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Conserved domains on  [gi|494600084|ref|WP_007358337|]
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MULTISPECIES: glutamine-hydrolyzing carbamoyl-phosphate synthase small subunit [Kamptonema]

Protein Classification

carbamoyl-phosphate synthase small subunit( domain architecture ID 11423442)

small subunit of carbamoyl phosphate synthetase (CPS) which plays a key role in both arginine and pyrimidine biosynthesis

CATH:  3.40.50.880|3.50.30.20
EC:  6.3.5.5
Gene Ontology:  GO:0005524|GO:0046982|GO:0004359|GO:0004088|GO:0019856|GO:0006526

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 5-375 0e+00

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: 699.47  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084   5 TAQPALLVLADGTAYRGWSFGANGTVVGEVVFNTGMTGYQEVLTDPSYCGQIVTFTYPELGNTGVNVEDEESHGPQVRAA 84
Cdd:COG0505    1 MMMKALLVLEDGTVFEGKSFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVTFTYPHIGNYGVNDEDFESDRPWVAGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084  85 IARNICHKPSNWRSTQSLPDYLKHHSIPGIYGIDTRALTRKIRTVGAMNGGISTEILDPAELLEQVQEAPSMAGLNLVRQ 164
Cdd:COG0505   81 VVRELSRRPSNWRSEESLDEYLKEHGIPGISGIDTRALTRHLREKGAMKGVISTGDLDIEELLEKARAAPGMEGLDLVKE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084 165 VTTSEVYEWSEPTESNwefsdginsdaeiLTVVAIDFGIKRNILRRLASYGCRVVVVPANTPPEEILKYKPDGIFLSNGP 244
Cdd:COG0505  161 VSTKEPYEWTEAPGAG-------------FHVVALDFGVKRNILRELAERGCRVTVVPATTSAEEILALNPDGVFLSNGP 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084 245 GDPATVIEGIETTKALLKSEKPIFGICMGHQILGRSLGADTFKLKFGHRGLNQPAG--LTERIEITSQNHGFAIDPDSL- 321
Cdd:COG0505  228 GDPAALDYAIETIRELLGKGIPIFGICLGHQLLALALGAKTYKLKFGHRGANHPVKdlETGRVEITSQNHGFAVDEDSLp 307

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 494600084 322 AADVEITHLNLNDRTVAGLRHKSLPLFSVQYHPEASPGPHDADYLFERFVEAMR 375
Cdd:COG0505  308 ATDLEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDRFIELME 361
 
Name Accession Description Interval E-value
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 5-375 0e+00

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: 699.47  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084   5 TAQPALLVLADGTAYRGWSFGANGTVVGEVVFNTGMTGYQEVLTDPSYCGQIVTFTYPELGNTGVNVEDEESHGPQVRAA 84
Cdd:COG0505    1 MMMKALLVLEDGTVFEGKSFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVTFTYPHIGNYGVNDEDFESDRPWVAGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084  85 IARNICHKPSNWRSTQSLPDYLKHHSIPGIYGIDTRALTRKIRTVGAMNGGISTEILDPAELLEQVQEAPSMAGLNLVRQ 164
Cdd:COG0505   81 VVRELSRRPSNWRSEESLDEYLKEHGIPGISGIDTRALTRHLREKGAMKGVISTGDLDIEELLEKARAAPGMEGLDLVKE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084 165 VTTSEVYEWSEPTESNwefsdginsdaeiLTVVAIDFGIKRNILRRLASYGCRVVVVPANTPPEEILKYKPDGIFLSNGP 244
Cdd:COG0505  161 VSTKEPYEWTEAPGAG-------------FHVVALDFGVKRNILRELAERGCRVTVVPATTSAEEILALNPDGVFLSNGP 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084 245 GDPATVIEGIETTKALLKSEKPIFGICMGHQILGRSLGADTFKLKFGHRGLNQPAG--LTERIEITSQNHGFAIDPDSL- 321
Cdd:COG0505  228 GDPAALDYAIETIRELLGKGIPIFGICLGHQLLALALGAKTYKLKFGHRGANHPVKdlETGRVEITSQNHGFAVDEDSLp 307

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 494600084 322 AADVEITHLNLNDRTVAGLRHKSLPLFSVQYHPEASPGPHDADYLFERFVEAMR 375
Cdd:COG0505  308 ATDLEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDRFIELME 361
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
7-374 0e+00

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 689.89  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084   7 QPALLVLADGTAYRGWSFGANGTVVGEVVFNTGMTGYQEVLTDPSYCGQIVTFTYPELGNTGVNVEDEESHGPQVRAAIA 86
Cdd:PRK12564   3 MKAYLVLEDGTVFEGKAFGAEGETVGEVVFNTSMTGYQEILTDPSYAGQIVTFTYPLIGNYGVNREDFESDRPHAKGLIV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084  87 RNICHKPSNWRSTQSLPDYLKHHSIPGIYGIDTRALTRKIRTVGAMNGGISTEILDPAELLEQVQEAPSMAGLNLVRQVT 166
Cdd:PRK12564  83 RELSDIPSNWRSEMSLDEYLKENGIPGISGIDTRALTRKLREKGAMKGVIATEDFDAEELLEKARAFPGLLGLDLVKEVS 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084 167 TSEVYEWSEPTESnwefsdginsdaEILTVVAIDFGIKRNILRRLASYGCRVVVVPANTPPEEILKYKPDGIFLSNGPGD 246
Cdd:PRK12564 163 TKEPYPWPGPGGE------------LKYKVVAIDFGVKRNILRELAERGCRVTVVPATTTAEEILALNPDGVFLSNGPGD 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084 247 PATVIEGIETTKALLKSEKPIFGICMGHQILGRSLGADTFKLKFGHRGLNQPAG--LTERIEITSQNHGFAIDPDSLAAD 324
Cdd:PRK12564 231 PAALDYAIEMIRELLEKKIPIFGICLGHQLLALALGAKTYKMKFGHRGANHPVKdlETGKVEITSQNHGFAVDEDSLPAN 310

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 494600084 325 VEITHLNLNDRTVAGLRHKSLPLFSVQYHPEASPGPHDADYLFERFVEAM 374
Cdd:PRK12564 311 LEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDEFVELM 360
CPSaseIIsmall TIGR01368
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ...
 9-376 0e+00

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: 594.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084    9 ALLVLADGTAYRGWSFGANGTVVGEVVFNTGMTGYQEVLTDPSYCGQIVTFTYPELGNTGVNVEDEESHGPQVRAAIARN 88
Cdd:TIGR01368   1 AYLVLEDGTVFRGYSFGAEGTVAGEVVFNTGMTGYQEILTDPSYKGQIVVFTYPLIGNYGVNDEDAESKGIHVSGLVVRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084   89 ICHKPSNWRSTQSLPDYLKHHSIPGIYGIDTRALTRKIRTVGAMNGGISTEILDPAELLEQVQEAPSMAGLNLVRQVTTS 168
Cdd:TIGR01368  81 LSDRYSNWRATESLDQFLKRHGIPGIYGVDTRALVKKIREKGTMKGVISTEDSNDEELVEKARVSPDITGINLVAEVSTK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084  169 EVYEWSEPTESNwefsdginsdaeiLTVVAIDFGIKRNILRRLASYGCRVVVVPANTPPEEILKYKPDGIFLSNGPGDPA 248
Cdd:TIGR01368 161 EPYTWGQRGGKG-------------KRVVVIDFGVKRNILRRLVKRGCEVTVVPYDTDAEEIKKYNPDGIFLSNGPGDPA 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084  249 TVIEGIETTKALLkSEKPIFGICMGHQILGRSLGADTFKLKFGHRGLNQPAG--LTERIEITSQNHGFAIDPDSLAA-DV 325
Cdd:TIGR01368 228 AVEPAIETIRKLL-EKIPIFGICLGHQLLALAFGAKTYKMKFGHRGGNHPVKdlITGRVEITSQNHGYAVDPDSLPAgDL 306

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 494600084  326 EITHLNLNDRTVAGLRHKSLPLFSVQYHPEASPGPHDADYLFERFVEAMRE 376
Cdd:TIGR01368 307 EVTHVNLNDGTVEGIRHKDLPVFSVQYHPEASPGPHDTEYLFDEFIDLMKK 357
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 196-371 3.58e-118

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: 340.24  E-value: 3.58e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084 196 VVAIDFGIKRNILRRLASYGCRVVVVPANTPPEEILKYKPDGIFLSNGPGDPATVIEGIETTKALLKSEKPIFGICMGHQ 275
Cdd:cd01744    1 VVVIDFGVKHNILRELLKRGCEVTVVPYNTDAEEILKLDPDGIFLSNGPGDPALLDEAIKTVRKLLGKKIPIFGICLGHQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084 276 ILGRSLGADTFKLKFGHRGLNQPAG--LTERIEITSQNHGFAIDPDSLAADVEITHLNLNDRTVAGLRHKSLPLFSVQYH 353
Cdd:cd01744   81 LLALALGAKTYKMKFGHRGSNHPVKdlITGRVYITSQNHGYAVDPDSLPGGLEVTHVNLNDGTVEGIRHKDLPVFSVQFH 160

                        170
                 ....*....|....*...
gi 494600084 354 PEASPGPHDADYLFERFV 371
Cdd:cd01744  161 PEASPGPHDTEYLFDEFL 178
CPSase_sm_chain pfam00988
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 11-136 6.55e-87

Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase domain is in the amino terminus of protein. 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 pfam00289. The small chain has a GATase domain in the carboxyl terminus. See pfam00117.


Pssm-ID: 460017 [Multi-domain]  Cd Length: 126  Bit Score: 258.79  E-value: 6.55e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084   11 LVLADGTAYRGWSFGANGTVVGEVVFNTGMTGYQEVLTDPSYCGQIVTFTYPELGNTGVNVEDEESHGPQVRAAIARNIC 90
Cdd:pfam00988   1 LVLEDGTVFEGKSFGAAGSTVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNPEDFESDKIHVAGLVVREYS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 494600084   91 HKPSNWRSTQSLPDYLKHHSIPGIYGIDTRALTRKIRTVGAMNGGI 136
Cdd:pfam00988  81 DEPSNWRAEESLDEWLKEQGIPGISGVDTRALTRKIREKGAMKGVI 126
CPSase_sm_chain smart01097
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 7-136 2.10e-86

Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase domain is in the amino terminus of protein. Carbamoyl-phosphate synthase catalyses 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 synthesise carbamoyl phosphate. The small chain has a GATase domain in the carboxyl terminus.


Pssm-ID: 198165 [Multi-domain]  Cd Length: 130  Bit Score: 257.69  E-value: 2.10e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084     7 QPALLVLADGTAYRGWSFGANGTVVGEVVFNTGMTGYQEVLTDPSYCGQIVTFTYPELGNTGVNVEDEESHGPQVRAAIA 86
Cdd:smart01097   1 MKAYLVLEDGTVFEGESFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNDEDFESDKIQVKGLVV 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 494600084    87 RNICHKPSNWRSTQSLPDYLKHHSIPGIYGIDTRALTRKIRTVGAMNGGI 136
Cdd:smart01097  81 RELSDEPSNWRSEQSLDEFLKENGIPGISGIDTRALTRKLREKGAMKGVI 130
 
Name Accession Description Interval E-value
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 5-375 0e+00

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: 699.47  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084   5 TAQPALLVLADGTAYRGWSFGANGTVVGEVVFNTGMTGYQEVLTDPSYCGQIVTFTYPELGNTGVNVEDEESHGPQVRAA 84
Cdd:COG0505    1 MMMKALLVLEDGTVFEGKSFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVTFTYPHIGNYGVNDEDFESDRPWVAGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084  85 IARNICHKPSNWRSTQSLPDYLKHHSIPGIYGIDTRALTRKIRTVGAMNGGISTEILDPAELLEQVQEAPSMAGLNLVRQ 164
Cdd:COG0505   81 VVRELSRRPSNWRSEESLDEYLKEHGIPGISGIDTRALTRHLREKGAMKGVISTGDLDIEELLEKARAAPGMEGLDLVKE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084 165 VTTSEVYEWSEPTESNwefsdginsdaeiLTVVAIDFGIKRNILRRLASYGCRVVVVPANTPPEEILKYKPDGIFLSNGP 244
Cdd:COG0505  161 VSTKEPYEWTEAPGAG-------------FHVVALDFGVKRNILRELAERGCRVTVVPATTSAEEILALNPDGVFLSNGP 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084 245 GDPATVIEGIETTKALLKSEKPIFGICMGHQILGRSLGADTFKLKFGHRGLNQPAG--LTERIEITSQNHGFAIDPDSL- 321
Cdd:COG0505  228 GDPAALDYAIETIRELLGKGIPIFGICLGHQLLALALGAKTYKLKFGHRGANHPVKdlETGRVEITSQNHGFAVDEDSLp 307

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 494600084 322 AADVEITHLNLNDRTVAGLRHKSLPLFSVQYHPEASPGPHDADYLFERFVEAMR 375
Cdd:COG0505  308 ATDLEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDRFIELME 361
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
7-374 0e+00

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 689.89  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084   7 QPALLVLADGTAYRGWSFGANGTVVGEVVFNTGMTGYQEVLTDPSYCGQIVTFTYPELGNTGVNVEDEESHGPQVRAAIA 86
Cdd:PRK12564   3 MKAYLVLEDGTVFEGKAFGAEGETVGEVVFNTSMTGYQEILTDPSYAGQIVTFTYPLIGNYGVNREDFESDRPHAKGLIV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084  87 RNICHKPSNWRSTQSLPDYLKHHSIPGIYGIDTRALTRKIRTVGAMNGGISTEILDPAELLEQVQEAPSMAGLNLVRQVT 166
Cdd:PRK12564  83 RELSDIPSNWRSEMSLDEYLKENGIPGISGIDTRALTRKLREKGAMKGVIATEDFDAEELLEKARAFPGLLGLDLVKEVS 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084 167 TSEVYEWSEPTESnwefsdginsdaEILTVVAIDFGIKRNILRRLASYGCRVVVVPANTPPEEILKYKPDGIFLSNGPGD 246
Cdd:PRK12564 163 TKEPYPWPGPGGE------------LKYKVVAIDFGVKRNILRELAERGCRVTVVPATTTAEEILALNPDGVFLSNGPGD 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084 247 PATVIEGIETTKALLKSEKPIFGICMGHQILGRSLGADTFKLKFGHRGLNQPAG--LTERIEITSQNHGFAIDPDSLAAD 324
Cdd:PRK12564 231 PAALDYAIEMIRELLEKKIPIFGICLGHQLLALALGAKTYKMKFGHRGANHPVKdlETGKVEITSQNHGFAVDEDSLPAN 310

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 494600084 325 VEITHLNLNDRTVAGLRHKSLPLFSVQYHPEASPGPHDADYLFERFVEAM 374
Cdd:PRK12564 311 LEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDEFVELM 360
CPSaseIIsmall TIGR01368
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ...
 9-376 0e+00

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: 594.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084    9 ALLVLADGTAYRGWSFGANGTVVGEVVFNTGMTGYQEVLTDPSYCGQIVTFTYPELGNTGVNVEDEESHGPQVRAAIARN 88
Cdd:TIGR01368   1 AYLVLEDGTVFRGYSFGAEGTVAGEVVFNTGMTGYQEILTDPSYKGQIVVFTYPLIGNYGVNDEDAESKGIHVSGLVVRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084   89 ICHKPSNWRSTQSLPDYLKHHSIPGIYGIDTRALTRKIRTVGAMNGGISTEILDPAELLEQVQEAPSMAGLNLVRQVTTS 168
Cdd:TIGR01368  81 LSDRYSNWRATESLDQFLKRHGIPGIYGVDTRALVKKIREKGTMKGVISTEDSNDEELVEKARVSPDITGINLVAEVSTK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084  169 EVYEWSEPTESNwefsdginsdaeiLTVVAIDFGIKRNILRRLASYGCRVVVVPANTPPEEILKYKPDGIFLSNGPGDPA 248
Cdd:TIGR01368 161 EPYTWGQRGGKG-------------KRVVVIDFGVKRNILRRLVKRGCEVTVVPYDTDAEEIKKYNPDGIFLSNGPGDPA 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084  249 TVIEGIETTKALLkSEKPIFGICMGHQILGRSLGADTFKLKFGHRGLNQPAG--LTERIEITSQNHGFAIDPDSLAA-DV 325
Cdd:TIGR01368 228 AVEPAIETIRKLL-EKIPIFGICLGHQLLALAFGAKTYKMKFGHRGGNHPVKdlITGRVEITSQNHGYAVDPDSLPAgDL 306

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 494600084  326 EITHLNLNDRTVAGLRHKSLPLFSVQYHPEASPGPHDADYLFERFVEAMRE 376
Cdd:TIGR01368 307 EVTHVNLNDGTVEGIRHKDLPVFSVQYHPEASPGPHDTEYLFDEFIDLMKK 357
carA CHL00197
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
 8-381 0e+00

carbamoyl-phosphate synthase arginine-specific small subunit; Provisional


Pssm-ID: 214392 [Multi-domain]  Cd Length: 382  Bit Score: 549.01  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084   8 PALLVLADGTAYRGWSFGANGTVVGEVVFNTGMTGYQEVLTDPSYCGQIVTFTYPELGNTGVNVEDEESHGPQVRAAIAR 87
Cdd:CHL00197   6 PAILVLEDGTYYRGWSFSNPITTIGEVVFNTGMTGYQEIITDPSYFEQIVTFTYPEIGNTGINLEDIESVKIQVKGIIAK 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084  88 NICHKPSNWRSTQSLPDYLKHHSIPGIYGIDTRALTRKIRTVGAMNGGISTEILDPAELLEQVQEAPSMAGLNLVRQVTT 167
Cdd:CHL00197  86 NICKSSSNWRQQESLVSYLQRHKIPFIFGIDTRALTQHLRRFGTMNGCISNQNLNLSYLRAKIKESPHMPSSDLIPRVTT 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084 168 SEVYEWSEPTESNWEFSDGINSDAEI-LTVVAIDFGIKRNILRRLASYGCRVVVVPANTPPEEILKYKPDGIFLSNGPGD 246
Cdd:CHL00197 166 SSYYEWDEKSHPSFYLADNKRPHSSYqLKIIVIDFGVKYNILRRLKSFGCSITVVPATSPYQDILSYQPDGILLSNGPGD 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084 247 PATVIEGIETTKALLKSEKPIFGICMGHQILGRSLGADTFKLKFGHRGLNQPAGLTERIEITSQNHGFAIDPDSLAAD-V 325
Cdd:CHL00197 246 PSAIHYGIKTVKKLLKYNIPIFGICMGHQILSLALEAKTFKLKFGHRGLNHPSGLNQQVEITSQNHGFAVNLESLAKNkF 325

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 494600084 326 EITHLNLNDRTVAGLRHKSLPLFSVQYHPEASPGPHDADYLFERFVEAMRENRKVA 381
Cdd:CHL00197 326 YITHFNLNDGTVAGISHSPKPYFSVQYHPEASPGPHDADYLFEYFIEIIKHSKSSK 381
PRK12838 PRK12838
carbamoyl phosphate synthase small subunit; Reviewed
 8-378 6.13e-173

carbamoyl phosphate synthase small subunit; Reviewed


Pssm-ID: 183784 [Multi-domain]  Cd Length: 354  Bit Score: 485.94  E-value: 6.13e-173
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084   8 PALLVLADGTAYRGWSFGANGTVVGEVVFNTGMTGYQEVLTDPSYCGQIVTFTYPELGNTGVNVEDEESHGPQVRAAIAR 87
Cdd:PRK12838   2 KAYLILEDGTVFEGELIGAPIDVTGEIVFNTGMTGYQEVLTDPSYKGQIVVFTYPLIGNYGINADDYESKQPQVKGVIVY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084  88 NICHKPSNWRSTQSLPDYLKHHSIPGIYGIDTRALTRKIRTVGAMNGGISTeilDPAELLEqVQEAPSMAGLNLVRQVTT 167
Cdd:PRK12838  82 ELSREGSHYRAKQSLDDFLKEWNIPGISGVDTRALVKHIREKGTMKASITT---TDDAHAF-DQIKALVLPKNVVAQVST 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084 168 SEVYewseptesnweFSDGINsdaeiLTVVAIDFGIKRNILRRLASYGCRVVVVPANTPPEEILKYKPDGIFLSNGPGDP 247
Cdd:PRK12838 158 KEPY-----------TYGNGG-----KHVALIDFGYKKSILRSLSKRGCKVTVLPYDTSLEEIKNLNPDGIVLSNGPGDP 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084 248 ATVIEGIETTKALLKSeKPIFGICMGHQILGRSLGADTFKLKFGHRGLNQP--AGLTERIEITSQNHGFAIDPDSLAADV 325
Cdd:PRK12838 222 KELQPYLPEIKKLISS-YPILGICLGHQLIALALGADTEKLPFGHRGANHPviDLTTGRVWMTSQNHGYVVDEDSLDGTP 300

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 494600084 326 -EITHLNLNDRTVAGLRHKSLPLFSVQYHPEASPGPHDADYLFERFVEAMRENR 378
Cdd:PRK12838 301 lSVRFFNVNDGSIEGLRHKKKPVLSVQFHPEAHPGPHDAEYIFDEFLEMMEKAR 354
PLN02771 PLN02771
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
 9-367 8.54e-148

carbamoyl-phosphate synthase (glutamine-hydrolyzing)


Pssm-ID: 178370 [Multi-domain]  Cd Length: 415  Bit Score: 424.78  E-value: 8.54e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084   9 ALLVLADGTAYRGWSFGANGTVVGEVVFNTGMTGYQEVLTDPSYCGQIVTFTYPELGNTGVNVEDEESHGPQVRAAIARN 88
Cdd:PLN02771  57 ARLVLEDGSVWKAKSFGARGTQVGEVVFNTSLTGYQEILTDPSYAGQFVLMTNPHIGNTGVNFDDEESRQCFLAGLVIRS 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084  89 ICHKPSNWRSTQSLPDYLKHHSIPGIYGIDTRALTRKIRTVGAMNGGISTEILDPAELLEQVQEAPSMAGLNLVRQVTTS 168
Cdd:PLN02771 137 LSISTSNWRCTKTLGDYLAERNIMGIYDVDTRAITRRLREDGSLIGVLSTEDSKTDEELLKMSRSWDIVGIDLISGVSCK 216

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084 169 EVYEWSEPTESNWEFSDGiNSDAEILTVVAIDFGIKRNILRRLASYGCRVVVVPANTPPEEILKYKPDGIFLSNGPGDPA 248
Cdd:PLN02771 217 SPYEWVDKTNPEWDFNTN-SRDGESYHVIAYDFGIKHNILRRLASYGCKITVVPSTWPASEALKMKPDGVLFSNGPGDPS 295

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084 249 TVIEGIETTKALLkSEKPIFGICMGHQILGRSLGADTFKLKFGHRGLNQPA--GLTERIEITSQNHGFAIDPDSLAADVE 326
Cdd:PLN02771 296 AVPYAVETVKELL-GKVPVFGICMGHQLLGQALGGKTFKMKFGHHGGNHPVrnNRTGRVEISAQNHNYAVDPASLPEGVE 374

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 494600084 327 ITHLNLNDRTVAGLRHKSLPLFSVQYHPEASPGPHDADYLF 367
Cdd:PLN02771 375 VTHVNLNDGSCAGLAFPALNVMSLQYHPEASPGPHDSDNAF 415
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 196-371 3.58e-118

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: 340.24  E-value: 3.58e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084 196 VVAIDFGIKRNILRRLASYGCRVVVVPANTPPEEILKYKPDGIFLSNGPGDPATVIEGIETTKALLKSEKPIFGICMGHQ 275
Cdd:cd01744    1 VVVIDFGVKHNILRELLKRGCEVTVVPYNTDAEEILKLDPDGIFLSNGPGDPALLDEAIKTVRKLLGKKIPIFGICLGHQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084 276 ILGRSLGADTFKLKFGHRGLNQPAG--LTERIEITSQNHGFAIDPDSLAADVEITHLNLNDRTVAGLRHKSLPLFSVQYH 353
Cdd:cd01744   81 LLALALGAKTYKMKFGHRGSNHPVKdlITGRVYITSQNHGYAVDPDSLPGGLEVTHVNLNDGTVEGIRHKDLPVFSVQFH 160

                        170
                 ....*....|....*...
gi 494600084 354 PEASPGPHDADYLFERFV 371
Cdd:cd01744  161 PEASPGPHDTEYLFDEFL 178
CPSase_sm_chain pfam00988
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 11-136 6.55e-87

Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase domain is in the amino terminus of protein. 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 pfam00289. The small chain has a GATase domain in the carboxyl terminus. See pfam00117.


Pssm-ID: 460017 [Multi-domain]  Cd Length: 126  Bit Score: 258.79  E-value: 6.55e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084   11 LVLADGTAYRGWSFGANGTVVGEVVFNTGMTGYQEVLTDPSYCGQIVTFTYPELGNTGVNVEDEESHGPQVRAAIARNIC 90
Cdd:pfam00988   1 LVLEDGTVFEGKSFGAAGSTVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNPEDFESDKIHVAGLVVREYS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 494600084   91 HKPSNWRSTQSLPDYLKHHSIPGIYGIDTRALTRKIRTVGAMNGGI 136
Cdd:pfam00988  81 DEPSNWRAEESLDEWLKEQGIPGISGVDTRALTRKIREKGAMKGVI 126
CPSase_sm_chain smart01097
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 7-136 2.10e-86

Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase domain is in the amino terminus of protein. Carbamoyl-phosphate synthase catalyses 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 synthesise carbamoyl phosphate. The small chain has a GATase domain in the carboxyl terminus.


Pssm-ID: 198165 [Multi-domain]  Cd Length: 130  Bit Score: 257.69  E-value: 2.10e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084     7 QPALLVLADGTAYRGWSFGANGTVVGEVVFNTGMTGYQEVLTDPSYCGQIVTFTYPELGNTGVNVEDEESHGPQVRAAIA 86
Cdd:smart01097   1 MKAYLVLEDGTVFEGESFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNDEDFESDKIQVKGLVV 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 494600084    87 RNICHKPSNWRSTQSLPDYLKHHSIPGIYGIDTRALTRKIRTVGAMNGGI 136
Cdd:smart01097  81 RELSDEPSNWRSEQSLDEFLKENGIPGISGIDTRALTRKLREKGAMKGVI 130
GATase pfam00117
Glutamine amidotransferase class-I;
197-373 6.57e-69

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 215.18  E-value: 6.57e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084  197 VAIDFG--IKRNILRRLASYGCRVVVVPANTPPEEILKYKPDGIFLSNGPGDPATVIEGIETTKALLKSEKPIFGICMGH 274
Cdd:pfam00117   1 LLIDNGdsFTYNLARALRELGVEVTVVPNDTPAEEILEENPDGIILSGGPGSPGAAGGAIEAIREARELKIPILGICLGH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084  275 QILGRSLGADTFKLK-FGHRGLNQPAGLTE--------RIEITSQNHGFAIDPDSLAADVEITHLNLNDRTVAGLRHKSL 345
Cdd:pfam00117  81 QLLALAFGGKVVKAKkFGHHGKNSPVGDDGcglfyglpNVFIVRRYHSYAVDPDTLPDGLEVTATSENDGTIMGIRHKKL 160

                         170       180
                  ....*....|....*....|....*...
gi 494600084  346 PLFSVQYHPEASPGPHDADYLFERFVEA 373
Cdd:pfam00117 161 PIFGVQFHPESILTPHGPEILFNFFIKA 188
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 206-355 8.52e-29

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: 110.70  E-value: 8.52e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084 206 NILRRLASYGCRVVVVPANTPPEEILKY-KPDGIFLSNGPGDPATVIEGIETTKALLKsEKPIFGICMGHQILGRSLGAD 284
Cdd:cd01743   13 NLVQYLRELGAEVVVVRNDEITLEELELlNPDAIVISPGPGHPEDAGISLEIIRALAG-KVPILGVCLGHQAIAEAFGGK 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084 285 TFKLKFG---------HRGLNQPAGLTERIEITsQNHGFAIDPDSLAADVEITHLNlNDRTVAGLRHKSLPLFSVQYHPE 355
Cdd:cd01743   92 VVRAPEPmhgktseihHDGSGLFKGLPQPFTVG-RYHSLVVDPDPLPDLLEVTAST-EDGVIMALRHRDLPIYGVQFHPE 169
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 206-376 2.70e-25

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: 101.27  E-value: 2.70e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084 206 NILRRLASYGCRVVVVPAN-TPPEEILKYKPDGIFLSNGPGDPA------TVIEgiettkaLLKSEKPIFGICMGHQILG 278
Cdd:COG0512   13 NLVQYLGELGAEVVVVRNDeITLEEIEALAPDGIVLSPGPGTPEeagislEVIR-------AFAGKIPILGVCLGHQAIG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084 279 RSLGADTFKLKfghrglnQPA-GLTERIEITSQN--------------HGFAIDPDSLAADVEITHLNlNDRTVAGLRHK 343
Cdd:COG0512   86 EAFGGKVVRAP-------EPMhGKTSPITHDGSGlfaglpnpftatryHSLVVDRETLPDELEVTAWT-EDGEIMGIRHR 157

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 494600084 344 SLPLFSVQYHPEA--SPGPHDadyLFERFVEAMRE 376
Cdd:COG0512  158 ELPIEGVQFHPESilTEHGHQ---LLANFLELAGE 189
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 206-375 4.54e-24

anthranilate synthase component II; Provisional


Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 97.89  E-value: 4.54e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084 206 NILRRLASYGCRVVVVPANTPP-EEILKYKPDGIFLSNGPGDPATV---IEGIETtkalLKSEKPIFGICMGHQILGRSL 281
Cdd:PRK05670  14 NLVQYLGELGAEVVVYRNDEITlEEIEALNPDAIVLSPGPGTPAEAgisLELIRE----FAGKVPILGVCLGHQAIGEAF 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084 282 GADTFKLKF---G------HRGLNQPAGLTERIEITsQNHGFAIDPDSLAADVEITHLnLNDRTVAGLRHKSLPLFSVQY 352
Cdd:PRK05670  90 GGKVVRAKEimhGktspieHDGSGIFAGLPNPFTVT-RYHSLVVDRESLPDCLEVTAW-TDDGEIMGVRHKELPIYGVQF 167

                        170       180
                 ....*....|....*....|....*
gi 494600084 353 HPEA--SPGPHDadyLFERFVEAMR 375
Cdd:PRK05670 168 HPESilTEHGHK---LLENFLELAR 189
PRK14607 PRK14607
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
215-376 3.94e-19

bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;


Pssm-ID: 237764 [Multi-domain]  Cd Length: 534  Bit Score: 89.01  E-value: 3.94e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084 215 GCRVVVVPANTPPEEILKYKPDGIFLSNGPGDPATVIEGIETTKALLKsEKPIFGICMGHQILGRSLGADTFKLKFGHRG 294
Cdd:PRK14607  25 EEIEVVRNDEITIEEIEALNPSHIVISPGPGRPEEAGISVEVIRHFSG-KVPILGVCLGHQAIGYAFGGKIVHAKRILHG 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084 295 LNQP---------AGLTERIEITsQNHGFAIDPDSLAADVEITHLNlNDRTVAGLRHKSLPLFSVQYHPEaSPGPHDADY 365
Cdd:PRK14607 104 KTSPidhngkglfRGIPNPTVAT-RYHSLVVEEASLPECLEVTAKS-DDGEIMGIRHKEHPIFGVQFHPE-SILTEEGKR 180

                        170
                 ....*....|.
gi 494600084 366 LFERFVEAMRE 376
Cdd:PRK14607 181 ILKNFLNYQRE 191
GATase1_GMP_Synthase cd01742
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ...
 196-371 4.87e-19

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: 83.74  E-value: 4.87e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084 196 VVAIDFGIKRN--ILRRLASYGCRVVVVPANTPPEEILKYKPDGIFLSNGpgdPATVIEGIETT--KALLKSEKPIFGIC 271
Cdd:cd01742    1 ILILDFGSQYThlIARRVRELGVYSEILPNTTPLEEIKLKNPKGIILSGG---PSSVYEEDAPRvdPEIFELGVPVLGIC 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084 272 MGHQILGRSLGADTfklkfgHRGLNQPAGLTErIEITSQNHGFAIDPDSLaaDVEITHlnlNDR---------------- 335
Cdd:cd01742   78 YGMQLIAKALGGKV------ERGDKREYGKAE-IEIDDSSPLFEGLPDEQ--TVWMSH---GDEvvklpegfkviassdn 145

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 494600084 336 -TVAGLRHKSLPLFSVQYHPEASPGPHDADyLFERFV 371
Cdd:cd01742  146 cPVAAIANEEKKIYGVQFHPEVTHTEKGKE-ILKNFL 181
PRK07765 PRK07765
aminodeoxychorismate/anthranilate synthase component II;
236-355 8.57e-16

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181107 [Multi-domain]  Cd Length: 214  Bit Score: 75.47  E-value: 8.57e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084 236 DGIFLSNGPGDPATVIEGIETTKALLKSEKPIFGICMGHQILGRSLGADTFK---LKFG------HRGLNQPAGLTERIE 306
Cdd:PRK07765  48 DGVLLSPGPGTPERAGASIDMVRACAAAGTPLLGVCLGHQAIGVAFGATVDRapeLLHGktssvhHTGVGVLAGLPDPFT 127

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 494600084 307 ITsQNHGFAIDPDSLAADVEIThlnlnDRT----VAGLRHKSLPLFSVQYHPE 355
Cdd:PRK07765 128 AT-RYHSLTILPETLPAELEVT-----ARTdsgvIMAVRHRELPIHGVQFHPE 174
trpG_papA TIGR00566
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ...
 206-356 1.13e-15

glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This model describes the glutamine amidotransferase domain or peptide of the tryptophan-biosynthetic pathway enzyme anthranilate synthase or of the folate biosynthetic pathway enzyme para-aminobenzoate synthase. In at least one case, a single polypeptide from Bacillus subtilis was shown to have both functions. This model covers a subset of the sequences described by the Pfam model GATase.


Pssm-ID: 273144 [Multi-domain]  Cd Length: 188  Bit Score: 74.44  E-value: 1.13e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084  206 NILRRLASYGcRVVVVPANTPP--EEILKYKPDGIFLSNGPGDPATVIEGIETTKALlKSEKPIFGICMGHQILGRSLGA 283
Cdd:TIGR00566  14 NLVQYFCELG-AEVVVKRNDSLtlQEIEALLPLLIVISPGPCTPNEAGISLEAIRHF-AGKLPILGVCLGHQAMGQAFGG 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084  284 DTF---KLKFG------HRGLNQPAGLTERIEITsQNHGFAIDPDSLAADVEITHLNLNDRTVAGLRHKSLPLFSVQYHP 354
Cdd:TIGR00566  92 DVVranTVMHGktseieHNGAGIFRGLFNPLTAT-RYHSLVVEPETLPTCFPVTAWEEENIEIMAIRHRDLPLEGVQFHP 170


                  ..
gi 494600084  355 EA 356
Cdd:TIGR00566 171 ES 172
guaA_Nterm TIGR00888
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ...
 196-372 1.95e-15

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: 73.89  E-value: 1.95e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084  196 VVAIDFGIKRN--ILRRLASYGCRVVVVPANTPPEEILKYKPDGIFLSNGPgdpATVIEG--IETTKALLKSEKPIFGIC 271
Cdd:TIGR00888   1 ILVLDFGSQYTqlIARRLRELGVYSELVPNTTPLEEIREKNPKGIILSGGP---SSVYAEnaPRADEKIFELGVPVLGIC 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084  272 MGHQILGRSLGADTfklkfgHRGLNQPAGLTErIEITSQNHGFAIDPDSLaaDVEITHLNLNDRT--------------V 337
Cdd:TIGR00888  78 YGMQLMAKQLGGEV------GRAEKREYGKAE-LEILDEDDLFRGLPDES--TVWMSHGDKVKELpegfkvlatsdncpV 148

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 494600084  338 AGLRHKSLPLFSVQYHPEASPGPHDADyLFERFVE 372
Cdd:TIGR00888 149 AAMAHEEKPIYGVQFHPEVTHTEYGNE-LLENFVY 182
PRK00758 PRK00758
GMP synthase subunit A; Validated
 207-372 3.89e-15

GMP synthase subunit A; Validated


Pssm-ID: 179112 [Multi-domain]  Cd Length: 184  Bit Score: 72.96  E-value: 3.89e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084 207 ILRRLASYGCRVVVVPANTPPEEILKYKpDGIFLSNGPG-DPATVIEGIettkaLLKSEKPIFGICMGHQILGRSLGADT 285
Cdd:PRK00758  15 IHRTLRYLGVDAKIIPNTTPVEEIKAFE-DGLILSGGPDiERAGNCPEY-----LKELDVPILGICLGHQLIAKAFGGEV 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084 286 fklkfgHRGLNQPAGLTErIEITSQNHGFAIDPDSLAA-----DvEITHLNLNDRTVA--------GLRHKSLPLFSVQY 352
Cdd:PRK00758  89 ------GRGEYGEYALVE-VEILDEDDILKGLPPEIRVwashaD-EVKELPDGFEILArsdiceveAMKHKEKPIYGVQF 160

                        170       180
                 ....*....|....*....|
gi 494600084 353 HPEASPGPHdADYLFERFVE 372
Cdd:PRK00758 161 HPEVAHTEY-GEEIFKNFLE 179
PRK13566 PRK13566
anthranilate synthase component I;
211-355 3.88e-14

anthranilate synthase component I;


Pssm-ID: 237429 [Multi-domain]  Cd Length: 720  Bit Score: 73.80  E-value: 3.88e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084 211 LASY----GCRVVVVPANTPPEEILKYKPDGIFLSNGPGDPATVieGI-ETTKALLKSEKPIFGICMGHQILGRSLGAdt 285
Cdd:PRK13566 542 LANYfrqtGAEVTTVRYGFAEEMLDRVNPDLVVLSPGPGRPSDF--DCkATIDAALARNLPIFGVCLGLQAIVEAFGG-- 617

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084 286 fklKFGHrgLNQPA-GLTERIEITSQN---------------HGFAIDPDSLAADVEITHLNlNDRTVAGLRHKSLPLFS 349
Cdd:PRK13566 618 ---ELGQ--LAYPMhGKPSRIRVRGPGrlfsglpeeftvgryHSLFADPETLPDELLVTAET-EDGVIMAIEHKTLPVAA 691


                 ....*.
gi 494600084 350 VQYHPE 355
Cdd:PRK13566 692 VQFHPE 697
PLN02335 PLN02335
anthranilate synthase
 187-356 5.30e-14

anthranilate synthase


Pssm-ID: 177969 [Multi-domain]  Cd Length: 222  Bit Score: 70.60  E-value: 5.30e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084 187 INSDAEILTVVAIDF--GIKRNILRRLASYGCRVVVVPANTPP-EEILKYKPDGIFLSNGPGDPATviEGIETTKAL-LK 262
Cdd:PLN02335  12 INSSKQNGPIIVIDNydSFTYNLCQYMGELGCHFEVYRNDELTvEELKRKNPRGVLISPGPGTPQD--SGISLQTVLeLG 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084 263 SEKPIFGICMGHQILGRSLGADTFKLKFG--HrGLNQPAGLTERIEIT-----------SQNHGFAIDPDSLAAD-VEIT 328
Cdd:PLN02335  90 PLVPLFGVCMGLQCIGEAFGGKIVRSPFGvmH-GKSSPVHYDEKGEEGlfsglpnpftaGRYHSLVIEKDTFPSDeLEVT 168

                        170       180
                 ....*....|....*....|....*....
gi 494600084 329 HLNlNDRTVAGLRHKSLP-LFSVQYHPEA 356
Cdd:PLN02335 169 AWT-EDGLIMAARHRKYKhIQGVQFHPES 196
PRK06774 PRK06774
aminodeoxychorismate synthase component II;
228-356 1.20e-13

aminodeoxychorismate synthase component II;


Pssm-ID: 180689 [Multi-domain]  Cd Length: 191  Bit Score: 68.73  E-value: 1.20e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084 228 EEILKYKPDGIFLSNGPGDPATVIEGIETTKALlKSEKPIFGICMGHQILGRSLGADTFKLK---------FGH------ 292
Cdd:PRK06774  37 TDIEQLAPSHLVISPGPCTPNEAGISLAVIRHF-ADKLPILGVCLGHQALGQAFGARVVRARqvmhgktsaICHsgqgvf 115

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494600084 293 RGLNQPAGLTerieitsQNHGFAIDPDSLAADVEITHLNLNDRTV---AGLRHKSLPLFSVQYHPEA 356
Cdd:PRK06774 116 RGLNQPLTVT-------RYHSLVIAADSLPGCFELTAWSERGGEMdeiMGIRHRTLPLEGVQFHPES 175
guaA PRK00074
GMP synthase; Reviewed
 195-371 1.78e-12

GMP synthase; Reviewed


Pssm-ID: 234614 [Multi-domain]  Cd Length: 511  Bit Score: 68.54  E-value: 1.78e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084 195 TVVAIDFG------IKRNIlRRLASYgCrvVVVPANTPPEEILKYKPDGIFLSNGPgdpATVIE--GIETTKALLKSEKP 266
Cdd:PRK00074   5 KILILDFGsqytqlIARRV-RELGVY-S--EIVPYDISAEEIRAFNPKGIILSGGP---ASVYEegAPRADPEIFELGVP 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084 267 IFGICMGHQILGRSLG---ADTFKLKFGHRGLN--QPAGLTERIEITSQ---NHGfaidpDS---LAADVEIThlnlnDR 335
Cdd:PRK00074  78 VLGICYGMQLMAHQLGgkvERAGKREYGRAELEvdNDSPLFKGLPEEQDvwmSHG-----DKvteLPEGFKVI-----AS 147

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 494600084 336 T----VAGLRHKSLPLFSVQYHPEASPGPHDADYLfERFV 371
Cdd:PRK00074 148 TencpIAAIANEERKFYGVQFHPEVTHTPQGKKLL-ENFV 186
PRK07649 PRK07649
aminodeoxychorismate/anthranilate synthase component II;
228-375 9.09e-12

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181066 [Multi-domain]  Cd Length: 195  Bit Score: 63.67  E-value: 9.09e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084 228 EEILKYKPDGIFLSNGPGDPATVIEGIETTKALlKSEKPIFGICMGHQILGRSLGADTF---KLKFG------HRGLNQP 298
Cdd:PRK07649  37 SDIENMKPDFLMISPGPCSPNEAGISMEVIRYF-AGKIPIFGVCLGHQSIAQVFGGEVVraeRLMHGktslmhHDGKTIF 115

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494600084 299 AGLTERIEITsQNHGFAIDPDSLAADVEITHLNLNDRTVAgLRHKSLPLFSVQYHPEASPGPHDADyLFERFVEAMR 375
Cdd:PRK07649 116 SDIPNPFTAT-RYHSLIVKKETLPDCLEVTSWTEEGEIMA-IRHKTLPIEGVQFHPESIMTSHGKE-LLQNFIRKYS 189
PRK06895 PRK06895
anthranilate synthase component II;
238-356 1.09e-11

anthranilate synthase component II;


Pssm-ID: 235882 [Multi-domain]  Cd Length: 190  Bit Score: 63.22  E-value: 1.09e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084 238 IFLSNGPGDPatviEGIETTKALLK---SEKPIFGICMGHQILGRSLGADTFKLKFGHRGLNQP----------AGLTER 304
Cdd:PRK06895  47 ILISPGPDVP----RAYPQLFAMLEryhQHKSILGVCLGHQTLCEFFGGELYNLNNVRHGQQRPlkvrsnsplfDGLPEE 122

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 494600084 305 IEItSQNHGFAIDPDSLAADVEITHLnLNDRTVAGLRHKSLPLFSVQYHPEA 356
Cdd:PRK06895 123 FNI-GLYHSWAVSEENFPTPLEITAV-CDENVVMAMQHKTLPIYGVQFHPES 172
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 207-358 1.65e-11

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: 63.43  E-value: 1.65e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084 207 ILRRLASYGCRVVVV--------PANTPPEEilkykPDGIFLSNGPGDPATVIEGIETTKALLK----SEKPIFGICMGH 274
Cdd:COG0518   18 IARRLREAGIELDVLrvyageilPYDPDLED-----PDGLILSGGPMSVYDEDPWLEDEPALIReafeLGKPVLGICYGA 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084 275 QILGRSLGADTFKLkfGHRGLnqpaGLTErIEITSQNHGFAIDPDSLAA-----D--VEI----THLNLNDRT-VAGLRH 342
Cdd:COG0518   93 QLLAHALGGKVEPG--PGREI----GWAP-VELTEADPLFAGLPDEFTVwmshgDtvTELpegaEVLASSDNCpNQAFRY 165

                        170
                 ....*....|....*.
gi 494600084 343 KSlPLFSVQYHPEASP 358
Cdd:COG0518  166 GR-RVYGVQFHPEVTH 180
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 205-371 2.08e-11

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: 62.21  E-value: 2.08e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084 205 RNILRRLASYGCRVVVVPANTPPEEILKY--KPDGIFLSNGP--------GDPATVIEGI-----ETTKALLK----SEK 265
Cdd:cd01745   22 QYYVDAVRKAGGLPVLLPPVDDEEDLEQYleLLDGLLLTGGGdvdpplygEEPHPELGPIdperdAFELALLRaaleRGK 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084 266 PIFGICMGHQILGRSLGADtfklkfghrgLNQpaglteRIEITSqNHGFAIDPdsLAADVEITHLNlNDRTVAGLRHKSL 345
Cdd:cd01745  102 PILGICRGMQLLNVALGGT----------LYQ------DIRVNS-LHHQAIKR--LADGLRVEARA-PDGVIEAIESPDR 161

                        170       180
                 ....*....|....*....|....*....
gi 494600084 346 P-LFSVQYHPE--ASPGPHDADyLFERFV 371
Cdd:cd01745  162 PfVLGVQWHPEwlADTDPDSLK-LFEAFV 189
trpG CHL00101
anthranilate synthase component 2
 229-356 7.62e-11

anthranilate synthase component 2


Pssm-ID: 214365 [Multi-domain]  Cd Length: 190  Bit Score: 60.90  E-value: 7.62e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084 229 EILKYKPDGIFLSNGPGDPATVIEGIETTKALLkSEKPIFGICMGHQILGRSLGADTFKL-KFGHRGLNQPAGLTERIEI 307
Cdd:CHL00101  38 KIKNLNIRHIIISPGPGHPRDSGISLDVISSYA-PYIPILGVCLGHQSIGYLFGGKIIKApKPMHGKTSKIYHNHDDLFQ 116

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 494600084 308 TSQN-------HGFAIDPDSLAADVEITHLNlNDRTVAGLRHKSLP-LFSVQYHPEA 356
Cdd:CHL00101 117 GLPNpftatryHSLIIDPLNLPSPLEITAWT-EDGLIMACRHKKYKmLRGIQFHPES 172
PuuD COG2071
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ...
 205-376 8.83e-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: 61.34  E-value: 8.83e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084 205 RNILRRLASYGCRVVVVPANTPPEEILKYKP--DGIFLSNGP--------GDPATVIEGI-----ETTKAL----LKSEK 265
Cdd:COG2071   18 EDYVRAVRAAGGLPVLLPPVGDEEDLDELLDrlDGLVLTGGAdvdpalygEEPHPELGPIdperdAFELALiraaLERGK 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084 266 PIFGICMGHQILGRSLG-------ADTFKLKFGHRGLNQPAGLTERIEITSQ--------------N--HGFAIdpDSLA 322
Cdd:COG2071   98 PVLGICRGMQLLNVALGgtlyqdlPDQVPGALDHRQPAPRYAPRHTVEIEPGsrlarilgeeeirvNslHHQAV--KRLG 175

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 494600084 323 ADVEIT---HlnlnDRTVAGLRHKSLP-LFSVQYHPEASPGPHDADY-LFERFVEAMRE 376
Cdd:COG2071  176 PGLRVSaraP----DGVIEAIESPGAPfVLGVQWHPEWLAASDPLSRrLFEAFVEAARA 230
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 205-277 1.47e-10

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: 57.99  E-value: 1.47e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494600084 205 RNILRRLASYGCRVVVVPANTPPEEILKY--KPDGIFLSNGPGDPATVI---EGIETTKALLKSEKPIFGICMGHQIL 277
Cdd:cd01653   15 ASPLDALREAGAEVDVVSPDGGPVESDVDldDYDGLILPGGPGTPDDLArdeALLALLREAAAAGKPILGICLGAQLL 92
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 205-277 2.29e-10

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: 56.83  E-value: 2.29e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494600084 205 RNILRRLASYGCRVVVVPANTPPEEILKY--KPDGIFLSNGPGDPATVI---EGIETTKALLKSEKPIFGICMGHQIL 277
Cdd:cd03128   15 ASPLDALREAGAEVDVVSPDGGPVESDVDldDYDGLILPGGPGTPDDLAwdeALLALLREAAAAGKPVLGICLGAQLL 92
PRK08007 PRK08007
aminodeoxychorismate synthase component 2;
228-356 5.78e-10

aminodeoxychorismate synthase component 2;


Pssm-ID: 181194 [Multi-domain]  Cd Length: 187  Bit Score: 58.00  E-value: 5.78e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084 228 EEILKYKPDGIFLSNGPGDPATVIEGIETTKALlKSEKPIFGICMGHQILGRSLGADTF---KLKFG------HRGLNQP 298
Cdd:PRK08007  37 ADIDALKPQKIVISPGPCTPDEAGISLDVIRHY-AGRLPILGVCLGHQAMAQAFGGKVVraaKVMHGktspitHNGEGVF 115

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 494600084 299 AGLTERIEITsQNHGFAIDPDSLAADVEITHLNlNDRTVAGLRHKSLPLFSVQYHPEA 356
Cdd:PRK08007 116 RGLANPLTVT-RYHSLVVEPDSLPACFEVTAWS-ETREIMGIRHRQWDLEGVQFHPES 171
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 193-371 1.13e-08

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: 54.56  E-value: 1.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084 193 ILTVVAIDFGIKRNILRRLASYGCRVVV--VPANTPPEEILKYkpDGIFLSNGPGDPATV-IEGIETTKALLK----SEK 265
Cdd:cd01741    5 LQHDTPEGPGLFEDLLREAGAETIEIDVvdVYAGELLPDLDDY--DGLVILGGPMSVDEDdYPWLKKLKELIRqalaAGK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084 266 PIFGICMGHQILGRSLGAdtfklKFGHRGLNQPAGLTeRIEITSQnhgFAIDPDSLAADVEITHLNLNDRTVAGLRHKSL 345
Cdd:cd01741   83 PVLGICLGHQLLARALGG-----KVGRNPKGWEIGWF-PVTLTEA---GKADPLFAGLPDEFPVFHWHGDTVVELPPGAV 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 494600084 346 PLFS-----------------VQYHPEASpgphdadyLFERFV 371
Cdd:cd01741  154 LLASseacpnqafrygdralgLQFHPEER--------LLRNFL 188
PRK08857 PRK08857
aminodeoxychorismate/anthranilate synthase component II;
235-356 1.71e-08

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181566 [Multi-domain]  Cd Length: 193  Bit Score: 54.11  E-value: 1.71e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084 235 PDGIFLSNGPGDPATVIEGIETTKALLkSEKPIFGICMGHQILGRSLGADTFKLK---------FGHRGLNQPAGLTERI 305
Cdd:PRK08857  44 PTHLVISPGPCTPNEAGISLQAIEHFA-GKLPILGVCLGHQAIAQVFGGQVVRARqvmhgktspIRHTGRSVFKGLNNPL 122

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 494600084 306 EITsQNHGFAIDPDSLAADVEITHLNLNDR----TVAGLRHKSLPLFSVQYHPEA 356
Cdd:PRK08857 123 TVT-RYHSLVVKNDTLPECFELTAWTELEDgsmdEIMGFQHKTLPIEAVQFHPES 176
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 215-355 1.90e-08

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: 54.19  E-value: 1.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084  215 GCRVVVVPANTPPEEILKY--KPDGIFLSNGP-------GDPATVIEGI------ETTKAL----LKSEKPIFGICMGHQ 275
Cdd:pfam07722  37 GGLPVLLPILGDPEDAAAIldRLDGLLLTGGPnvdphfyGEEPSESGGPydpardAYELALiraaLARGKPILGICRGFQ 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084  276 ILGRSLG-----------------ADTFKLKFGHR--------GLNQPAGLTERIEITSQnHGFAIdpDSLAADVEITHL 330
Cdd:pfam07722 117 LLNVALGgtlyqdiqeqpgftdhrEHCQVAPYAPShavnvepgSLLASLLGSEEFRVNSL-HHQAI--DRLAPGLRVEAV 193

                         170       180
                  ....*....|....*....|....*..
gi 494600084  331 NlNDRTVAGLRHKSLPLF--SVQYHPE 355
Cdd:pfam07722 194 A-PDGTIEAIESPNAKGFalGVQWHPE 219
PLN02347 PLN02347
GMP synthetase
 195-371 7.69e-08

GMP synthetase


Pssm-ID: 215197 [Multi-domain]  Cd Length: 536  Bit Score: 53.92  E-value: 7.69e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084 195 TVVAIDFGIKRN--ILRRLASYGCRVVVVPANTPPEEILKYKPDGIFLSNGPGD---------PATVIEGIETTKAllks 263
Cdd:PLN02347  12 VVLILDYGSQYThlITRRVRELGVYSLLLSGTASLDRIASLNPRVVILSGGPHSvhvegaptvPEGFFDYCRERGV---- 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084 264 ekPIFGICMGHQILGRSLGAdtfKLKFGHRglnQPAGLTErIEITSQNHGFAIDPDSLAADVEITH----------LNLN 333
Cdd:PLN02347  88 --PVLGICYGMQLIVQKLGG---EVKPGEK---QEYGRME-IRVVCGSQLFGDLPSGETQTVWMSHgdeavklpegFEVV 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 494600084 334 DRTVAG----LRHKSLPLFSVQYHPEASPGPHDADYLfERFV 371
Cdd:PLN02347 159 AKSVQGavvaIENRERRIYGLQYHPEVTHSPKGMETL-RHFL 199
PRK05637 PRK05637
anthranilate synthase component II; Provisional
 206-345 2.13e-07

anthranilate synthase component II; Provisional


Pssm-ID: 180178 [Multi-domain]  Cd Length: 208  Bit Score: 51.00  E-value: 2.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084 206 NILRRLASYGCRVVVVPANTPPEEILKYKPDGIFLSNGPGDPATVIEGIETTKALLkSEKPIFGICMGHQILGRSLGADT 285
Cdd:PRK05637  16 NLVDAFAVAGYKCTVFRNTVPVEEILAANPDLICLSPGPGHPRDAGNMMALIDRTL-GQIPLLGICLGFQALLEHHGGKV 94

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084 286 FKLKFGHrGLNQPAGLTERIEITSQNHGfaidpdsLAADVEITHLNLNDRTVAGLRHKSL 345
Cdd:PRK05637  95 EPCGPVH-GTTDNMILTDAGVQSPVFAG-------LATDVEPDHPEIPGRKVPIARYHSL 146
hisH PRK13143
imidazole glycerol phosphate synthase subunit HisH; Provisional
 196-376 7.58e-06

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237289 [Multi-domain]  Cd Length: 200  Bit Score: 46.40  E-value: 7.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084 196 VVAIDFGIK--RNILRRLASYGCRVVVVpanTPPEEILKYkpDGIFLSnGPGDPATVIEGIETTKALL----KSEKPIFG 269
Cdd:PRK13143   3 IVIIDYGVGnlRSVSKALERAGAEVVIT---SDPEEILDA--DGIVLP-GVGAFGAAMENLSPLRDVIleaaRSGKPFLG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084 270 ICMGHQIL---------GRSLG-----ADTFK--LKFGHRGLNQ-----PAGLTERIEitsqN------HGFAIDPDSLA 322
Cdd:PRK13143  77 ICLGMQLLfesseegggVRGLGlfpgrVVRFPagVKVPHMGWNTvkvvkDCPLFEGID----GeyvyfvHSYYAYPDDED 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084 323 ADVEITHLnlndrtvaGLRHKSL----PLFSVQYHPEAS--PGPHdadyLFERFVEAMRE 376
Cdd:PRK13143 153 YVVATTDY--------GIEFPAAvcndNVFGTQFHPEKSgeTGLK----ILENFVELIKR 200
GATase1_Glutamyl_Hydrolase cd01747
Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase; Type 1 ...
 212-378 2.49e-05

Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase; Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase. gamma-Glutamyl Hydrolase catalyzes the cleavage of the gamma-glutamyl chain of folylpoly-gamma-glutamyl substrates and is a central enzyme in folyl and antifolyl poly-gamma-glutamate metabolism. GATase activity involves the removal of the ammonia group from a glutamate molecule and its subsequent transfer to a specific substrate, thus creating a new carbon-nitrogen group on the substrate. gamma-Glutamyl hydrolases belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.


Pssm-ID: 153218 [Multi-domain]  Cd Length: 273  Bit Score: 45.39  E-value: 2.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084 212 ASY-------GCRVVVVPANTPPEE---ILKyKPDGIFLSNGpgdpATVIEGIETTKAL-------LKSEK-----PIFG 269
Cdd:cd01747   23 ASYvkflesaGARVVPIWINESEEYydkLFK-SINGILFPGG----AVDIDTSGYARTAkiiynlaLERNDagdyfPVWG 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084 270 ICMGHQILGRSL-GADTFKLKFGHRGLNQPAGLTE-----RIE---------------ITSQNHGFAIDPDSLAADV--- 325
Cdd:cd01747   98 TCLGFELLTYLTsGETLLLEATEATNSALPLNFTEdalqsRLFkrfppdllkslatepLTMNNHRYGISPENFTENGlls 177

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494600084 326 ---EITHLNlNDRT----VAGLRHKSLPLFSVQYHPEASP--------GPHDAD------YLFERFVEAMRENR 378
Cdd:cd01747  178 dffNVLTTN-DDWNgvefISTVEAYKYPIYGVQWHPEKNAfewkksssIPHSEEairltqYFANFFVNEARKSN 250
GATase1_IGP_Synthase cd01748
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ...
 196-357 3.35e-05

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: 44.41  E-value: 3.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084 196 VVAIDFGIK--RNILRRLASYGCRVVVVPAntpPEEILKYkpDGIFLsngPGDPA--TVIEGIETT------KALLKSEK 265
Cdd:cd01748    1 IAIIDYGMGnlRSVANALERLGAEVIITSD---PEEILSA--DKLIL---PGVGAfgDAMANLRERgliealKEAIASGK 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084 266 PIFGICMGHQILGRS---------LG---------ADTFKLKFGHRGLNQpaglterIEITSQN---------------H 312
Cdd:cd01748   73 PFLGICLGMQLLFESseegggtkgLGlipgkvvrfPASEGLKVPHMGWNQ-------LEITKESplfkgipdgsyfyfvH 145

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 494600084 313 GFAIDPDSlaADVEITHLNLNDRTVAGLRHKSlpLFSVQYHPEAS 357
Cdd:cd01748  146 SYYAPPDD--PDYILATTDYGGKFPAAVEKDN--IFGTQFHPEKS 186
PRK09522 PRK09522
bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate ...
 191-356 5.39e-05

bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate phosphoribosyltransferase TrpD;


Pssm-ID: 181927 [Multi-domain]  Cd Length: 531  Bit Score: 45.02  E-value: 5.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084 191 AEILTVVAIDfGIKRNILRRLASYGCRVVV----VPANTPPEEILKYKPDGIFLSNGPGDP--ATVIEGIETTkalLKSE 264
Cdd:PRK09522   2 ADILLLDNID-SFTYNLADQLRSNGHNVVIyrnhIPAQTLIERLATMSNPVLMLSPGPGVPseAGCMPELLTR---LRGK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084 265 KPIFGICMGHQILGRSLGADTFKL---------KFGHRGLNQPAGLTERIEITSQNHGFAID-PDSLAADveiTHLNlnd 334
Cdd:PRK09522  78 LPIIGICLGHQAIVEAYGGYVGQAgeilhgkasSIEHDGQAMFAGLTNPLPVARYHSLVGSNiPAGLTIN---AHFN--- 151

                        170       180
                 ....*....|....*....|..
gi 494600084 335 RTVAGLRHKSLPLFSVQYHPEA 356
Cdd:PRK09522 152 GMVMAVRHDADRVCGFQFHPES 173
GATase1_CobQ cd01750
Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ); Type ...
 209-281 4.28e-04

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: 41.08  E-value: 4.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084 209 RRLASYGCRVVVVPANTPPEeilkyKPDGIFLsngPGDPATV-------IEGI-ETTKALLKSEKPIFGICMGHQILGRS 280
Cdd:cd01750   17 PLAREPGVDVRYVEVPEGLG-----DADLIIL---PGSKDTIqdlawlrKRGLaEAIKNYARAGGPVLGICGGYQMLGKY 88


                 .
gi 494600084 281 L 281
Cdd:cd01750   89 I 89
HisH COG0118
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ...
 195-277 1.27e-03

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: 39.64  E-value: 1.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084 195 TVVAIDFG---IK--RNILRRLasyGCRVVVVpanTPPEEILKYkpDGIFLsngPGD---PATV-----IEGIETTKALL 261
Cdd:COG0118    2 MIAIIDYGmgnLRsvAKALERL---GAEVVVT---SDPDEIRAA--DRLVL---PGVgafGDAMenlreRGLDEAIREAV 70

                         90
                 ....*....|....*.
gi 494600084 262 KSEKPIFGICMGHQIL 277
Cdd:COG0118   71 AGGKPVLGICLGMQLL 86
IMP_synth_hisH TIGR01855
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model ...
 196-280 2.21e-03

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: 38.85  E-value: 2.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084  196 VVAIDFGIK--RNILRRLASYGCRVVVVpanTPPEEILKYkpDGIFLSnGPGDPATVIEGIE------TTKALLKSEKPI 267
Cdd:TIGR01855   1 IVIIDYGVGnlGSVKRALKRVGAEPVVV---KDSKEAELA--DKLILP-GVGAFGAAMARLRengldlFVELVVRLGKPV 74

                          90
                  ....*....|...
gi 494600084  268 FGICMGHQILGRS 280
Cdd:TIGR01855  75 LGICLGMQLLFER 87
PRK06490 PRK06490
glutamine amidotransferase; Provisional
 261-319 2.30e-03

glutamine amidotransferase; Provisional


Pssm-ID: 180590 [Multi-domain]  Cd Length: 239  Bit Score: 39.17  E-value: 2.30e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494600084 261 LKSEKPIFGICMGHQILGRSLGAdtfklkfghRGLNQPAGLTE----RIEITSQNHGFAIDPD 319
Cdd:PRK06490  83 LKENKPFLGICLGAQMLARHLGA---------RVAPHPDGRVEigyyPLRPTEAGRALMHWPE 136
hisH PRK13141
imidazole glycerol phosphate synthase subunit HisH; Provisional
 199-357 2.71e-03

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237288 [Multi-domain]  Cd Length: 205  Bit Score: 38.57  E-value: 2.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084 199 IDFGIK--RNILRRLASYGCRVVVVpANtpPEEILKYkpDGIFLsngPG----DPAtvIEGIETT------KALLKSEKP 266
Cdd:PRK13141   5 IDYGMGnlRSVEKALERLGAEAVIT-SD--PEEILAA--DGVIL---PGvgafPDA--MANLRERgldeviKEAVASGKP 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494600084 267 IFGICMGHQILGRS---------LG---------ADTFKLKFGHRGLNQ-----PAGLTERIEitsQN------HGFAI- 316
Cdd:PRK13141  75 LLGICLGMQLLFESseefgetegLGllpgrvrrfPPEEGLKVPHMGWNQlelkkESPLLKGIP---DGayvyfvHSYYAd 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 494600084 317 --DPDSLAADVEitHlnlnDRTVAGLRHKSLpLFSVQYHPEAS 357
Cdd:PRK13141 152 pcDEEYVAATTD--Y----GVEFPAAVGKDN-VFGAQFHPEKS 187
PLN02889 PLN02889
oxo-acid-lyase/anthranilate synthase
 236-283 6.94e-03

oxo-acid-lyase/anthranilate synthase


Pssm-ID: 215481 [Multi-domain]  Cd Length: 918  Bit Score: 38.68  E-value: 6.94e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 494600084 236 DGIFLSNGPGDPATVIE-GIETTKALLKSEKPIFGICMGHQILGRSLGA 283
Cdd:PLN02889 133 DNIVISPGPGSPTCPADiGICLRLLLECRDIPILGVCLGHQALGYVHGA 181
 
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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