In the second pathway CP is condensed with ornithine at the start of the urea cycle and is utilized for the detoxification of ammonia and biosynthesis of arginine. CPSases may be encoded by one or by several genes, depending on the species. The E.coli enzyme is a heterodimer consisting of two polypeptide chains referred to as the small and large subunit. Ammonia an intermediate during the biosynthesis of carbomyl phosphate produced by the hydrolysis of glutamine in the small subunit of the enzyme is delivered via a molecular tunnel between the remotely located carboxyphosphate active site in the large subunit. CPSase IIs belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site. This group also contains the sequence from the mammalian urea cycle form which has lost the active site Cys, resulting in an ammonia-dependent form, CPSase I. Pssm-ID: 153215 [Multi-domain] Cd Length: 178 Bit Score: 61.74 E-value: 6.76e-11
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| PRK07053 | PRK07053 | glutamine amidotransferase; Provisional |
21-195 | 8.94e-11 | ||||||||||
glutamine amidotransferase; Provisional Pssm-ID: 235919 [Multi-domain] Cd Length: 234 Bit Score: 62.65 E-value: 8.94e-11
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| PRK07765 | PRK07765 | aminodeoxychorismate/anthranilate synthase component II; |
97-207 | 9.98e-11 | ||||||||||
aminodeoxychorismate/anthranilate synthase component II; Pssm-ID: 181107 [Multi-domain] Cd Length: 214 Bit Score: 61.99 E-value: 9.98e-11
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| COG1606 | COG1606 | ATP-utilizing enzyme, PP-loop superfamily [General function prediction only]; |
238-429 | 1.50e-10 | ||||||||||
ATP-utilizing enzyme, PP-loop superfamily [General function prediction only]; Pssm-ID: 441214 [Multi-domain] Cd Length: 265 Bit Score: 62.44 E-value: 1.50e-10
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| PRK13980 | PRK13980 | NAD synthetase; Provisional |
219-440 | 1.58e-10 | ||||||||||
NAD synthetase; Provisional Pssm-ID: 184435 [Multi-domain] Cd Length: 265 Bit Score: 62.15 E-value: 1.58e-10
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| PRK08857 | PRK08857 | aminodeoxychorismate/anthranilate synthase component II; |
99-207 | 2.31e-10 | ||||||||||
aminodeoxychorismate/anthranilate synthase component II; Pssm-ID: 181566 [Multi-domain] Cd Length: 193 Bit Score: 60.28 E-value: 2.31e-10
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| PRK06774 | PRK06774 | aminodeoxychorismate synthase component II; |
99-207 | 7.96e-10 | ||||||||||
aminodeoxychorismate synthase component II; Pssm-ID: 180689 [Multi-domain] Cd Length: 191 Bit Score: 58.72 E-value: 7.96e-10
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| AANH-like | cd01986 | adenine nucleotide alpha hydrolase (AANH)-like proteins; This group of adenine nucleotide ... |
239-289 | 2.19e-09 | ||||||||||
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: 54.38 E-value: 2.19e-09
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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 ... |
227-510 | 2.43e-09 | ||||||||||
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: 58.34 E-value: 2.43e-09
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| NAD_synthase | pfam02540 | NAD synthase; NAD synthase (EC:6.3.5.1) is involved in the de novo synthesis of NAD and is ... |
227-440 | 4.62e-09 | ||||||||||
NAD synthase; NAD synthase (EC:6.3.5.1) is involved in the de novo synthesis of NAD and is induced by stress factors such as heat shock and glucose limitation. Pssm-ID: 396888 [Multi-domain] Cd Length: 241 Bit Score: 57.39 E-value: 4.62e-09
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| PLN02335 | PLN02335 | anthranilate synthase |
64-207 | 1.13e-08 | ||||||||||
anthranilate synthase Pssm-ID: 177969 [Multi-domain] Cd Length: 222 Bit Score: 55.96 E-value: 1.13e-08
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| QueC-like | cd01995 | 7-cyano-7-deazaguanine synthase QueC and similar proteins; 7-cyano-7-deazaguanine synthase (EC ... |
238-432 | 1.18e-08 | ||||||||||
7-cyano-7-deazaguanine synthase QueC and similar proteins; 7-cyano-7-deazaguanine synthase (EC 6.3.4.20) is also called 7-cyano-7-carbaguanine synthase, preQ(0) synthase, or queuosine biosynthesis protein QueC. It catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)), as part of the biosynthesis pathway of queuosine (Q). Q is one of the most complex modifications occurring at the wobble position of tRNAs with GUN anticodons, and is implicated in a number of biological activities, including accuracy of decoding, virulence, and cellular differentiation. This subfamily 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: 467499 [Multi-domain] Cd Length: 208 Bit Score: 55.70 E-value: 1.18e-08
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| PRK13566 | PRK13566 | anthranilate synthase component I; |
54-205 | 1.19e-08 | ||||||||||
anthranilate synthase component I; Pssm-ID: 237429 [Multi-domain] Cd Length: 720 Bit Score: 58.39 E-value: 1.19e-08
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| GATase1_IGP_Synthase | cd01748 | Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ... |
97-207 | 1.62e-08 | ||||||||||
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate synthase (IGPS); Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate synthase (IGPS). IGPS incorporates ammonia derived from glutamine into N1-[(5'-phosphoribulosyl)-formimino]-5-aminoimidazole-4-carboxamide ribonucleotide (PRFAR) to form 5'-(5-aminoimidazole-4-carboxamide) ribonucleotide (AICAR) and imidazole glycerol phosphate (IGP). The glutamine amidotransferase domain generates the ammonia nucleophile which is channeled from the glutaminase active site to the PRFAR active site. IGPS belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site. Pssm-ID: 153219 [Multi-domain] Cd Length: 198 Bit Score: 55.20 E-value: 1.62e-08
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| hisH | PRK13181 | imidazole glycerol phosphate synthase subunit HisH; Provisional |
97-207 | 2.05e-08 | ||||||||||
imidazole glycerol phosphate synthase subunit HisH; Provisional Pssm-ID: 183878 [Multi-domain] Cd Length: 199 Bit Score: 54.87 E-value: 2.05e-08
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| LarE-like | cd01990 | Lactate racemization operon protein LarE and similar proteins; This subfamily includes ... |
238-438 | 3.55e-08 | ||||||||||
Lactate racemization operon protein LarE and similar proteins; This subfamily includes Lactiplantibacillus plantarum LarE, a sacrificial sulfur insertase of the N-type ATP pyrophosphatase family. LarE is part of the lar operon, encoding five Lar proteins (LarA-E) that collaboratively synthesize and incorporate a niacin-derived Ni-containing cofactor into LarA, an Ni-dependent lactate racemase. It catalyzes successive thiolation reactions by donating the sulfur atom of their exclusive cysteine residues to the substrate. The LarE-like subfamily belongs to the nucleotide alpha hydrolase (AANH) superfamily that includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group. Proteins from this subfamily probably binds ATP. This domain is about 200 amino acids long with a strongly conserved motif SGGxDS at the N-terminus. Pssm-ID: 467494 [Multi-domain] Cd Length: 222 Bit Score: 54.57 E-value: 3.55e-08
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| hisH | PRK13141 | imidazole glycerol phosphate synthase subunit HisH; Provisional |
97-207 | 6.07e-08 | ||||||||||
imidazole glycerol phosphate synthase subunit HisH; Provisional Pssm-ID: 237288 [Multi-domain] Cd Length: 205 Bit Score: 53.60 E-value: 6.07e-08
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| GATase1 | cd01653 | Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
28-119 | 7.18e-08 | ||||||||||
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group includes proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA. and, the A4 beta-galactosidase middle domain. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase. Pssm-ID: 153210 [Multi-domain] Cd Length: 115 Bit Score: 51.45 E-value: 7.18e-08
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| GAT_1 | cd03128 | Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
28-110 | 2.46e-07 | ||||||||||
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group contains proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA, the A4 beta-galactosidase middle domain and peptidase E. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase (CPSase), cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. Peptidase E is believed to be a serine peptidase having a Ser-His-Glu catalytic triad which differs from the Cys-His-Glu catalytic triad of typical GATase1 domains, by having a Ser in place of the reactive Cys at the nucleophile elbow. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase. Peptidase E has a circular permutation in the common core of a typical GTAse1 domain. Pssm-ID: 153222 [Multi-domain] Cd Length: 92 Bit Score: 49.12 E-value: 2.46e-07
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| PRK07649 | PRK07649 | aminodeoxychorismate/anthranilate synthase component II; |
99-207 | 2.94e-07 | ||||||||||
aminodeoxychorismate/anthranilate synthase component II; Pssm-ID: 181066 [Multi-domain] Cd Length: 195 Bit Score: 51.34 E-value: 2.94e-07
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| QueC | pfam06508 | Queuosine biosynthesis protein QueC; This family of proteins participate in the biosynthesis ... |
238-298 | 6.59e-07 | ||||||||||
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: 50.69 E-value: 6.59e-07
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| QueC | COG0603 | 7-cyano-7-deazaguanine synthase (queuosine biosynthesis) [Translation, ribosomal structure and ... |
238-298 | 8.87e-07 | ||||||||||
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: 50.55 E-value: 8.87e-07
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| PRK09522 | PRK09522 | bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate ... |
91-207 | 1.14e-06 | ||||||||||
bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate phosphoribosyltransferase TrpD; Pssm-ID: 181927 [Multi-domain] Cd Length: 531 Bit Score: 51.57 E-value: 1.14e-06
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| hisH | PRK13146 | imidazole glycerol phosphate synthase subunit HisH; Provisional |
97-207 | 1.56e-06 | ||||||||||
imidazole glycerol phosphate synthase subunit HisH; Provisional Pssm-ID: 237290 [Multi-domain] Cd Length: 209 Bit Score: 49.40 E-value: 1.56e-06
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| NadE | COG0171 | NH3-dependent NAD+ synthetase [Coenzyme transport and metabolism]; NH3-dependent NAD+ ... |
230-298 | 2.29e-06 | ||||||||||
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: 50.62 E-value: 2.29e-06
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| MnmA_TRMU-like | cd01998 | MnmA/TRMU family 2-thiouridylases and similar proteins; This family is composed of bacterial ... |
238-305 | 3.32e-06 | ||||||||||
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: 49.81 E-value: 3.32e-06
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| TilS | COG0037 | tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA ... |
237-304 | 3.52e-06 | ||||||||||
tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA(Ile)-lysidine synthase TilS/MesJ is part of the Pathway/BioSystem: tRNA modification Pssm-ID: 439807 [Multi-domain] Cd Length: 235 Bit Score: 48.68 E-value: 3.52e-06
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| HisH | COG0118 | Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ... |
97-195 | 3.56e-06 | ||||||||||
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid transport and metabolism]; Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH is part of the Pathway/BioSystem: Histidine biosynthesis Pssm-ID: 439888 [Multi-domain] Cd Length: 196 Bit Score: 48.11 E-value: 3.56e-06
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| TilS_N | cd01992 | N-terminal domain of tRNA(Ile)-lysidine synthase and similar proteins; tRNA(Ile)-lysidine ... |
238-298 | 4.24e-06 | ||||||||||
N-terminal domain of tRNA(Ile)-lysidine synthase and similar proteins; tRNA(Ile)-lysidine synthase (EC 6.3.4.19), also called tRNA(Ile)-2-lysyl-cytidine synthase or tRNA(Ile)-lysidine synthetase, catalyzes the ligation of lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine. This subfamily belongs to the adenine nucleotide alpha hydrolase superfamily that also includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to adenosine group. This domain has a strongly conserved motif SGGXD at the N-terminus. Pssm-ID: 467496 [Multi-domain] Cd Length: 185 Bit Score: 47.59 E-value: 4.24e-06
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| carA | CHL00197 | carbamoyl-phosphate synthase arginine-specific small subunit; Provisional |
16-192 | 4.97e-06 | ||||||||||
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional Pssm-ID: 214392 [Multi-domain] Cd Length: 382 Bit Score: 49.41 E-value: 4.97e-06
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| MnmA | COG0482 | tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain [Translation, ... |
238-304 | 8.57e-06 | ||||||||||
tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain [Translation, ribosomal structure and biogenesis]; tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain is part of the Pathway/BioSystem: tRNA modification Pssm-ID: 440250 [Multi-domain] Cd Length: 353 Bit Score: 48.51 E-value: 8.57e-06
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| Asn_synthase_B_C | cd01991 | C-terminal domain of asparagine synthase B; The C-terminal domain of asparagine synthase (or ... |
238-297 | 1.34e-05 | ||||||||||
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: 46.88 E-value: 1.34e-05
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| mnmA | PRK00143 | tRNA-specific 2-thiouridylase MnmA; Reviewed |
238-305 | 1.56e-05 | ||||||||||
tRNA-specific 2-thiouridylase MnmA; Reviewed Pssm-ID: 234664 [Multi-domain] Cd Length: 346 Bit Score: 47.76 E-value: 1.56e-05
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| tRNA_Me_trans | pfam03054 | tRNA methyl transferase HUP domain; This family represents the N-terminal HUP domain in tRNA ... |
238-305 | 3.95e-05 | ||||||||||
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: 45.32 E-value: 3.95e-05
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| PRK08250 | PRK08250 | glutamine amidotransferase; Provisional |
68-192 | 4.04e-05 | ||||||||||
glutamine amidotransferase; Provisional Pssm-ID: 181323 [Multi-domain] Cd Length: 235 Bit Score: 45.73 E-value: 4.04e-05
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| PAPS_reductase-like_YbdN | cd23947 | uncharacterized phosphoadenosine phosphosulfate reductase-like proteins, similar to ... |
228-429 | 4.87e-05 | ||||||||||
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: 45.07 E-value: 4.87e-05
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| PPase_ThiI | cd01712 | pyrophosphatase domain of thiamine biosynthesis protein ThiI; ThiI is required for thiazole ... |
234-438 | 3.19e-04 | ||||||||||
pyrophosphatase domain of thiamine biosynthesis protein ThiI; ThiI is required for thiazole synthesis in the thiamine biosynthesis pathway. ThiI is also responsible for the 4-thiouridine (S4U) modification at position 8 in some prokaryotic tRNAs. ThiI contains a PP-loop pyrophosphatase domain which binds ATP and activates tRNA by adenylation. The PP-loop pyrophosphatase catalytic domain of ThiI proteins is always accompanied by a THUMP domain towards the N terminus. THUMP domains are predicted to bind RNA and are widespread in bacteria, archaea, and eukaryotes. The acronym was derived from the names of RNA-modifying enzymes in which this domain is found, namely, thiouridine synthases (ThiI), methylases, and archaeal pseudouridine synthases. ThiI proteins from gamma-proteobacteria and from archaea of the genus Thermoplasma also contain a C-terminal extension of approximately 100 amino acid residues which accepts sulfur in the form of a persulfide on a cysteine residue. This persulfide is responsible for a nucleophilic attack of the adenylated tRNA substrate, completing the sulfur insertion forming a disulfide-bridge between the rhodanese-like domain and a second cysteine residue located in the PP-loop domain. The reaction releases AMP and modified tRNA, and leaves the enzyme in an oxidized state. The disulfide is then reductively cleaved to complete the enzymatic cycle. The pyrophosphatase domain of ThiI belongs to the adenine nucleotide hydrolase (AANH) superfamily and it binds to adenosine nucleotide. Pssm-ID: 467485 [Multi-domain] Cd Length: 185 Bit Score: 42.15 E-value: 3.19e-04
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| CarA | COG0505 | Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ... |
28-192 | 4.06e-04 | ||||||||||
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase small subunit is part of the Pathway/BioSystem: Arginine biosynthesis Pssm-ID: 440271 [Multi-domain] Cd Length: 361 Bit Score: 43.09 E-value: 4.06e-04
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| lysidine_TilS_N | TIGR02432 | tRNA(Ile)-lysidine synthetase, N-terminal domain; The only examples in which the wobble ... |
238-298 | 4.62e-04 | ||||||||||
tRNA(Ile)-lysidine synthetase, N-terminal domain; The only examples in which the wobble position of a tRNA must discriminate between G and A of mRNA are AUA (Ile) vs. AUG (Met) and UGA (stop) vs. UGG (Trp). In all bacteria, the wobble position of the tRNA(Ile) recognizing AUA is lysidine, a lysine derivative of cytidine. This family describes a protein domain found, apparently, in all bacteria in a single copy. Eukaryotic sequences appear to be organellar. The domain archictecture of this protein family is variable; some, including characterized proteins of E. coli and B. subtilis known to be tRNA(Ile)-lysidine synthetase, include a conserved 50-residue domain that many other members lack. This protein belongs to the ATP-binding PP-loop family ( pfam01171). It appears in the literature and protein databases as TilS, YacA, and putative cell cycle protein MesJ (a misnomer). [Protein synthesis, tRNA and rRNA base modification] Pssm-ID: 274129 [Multi-domain] Cd Length: 189 Bit Score: 41.85 E-value: 4.62e-04
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| TIGR00364 | TIGR00364 | queuosine biosynthesis protein QueC; Members of this protein family are QueC, involved in ... |
240-298 | 5.60e-04 | ||||||||||
queuosine biosynthesis protein QueC; Members of this protein family are QueC, involved in synthesizing pre-Q0 from GTP en route to tRNA modification with queuosine. This protein family is represented by a single member in nearly every completed large (> 1000 genes) prokaryotic genome. In Rhizobium meliloti, the gene was designated exsB, possibly because of polar effects on exsA expression in a shared polycistronic mRNA. In Arthrobacter viscosus, the homologous gene was designated ALU1 and was associated with an aluminum tolerance phenotype. [Unknown function, General] Pssm-ID: 129461 [Multi-domain] Cd Length: 201 Bit Score: 41.61 E-value: 5.60e-04
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| PRK12838 | PRK12838 | carbamoyl phosphate synthase small subunit; Reviewed |
28-192 | 8.53e-04 | ||||||||||
carbamoyl phosphate synthase small subunit; Reviewed Pssm-ID: 183784 [Multi-domain] Cd Length: 354 Bit Score: 42.19 E-value: 8.53e-04
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| trmU | TIGR00420 | tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase; tRNA ... |
238-305 | 1.35e-03 | ||||||||||
tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase; tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase (trmU, asuE, or mnmA) is involved in the biosynthesis of the modified nucleoside 5-methylaminomethyl-2-thiouridine (mnm5s2U34) present in the wobble position of some tRNAs. This enzyme appears not to occur in the Archaea. [Protein synthesis, tRNA and rRNA base modification] Pssm-ID: 273069 [Multi-domain] Cd Length: 352 Bit Score: 41.60 E-value: 1.35e-03
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| nadE | PRK00876 | NAD(+) synthase; |
239-280 | 2.07e-03 | ||||||||||
NAD(+) synthase; Pssm-ID: 179150 [Multi-domain] Cd Length: 326 Bit Score: 40.71 E-value: 2.07e-03
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| PRK06490 | PRK06490 | glutamine amidotransferase; Provisional |
73-193 | 3.10e-03 | ||||||||||
glutamine amidotransferase; Provisional Pssm-ID: 180590 [Multi-domain] Cd Length: 239 Bit Score: 39.94 E-value: 3.10e-03
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| hisH | PRK13152 | imidazole glycerol phosphate synthase subunit HisH; Provisional |
98-207 | 3.29e-03 | ||||||||||
imidazole glycerol phosphate synthase subunit HisH; Provisional Pssm-ID: 171876 [Multi-domain] Cd Length: 201 Bit Score: 39.44 E-value: 3.29e-03
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| GATase1_CobQ | cd01750 | Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ); Type ... |
71-110 | 5.55e-03 | ||||||||||
Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ); Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ). CobQ plays a role in cobalamin biosythesis. CobQ catalyses amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide in the biosynthesis of cobalamin. CobQ belongs to the triad family of amidotransferases. Two of the three residues of the catalytic triad that are involved in glutamine binding, hydrolysis and transfer of the resulting ammonia to the acceptor substrate in other triad aminodotransferases are conserved in CobQ. Pssm-ID: 153221 [Multi-domain] Cd Length: 194 Bit Score: 38.77 E-value: 5.55e-03
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| TtuA-like | cd01993 | tRNA-5-methyluridine(54) 2-sulfurtransferase and similar proteins; tRNA-5-methyluridine(54) ... |
236-307 | 5.65e-03 | ||||||||||
tRNA-5-methyluridine(54) 2-sulfurtransferase and similar proteins; tRNA-5-methyluridine(54) 2-sulfurtransferase, also called tRNA thiouridine synthetase TtuA, catalyzes the ATP-dependent 2-thiolation of 5-methyluridine residue at position 54 in the T loop of tRNAs, leading to 5-methyl-2-thiouridine (m(5)s(2)U or s(2)T). TtuA belongs to the adenine nucleotide alpha hydrolase superfamily (AANH) that includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group. This domain has a strongly conserved motif SGGKD at the N-terminus. Pssm-ID: 467497 [Multi-domain] Cd Length: 190 Bit Score: 38.46 E-value: 5.65e-03
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| PRK13820 | PRK13820 | argininosuccinate synthase; Provisional |
235-303 | 9.21e-03 | ||||||||||
argininosuccinate synthase; Provisional Pssm-ID: 237521 Cd Length: 394 Bit Score: 39.14 E-value: 9.21e-03
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