GMP synthase [glutamine-hydrolyzing] [Plasmodium falciparum 3D7]
Protein Classification
glutamine-hydrolyzing GMP synthase( domain architecture ID 11477919)
glutamine-hydrolyzing GMP synthase catalyzes the amination of the nucleotide precursor xanthosine 5'-monophosphate to form GMP
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||||||
| guaA | PRK00074 | GMP synthase; Reviewed |
7-555 | 0e+00 | ||||||||
GMP synthase; Reviewed : Pssm-ID: 234614 [Multi-domain] Cd Length: 511 Bit Score: 753.04 E-value: 0e+00
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| Name | Accession | Description | Interval | E-value | ||||||||
| guaA | PRK00074 | GMP synthase; Reviewed |
7-555 | 0e+00 | ||||||||
GMP synthase; Reviewed Pssm-ID: 234614 [Multi-domain] Cd Length: 511 Bit Score: 753.04 E-value: 0e+00
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| GuaA2 | COG0519 | GMP synthase, PP-ATPase domain/subunit [Nucleotide transport and metabolism]; GMP synthase, ... |
7-555 | 0e+00 | ||||||||
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: 666.15 E-value: 0e+00
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| GMP_synthase_C | cd01997 | C-terminal domain of GMP synthetase (glutamine-hydrolyzing); The C-terminal domain of GMP ... |
248-555 | 1.31e-174 | ||||||||
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: 495.52 E-value: 1.31e-174
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| guaA_Cterm | TIGR00884 | GMP synthase (glutamine-hydrolyzing), C-terminal domain or B subunit; This protein of purine ... |
242-555 | 2.00e-155 | ||||||||
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: 446.79 E-value: 2.00e-155
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| GMP_synt_C | pfam00958 | GMP synthase C terminal domain; GMP synthetase is a glutamine amidotransferase from the de ... |
465-554 | 2.34e-54 | ||||||||
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: 178.37 E-value: 2.34e-54
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| Name | Accession | Description | Interval | E-value | |||||||||
| guaA | PRK00074 | GMP synthase; Reviewed |
7-555 | 0e+00 | |||||||||
GMP synthase; Reviewed Pssm-ID: 234614 [Multi-domain] Cd Length: 511 Bit Score: 753.04 E-value: 0e+00
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| GuaA2 | COG0519 | GMP synthase, PP-ATPase domain/subunit [Nucleotide transport and metabolism]; GMP synthase, ... |
7-555 | 0e+00 | |||||||||
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: 666.15 E-value: 0e+00
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| PLN02347 | PLN02347 | GMP synthetase |
2-555 | 0e+00 | |||||||||
GMP synthetase Pssm-ID: 215197 [Multi-domain] Cd Length: 536 Bit Score: 599.75 E-value: 0e+00
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| GMP_synthase_C | cd01997 | C-terminal domain of GMP synthetase (glutamine-hydrolyzing); The C-terminal domain of GMP ... |
248-555 | 1.31e-174 | |||||||||
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: 495.52 E-value: 1.31e-174
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| guaA_Cterm | TIGR00884 | GMP synthase (glutamine-hydrolyzing), C-terminal domain or B subunit; This protein of purine ... |
242-555 | 2.00e-155 | |||||||||
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: 446.79 E-value: 2.00e-155
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| GATase1_GMP_Synthase | cd01742 | Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ... |
9-225 | 7.86e-80 | |||||||||
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: 248.22 E-value: 7.86e-80
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| guaA_Nterm | TIGR00888 | GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ... |
9-232 | 4.91e-66 | |||||||||
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: 212.56 E-value: 4.91e-66
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| GMP_synt_C | pfam00958 | GMP synthase C terminal domain; GMP synthetase is a glutamine amidotransferase from the de ... |
465-554 | 2.34e-54 | |||||||||
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: 178.37 E-value: 2.34e-54
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| PRK00758 | PRK00758 | GMP synthase subunit A; Validated |
8-230 | 5.47e-47 | |||||||||
GMP synthase subunit A; Validated Pssm-ID: 179112 [Multi-domain] Cd Length: 184 Bit Score: 162.33 E-value: 5.47e-47
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| GuaA1 | COG0518 | GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ... |
8-214 | 1.38e-38 | |||||||||
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: 141.24 E-value: 1.38e-38
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| GATase | pfam00117 | Glutamine amidotransferase class-I; |
10-228 | 1.02e-33 | |||||||||
Glutamine amidotransferase class-I; Pssm-ID: 395067 [Multi-domain] Cd Length: 188 Bit Score: 126.58 E-value: 1.02e-33
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| PabA | COG0512 | Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ... |
40-224 | 1.01e-16 | |||||||||
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: 78.54 E-value: 1.01e-16
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| GATase1_1 | cd01741 | Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ... |
49-210 | 1.14e-15 | |||||||||
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: 75.36 E-value: 1.14e-15
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| GATase1_Anthranilate_Synthase | cd01743 | Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ... |
10-224 | 2.63e-13 | |||||||||
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: 68.33 E-value: 2.63e-13
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| PRK05670 | PRK05670 | anthranilate synthase component II; Provisional |
42-224 | 3.76e-12 | |||||||||
anthranilate synthase component II; Provisional Pssm-ID: 235552 [Multi-domain] Cd Length: 189 Bit Score: 65.15 E-value: 3.76e-12
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| PRK14607 | PRK14607 | bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase; |
42-226 | 7.82e-11 | |||||||||
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase; Pssm-ID: 237764 [Multi-domain] Cd Length: 534 Bit Score: 64.74 E-value: 7.82e-11
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| PRK07649 | PRK07649 | aminodeoxychorismate/anthranilate synthase component II; |
21-224 | 4.75e-10 | |||||||||
aminodeoxychorismate/anthranilate synthase component II; Pssm-ID: 181066 [Multi-domain] Cd Length: 195 Bit Score: 59.05 E-value: 4.75e-10
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| GATase1_CPSase | cd01744 | Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ... |
9-210 | 5.45e-10 | |||||||||
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: 58.66 E-value: 5.45e-10
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| PRK12564 | PRK12564 | carbamoyl-phosphate synthase small subunit; |
8-210 | 3.63e-09 | |||||||||
carbamoyl-phosphate synthase small subunit; Pssm-ID: 237139 [Multi-domain] Cd Length: 360 Bit Score: 58.55 E-value: 3.63e-09
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| trpG | CHL00101 | anthranilate synthase component 2 |
40-224 | 1.06e-08 | |||||||||
anthranilate synthase component 2 Pssm-ID: 214365 [Multi-domain] Cd Length: 190 Bit Score: 55.12 E-value: 1.06e-08
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| GATase1 | cd01653 | Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
9-97 | 3.70e-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: 51.83 E-value: 3.70e-08
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| GAT_1 | cd03128 | Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
9-93 | 1.64e-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: 1.64e-07
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| GATase1_2 | cd01745 | Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ... |
49-101 | 3.24e-07 | |||||||||
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: 50.65 E-value: 3.24e-07
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| CarA | COG0505 | Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ... |
8-107 | 9.84e-07 | |||||||||
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: 51.17 E-value: 9.84e-07
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| PuuD | COG2071 | Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ... |
52-97 | 1.15e-06 | |||||||||
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: 49.78 E-value: 1.15e-06
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| PRK08857 | PRK08857 | aminodeoxychorismate/anthranilate synthase component II; |
40-224 | 1.20e-06 | |||||||||
aminodeoxychorismate/anthranilate synthase component II; Pssm-ID: 181566 [Multi-domain] Cd Length: 193 Bit Score: 49.10 E-value: 1.20e-06
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| Peptidase_C26 | pfam07722 | Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ... |
49-210 | 2.00e-05 | |||||||||
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: 46.10 E-value: 2.00e-05
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| carA | CHL00197 | carbamoyl-phosphate synthase arginine-specific small subunit; Provisional |
8-107 | 2.15e-05 | |||||||||
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional Pssm-ID: 214392 [Multi-domain] Cd Length: 382 Bit Score: 47.10 E-value: 2.15e-05
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| PRK12838 | PRK12838 | carbamoyl phosphate synthase small subunit; Reviewed |
8-105 | 3.74e-05 | |||||||||
carbamoyl phosphate synthase small subunit; Reviewed Pssm-ID: 183784 [Multi-domain] Cd Length: 354 Bit Score: 46.04 E-value: 3.74e-05
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| PRK06774 | PRK06774 | aminodeoxychorismate synthase component II; |
17-224 | 1.74e-04 | |||||||||
aminodeoxychorismate synthase component II; Pssm-ID: 180689 [Multi-domain] Cd Length: 191 Bit Score: 42.93 E-value: 1.74e-04
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| PRK07765 | PRK07765 | aminodeoxychorismate/anthranilate synthase component II; |
52-223 | 4.84e-04 | |||||||||
aminodeoxychorismate/anthranilate synthase component II; Pssm-ID: 181107 [Multi-domain] Cd Length: 214 Bit Score: 41.57 E-value: 4.84e-04
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| AANH-like | cd01986 | adenine nucleotide alpha hydrolase (AANH)-like proteins; This group of adenine nucleotide ... |
257-300 | 5.08e-04 | |||||||||
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: 38.97 E-value: 5.08e-04
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| PRK08557 | PRK08557 | hypothetical protein; Provisional |
214-327 | 9.60e-04 | |||||||||
hypothetical protein; Provisional Pssm-ID: 181465 [Multi-domain] Cd Length: 417 Bit Score: 41.66 E-value: 9.60e-04
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| puuD | PRK11366 | gamma-glutamyl-gamma-aminobutyrate hydrolase; Provisional |
50-101 | 1.48e-03 | |||||||||
gamma-glutamyl-gamma-aminobutyrate hydrolase; Provisional Pssm-ID: 183101 [Multi-domain] Cd Length: 254 Bit Score: 40.65 E-value: 1.48e-03
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| GATase1_Glutamyl_Hydrolase | cd01747 | Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase; Type 1 ... |
50-210 | 2.39e-03 | |||||||||
Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase; Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase. gamma-Glutamyl Hydrolase catalyzes the cleavage of the gamma-glutamyl chain of folylpoly-gamma-glutamyl substrates and is a central enzyme in folyl and antifolyl poly-gamma-glutamate metabolism. GATase activity involves the removal of the ammonia group from a glutamate molecule and its subsequent transfer to a specific substrate, thus creating a new carbon-nitrogen group on the substrate. gamma-Glutamyl hydrolases belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site. Pssm-ID: 153218 [Multi-domain] Cd Length: 273 Bit Score: 40.00 E-value: 2.39e-03
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| MnmA | COG0482 | tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain [Translation, ... |
257-272 | 2.86e-03 | |||||||||
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: 40.04 E-value: 2.86e-03
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| mnmA | PRK00143 | tRNA-specific 2-thiouridylase MnmA; Reviewed |
257-272 | 8.95e-03 | |||||||||
tRNA-specific 2-thiouridylase MnmA; Reviewed Pssm-ID: 234664 [Multi-domain] Cd Length: 346 Bit Score: 38.51 E-value: 8.95e-03
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| PRK05665 | PRK05665 | amidotransferase; Provisional |
165-220 | 9.74e-03 | |||||||||
amidotransferase; Provisional Pssm-ID: 168162 [Multi-domain] Cd Length: 240 Bit Score: 37.87 E-value: 9.74e-03
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