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Conserved domains on  [gi|357528213|gb|AET80346|]
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carbamoylphosphate synthetase, partial [Heterospilus sp. ST28]

Protein Classification

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 ...
 104-318 3.52e-119

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: 367.02  E-value: 3.52e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357528213   104 PKKVLILGSGGLSIGQAGEFDYSGSQAMKALKEENIQTVLINPNIATVQTSKGMADKVYFLPIIPEYVEQVIRSERPDGV 183
Cdd:TIGR01369    6 IKKILVIGSGPIVIGQAAEFDYSGSQACKALKEEGYRVILVNSNPATIMTDPEMADKVYIEPLTPEAVEKIIEKERPDAI 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357528213   184 LLTFGGQTALNCGVELEKAGTFAKYGVKILGTPIKSIIETEDRKLFSDHISNIEEKVAPSAAVYSIQEALDAAEKLGYPV 263
Cdd:TIGR01369   86 LPTFGGQTALNLAVELEESGVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESEIAHSVEEALAAAKEIGYPV 165

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 357528213   264 MARAAFSLGGLGSGFANTREELRTLAQQALAHS--SQLIIDKSLKGWKEVEYEVVRD 318
Cdd:TIGR01369  166 IVRPAFTLGGTGGGIAYNREELKEIAERALSASpiNQVLVEKSLAGWKEIEYEVMRD 222
GAT_1 super family cl00020
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 1-68 1.33e-36

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: 129.54  E-value: 1.33e-36
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 357528213   1 RCYMTSQNHGFAIDAKDLPNGWEALFTNANDESNEGIVHTSLPYFSVQFHPEHTAGPEDLECLFDVFL 68
Cdd:cd01744  111 RVYITSQNHGYAVDPDSLPGGLEVTHVNLNDGTVEGIRHKDLPVFSVQFHPEASPGPHDTEYLFDEFL 178
 
Name Accession Description Interval E-value
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 104-318 3.52e-119

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: 367.02  E-value: 3.52e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357528213   104 PKKVLILGSGGLSIGQAGEFDYSGSQAMKALKEENIQTVLINPNIATVQTSKGMADKVYFLPIIPEYVEQVIRSERPDGV 183
Cdd:TIGR01369    6 IKKILVIGSGPIVIGQAAEFDYSGSQACKALKEEGYRVILVNSNPATIMTDPEMADKVYIEPLTPEAVEKIIEKERPDAI 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357528213   184 LLTFGGQTALNCGVELEKAGTFAKYGVKILGTPIKSIIETEDRKLFSDHISNIEEKVAPSAAVYSIQEALDAAEKLGYPV 263
Cdd:TIGR01369   86 LPTFGGQTALNLAVELEESGVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESEIAHSVEEALAAAKEIGYPV 165

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 357528213   264 MARAAFSLGGLGSGFANTREELRTLAQQALAHS--SQLIIDKSLKGWKEVEYEVVRD 318
Cdd:TIGR01369  166 IVRPAFTLGGTGGGIAYNREELKEIAERALSASpiNQVLVEKSLAGWKEIEYEVMRD 222
carB PRK05294
carbamoyl-phosphate synthase large subunit;
105-318 1.21e-108

carbamoyl-phosphate synthase large subunit;


Pssm-ID: 235393 [Multi-domain]  Cd Length: 1066  Bit Score: 339.77  E-value: 1.21e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357528213  105 KKVLILGSGGLSIGQAGEFDYSGSQAMKALKEENIQTVLINPNIATVQTSKGMADKVYFLPIIPEYVEQVIRSERPDGVL 184
Cdd:PRK05294    8 KKILIIGSGPIVIGQACEFDYSGTQACKALREEGYRVVLVNSNPATIMTDPEMADATYIEPITPEFVEKIIEKERPDAIL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357528213  185 LTFGGQTALNCGVELEKAGTFAKYGVKILGTPIKSIIETEDRKLFSDHISNIEEKVAPSAAVYSIQEALDAAEKLGYPVM 264
Cdd:PRK05294   88 PTMGGQTALNLAVELAESGVLEKYGVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRSGIAHSMEEALEVAEEIGYPVI 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 357528213  265 ARAAFSLGGLGSGFANTREELRTLAQQALAHS--SQLIIDKSLKGWKEVEYEVVRD 318
Cdd:PRK05294  168 IRPSFTLGGTGGGIAYNEEELEEIVERGLDLSpvTEVLIEESLLGWKEYEYEVMRD 223
CarB COG0458
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ...
 110-318 9.20e-101

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: 306.03  E-value: 9.20e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357528213 110 LGSGGLSIGQAGEFDYSGSQAMKALKEENIQTVLINPNIATVQTSKGMADKVYFLPIIPEYVEQVIRSERPDGVLLTFGG 189
Cdd:COG0458    1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357528213 190 QTALNCGVELEKAGTFAkyGVKILGTPIKSIIETEDRKLFSDHISNIEEKVAPSAAVYSIQEALDAAEKLGYPVMARAAF 269
Cdd:COG0458   81 QTALNLAVELEEAGILE--GVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSY 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 357528213 270 SLGGLGSGFANTREELRTLAQQALAHS--SQLIIDKSLKGWKEVEYEVVRD 318
Cdd:COG0458  159 VLGGRGMGIVYNEEELEEYLERALKVSpdHPVLIDESLLGAKEIEVDVVRD 209
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 1-68 1.33e-36

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: 129.54  E-value: 1.33e-36
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 357528213   1 RCYMTSQNHGFAIDAKDLPNGWEALFTNANDESNEGIVHTSLPYFSVQFHPEHTAGPEDLECLFDVFL 68
Cdd:cd01744  111 RVYITSQNHGYAVDPDSLPGGLEVTHVNLNDGTVEGIRHKDLPVFSVQFHPEASPGPHDTEYLFDEFL 178
CPSase_L_D2 pfam02786
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ...
 225-318 4.00e-32

Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00988. The small chain has a GATase domain in the carboxyl terminus. See pfam00117. The ATP binding domain (this one) has an ATP-grasp fold.


Pssm-ID: 397079 [Multi-domain]  Cd Length: 209  Bit Score: 118.56  E-value: 4.00e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357528213  225 DRKLFSDHISNIEEKVAPSAAVY--SIQEALDAAEKLGYPVMARAAFSLGGLGSGFANTREELRTLAQQALAHS------ 296
Cdd:pfam02786   1 DKVLFKAAMKEAGVPTVPGTAGPveTEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEApaafgn 80

                          90       100
                  ....*....|....*....|..
gi 357528213  297 SQLIIDKSLKGWKEVEYEVVRD 318
Cdd:pfam02786  81 PQVLVEKSLKGPKHIEYQVLRD 102
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
1-71 1.39e-28

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 112.86  E-value: 1.39e-28
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 357528213   1 RCYMTSQNHGFAIDAKDLPNGWEALFTNANDESNEGIVHTSLPYFSVQFHPEHTAGPEDLECLFDVFLEAV 71
Cdd:PRK12564 290 KVEITSQNHGFAVDEDSLPANLEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDEFVELM 360
CPSaseIIsmall TIGR01368
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ...
 1-72 2.07e-27

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: 109.64  E-value: 2.07e-27
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 357528213    1 RCYMTSQNHGFAIDAKDLP-NGWEALFTNANDESNEGIVHTSLPYFSVQFHPEHTAGPEDLECLFDVFLEAVN 72
Cdd:TIGR01368 284 RVEITSQNHGYAVDPDSLPaGDLEVTHVNLNDGTVEGIRHKDLPVFSVQYHPEASPGPHDTEYLFDEFIDLMK 356
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 1-72 8.83e-27

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: 107.80  E-value: 8.83e-27
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 357528213   1 RCYMTSQNHGFAIDAKDLPN-GWEALFTNANDESNEGIVHTSLPYFSVQFHPEHTAGPEDLECLFDVFLEAVN 72
Cdd:COG0505  289 RVEITSQNHGFAVDEDSLPAtDLEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDRFIELME 361
GATase pfam00117
Glutamine amidotransferase class-I;
1-70 8.31e-23

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 93.46  E-value: 8.31e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357528213    1 RCYMTSQNHGFAIDAKDLPNGWEALFTNANDESNEGIVHTSLPYFSVQFHPEHTAGPEDLECLFDVFLEA 70
Cdd:pfam00117 119 NVFIVRRYHSYAVDPDTLPDGLEVTATSENDGTIMGIRHKKLPIFGVQFHPESILTPHGPEILFNFFIKA 188
 
Name Accession Description Interval E-value
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 104-318 3.52e-119

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: 367.02  E-value: 3.52e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357528213   104 PKKVLILGSGGLSIGQAGEFDYSGSQAMKALKEENIQTVLINPNIATVQTSKGMADKVYFLPIIPEYVEQVIRSERPDGV 183
Cdd:TIGR01369    6 IKKILVIGSGPIVIGQAAEFDYSGSQACKALKEEGYRVILVNSNPATIMTDPEMADKVYIEPLTPEAVEKIIEKERPDAI 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357528213   184 LLTFGGQTALNCGVELEKAGTFAKYGVKILGTPIKSIIETEDRKLFSDHISNIEEKVAPSAAVYSIQEALDAAEKLGYPV 263
Cdd:TIGR01369   86 LPTFGGQTALNLAVELEESGVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESEIAHSVEEALAAAKEIGYPV 165

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 357528213   264 MARAAFSLGGLGSGFANTREELRTLAQQALAHS--SQLIIDKSLKGWKEVEYEVVRD 318
Cdd:TIGR01369  166 IVRPAFTLGGTGGGIAYNREELKEIAERALSASpiNQVLVEKSLAGWKEIEYEVMRD 222
carB PRK05294
carbamoyl-phosphate synthase large subunit;
105-318 1.21e-108

carbamoyl-phosphate synthase large subunit;


Pssm-ID: 235393 [Multi-domain]  Cd Length: 1066  Bit Score: 339.77  E-value: 1.21e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357528213  105 KKVLILGSGGLSIGQAGEFDYSGSQAMKALKEENIQTVLINPNIATVQTSKGMADKVYFLPIIPEYVEQVIRSERPDGVL 184
Cdd:PRK05294    8 KKILIIGSGPIVIGQACEFDYSGTQACKALREEGYRVVLVNSNPATIMTDPEMADATYIEPITPEFVEKIIEKERPDAIL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357528213  185 LTFGGQTALNCGVELEKAGTFAKYGVKILGTPIKSIIETEDRKLFSDHISNIEEKVAPSAAVYSIQEALDAAEKLGYPVM 264
Cdd:PRK05294   88 PTMGGQTALNLAVELAESGVLEKYGVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRSGIAHSMEEALEVAEEIGYPVI 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 357528213  265 ARAAFSLGGLGSGFANTREELRTLAQQALAHS--SQLIIDKSLKGWKEVEYEVVRD 318
Cdd:PRK05294  168 IRPSFTLGGTGGGIAYNEEELEEIVERGLDLSpvTEVLIEESLLGWKEYEYEVMRD 223
CarB COG0458
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ...
 110-318 9.20e-101

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: 306.03  E-value: 9.20e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357528213 110 LGSGGLSIGQAGEFDYSGSQAMKALKEENIQTVLINPNIATVQTSKGMADKVYFLPIIPEYVEQVIRSERPDGVLLTFGG 189
Cdd:COG0458    1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357528213 190 QTALNCGVELEKAGTFAkyGVKILGTPIKSIIETEDRKLFSDHISNIEEKVAPSAAVYSIQEALDAAEKLGYPVMARAAF 269
Cdd:COG0458   81 QTALNLAVELEEAGILE--GVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSY 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 357528213 270 SLGGLGSGFANTREELRTLAQQALAHS--SQLIIDKSLKGWKEVEYEVVRD 318
Cdd:COG0458  159 VLGGRGMGIVYNEEELEEYLERALKVSpdHPVLIDESLLGAKEIEVDVVRD 209
carB PRK12815
carbamoyl phosphate synthase large subunit; Reviewed
 105-318 1.82e-78

carbamoyl phosphate synthase large subunit; Reviewed


Pssm-ID: 237215 [Multi-domain]  Cd Length: 1068  Bit Score: 258.36  E-value: 1.82e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357528213  105 KKVLILGSGGLSIGQAGEFDYSGSQAMKALKEENIQTVLINPNIATVQTSKGMADKVYFLPIIPEYVEQVIRSERPDGVL 184
Cdd:PRK12815    8 QKILVIGSGPIVIGQAAEFDYSGTQACLALKEEGYQVVLVNPNPATIMTDPAPADTVYFEPLTVEFVKRIIAREKPDALL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357528213  185 LTFGGQTALNCGVELEKAGTFAKYGVKILGTPIKSIIETEDRKLFSDHISNIEEKVAPSAAVYSIQEALDAAEKLGYPVM 264
Cdd:PRK12815   88 ATLGGQTALNLAVKLHEDGILEQYGVELLGTNIEAIQKGEDRERFRALMKELGEPVPESEIVTSVEEALAFAEKIGFPII 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 357528213  265 ARAAFSLGGLGSGFANTREELRTLAQQALAHS--SQLIIDKSLKGWKEVEYEVVRD 318
Cdd:PRK12815  168 VRPAYTLGGTGGGIAENLEELEQLFKQGLQASpiHQCLLEESIAGWKEIEYEVMRD 223
PLN02735 PLN02735
carbamoyl-phosphate synthase
 98-318 1.85e-69

carbamoyl-phosphate synthase


Pssm-ID: 215391 [Multi-domain]  Cd Length: 1102  Bit Score: 233.90  E-value: 1.85e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357528213   98 PEAIKRP--KKVLILGSGGLSIGQAGEFDYSGSQAMKALKEENIQTVLINPNIATVQTSKGMADKVYFLPIIPEYVEQVI 175
Cdd:PLN02735   15 TKAGKRTdlKKIMILGAGPIVIGQACEFDYSGTQACKALKEEGYEVVLINSNPATIMTDPETADRTYIAPMTPELVEQVI 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357528213  176 RSERPDGVLLTFGGQTALNCGVELEKAGTFAKYGVKILGTPIKSIIETEDRKLFSDHISNIEEKVAPSAAVYSIQEALDA 255
Cdd:PLN02735   95 AKERPDALLPTMGGQTALNLAVALAESGILEKYGVELIGAKLDAIKKAEDRELFKQAMEKIGLKTPPSGIATTLDECFEI 174

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 357528213  256 AEKLG-YPVMARAAFSLGGLGSGFANTREELRTLAQQALAHS--SQLIIDKSLKGWKEVEYEVVRD 318
Cdd:PLN02735  175 AEDIGeFPLIIRPAFTLGGTGGGIAYNKEEFETICKAGLAASitSQVLVEKSLLGWKEYELEVMRD 240
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 100-318 6.85e-54

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: 189.44  E-value: 6.85e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357528213   100 AIKRPKKVLILGSGGLSIGQAGEFDYSGSQAMKALKEENIQTVLINPNIATVQTSKGMADKVYFLPIIPEYVEQVIRSER 179
Cdd:TIGR01369  550 PFTDKKKVLVLGSGPNRIGQGVEFDYCCVHAVLALRELGYETIMINYNPETVSTDYDTSDRLYFEPLTFEDVMNIIELEK 629

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357528213   180 PDGVLLTFGGQTALNCGVELEKAgtfakyGVKILGTPIKSIIETEDRKLFSDHISNIEEKVAPSAAVYSIQEALDAAEKL 259
Cdd:TIGR01369  630 PEGVIVQFGGQTPLNLAKALEEA------GVPILGTSPESIDRAEDREKFSELLDELGIPQPKWKTATSVEEAVEFASEI 703

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 357528213   260 GYPVMARAAFSLGGLGSGFANTREELRTLAQQALAHSSQ--LIIDKSLKGWKEVEYEVVRD 318
Cdd:TIGR01369  704 GYPVLVRPSYVLGGRAMEIVYNEEELRRYLEEAVAVSPEhpVLIDKYLEDAVEVDVDAVSD 764
carB PRK05294
carbamoyl-phosphate synthase large subunit;
105-312 5.96e-50

carbamoyl-phosphate synthase large subunit;


Pssm-ID: 235393 [Multi-domain]  Cd Length: 1066  Bit Score: 177.98  E-value: 5.96e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357528213  105 KKVLILGSGGLSIGQAGEFDYSGSQAMKALKEENIQTVLINPNIATVQTSKGMADKVYFLPIIPEYVEQVIRSERPDGVL 184
Cdd:PRK05294  555 KKVLVLGSGPNRIGQGIEFDYCCVHAVLALREAGYETIMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEIIEKEKPKGVI 634

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357528213  185 LTFGGQTALNCGVELEKAgtfakyGVKILGTPIKSIIETEDRKLFSDHISNIEEKVAPSAAVYSIQEALDAAEKLGYPVM 264
Cdd:PRK05294  635 VQFGGQTPLKLAKALEAA------GVPILGTSPDAIDLAEDRERFSKLLEKLGIPQPPNGTATSVEEALEVAEEIGYPVL 708

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 357528213  265 ARAAFSLGGLGSGFANTREELRTLAQQALAHSSQ--LIIDKSLKGWKEVE 312
Cdd:PRK05294  709 VRPSYVLGGRAMEIVYDEEELERYMREAVKVSPDhpVLIDKFLEGAIEVD 758
carB PRK12815
carbamoyl phosphate synthase large subunit; Reviewed
 105-318 2.99e-47

carbamoyl phosphate synthase large subunit; Reviewed


Pssm-ID: 237215 [Multi-domain]  Cd Length: 1068  Bit Score: 170.15  E-value: 2.99e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357528213  105 KKVLILGSGGLSIGQAGEFDYSGSQAMKALKEENIQTVLINPNIATVQTSKGMADKVYFLPIIPEYVEQVIRSERPDGVL 184
Cdd:PRK12815  556 KKVLILGSGPIRIGQGIEFDYSSVHAAFALKKEGYETIMINNNPETVSTDYDTADRLYFEPLTLEDVLNVAEAENIKGVI 635

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357528213  185 LTFGGQTALNCGVELEKAgtfakyGVKILGTPIKSIIETEDRKLFSDHISNIEEKVAPSAAVYSIQEALDAAEKLGYPVM 264
Cdd:PRK12815  636 VQFGGQTAINLAKGLEEA------GLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPGLTATDEEEAFAFAKRIGYPVL 709

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 357528213  265 ARAAFSLGGLGSGFANTREELRTLAQQALAHSSQLIIDKSLKGwKEVEYEVVRD 318
Cdd:PRK12815  710 IRPSYVIGGQGMAVVYDEPALEAYLAENASQLYPILIDQFIDG-KEYEVDAISD 762
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 1-68 1.33e-36

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: 129.54  E-value: 1.33e-36
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 357528213   1 RCYMTSQNHGFAIDAKDLPNGWEALFTNANDESNEGIVHTSLPYFSVQFHPEHTAGPEDLECLFDVFL 68
Cdd:cd01744  111 RVYITSQNHGYAVDPDSLPGGLEVTHVNLNDGTVEGIRHKDLPVFSVQFHPEASPGPHDTEYLFDEFL 178
PLN02735 PLN02735
carbamoyl-phosphate synthase
 105-318 1.99e-35

carbamoyl-phosphate synthase


Pssm-ID: 215391 [Multi-domain]  Cd Length: 1102  Bit Score: 136.06  E-value: 1.99e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357528213  105 KKVLILGSGGLSIGQAGEFDYSGSQAMKALKEENIQTVLINPNIATVQTSKGMADKVYFLPIIPEYVEQVIRSERPDGVL 184
Cdd:PLN02735  575 KKVLILGGGPNRIGQGIEFDYCCCHASFALQDAGYETIMMNSNPETVSTDYDTSDRLYFEPLTVEDVLNVIDLERPDGII 654

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357528213  185 LTFGGQTALNCGVELEKAGT----FAKYG---VKILGTPIKSIIETEDRKLFSDHISNIEEKVAPSAAVYSIQEALDAAE 257
Cdd:PLN02735  655 VQFGGQTPLKLALPIQKYLDknppPSASGngnVKIWGTSPDSIDAAEDRERFNAILNELKIEQPKGGIARSEADALAIAK 734

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 357528213  258 KLGYPVMARAAFSLGGLGSGFANTREELRTLAQQALAHSSQ--LIIDKSLKGWKEVEYEVVRD 318
Cdd:PLN02735  735 RIGYPVVVRPSYVLGGRAMEIVYSDDKLKTYLETAVEVDPErpVLVDKYLSDATEIDVDALAD 797
CPSase_L_D2 pfam02786
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ...
 225-318 4.00e-32

Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00988. The small chain has a GATase domain in the carboxyl terminus. See pfam00117. The ATP binding domain (this one) has an ATP-grasp fold.


Pssm-ID: 397079 [Multi-domain]  Cd Length: 209  Bit Score: 118.56  E-value: 4.00e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357528213  225 DRKLFSDHISNIEEKVAPSAAVY--SIQEALDAAEKLGYPVMARAAFSLGGLGSGFANTREELRTLAQQALAHS------ 296
Cdd:pfam02786   1 DKVLFKAAMKEAGVPTVPGTAGPveTEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEApaafgn 80

                          90       100
                  ....*....|....*....|..
gi 357528213  297 SQLIIDKSLKGWKEVEYEVVRD 318
Cdd:pfam02786  81 PQVLVEKSLKGPKHIEYQVLRD 102
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
1-71 1.39e-28

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 112.86  E-value: 1.39e-28
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 357528213   1 RCYMTSQNHGFAIDAKDLPNGWEALFTNANDESNEGIVHTSLPYFSVQFHPEHTAGPEDLECLFDVFLEAV 71
Cdd:PRK12564 290 KVEITSQNHGFAVDEDSLPANLEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDEFVELM 360
CPSaseIIsmall TIGR01368
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ...
 1-72 2.07e-27

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: 109.64  E-value: 2.07e-27
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 357528213    1 RCYMTSQNHGFAIDAKDLP-NGWEALFTNANDESNEGIVHTSLPYFSVQFHPEHTAGPEDLECLFDVFLEAVN 72
Cdd:TIGR01368 284 RVEITSQNHGYAVDPDSLPaGDLEVTHVNLNDGTVEGIRHKDLPVFSVQYHPEASPGPHDTEYLFDEFIDLMK 356
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 1-72 8.83e-27

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: 107.80  E-value: 8.83e-27
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 357528213   1 RCYMTSQNHGFAIDAKDLPN-GWEALFTNANDESNEGIVHTSLPYFSVQFHPEHTAGPEDLECLFDVFLEAVN 72
Cdd:COG0505  289 RVEITSQNHGFAVDEDSLPAtDLEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDRFIELME 361
PRK12838 PRK12838
carbamoyl phosphate synthase small subunit; Reviewed
 1-74 1.97e-23

carbamoyl phosphate synthase small subunit; Reviewed


Pssm-ID: 183784 [Multi-domain]  Cd Length: 354  Bit Score: 98.43  E-value: 1.97e-23
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 357528213   1 RCYMTSQNHGFAIDAKDL-PNGWEALFTNANDESNEGIVHTSLPYFSVQFHPEHTAGPEDLECLFDVFLEAVNVQ 74
Cdd:PRK12838 279 RVWMTSQNHGYVVDEDSLdGTPLSVRFFNVNDGSIEGLRHKKKPVLSVQFHPEAHPGPHDAEYIFDEFLEMMEKA 353
GATase pfam00117
Glutamine amidotransferase class-I;
1-70 8.31e-23

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 93.46  E-value: 8.31e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357528213    1 RCYMTSQNHGFAIDAKDLPNGWEALFTNANDESNEGIVHTSLPYFSVQFHPEHTAGPEDLECLFDVFLEA 70
Cdd:pfam00117 119 NVFIVRRYHSYAVDPDTLPDGLEVTATSENDGTIMGIRHKKLPIFGVQFHPESILTPHGPEILFNFFIKA 188
carA CHL00197
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
 4-80 8.60e-14

carbamoyl-phosphate synthase arginine-specific small subunit; Provisional


Pssm-ID: 214392 [Multi-domain]  Cd Length: 382  Bit Score: 71.37  E-value: 8.60e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 357528213   4 MTSQNHGFAIDAKDL-PNGWEALFTNANDESNEGIVHTSLPYFSVQFHPEHTAGPEDLECLFDVFLEAVnVQIKEKAN 80
Cdd:CHL00197 306 ITSQNHGFAVNLESLaKNKFYITHFNLNDGTVAGISHSPKPYFSVQYHPEASPGPHDADYLFEYFIEII-KHSKSSKN 382
PRK12767 PRK12767
carbamoyl phosphate synthase-like protein; Provisional
 106-307 4.20e-06

carbamoyl phosphate synthase-like protein; Provisional


Pssm-ID: 237195 [Multi-domain]  Cd Length: 326  Bit Score: 47.57  E-value: 4.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357528213 106 KVLILGSGGlsigqagefdysGSQAMKALKEE----NIQTVLINPNIATVQtskgMADKVYFLPII--PEYVEQVI---R 176
Cdd:PRK12767   3 NILVTSAGR------------RVQLVKALKKSllkgRVIGADISELAPALY----FADKFYVVPKVtdPNYIDRLLdicK 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357528213 177 SERPDGVLLTFGgqtalncgVELEK----AGTFAKYGVKILGTPiKSIIET-EDRKLFSDHISNIEEKVAPSAAVYSIQE 251
Cdd:PRK12767  67 KEKIDLLIPLID--------PELPLlaqnRDRFEEIGVKVLVSS-KEVIEIcNDKWLTYEFLKENGIPTPKSYLPESLED 137

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 357528213 252 AL--DAAEKLGYPVMARAAFSLGGLGSGFANTREELRTLaqqaLAHSSQLIIDKSLKG 307
Cdd:PRK12767 138 FKaaLAKGELQFPLFVKPRDGSASIGVFKVNDKEELEFL----LEYVPNLIIQEFIEG 191
AccC COG0439
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ...
 240-316 2.60e-05

Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440208 [Multi-domain]  Cd Length: 263  Bit Score: 44.86  E-value: 2.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357528213 240 VAPSAAVYSIQEALDAAEKLGYPVMARAAFSLGGLGSGFANTREELRTLAQQALAH------SSQLIIDKSLKGwKEVEY 313
Cdd:COG0439   69 VPGFALVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEakagspNGEVLVEEFLEG-REYSV 147


                 ...
gi 357528213 314 EVV 316
Cdd:COG0439  148 EGL 150
PRK08654 PRK08654
acetyl-CoA carboxylase biotin carboxylase subunit;
245-318 5.31e-05

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 236325 [Multi-domain]  Cd Length: 499  Bit Score: 44.59  E-value: 5.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357528213 245 AVYSIQEALDAAEKLGYPVMARAAFSLGGLGSGFANTREEL-------RTLAQQALAHSSqLIIDKSLKGWKEVEYEVVR 317
Cdd:PRK08654 137 GIEDIEEAKEIAEEIGYPVIIKASAGGGGIGMRVVYSEEELedaiestQSIAQSAFGDST-VFIEKYLEKPRHIEIQILA 215


                 .
gi 357528213 318 D 318
Cdd:PRK08654 216 D 216
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 9-52 1.03e-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: 42.52  E-value: 1.03e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 357528213   9 HGFAIDAKDLPNGWEalfTNANDESNE--GIVHTSLPYFSVQFHPE 52
Cdd:cd01743  127 HSLVVDPDPLPDLLE---VTASTEDGVimALRHRDLPIYGVQFHPE 169
PRK06111 PRK06111
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
 242-318 1.42e-04

acetyl-CoA carboxylase biotin carboxylase subunit; Validated


Pssm-ID: 180406 [Multi-domain]  Cd Length: 450  Bit Score: 43.09  E-value: 1.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357528213 242 PSAAVYSIQEALDAAEKLGYPVMARAAFSLGGLGSGFANTREELR-------TLAQQALAHSSqLIIDKSLKGWKEVEYE 314
Cdd:PRK06111 134 ITTNLEDAEEAIAIARQIGYPVMLKASAGGGGIGMQLVETEQELTkafesnkKRAANFFGNGE-MYIEKYIEDPRHIEIQ 212


                 ....
gi 357528213 315 VVRD 318
Cdd:PRK06111 213 LLAD 216
PRK07178 PRK07178
acetyl-CoA carboxylase biotin carboxylase subunit;
200-318 1.61e-04

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 180865 [Multi-domain]  Cd Length: 472  Bit Score: 43.17  E-value: 1.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357528213 200 EKAGTFAKYGVKILGTPIKSIIETEDRklfsdhisnIEEKVAPSAA-----------VYSIQEALDAAEKLGYPVMARAA 268
Cdd:PRK07178  89 ELAEICAERGIKFIGPSAEVIRRMGDK---------TEARRAMIKAgvpvtpgsegnLADLDEALAEAERIGYPVMLKAT 159

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 357528213 269 FSLGGLGSGFANTREELR-------TLAQQALAhSSQLIIDKSLKGWKEVEYEVVRD 318
Cdd:PRK07178 160 SGGGGRGIRRCNSREELEqnfprviSEATKAFG-SAEVFLEKCIVNPKHIEVQILAD 215
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 9-52 2.70e-04

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: 41.18  E-value: 2.70e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 357528213   9 HGFAIDAKDLPngwEALFTNANDESNE--GIVHTSLPYFSVQFHPE 52
Cdd:COG0512  127 HSLVVDRETLP---DELEVTAWTEDGEimGIRHRELPIEGVQFHPE 169
PRK08591 PRK08591
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
 245-292 2.89e-04

acetyl-CoA carboxylase biotin carboxylase subunit; Validated


Pssm-ID: 236307 [Multi-domain]  Cd Length: 451  Bit Score: 42.10  E-value: 2.89e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 357528213 245 AVYSIQEALDAAEKLGYPVMARAAFSLGGLGSGFANTREELRTLAQQA 292
Cdd:PRK08591 137 PVDDEEEALAIAKEIGYPVIIKATAGGGGRGMRVVRTEAELEKAFSMA 184
PycA COG1038
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ...
 245-286 5.45e-04

Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440660 [Multi-domain]  Cd Length: 1144  Bit Score: 41.60  E-value: 5.45e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 357528213  245 AVYSIQEALDAAEKLGYPVMARAAFSLGGLGSGFANTREELR 286
Cdd:COG1038   140 PVDDLEEALAFAEEIGYPVMLKAAAGGGGRGMRVVRSEEELE 181
GATase1_GMP_Synthase cd01742
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ...
 8-54 7.72e-04

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: 39.83  E-value: 7.72e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 357528213   8 NHGFAIDAkdLPNGWEALFTNANDEsNEGIVHTSLPYFSVQFHPE--HT 54
Cdd:cd01742  125 SHGDEVVK--LPEGFKVIASSDNCP-VAAIANEEKKIYGVQFHPEvtHT 170
PRK12999 PRK12999
pyruvate carboxylase; Reviewed
 248-292 8.40e-04

pyruvate carboxylase; Reviewed


Pssm-ID: 237263 [Multi-domain]  Cd Length: 1146  Bit Score: 41.28  E-value: 8.40e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 357528213  248 SIQEALDAAEKLGYPVMARAAFSLGGLGSGFANTREELRTLAQQA 292
Cdd:PRK12999  144 DIEEALEFAEEIGYPIMLKASAGGGGRGMRIVRSEEELEEAFERA 188
PRK12833 PRK12833
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
 245-318 1.57e-03

acetyl-CoA carboxylase biotin carboxylase subunit; Provisional


Pssm-ID: 183781 [Multi-domain]  Cd Length: 467  Bit Score: 40.12  E-value: 1.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357528213 245 AVYSIQEALDAAEKLGYPVMARAAFSLGGLGSGFANTREELRT---LAQ---QALAHSSQLIIDKSLKGWKEVEYEVVRD 318
Cdd:PRK12833 140 VVASLDAALEVAARIGYPLMIKAAAGGGGRGIRVAHDAAQLAAelpLAQreaQAAFGDGGVYLERFIARARHIEVQILGD 219
PRK05586 PRK05586
acetyl-CoA carboxylase biotin carboxylase subunit;
245-318 2.22e-03

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 180150 [Multi-domain]  Cd Length: 447  Bit Score: 39.31  E-value: 2.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357528213 245 AVYSIQEALDAAEKLGYPVMARAAFSLGGLGSGFANTREEL----RTLAQQALAH--SSQLIIDKSLKGWKEVEYEVVRD 318
Cdd:PRK05586 137 EIENEEEALEIAKEIGYPVMVKASAGGGGRGIRIVRSEEELikafNTAKSEAKAAfgDDSMYIEKFIENPKHIEFQILGD 216
PRK00758 PRK00758
GMP synthase subunit A; Validated
 16-69 2.38e-03

GMP synthase subunit A; Validated


Pssm-ID: 179112 [Multi-domain]  Cd Length: 184  Bit Score: 38.29  E-value: 2.38e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 357528213  16 KDLPNGWEALFTNANDEsNEGIVHTSLPYFSVQFHPE--HTagpEDLECLFDVFLE 69
Cdd:PRK00758 128 KELPDGFEILARSDICE-VEAMKHKEKPIYGVQFHPEvaHT---EYGEEIFKNFLE 179
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 7-55 4.09e-03

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: 38.00  E-value: 4.09e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 357528213   7 QNHGFAIDAkdLPNGWEALFTNANDEsNEGIVHTSlPYFSVQFHPEHTA 55
Cdd:COG0518  136 MSHGDTVTE--LPEGAEVLASSDNCP-NQAFRYGR-RVYGVQFHPEVTH 180
guaA_Nterm TIGR00888
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ...
 16-54 5.49e-03

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: 37.29  E-value: 5.49e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 357528213   16 KDLPNGWEALFTNANDEsNEGIVHTSLPYFSVQFHPE--HT 54
Cdd:TIGR00888 131 KELPEGFKVLATSDNCP-VAAMAHEEKPIYGVQFHPEvtHT 170
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 9-52 6.05e-03

anthranilate synthase component II; Provisional


Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 37.03  E-value: 6.05e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 357528213   9 HGFAIDAKDLPNGWEAlftNANDESNE--GIVHTSLPYFSVQFHPE 52
Cdd:PRK05670 128 HSLVVDRESLPDCLEV---TAWTDDGEimGVRHKELPIYGVQFHPE 170
PRK14607 PRK14607
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
9-68 8.32e-03

bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;


Pssm-ID: 237764 [Multi-domain]  Cd Length: 534  Bit Score: 37.77  E-value: 8.32e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 357528213   9 HGFAIDAKDLPngwEALFTNANDESNE--GIVHTSLPYFSVQFHPEhTAGPEDLECLFDVFL 68
Cdd:PRK14607 129 HSLVVEEASLP---ECLEVTAKSDDGEimGIRHKEHPIFGVQFHPE-SILTEEGKRILKNFL 186
 
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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