CTP synthase [Streptococcus thermophilus]
Protein Classification
CTP synthase( domain architecture ID 11480813)
cytidine triphosphate (CTP) synthase catalyzes the conversion of UTP to CTP in the last committed step in pyrimidine nucleotide biosynthesis
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||||||
| pyrG | PRK05380 | CTP synthetase; Validated |
1-534 | 0e+00 | ||||||||
CTP synthetase; Validated : Pssm-ID: 235437 [Multi-domain] Cd Length: 533 Bit Score: 1102.00 E-value: 0e+00
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| Name | Accession | Description | Interval | E-value | ||||||||
| pyrG | PRK05380 | CTP synthetase; Validated |
1-534 | 0e+00 | ||||||||
CTP synthetase; Validated Pssm-ID: 235437 [Multi-domain] Cd Length: 533 Bit Score: 1102.00 E-value: 0e+00
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| PyrG | COG0504 | CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase ... |
2-534 | 0e+00 | ||||||||
CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase (UTP-ammonia lyase) is part of the Pathway/BioSystem: Pyrimidine biosynthesis Pssm-ID: 440270 [Multi-domain] Cd Length: 535 Bit Score: 1093.51 E-value: 0e+00
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| PyrG | TIGR00337 | CTP synthase; CTP synthase is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. ... |
2-528 | 0e+00 | ||||||||
CTP synthase; CTP synthase is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. The enzyme catalyzes the reaction L-glutamine + H2O + UTP + ATP = CTP + phosphate + ADP + L-glutamate. The enzyme exists as a dimer of identical chains that aggregates as a tetramer. This gene has been found circa 500 bp 5' upstream of enolase in both beta (Nitrosomonas europaea) and gamma (E.coli) subdivisions of proteobacterium (FEMS Microbiol Lett 1998 Aug 1;165(1):153-7). [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis] Pssm-ID: 273021 [Multi-domain] Cd Length: 525 Bit Score: 895.53 E-value: 0e+00
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| CTP_synth_N | pfam06418 | CTP synthase N-terminus; This family consists of the N-terminal region of the CTP synthase ... |
3-267 | 0e+00 | ||||||||
CTP synthase N-terminus; This family consists of the N-terminal region of the CTP synthase protein (EC:6.3.4.2). This family is found in conjunction with pfam00117 located in the C-terminal region of the protein. CTP synthase catalyzes the synthesis of CTP from UTP by amination of the pyrimidine ring at the 4-position. Pssm-ID: 461903 Cd Length: 265 Bit Score: 575.83 E-value: 0e+00
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| CTPS_N | cd03113 | N-terminal domain of cytidine 5'-triphosphate synthase; Cytidine 5'-triphosphate synthase ... |
3-263 | 0e+00 | ||||||||
N-terminal domain of cytidine 5'-triphosphate synthase; Cytidine 5'-triphosphate synthase (CTPS) is a two-domain protein, which consists of an N-terminal synthetase domain and C-terminal glutaminase domain. The enzymes hydrolyze the amide bond of glutamine to ammonia and glutamate at the glutaminase domains and transfer nascent ammonia to the acceptor substrate at the synthetase domain to form an aminated product. Pssm-ID: 349767 Cd Length: 261 Bit Score: 508.95 E-value: 0e+00
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| Name | Accession | Description | Interval | E-value | ||||||||
| pyrG | PRK05380 | CTP synthetase; Validated |
1-534 | 0e+00 | ||||||||
CTP synthetase; Validated Pssm-ID: 235437 [Multi-domain] Cd Length: 533 Bit Score: 1102.00 E-value: 0e+00
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| PyrG | COG0504 | CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase ... |
2-534 | 0e+00 | ||||||||
CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase (UTP-ammonia lyase) is part of the Pathway/BioSystem: Pyrimidine biosynthesis Pssm-ID: 440270 [Multi-domain] Cd Length: 535 Bit Score: 1093.51 E-value: 0e+00
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| PyrG | TIGR00337 | CTP synthase; CTP synthase is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. ... |
2-528 | 0e+00 | ||||||||
CTP synthase; CTP synthase is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. The enzyme catalyzes the reaction L-glutamine + H2O + UTP + ATP = CTP + phosphate + ADP + L-glutamate. The enzyme exists as a dimer of identical chains that aggregates as a tetramer. This gene has been found circa 500 bp 5' upstream of enolase in both beta (Nitrosomonas europaea) and gamma (E.coli) subdivisions of proteobacterium (FEMS Microbiol Lett 1998 Aug 1;165(1):153-7). [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis] Pssm-ID: 273021 [Multi-domain] Cd Length: 525 Bit Score: 895.53 E-value: 0e+00
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| PLN02327 | PLN02327 | CTP synthase |
2-529 | 0e+00 | ||||||||
CTP synthase Pssm-ID: 215186 [Multi-domain] Cd Length: 557 Bit Score: 678.67 E-value: 0e+00
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| CTP_synth_N | pfam06418 | CTP synthase N-terminus; This family consists of the N-terminal region of the CTP synthase ... |
3-267 | 0e+00 | ||||||||
CTP synthase N-terminus; This family consists of the N-terminal region of the CTP synthase protein (EC:6.3.4.2). This family is found in conjunction with pfam00117 located in the C-terminal region of the protein. CTP synthase catalyzes the synthesis of CTP from UTP by amination of the pyrimidine ring at the 4-position. Pssm-ID: 461903 Cd Length: 265 Bit Score: 575.83 E-value: 0e+00
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| CTPS_N | cd03113 | N-terminal domain of cytidine 5'-triphosphate synthase; Cytidine 5'-triphosphate synthase ... |
3-263 | 0e+00 | ||||||||
N-terminal domain of cytidine 5'-triphosphate synthase; Cytidine 5'-triphosphate synthase (CTPS) is a two-domain protein, which consists of an N-terminal synthetase domain and C-terminal glutaminase domain. The enzymes hydrolyze the amide bond of glutamine to ammonia and glutamate at the glutaminase domains and transfer nascent ammonia to the acceptor substrate at the synthetase domain to form an aminated product. Pssm-ID: 349767 Cd Length: 261 Bit Score: 508.95 E-value: 0e+00
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| GATase1_CTP_Synthase | cd01746 | Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase; ... |
292-526 | 4.43e-136 | ||||||||
Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase; Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase (CTP). CTP is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. CTPs produce CTP from UTP and glutamine and regulate intracellular CTP levels through interactions with four ribonucleotide triphosphates. The enzyme exists as a dimer of identical chains that aggregates as a tetramer. CTP is derived form UTP in three separate steps involving two active sites. In one active site, the UTP O4 oxygen is activated by Mg-ATP-dependent phosphorylation, followed by displacement of the resulting 4-phosphate moiety by ammonia. At a separate site, ammonia is generated via rate limiting glutamine hydrolysis (glutaminase) activity. A gated channel that spans between the glutamine hydrolysis and amidoligase active sites provides a path for ammonia diffusion. CTPs belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site. Pssm-ID: 153217 [Multi-domain] Cd Length: 235 Bit Score: 393.46 E-value: 4.43e-136
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| GATase | pfam00117 | Glutamine amidotransferase class-I; |
304-526 | 4.60e-44 | ||||||||
Glutamine amidotransferase class-I; Pssm-ID: 395067 [Multi-domain] Cd Length: 188 Bit Score: 154.32 E-value: 4.60e-44
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| PRK06186 | PRK06186 | hypothetical protein; Validated |
290-531 | 3.58e-38 | ||||||||
hypothetical protein; Validated Pssm-ID: 180452 [Multi-domain] Cd Length: 229 Bit Score: 139.71 E-value: 3.58e-38
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| GATase1 | cd01653 | Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
293-402 | 3.86e-14 | ||||||||
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: 68.78 E-value: 3.86e-14
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| GAT_1 | cd03128 | Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
293-386 | 2.93e-13 | ||||||||
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: 65.68 E-value: 2.93e-13
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| PuuD | COG2071 | Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ... |
336-529 | 1.00e-11 | ||||||||
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: 64.80 E-value: 1.00e-11
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| Peptidase_C26 | pfam07722 | Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ... |
328-510 | 2.96e-09 | ||||||||
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: 57.27 E-value: 2.96e-09
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| HisH | COG0118 | Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ... |
308-386 | 2.90e-07 | ||||||||
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: 50.81 E-value: 2.90e-07
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| GATase1_2 | cd01745 | Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ... |
334-526 | 6.43e-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: 49.88 E-value: 6.43e-07
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| GATase1_IGP_Synthase | cd01748 | Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ... |
308-386 | 1.30e-06 | ||||||||
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: 49.03 E-value: 1.30e-06
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| hisH | PRK13141 | imidazole glycerol phosphate synthase subunit HisH; Provisional |
308-386 | 4.05e-06 | ||||||||
imidazole glycerol phosphate synthase subunit HisH; Provisional Pssm-ID: 237288 [Multi-domain] Cd Length: 205 Bit Score: 47.82 E-value: 4.05e-06
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| hisH | PRK13146 | imidazole glycerol phosphate synthase subunit HisH; Provisional |
308-386 | 4.41e-06 | ||||||||
imidazole glycerol phosphate synthase subunit HisH; Provisional Pssm-ID: 237290 [Multi-domain] Cd Length: 209 Bit Score: 47.85 E-value: 4.41e-06
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| guaA_Nterm | TIGR00888 | GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ... |
331-526 | 5.21e-06 | ||||||||
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: 47.31 E-value: 5.21e-06
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| GuaA1 | COG0518 | GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ... |
343-386 | 8.26e-06 | ||||||||
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: 47.25 E-value: 8.26e-06
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| hisH | PRK13181 | imidazole glycerol phosphate synthase subunit HisH; Provisional |
340-388 | 2.28e-05 | ||||||||
imidazole glycerol phosphate synthase subunit HisH; Provisional Pssm-ID: 183878 [Multi-domain] Cd Length: 199 Bit Score: 45.24 E-value: 2.28e-05
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| hisH | PRK13143 | imidazole glycerol phosphate synthase subunit HisH; Provisional |
343-386 | 2.37e-05 | ||||||||
imidazole glycerol phosphate synthase subunit HisH; Provisional Pssm-ID: 237289 [Multi-domain] Cd Length: 200 Bit Score: 45.24 E-value: 2.37e-05
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| GATase1_FGAR_AT | cd01740 | Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ... |
329-386 | 3.45e-05 | ||||||||
Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ribonucleotide amidotransferase; Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ribonucleotide amidotransferase (FGAR-AT). FGAR-AT catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to formylglycinamidine ribonucleotide (FGAM), ADP, Pi, and glutamate in the fourth step of the purine biosynthetic pathway. FGAR-AT is a glutamine amidotransferase. Glutamine amidotransferase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. FGAR-AT belongs to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site Pssm-ID: 153211 [Multi-domain] Cd Length: 238 Bit Score: 45.30 E-value: 3.45e-05
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| SIMIBI | cd01983 | SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ... |
3-109 | 1.03e-04 | ||||||||
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal recognition particle, MinD, and BioD), consists of signal recognition particle (SRP) GTPases, the assemblage of MinD-like ATPases, which are involved in protein localization, chromosome partitioning, and membrane transport, and a group of metabolic enzymes with kinase or related phosphate transferase activity. Functionally, proteins in this superfamily use the energy from hydrolysis of NTP to transfer electron or ion. Pssm-ID: 349751 [Multi-domain] Cd Length: 107 Bit Score: 41.65 E-value: 1.03e-04
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| PRK00758 | PRK00758 | GMP synthase subunit A; Validated |
332-395 | 1.05e-04 | ||||||||
GMP synthase subunit A; Validated Pssm-ID: 179112 [Multi-domain] Cd Length: 184 Bit Score: 43.30 E-value: 1.05e-04
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| IMP_synth_hisH | TIGR01855 | imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model ... |
308-386 | 2.31e-04 | ||||||||
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model represents the glutamine amidotransferase subunit (or domain, in eukaryotic systems) of imidazole glycerol phosphate synthase. This subunit catalyzes step 5 of histidine biosynthesis from PRPP. The other subunit, the cyclase, catalyzes step 6. [Amino acid biosynthesis, Histidine family] Pssm-ID: 273836 [Multi-domain] Cd Length: 196 Bit Score: 42.31 E-value: 2.31e-04
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| GATase1_1 | cd01741 | Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ... |
319-386 | 2.29e-03 | ||||||||
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: 39.15 E-value: 2.29e-03
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| GATase1_CobQ | cd01750 | Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ); Type ... |
318-386 | 2.89e-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: 39.15 E-value: 2.89e-03
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| PLN02617 | PLN02617 | imidazole glycerol phosphate synthase hisHF |
343-386 | 5.10e-03 | ||||||||
imidazole glycerol phosphate synthase hisHF Pssm-ID: 178226 [Multi-domain] Cd Length: 538 Bit Score: 39.69 E-value: 5.10e-03
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| GATase1_Anthranilate_Synthase | cd01743 | Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ... |
342-397 | 9.19e-03 | ||||||||
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: 37.51 E-value: 9.19e-03
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