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Conserved domains on  [gi|974739551|gb|ALZ44937|]
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carbomoylphosphate synthase, partial [Aphaenogaster rudis]

Protein Classification

type 1 glutamine amidotransferase family protein( domain architecture ID 73)

type 1 glutamine amidotransferase (GATase1) family protein

CATH:  3.40.50.880
PubMed:  10387030
SCOP:  3001405

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CPSaseII_lrg super family cl36884
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 97-181 3.15e-48

carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


The actual alignment was detected with superfamily member TIGR01369:

Pssm-ID: 273581 [Multi-domain]  Cd Length: 1050  Bit Score: 167.48  E-value: 3.15e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974739551    97 ERPKKILILGSGGLSIGQAGEFDYSGSQAIKALKEESIQTLLINPNIATVQTSKGMADKVYFLPIIPEYVEQVIRSERPD 176
Cdd:TIGR01369    4 TDIKKILVIGSGPIVIGQAAEFDYSGSQACKALKEEGYRVILVNSNPATIMTDPEMADKVYIEPLTPEAVEKIIEKERPD 83


                   ....*
gi 974739551   177 GVLLT 181
Cdd:TIGR01369   84 AILPT 88
GAT_1 super family cl00020
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 1-63 1.01e-32

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.


The actual alignment was detected with superfamily member cd01744:

Pssm-ID: 469582 [Multi-domain]  Cd Length: 178  Bit Score: 114.90  E-value: 1.01e-32
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 974739551   1 SQNHGFCVDAAQLPTDWEVLFTNANDNSNEGVVHSVLPYFSVQFHPEHTAGPEDLECLFDVFL 63
Cdd:cd01744  116 SQNHGYAVDPDSLPGGLEVTHVNLNDGTVEGIRHKDLPVFSVQFHPEASPGPHDTEYLFDEFL 178
 
Name Accession Description Interval E-value
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 97-181 3.15e-48

carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273581 [Multi-domain]  Cd Length: 1050  Bit Score: 167.48  E-value: 3.15e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974739551    97 ERPKKILILGSGGLSIGQAGEFDYSGSQAIKALKEESIQTLLINPNIATVQTSKGMADKVYFLPIIPEYVEQVIRSERPD 176
Cdd:TIGR01369    4 TDIKKILVIGSGPIVIGQAAEFDYSGSQACKALKEEGYRVILVNSNPATIMTDPEMADKVYIEPLTPEAVEKIIEKERPD 83


                   ....*
gi 974739551   177 GVLLT 181
Cdd:TIGR01369   84 AILPT 88
carB PRK05294
carbamoyl-phosphate synthase large subunit;
100-181 1.16e-41

carbamoyl-phosphate synthase large subunit;


Pssm-ID: 235393 [Multi-domain]  Cd Length: 1066  Bit Score: 148.71  E-value: 1.16e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974739551  100 KKILILGSGGLSIGQAGEFDYSGSQAIKALKEESIQTLLINPNIATVQTSKGMADKVYFLPIIPEYVEQVIRSERPDGVL 179
Cdd:PRK05294    8 KKILIIGSGPIVIGQACEFDYSGTQACKALREEGYRVVLVNSNPATIMTDPEMADATYIEPITPEFVEKIIEKERPDAIL 87


                  ..
gi 974739551  180 LT 181
Cdd:PRK05294   88 PT 89
CarB COG0458
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ...
 105-181 2.51e-35

Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase large subunit is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440226 [Multi-domain]  Cd Length: 536  Bit Score: 129.23  E-value: 2.51e-35
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 974739551 105 LGSGGLSIGQAGEFDYSGSQAIKALKEESIQTLLINPNIATVQTSKGMADKVYFLPIIPEYVEQVIRSERPDGVLLT 181
Cdd:COG0458    1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQ 77
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 1-63 1.01e-32

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: 114.90  E-value: 1.01e-32
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 974739551   1 SQNHGFCVDAAQLPTDWEVLFTNANDNSNEGVVHSVLPYFSVQFHPEHTAGPEDLECLFDVFL 63
Cdd:cd01744  116 SQNHGYAVDPDSLPGGLEVTHVNLNDGTVEGIRHKDLPVFSVQFHPEASPGPHDTEYLFDEFL 178
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
1-64 7.78e-27

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 104.00  E-value: 7.78e-27
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 974739551   1 SQNHGFCVDAAQLPTDWEVLFTNANDNSNEGVVHSVLPYFSVQFHPEHTAGPEDLECLFDVFLE 64
Cdd:PRK12564 295 SQNHGFAVDEDSLPANLEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDEFVE 358
CPSaseIIsmall TIGR01368
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ...
 1-68 5.90e-25

carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small chain of the glutamine-dependent form (EC 6.3.5.5) of carbamoyl phosphate synthase, CPSase II. The C-terminal domain has glutamine amidotransferase activity. Note that the sequence from the mammalian urea cycle form has lost the active site Cys, resulting in an ammonia-dependent form, CPSase I (EC 6.3.4.16). CPSases of pyrimidine biosynthesis, arginine biosynthesis, and the urea cycle may be encoded by one or by several genes, depending on the species. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273580 [Multi-domain]  Cd Length: 357  Bit Score: 98.85  E-value: 5.90e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 974739551    1 SQNHGFCVDAAQLP-TDWEVLFTNANDNSNEGVVHSVLPYFSVQFHPEHTAGPEDLECLFDVFLESVKD 68
Cdd:TIGR01368 289 SQNHGYAVDPDSLPaGDLEVTHVNLNDGTVEGIRHKDLPVFSVQYHPEASPGPHDTEYLFDEFIDLMKK 357
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 1-67 1.01e-24

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: 98.17  E-value: 1.01e-24
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 974739551   1 SQNHGFCVDAAQLP-TDWEVLFTNANDNSNEGVVHSVLPYFSVQFHPEHTAGPEDLECLFDVFLESVK 67
Cdd:COG0505  294 SQNHGFAVDEDSLPaTDLEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDRFIELME 361
GATase pfam00117
Glutamine amidotransferase class-I;
1-64 1.96e-20

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 83.44  E-value: 1.96e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 974739551    1 SQNHGFCVDAAQLPTDWEVLFTNANDNSNEGVVHSVLPYFSVQFHPEHTAGPEDLECLFDVFLE 64
Cdd:pfam00117 124 RRYHSYAVDPDTLPDGLEVTATSENDGTIMGIRHKKLPIFGVQFHPESILTPHGPEILFNFFIK 187
 
Name Accession Description Interval E-value
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 97-181 3.15e-48

carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273581 [Multi-domain]  Cd Length: 1050  Bit Score: 167.48  E-value: 3.15e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974739551    97 ERPKKILILGSGGLSIGQAGEFDYSGSQAIKALKEESIQTLLINPNIATVQTSKGMADKVYFLPIIPEYVEQVIRSERPD 176
Cdd:TIGR01369    4 TDIKKILVIGSGPIVIGQAAEFDYSGSQACKALKEEGYRVILVNSNPATIMTDPEMADKVYIEPLTPEAVEKIIEKERPD 83


                   ....*
gi 974739551   177 GVLLT 181
Cdd:TIGR01369   84 AILPT 88
carB PRK05294
carbamoyl-phosphate synthase large subunit;
100-181 1.16e-41

carbamoyl-phosphate synthase large subunit;


Pssm-ID: 235393 [Multi-domain]  Cd Length: 1066  Bit Score: 148.71  E-value: 1.16e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974739551  100 KKILILGSGGLSIGQAGEFDYSGSQAIKALKEESIQTLLINPNIATVQTSKGMADKVYFLPIIPEYVEQVIRSERPDGVL 179
Cdd:PRK05294    8 KKILIIGSGPIVIGQACEFDYSGTQACKALREEGYRVVLVNSNPATIMTDPEMADATYIEPITPEFVEKIIEKERPDAIL 87


                  ..
gi 974739551  180 LT 181
Cdd:PRK05294   88 PT 89
CarB COG0458
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ...
 105-181 2.51e-35

Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase large subunit is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440226 [Multi-domain]  Cd Length: 536  Bit Score: 129.23  E-value: 2.51e-35
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 974739551 105 LGSGGLSIGQAGEFDYSGSQAIKALKEESIQTLLINPNIATVQTSKGMADKVYFLPIIPEYVEQVIRSERPDGVLLT 181
Cdd:COG0458    1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQ 77
carB PRK12815
carbamoyl phosphate synthase large subunit; Reviewed
 100-181 5.79e-33

carbamoyl phosphate synthase large subunit; Reviewed


Pssm-ID: 237215 [Multi-domain]  Cd Length: 1068  Bit Score: 123.54  E-value: 5.79e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974739551  100 KKILILGSGGLSIGQAGEFDYSGSQAIKALKEESIQTLLINPNIATVQTSKGMADKVYFLPIIPEYVEQVIRSERPDGVL 179
Cdd:PRK12815    8 QKILVIGSGPIVIGQAAEFDYSGTQACLALKEEGYQVVLVNPNPATIMTDPAPADTVYFEPLTVEFVKRIIAREKPDALL 87


                  ..
gi 974739551  180 LT 181
Cdd:PRK12815   88 AT 89
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 1-63 1.01e-32

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: 114.90  E-value: 1.01e-32
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 974739551   1 SQNHGFCVDAAQLPTDWEVLFTNANDNSNEGVVHSVLPYFSVQFHPEHTAGPEDLECLFDVFL 63
Cdd:cd01744  116 SQNHGYAVDPDSLPGGLEVTHVNLNDGTVEGIRHKDLPVFSVQFHPEASPGPHDTEYLFDEFL 178
PLN02735 PLN02735
carbamoyl-phosphate synthase
 100-181 7.70e-29

carbamoyl-phosphate synthase


Pssm-ID: 215391 [Multi-domain]  Cd Length: 1102  Bit Score: 111.79  E-value: 7.70e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974739551  100 KKILILGSGGLSIGQAGEFDYSGSQAIKALKEESIQTLLINPNIATVQTSKGMADKVYFLPIIPEYVEQVIRSERPDGVL 179
Cdd:PLN02735   24 KKIMILGAGPIVIGQACEFDYSGTQACKALKEEGYEVVLINSNPATIMTDPETADRTYIAPMTPELVEQVIAKERPDALL 103


                  ..
gi 974739551  180 LT 181
Cdd:PLN02735  104 PT 105
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
1-64 7.78e-27

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 104.00  E-value: 7.78e-27
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 974739551   1 SQNHGFCVDAAQLPTDWEVLFTNANDNSNEGVVHSVLPYFSVQFHPEHTAGPEDLECLFDVFLE 64
Cdd:PRK12564 295 SQNHGFAVDEDSLPANLEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDEFVE 358
CPSaseIIsmall TIGR01368
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ...
 1-68 5.90e-25

carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small chain of the glutamine-dependent form (EC 6.3.5.5) of carbamoyl phosphate synthase, CPSase II. The C-terminal domain has glutamine amidotransferase activity. Note that the sequence from the mammalian urea cycle form has lost the active site Cys, resulting in an ammonia-dependent form, CPSase I (EC 6.3.4.16). CPSases of pyrimidine biosynthesis, arginine biosynthesis, and the urea cycle may be encoded by one or by several genes, depending on the species. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273580 [Multi-domain]  Cd Length: 357  Bit Score: 98.85  E-value: 5.90e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 974739551    1 SQNHGFCVDAAQLP-TDWEVLFTNANDNSNEGVVHSVLPYFSVQFHPEHTAGPEDLECLFDVFLESVKD 68
Cdd:TIGR01368 289 SQNHGYAVDPDSLPaGDLEVTHVNLNDGTVEGIRHKDLPVFSVQYHPEASPGPHDTEYLFDEFIDLMKK 357
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 1-67 1.01e-24

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: 98.17  E-value: 1.01e-24
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 974739551   1 SQNHGFCVDAAQLP-TDWEVLFTNANDNSNEGVVHSVLPYFSVQFHPEHTAGPEDLECLFDVFLESVK 67
Cdd:COG0505  294 SQNHGFAVDEDSLPaTDLEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDRFIELME 361
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 98-180 3.95e-22

carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273581 [Multi-domain]  Cd Length: 1050  Bit Score: 92.37  E-value: 3.95e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974739551    98 RPKKILILGSGGLSIGQAGEFDYSGSQAIKALKEESIQTLLINPNIATVQTSKGMADKVYFLPIIPEYVEQVIRSERPDG 177
Cdd:TIGR01369  553 DKKKVLVLGSGPNRIGQGVEFDYCCVHAVLALRELGYETIMINYNPETVSTDYDTSDRLYFEPLTFEDVMNIIELEKPEG 632


                   ...
gi 974739551   178 VLL 180
Cdd:TIGR01369  633 VIV 635
carB PRK12815
carbamoyl phosphate synthase large subunit; Reviewed
 100-180 8.96e-21

carbamoyl phosphate synthase large subunit; Reviewed


Pssm-ID: 237215 [Multi-domain]  Cd Length: 1068  Bit Score: 88.49  E-value: 8.96e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974739551  100 KKILILGSGGLSIGQAGEFDYSGSQAIKALKEESIQTLLINPNIATVQTSKGMADKVYFLPIIPEYVEQVIRSERPDGVL 179
Cdd:PRK12815  556 KKVLILGSGPIRIGQGIEFDYSSVHAAFALKKEGYETIMINNNPETVSTDYDTADRLYFEPLTLEDVLNVAEAENIKGVI 635


                  .
gi 974739551  180 L 180
Cdd:PRK12815  636 V 636
carB PRK05294
carbamoyl-phosphate synthase large subunit;
94-178 1.00e-20

carbamoyl-phosphate synthase large subunit;


Pssm-ID: 235393 [Multi-domain]  Cd Length: 1066  Bit Score: 88.62  E-value: 1.00e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974739551   94 IVTERpKKILILGSGGLSIGQAGEFDYSGSQAIKALKEESIQTLLINPNIATVQTSKGMADKVYFLPIIPEYVEQVIRSE 173
Cdd:PRK05294  550 NPSDR-KKVLVLGSGPNRIGQGIEFDYCCVHAVLALREAGYETIMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEIIEKE 628


                  ....*
gi 974739551  174 RPDGV 178
Cdd:PRK05294  629 KPKGV 633
GATase pfam00117
Glutamine amidotransferase class-I;
1-64 1.96e-20

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 83.44  E-value: 1.96e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 974739551    1 SQNHGFCVDAAQLPTDWEVLFTNANDNSNEGVVHSVLPYFSVQFHPEHTAGPEDLECLFDVFLE 64
Cdd:pfam00117 124 RRYHSYAVDPDTLPDGLEVTATSENDGTIMGIRHKKLPIFGVQFHPESILTPHGPEILFNFFIK 187
PRK12838 PRK12838
carbamoyl phosphate synthase small subunit; Reviewed
 1-67 1.25e-19

carbamoyl phosphate synthase small subunit; Reviewed


Pssm-ID: 183784 [Multi-domain]  Cd Length: 354  Bit Score: 84.17  E-value: 1.25e-19
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 974739551   1 SQNHGFCVDAAQL-PTDWEVLFTNANDNSNEGVVHSVLPYFSVQFHPEHTAGPEDLECLFDVFLESVK 67
Cdd:PRK12838 284 SQNHGYVVDEDSLdGTPLSVRFFNVNDGSIEGLRHKKKPVLSVQFHPEAHPGPHDAEYIFDEFLEMME 351
PLN02735 PLN02735
carbamoyl-phosphate synthase
 100-180 6.12e-16

carbamoyl-phosphate synthase


Pssm-ID: 215391 [Multi-domain]  Cd Length: 1102  Bit Score: 74.81  E-value: 6.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974739551  100 KKILILGSGGLSIGQAGEFDYSGSQAIKALKEESIQTLLINPNIATVQTSKGMADKVYFLPIIPEYVEQVIRSERPDGVL 179
Cdd:PLN02735  575 KKVLILGGGPNRIGQGIEFDYCCCHASFALQDAGYETIMMNSNPETVSTDYDTSDRLYFEPLTVEDVLNVIDLERPDGII 654


                  .
gi 974739551  180 L 180
Cdd:PLN02735  655 V 655
carA CHL00197
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
 1-74 6.82e-13

carbamoyl-phosphate synthase arginine-specific small subunit; Provisional


Pssm-ID: 214392 [Multi-domain]  Cd Length: 382  Bit Score: 65.59  E-value: 6.82e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 974739551   1 SQNHGFCVDAAQLPTD-WEVLFTNANDNSNEGVVHSVLPYFSVQFHPEHTAGPEDLECLFDVFLESVKDYMNNRS 74
Cdd:CHL00197 308 SQNHGFAVNLESLAKNkFYITHFNLNDGTVAGISHSPKPYFSVQYHPEASPGPHDADYLFEYFIEIIKHSKSSKN 382
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 4-47 1.53e-04

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: 40.60  E-value: 1.53e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 974739551   4 HGFCVDAAQLPTDWEVlfTNANDnsnEGVVHSV----LPYFSVQFHPE 47
Cdd:cd01743  127 HSLVVDPDPLPDLLEV--TASTE---DGVIMALrhrdLPIYGVQFHPE 169
PRK14607 PRK14607
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
4-63 5.40e-04

bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;


Pssm-ID: 237764 [Multi-domain]  Cd Length: 534  Bit Score: 39.70  E-value: 5.40e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 974739551   4 HGFCVDAAQLPTDWEVLfTNANDNSNEGVVHSVLPYFSVQFHPEhTAGPEDLECLFDVFL 63
Cdd:PRK14607 129 HSLVVEEASLPECLEVT-AKSDDGEIMGIRHKEHPIFGVQFHPE-SILTEEGKRILKNFL 186
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 4-47 2.86e-03

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: 36.94  E-value: 2.86e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 974739551   4 HGFCVDAAQLPTDWEVlftNANDNSNE--GVVHSVLPYFSVQFHPE 47
Cdd:COG0512  127 HSLVVDRETLPDELEV---TAWTEDGEimGIRHRELPIEGVQFHPE 169
PLN02889 PLN02889
oxo-acid-lyase/anthranilate synthase
 31-97 3.50e-03

oxo-acid-lyase/anthranilate synthase


Pssm-ID: 215481 [Multi-domain]  Cd Length: 918  Bit Score: 37.52  E-value: 3.50e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 974739551  31 GVVHSVLPYFSVQFHPEHTAGPEDLEcLFDVFLESVKDYMNNRSPVSVKNRlTERLVYRPSVPIVTE 97
Cdd:PLN02889 301 GIMHSTRPHYGLQFHPESIATCYGRQ-IFKNFREITQDYWLRLRSTSLRRR-NSNLTANMQVPDASQ 365
PRK06774 PRK06774
aminodeoxychorismate synthase component II;
4-65 4.51e-03

aminodeoxychorismate synthase component II;


Pssm-ID: 180689 [Multi-domain]  Cd Length: 191  Bit Score: 36.38  E-value: 4.51e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 974739551   4 HGFCVDAAQLPTDWEVL-FTNANDNSNE--GVVHSVLPYFSVQFHPEHTAGPEDLEcLFDVFLES 65
Cdd:PRK06774 128 HSLVIAADSLPGCFELTaWSERGGEMDEimGIRHRTLPLEGVQFHPESILSEQGHQ-LLDNFLKN 191
GATase1_GMP_Synthase cd01742
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ...
 3-49 7.79e-03

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: 35.59  E-value: 7.79e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 974739551   3 NHGFCVDaaQLPTDWEVLFTNANdNSNEGVVHSVLPYFSVQFHPE--HT 49
Cdd:cd01742  125 SHGDEVV--KLPEGFKVIASSDN-CPVAAIANEEKKIYGVQFHPEvtHT 170
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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