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Conserved domains on  [gi|1234979156|gb|OZO95522|]
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carbamoyl-phosphate synthase small subunit [Escherichia coli]

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 ...
 1-375 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: 727.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156   1 MIKSALLVLEDGTQFHGRAIGATGSAVGEVVFNTSMTGYQEILTDPSYSRQIVTLTYPHIGNVGTNDADEESSQVHAQGL 80
Cdd:COG0505     1 MMMKALLVLEDGTVFEGKSFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVTFTYPHIGNYGVNDEDFESDRPWVAGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156  81 VIRDLPLIASNFRNTEDLSSYLKRHNIVAIADIDTRKLTRLLREKGAQNGCIIAGDNpDAALALEKARAFPGLNGMDLAK 160
Cdd:COG0505    81 VVRELSRRPSNWRSEESLDEYLKEHGIPGISGIDTRALTRHLREKGAMKGVISTGDL-DIEELLEKARAAPGMEGLDLVK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156 161 EVTTAEAYSWTQgswtltggmpeakkEDELPFHVVAYDFGAKRNILRMLVDRGCRLTIVPAQTSAEDVLKMNPDGIFLSN 240
Cdd:COG0505   160 EVSTKEPYEWTE--------------APGAGFHVVALDFGVKRNILRELAERGCRVTVVPATTSAEEILALNPDGVFLSN 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156 241 GPGDPAPCDYAITAIQKFLETDIPVFGICLGHQLLALASGAKTVKMKFGHHGGNHPVKDVEKNVVMITAQNHGFAVDEAT 320
Cdd:COG0505   226 GPGDPAALDYAIETIRELLGKGIPIFGICLGHQLLALALGAKTYKLKFGHRGANHPVKDLETGRVEITSQNHGFAVDEDS 305

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1234979156 321 LPA-NLRVTHKSLFDGTLQGIHRTDKPAFSFQGHPEASPGPHDAAPLFDHFIELIE 375
Cdd:COG0505   306 LPAtDLEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDRFIELME 361
 
Name Accession Description Interval E-value
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 1-375 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: 727.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156   1 MIKSALLVLEDGTQFHGRAIGATGSAVGEVVFNTSMTGYQEILTDPSYSRQIVTLTYPHIGNVGTNDADEESSQVHAQGL 80
Cdd:COG0505     1 MMMKALLVLEDGTVFEGKSFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVTFTYPHIGNYGVNDEDFESDRPWVAGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156  81 VIRDLPLIASNFRNTEDLSSYLKRHNIVAIADIDTRKLTRLLREKGAQNGCIIAGDNpDAALALEKARAFPGLNGMDLAK 160
Cdd:COG0505    81 VVRELSRRPSNWRSEESLDEYLKEHGIPGISGIDTRALTRHLREKGAMKGVISTGDL-DIEELLEKARAAPGMEGLDLVK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156 161 EVTTAEAYSWTQgswtltggmpeakkEDELPFHVVAYDFGAKRNILRMLVDRGCRLTIVPAQTSAEDVLKMNPDGIFLSN 240
Cdd:COG0505   160 EVSTKEPYEWTE--------------APGAGFHVVALDFGVKRNILRELAERGCRVTVVPATTSAEEILALNPDGVFLSN 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156 241 GPGDPAPCDYAITAIQKFLETDIPVFGICLGHQLLALASGAKTVKMKFGHHGGNHPVKDVEKNVVMITAQNHGFAVDEAT 320
Cdd:COG0505   226 GPGDPAALDYAIETIRELLGKGIPIFGICLGHQLLALALGAKTYKLKFGHRGANHPVKDLETGRVEITSQNHGFAVDEDS 305

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1234979156 321 LPA-NLRVTHKSLFDGTLQGIHRTDKPAFSFQGHPEASPGPHDAAPLFDHFIELIE 375
Cdd:COG0505   306 LPAtDLEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDRFIELME 361
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
1-374 0e+00

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 707.22  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156   1 MIKSALLVLEDGTQFHGRAIGATGSAVGEVVFNTSMTGYQEILTDPSYSRQIVTLTYPHIGNVGTNDADEESSQVHAQGL 80
Cdd:PRK12564    1 MMMKAYLVLEDGTVFEGKAFGAEGETVGEVVFNTSMTGYQEILTDPSYAGQIVTFTYPLIGNYGVNREDFESDRPHAKGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156  81 VIRDLPLIASNFRNTEDLSSYLKRHNIVAIADIDTRKLTRLLREKGAQNGCIIAGDnPDAALALEKARAFPGLNGMDLAK 160
Cdd:PRK12564   81 IVRELSDIPSNWRSEMSLDEYLKENGIPGISGIDTRALTRKLREKGAMKGVIATED-FDAEELLEKARAFPGLLGLDLVK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156 161 EVTTAEAYSWTqgswtltggmpeaKKEDELPFHVVAYDFGAKRNILRMLVDRGCRLTIVPAQTSAEDVLKMNPDGIFLSN 240
Cdd:PRK12564  160 EVSTKEPYPWP-------------GPGGELKYKVVAIDFGVKRNILRELAERGCRVTVVPATTTAEEILALNPDGVFLSN 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156 241 GPGDPAPCDYAITAIQKFLETDIPVFGICLGHQLLALASGAKTVKMKFGHHGGNHPVKDVEKNVVMITAQNHGFAVDEAT 320
Cdd:PRK12564  227 GPGDPAALDYAIEMIRELLEKKIPIFGICLGHQLLALALGAKTYKMKFGHRGANHPVKDLETGKVEITSQNHGFAVDEDS 306

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1234979156 321 LPANLRVTHKSLFDGTLQGIHRTDKPAFSFQGHPEASPGPHDAAPLFDHFIELI 374
Cdd:PRK12564  307 LPANLEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDEFVELM 360
CPSaseIIsmall TIGR01368
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ...
 5-376 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: 590.37  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156   5 ALLVLEDGTQFHGRAIGATGSAVGEVVFNTSMTGYQEILTDPSYSRQIVTLTYPHIGNVGTNDADEESSQVHAQGLVIRD 84
Cdd:TIGR01368   1 AYLVLEDGTVFRGYSFGAEGTVAGEVVFNTGMTGYQEILTDPSYKGQIVVFTYPLIGNYGVNDEDAESKGIHVSGLVVRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156  85 LPLIASNFRNTEDLSSYLKRHNIVAIADIDTRKLTRLLREKGAQNGCIIAGDNPDAALaLEKARAFPGLNGMDLAKEVTT 164
Cdd:TIGR01368  81 LSDRYSNWRATESLDQFLKRHGIPGIYGVDTRALVKKIREKGTMKGVISTEDSNDEEL-VEKARVSPDITGINLVAEVST 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156 165 AEAYSWTQgswtltggmpeakkEDELPFHVVAYDFGAKRNILRMLVDRGCRLTIVPAQTSAEDVLKMNPDGIFLSNGPGD 244
Cdd:TIGR01368 160 KEPYTWGQ--------------RGGKGKRVVVIDFGVKRNILRRLVKRGCEVTVVPYDTDAEEIKKYNPDGIFLSNGPGD 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156 245 PAPCDYAITAIQKFLEtDIPVFGICLGHQLLALASGAKTVKMKFGHHGGNHPVKDVEKNVVMITAQNHGFAVDEATLPAN 324
Cdd:TIGR01368 226 PAAVEPAIETIRKLLE-KIPIFGICLGHQLLALAFGAKTYKMKFGHRGGNHPVKDLITGRVEITSQNHGYAVDPDSLPAG 304

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1234979156 325 -LRVTHKSLFDGTLQGIHRTDKPAFSFQGHPEASPGPHDAAPLFDHFIELIEQ 376
Cdd:TIGR01368 305 dLEVTHVNLNDGTVEGIRHKDLPVFSVQYHPEASPGPHDTEYLFDEFIDLMKK 357
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 194-371 1.63e-114

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: 331.00  E-value: 1.63e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156 194 VVAYDFGAKRNILRMLVDRGCRLTIVPAQTSAEDVLKMNPDGIFLSNGPGDPAPCDYAITAIQKFLETDIPVFGICLGHQ 273
Cdd:cd01744     1 VVVIDFGVKHNILRELLKRGCEVTVVPYNTDAEEILKLDPDGIFLSNGPGDPALLDEAIKTVRKLLGKKIPIFGICLGHQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156 274 LLALASGAKTVKMKFGHHGGNHPVKDVEKNVVMITAQNHGFAVDEATLPANLRVTHKSLFDGTLQGIHRTDKPAFSFQGH 353
Cdd:cd01744    81 LLALALGAKTYKMKFGHRGSNHPVKDLITGRVYITSQNHGYAVDPDSLPGGLEVTHVNLNDGTVEGIRHKDLPVFSVQFH 160

                         170
                  ....*....|....*...
gi 1234979156 354 PEASPGPHDAAPLFDHFI 371
Cdd:cd01744   161 PEASPGPHDTEYLFDEFL 178
CPSase_sm_chain smart01097
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 3-132 1.64e-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: 1.64e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156    3 KSALLVLEDGTQFHGRAIGATGSAVGEVVFNTSMTGYQEILTDPSYSRQIVTLTYPHIGNVGTNDADEESSQVHAQGLVI 82
Cdd:smart01097   1 MKAYLVLEDGTVFEGESFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNDEDFESDKIQVKGLVV 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1234979156   83 RDLPLIASNFRNTEDLSSYLKRHNIVAIADIDTRKLTRLLREKGAQNGCI 132
Cdd:smart01097  81 RELSDEPSNWRSEQSLDEFLKENGIPGISGIDTRALTRKLREKGAMKGVI 130
CPSase_sm_chain pfam00988
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 7-132 2.64e-86

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: 257.25  E-value: 2.64e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156   7 LVLEDGTQFHGRAIGATGSAVGEVVFNTSMTGYQEILTDPSYSRQIVTLTYPHIGNVGTNDADEESSQVHAQGLVIRDLP 86
Cdd:pfam00988   1 LVLEDGTVFEGKSFGAAGSTVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNPEDFESDKIHVAGLVVREYS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1234979156  87 LIASNFRNTEDLSSYLKRHNIVAIADIDTRKLTRLLREKGAQNGCI 132
Cdd:pfam00988  81 DEPSNWRAEESLDEWLKEQGIPGISGVDTRALTRKIREKGAMKGVI 126
 
Name Accession Description Interval E-value
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 1-375 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: 727.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156   1 MIKSALLVLEDGTQFHGRAIGATGSAVGEVVFNTSMTGYQEILTDPSYSRQIVTLTYPHIGNVGTNDADEESSQVHAQGL 80
Cdd:COG0505     1 MMMKALLVLEDGTVFEGKSFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVTFTYPHIGNYGVNDEDFESDRPWVAGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156  81 VIRDLPLIASNFRNTEDLSSYLKRHNIVAIADIDTRKLTRLLREKGAQNGCIIAGDNpDAALALEKARAFPGLNGMDLAK 160
Cdd:COG0505    81 VVRELSRRPSNWRSEESLDEYLKEHGIPGISGIDTRALTRHLREKGAMKGVISTGDL-DIEELLEKARAAPGMEGLDLVK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156 161 EVTTAEAYSWTQgswtltggmpeakkEDELPFHVVAYDFGAKRNILRMLVDRGCRLTIVPAQTSAEDVLKMNPDGIFLSN 240
Cdd:COG0505   160 EVSTKEPYEWTE--------------APGAGFHVVALDFGVKRNILRELAERGCRVTVVPATTSAEEILALNPDGVFLSN 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156 241 GPGDPAPCDYAITAIQKFLETDIPVFGICLGHQLLALASGAKTVKMKFGHHGGNHPVKDVEKNVVMITAQNHGFAVDEAT 320
Cdd:COG0505   226 GPGDPAALDYAIETIRELLGKGIPIFGICLGHQLLALALGAKTYKLKFGHRGANHPVKDLETGRVEITSQNHGFAVDEDS 305

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1234979156 321 LPA-NLRVTHKSLFDGTLQGIHRTDKPAFSFQGHPEASPGPHDAAPLFDHFIELIE 375
Cdd:COG0505   306 LPAtDLEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDRFIELME 361
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
1-374 0e+00

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 707.22  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156   1 MIKSALLVLEDGTQFHGRAIGATGSAVGEVVFNTSMTGYQEILTDPSYSRQIVTLTYPHIGNVGTNDADEESSQVHAQGL 80
Cdd:PRK12564    1 MMMKAYLVLEDGTVFEGKAFGAEGETVGEVVFNTSMTGYQEILTDPSYAGQIVTFTYPLIGNYGVNREDFESDRPHAKGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156  81 VIRDLPLIASNFRNTEDLSSYLKRHNIVAIADIDTRKLTRLLREKGAQNGCIIAGDnPDAALALEKARAFPGLNGMDLAK 160
Cdd:PRK12564   81 IVRELSDIPSNWRSEMSLDEYLKENGIPGISGIDTRALTRKLREKGAMKGVIATED-FDAEELLEKARAFPGLLGLDLVK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156 161 EVTTAEAYSWTqgswtltggmpeaKKEDELPFHVVAYDFGAKRNILRMLVDRGCRLTIVPAQTSAEDVLKMNPDGIFLSN 240
Cdd:PRK12564  160 EVSTKEPYPWP-------------GPGGELKYKVVAIDFGVKRNILRELAERGCRVTVVPATTTAEEILALNPDGVFLSN 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156 241 GPGDPAPCDYAITAIQKFLETDIPVFGICLGHQLLALASGAKTVKMKFGHHGGNHPVKDVEKNVVMITAQNHGFAVDEAT 320
Cdd:PRK12564  227 GPGDPAALDYAIEMIRELLEKKIPIFGICLGHQLLALALGAKTYKMKFGHRGANHPVKDLETGKVEITSQNHGFAVDEDS 306

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1234979156 321 LPANLRVTHKSLFDGTLQGIHRTDKPAFSFQGHPEASPGPHDAAPLFDHFIELI 374
Cdd:PRK12564  307 LPANLEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDEFVELM 360
CPSaseIIsmall TIGR01368
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ...
 5-376 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: 590.37  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156   5 ALLVLEDGTQFHGRAIGATGSAVGEVVFNTSMTGYQEILTDPSYSRQIVTLTYPHIGNVGTNDADEESSQVHAQGLVIRD 84
Cdd:TIGR01368   1 AYLVLEDGTVFRGYSFGAEGTVAGEVVFNTGMTGYQEILTDPSYKGQIVVFTYPLIGNYGVNDEDAESKGIHVSGLVVRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156  85 LPLIASNFRNTEDLSSYLKRHNIVAIADIDTRKLTRLLREKGAQNGCIIAGDNPDAALaLEKARAFPGLNGMDLAKEVTT 164
Cdd:TIGR01368  81 LSDRYSNWRATESLDQFLKRHGIPGIYGVDTRALVKKIREKGTMKGVISTEDSNDEEL-VEKARVSPDITGINLVAEVST 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156 165 AEAYSWTQgswtltggmpeakkEDELPFHVVAYDFGAKRNILRMLVDRGCRLTIVPAQTSAEDVLKMNPDGIFLSNGPGD 244
Cdd:TIGR01368 160 KEPYTWGQ--------------RGGKGKRVVVIDFGVKRNILRRLVKRGCEVTVVPYDTDAEEIKKYNPDGIFLSNGPGD 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156 245 PAPCDYAITAIQKFLEtDIPVFGICLGHQLLALASGAKTVKMKFGHHGGNHPVKDVEKNVVMITAQNHGFAVDEATLPAN 324
Cdd:TIGR01368 226 PAAVEPAIETIRKLLE-KIPIFGICLGHQLLALAFGAKTYKMKFGHRGGNHPVKDLITGRVEITSQNHGYAVDPDSLPAG 304

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1234979156 325 -LRVTHKSLFDGTLQGIHRTDKPAFSFQGHPEASPGPHDAAPLFDHFIELIEQ 376
Cdd:TIGR01368 305 dLEVTHVNLNDGTVEGIRHKDLPVFSVQYHPEASPGPHDTEYLFDEFIDLMKK 357
PRK12838 PRK12838
carbamoyl phosphate synthase small subunit; Reviewed
 5-378 2.44e-160

carbamoyl phosphate synthase small subunit; Reviewed


Pssm-ID: 183784 [Multi-domain]  Cd Length: 354  Bit Score: 453.96  E-value: 2.44e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156   5 ALLVLEDGTQFHGRAIGATGSAVGEVVFNTSMTGYQEILTDPSYSRQIVTLTYPHIGNVGTNDADEESSQVHAQGLVIRD 84
Cdd:PRK12838    3 AYLILEDGTVFEGELIGAPIDVTGEIVFNTGMTGYQEVLTDPSYKGQIVVFTYPLIGNYGINADDYESKQPQVKGVIVYE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156  85 LPLIASNFRNTEDLSSYLKRHNIVAIADIDTRKLTRLLREKGAQNGCIIagDNPDAALALEKARAFPGLNgmdLAKEVTT 164
Cdd:PRK12838   83 LSREGSHYRAKQSLDDFLKEWNIPGISGVDTRALVKHIREKGTMKASIT--TTDDAHAFDQIKALVLPKN---VVAQVST 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156 165 AEAYSWTQGSwtltggmpeakkedelpFHVVAYDFGAKRNILRMLVDRGCRLTIVPAQTSAEDVLKMNPDGIFLSNGPGD 244
Cdd:PRK12838  158 KEPYTYGNGG-----------------KHVALIDFGYKKSILRSLSKRGCKVTVLPYDTSLEEIKNLNPDGIVLSNGPGD 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156 245 PAPCDYAITAIQKfLETDIPVFGICLGHQLLALASGAKTVKMKFGHHGGNHPVKDVEKNVVMITAQNHGFAVDEATLPAN 324
Cdd:PRK12838  221 PKELQPYLPEIKK-LISSYPILGICLGHQLIALALGADTEKLPFGHRGANHPVIDLTTGRVWMTSQNHGYVVDEDSLDGT 299

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1234979156 325 -LRVTHKSLFDGTLQGIHRTDKPAFSFQGHPEASPGPHDAAPLFDHFIELIEQYR 378
Cdd:PRK12838  300 pLSVRFFNVNDGSIEGLRHKKKPVLSVQFHPEAHPGPHDAEYIFDEFLEMMEKAR 354
carA CHL00197
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
 3-381 3.36e-145

carbamoyl-phosphate synthase arginine-specific small subunit; Provisional


Pssm-ID: 214392 [Multi-domain]  Cd Length: 382  Bit Score: 416.51  E-value: 3.36e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156   3 KSALLVLEDGTQFHGRAIGATGSAVGEVVFNTSMTGYQEILTDPSYSRQIVTLTYPHIGNVGTNDADEESSQVHAQGLVI 82
Cdd:CHL00197    5 IPAILVLEDGTYYRGWSFSNPITTIGEVVFNTGMTGYQEIITDPSYFEQIVTFTYPEIGNTGINLEDIESVKIQVKGIIA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156  83 RDLPLIASNFRNTEDLSSYLKRHNIVAIADIDTRKLTRLLREKGAQNGCiIAGDNPDAALALEKARAFPGLNGMDLAKEV 162
Cdd:CHL00197   85 KNICKSSSNWRQQESLVSYLQRHKIPFIFGIDTRALTQHLRRFGTMNGC-ISNQNLNLSYLRAKIKESPHMPSSDLIPRV 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156 163 TTAEAYSWTQGS---WTLTggmPEAKKEDELPFHVVAYDFGAKRNILRMLVDRGCRLTIVPAQTSAEDVLKMNPDGIFLS 239
Cdd:CHL00197  164 TTSSYYEWDEKShpsFYLA---DNKRPHSSYQLKIIVIDFGVKYNILRRLKSFGCSITVVPATSPYQDILSYQPDGILLS 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156 240 NGPGDPAPCDYAITAIQKFLETDIPVFGICLGHQLLALASGAKTVKMKFGHHGGNHPVKdvEKNVVMITAQNHGFAVDEA 319
Cdd:CHL00197  241 NGPGDPSAIHYGIKTVKKLLKYNIPIFGICMGHQILSLALEAKTFKLKFGHRGLNHPSG--LNQQVEITSQNHGFAVNLE 318

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1234979156 320 TLPAN-LRVTHKSLFDGTLQGIHRTDKPAFSFQGHPEASPGPHDAAPLFDHFIELIEQYRKTA 381
Cdd:CHL00197  319 SLAKNkFYITHFNLNDGTVAGISHSPKPYFSVQYHPEASPGPHDADYLFEYFIEIIKHSKSSK 381
PLN02771 PLN02771
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
 5-367 1.33e-134

carbamoyl-phosphate synthase (glutamine-hydrolyzing)


Pssm-ID: 178370 [Multi-domain]  Cd Length: 415  Bit Score: 390.88  E-value: 1.33e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156   5 ALLVLEDGTQFHGRAIGATGSAVGEVVFNTSMTGYQEILTDPSYSRQIVTLTYPHIGNVGTNDADEESSQVHAQGLVIRD 84
Cdd:PLN02771   57 ARLVLEDGSVWKAKSFGARGTQVGEVVFNTSLTGYQEILTDPSYAGQFVLMTNPHIGNTGVNFDDEESRQCFLAGLVIRS 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156  85 LPLIASNFRNTEDLSSYLKRHNIVAIADIDTRKLTRLLREKGAQNGCIIAGDNPDAALALEKARAFpGLNGMDLAKEVTT 164
Cdd:PLN02771  137 LSISTSNWRCTKTLGDYLAERNIMGIYDVDTRAITRRLREDGSLIGVLSTEDSKTDEELLKMSRSW-DIVGIDLISGVSC 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156 165 AEAYSW---TQGSWTLTGGMPEAKKedelpFHVVAYDFGAKRNILRMLVDRGCRLTIVPAQTSAEDVLKMNPDGIFLSNG 241
Cdd:PLN02771  216 KSPYEWvdkTNPEWDFNTNSRDGES-----YHVIAYDFGIKHNILRRLASYGCKITVVPSTWPASEALKMKPDGVLFSNG 290

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156 242 PGDPAPCDYAITAIQKFLeTDIPVFGICLGHQLLALASGAKTVKMKFGHHGGNHPVKDVEKNVVMITAQNHGFAVDEATL 321
Cdd:PLN02771  291 PGDPSAVPYAVETVKELL-GKVPVFGICMGHQLLGQALGGKTFKMKFGHHGGNHPVRNNRTGRVEISAQNHNYAVDPASL 369

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1234979156 322 PANLRVTHKSLFDGTLQGIHRTDKPAFSFQGHPEASPGPHDAAPLF 367
Cdd:PLN02771  370 PEGVEVTHVNLNDGSCAGLAFPALNVMSLQYHPEASPGPHDSDNAF 415
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 194-371 1.63e-114

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: 331.00  E-value: 1.63e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156 194 VVAYDFGAKRNILRMLVDRGCRLTIVPAQTSAEDVLKMNPDGIFLSNGPGDPAPCDYAITAIQKFLETDIPVFGICLGHQ 273
Cdd:cd01744     1 VVVIDFGVKHNILRELLKRGCEVTVVPYNTDAEEILKLDPDGIFLSNGPGDPALLDEAIKTVRKLLGKKIPIFGICLGHQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156 274 LLALASGAKTVKMKFGHHGGNHPVKDVEKNVVMITAQNHGFAVDEATLPANLRVTHKSLFDGTLQGIHRTDKPAFSFQGH 353
Cdd:cd01744    81 LLALALGAKTYKMKFGHRGSNHPVKDLITGRVYITSQNHGYAVDPDSLPGGLEVTHVNLNDGTVEGIRHKDLPVFSVQFH 160

                         170
                  ....*....|....*...
gi 1234979156 354 PEASPGPHDAAPLFDHFI 371
Cdd:cd01744   161 PEASPGPHDTEYLFDEFL 178
CPSase_sm_chain smart01097
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 3-132 1.64e-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: 1.64e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156    3 KSALLVLEDGTQFHGRAIGATGSAVGEVVFNTSMTGYQEILTDPSYSRQIVTLTYPHIGNVGTNDADEESSQVHAQGLVI 82
Cdd:smart01097   1 MKAYLVLEDGTVFEGESFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNDEDFESDKIQVKGLVV 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1234979156   83 RDLPLIASNFRNTEDLSSYLKRHNIVAIADIDTRKLTRLLREKGAQNGCI 132
Cdd:smart01097  81 RELSDEPSNWRSEQSLDEFLKENGIPGISGIDTRALTRKLREKGAMKGVI 130
CPSase_sm_chain pfam00988
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 7-132 2.64e-86

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: 257.25  E-value: 2.64e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156   7 LVLEDGTQFHGRAIGATGSAVGEVVFNTSMTGYQEILTDPSYSRQIVTLTYPHIGNVGTNDADEESSQVHAQGLVIRDLP 86
Cdd:pfam00988   1 LVLEDGTVFEGKSFGAAGSTVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNPEDFESDKIHVAGLVVREYS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1234979156  87 LIASNFRNTEDLSSYLKRHNIVAIADIDTRKLTRLLREKGAQNGCI 132
Cdd:pfam00988  81 DEPSNWRAEESLDEWLKEQGIPGISGVDTRALTRKIREKGAMKGVI 126
GATase pfam00117
Glutamine amidotransferase class-I;
195-373 4.22e-74

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 228.28  E-value: 4.22e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156 195 VAYDFGA--KRNILRMLVDRGCRLTIVPAQTSAEDVLKMNPDGIFLSNGPGDPAPCDYAITAIQKFLETDIPVFGICLGH 272
Cdd:pfam00117   1 LLIDNGDsfTYNLARALRELGVEVTVVPNDTPAEEILEENPDGIILSGGPGSPGAAGGAIEAIREARELKIPILGICLGH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156 273 QLLALASGAKTVKMK-FGHHGGNHPVKDVEKNV------VMITAQNHGFAVDEATLPANLRVTHKSLFDGTLQGIHRTDK 345
Cdd:pfam00117  81 QLLALAFGGKVVKAKkFGHHGKNSPVGDDGCGLfyglpnVFIVRRYHSYAVDPDTLPDGLEVTATSENDGTIMGIRHKKL 160

                         170       180
                  ....*....|....*....|....*...
gi 1234979156 346 PAFSFQGHPEASPGPHDAAPLFDHFIEL 373
Cdd:pfam00117 161 PIFGVQFHPESILTPHGPEILFNFFIKA 188
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 204-355 4.18e-28

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: 108.78  E-value: 4.18e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156 204 NILRMLVDRGCRLTIVPAQTSAEDVLK-MNPDGIFLSNGPGDPApcDYAIT-AIQKFLETDIPVFGICLGHQLLALASGA 281
Cdd:cd01743    13 NLVQYLRELGAEVVVVRNDEITLEELElLNPDAIVISPGPGHPE--DAGISlEIIRALAGKVPILGVCLGHQAIAEAFGG 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156 282 KTVKMKFGHHGGNHPVKDVEKNVVMITAQN------HGFAVDEATLPANLRVTHKSlFDGTLQGIHRTDKPAFSFQGHPE 355
Cdd:cd01743    91 KVVRAPEPMHGKTSEIHHDGSGLFKGLPQPftvgryHSLVVDPDPLPDLLEVTAST-EDGVIMALRHRDLPIYGVQFHPE 169
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 206-355 1.80e-22

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: 93.56  E-value: 1.80e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156 206 LRMLvdrGCRLTIVPA-QTSAEDVLKMNPDGIFLSNGPGDPAPCDYAITAIQKFlETDIPVFGICLGHQLLALASGAKTV 284
Cdd:COG0512    18 LGEL---GAEVVVVRNdEITLEEIEALAPDGIVLSPGPGTPEEAGISLEVIRAF-AGKIPILGVCLGHQAIGEAFGGKVV 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156 285 KMKFGHHGgnhpvKdveknVVMITAQNHG-FA---------------VDEATLPANLRVTHKSLfDGTLQGIHRTDKPAF 348
Cdd:COG0512    94 RAPEPMHG-----K-----TSPITHDGSGlFAglpnpftatryhslvVDRETLPDELEVTAWTE-DGEIMGIRHRELPIE 162


                  ....*..
gi 1234979156 349 SFQGHPE 355
Cdd:COG0512   163 GVQFHPE 169
PRK14607 PRK14607
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
204-371 4.92e-21

bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;


Pssm-ID: 237764 [Multi-domain]  Cd Length: 534  Bit Score: 94.40  E-value: 4.92e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156 204 NILRMLVDRG--CRLTIVPAQTSAEDVLKMNPDGIFLSNGPGDPAPCDYAITAIQKFlETDIPVFGICLGHQLLALASGA 281
Cdd:PRK14607   14 NIYQYIGELGpeEIEVVRNDEITIEEIEALNPSHIVISPGPGRPEEAGISVEVIRHF-SGKVPILGVCLGHQAIGYAFGG 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156 282 KTVKMKFGHHGGNHPV----KDVEKNVV--MITAQNHGFAVDEATLPANLRVTHKSLfDGTLQGIHRTDKPAFSFQGHPE 355
Cdd:PRK14607   93 KIVHAKRILHGKTSPIdhngKGLFRGIPnpTVATRYHSLVVEEASLPECLEVTAKSD-DGEIMGIRHKEHPIFGVQFHPE 171

                         170
                  ....*....|....*.
gi 1234979156 356 aSPGPHDAAPLFDHFI 371
Cdd:PRK14607  172 -SILTEEGKRILKNFL 186
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 206-355 5.75e-21

anthranilate synthase component II; Provisional


Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 89.42  E-value: 5.75e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156 206 LRMLvdrGCRLTIVPAQT-SAEDVLKMNPDGIFLSNGPGDPAPCDYAITAIQKFLETdIPVFGICLGHQLLALASGAKTV 284
Cdd:PRK05670   19 LGEL---GAEVVVYRNDEiTLEEIEALNPDAIVLSPGPGTPAEAGISLELIREFAGK-VPILGVCLGHQAIGEAFGGKVV 94

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1234979156 285 KMKFGHHGGNHPV----KDVEKNV--VMITAQNHGFAVDEATLPANLRVTHKSlFDGTLQGIHRTDKPAFSFQGHPE 355
Cdd:PRK05670   95 RAKEIMHGKTSPIehdgSGIFAGLpnPFTVTRYHSLVVDRESLPDCLEVTAWT-DDGEIMGVRHKELPIYGVQFHPE 170
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 205-358 2.64e-18

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: 83.07  E-value: 2.64e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156 205 ILRMLVDRGCRLT--------IVPAQTSAEDvlkmnPDGIFLSNGPGDP-APCDY---AITAIQKFLETDIPVFGICLGH 272
Cdd:COG0518    18 IARRLREAGIELDvlrvyageILPYDPDLED-----PDGLILSGGPMSVyDEDPWledEPALIREAFELGKPVLGICYGA 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156 273 QLLALASGAKTVKMKfGHHGGNHPVKDVEKNVVM------ITA-QNHGFAVDEatLPANLRVTHKSLFDgTLQGIhRTDK 345
Cdd:COG0518    93 QLLAHALGGKVEPGP-GREIGWAPVELTEADPLFaglpdeFTVwMSHGDTVTE--LPEGAEVLASSDNC-PNQAF-RYGR 167

                         170
                  ....*....|...
gi 1234979156 346 PAFSFQGHPEASP 358
Cdd:COG0518   168 RVYGVQFHPEVTH 180
guaA_Nterm TIGR00888
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ...
 194-355 4.81e-17

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: 78.51  E-value: 4.81e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156 194 VVAYDFGAKRN--ILRMLVDRGCRLTIVPAQTSAEDVLKMNPDGIFLSNGPGDpapcDY---AITAIQKFLETDIPVFGI 268
Cdd:TIGR00888   1 ILVLDFGSQYTqlIARRLRELGVYSELVPNTTPLEEIREKNPKGIILSGGPSS----VYaenAPRADEKIFELGVPVLGI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156 269 CLGHQLLALASGAKTVKMKFGHHG--------GNHPVKDVEK--NVVMitaqNHGFAVDEatLPANLRVTHKSlfDGT-L 337
Cdd:TIGR00888  77 CYGMQLMAKQLGGEVGRAEKREYGkaeleildEDDLFRGLPDesTVWM----SHGDKVKE--LPEGFKVLATS--DNCpV 148

                         170
                  ....*....|....*...
gi 1234979156 338 QGIHRTDKPAFSFQGHPE 355
Cdd:TIGR00888 149 AAMAHEEKPIYGVQFHPE 166
PRK00758 PRK00758
GMP synthase subunit A; Validated
 205-377 1.72e-16

GMP synthase subunit A; Validated


Pssm-ID: 179112 [Multi-domain]  Cd Length: 184  Bit Score: 76.81  E-value: 1.72e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156 205 ILRMLVDRGCRLTIVPAQTSAEDVLKMNpDGIFLSNGP-----GDpapC-DYAitaiqkfLETDIPVFGICLGHQLLALA 278
Cdd:PRK00758   15 IHRTLRYLGVDAKIIPNTTPVEEIKAFE-DGLILSGGPdieraGN---CpEYL-------KELDVPILGICLGHQLIAKA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156 279 SGAKTVKMKFGHHGgnhpvkDVEKNVV------------MITAQNHGfavDE-ATLPANLRVTHKSLFDGtLQGIHRTDK 345
Cdd:PRK00758   84 FGGEVGRGEYGEYA------LVEVEILdeddilkglppeIRVWASHA---DEvKELPDGFEILARSDICE-VEAMKHKEK 153

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1234979156 346 PAFSFQGHPEASPGPHDAApLFDHFIELIEQY 377
Cdd:PRK00758  154 PIYGVQFHPEVAHTEYGEE-IFKNFLEICGKY 184
GATase1_GMP_Synthase cd01742
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ...
 194-355 3.63e-16

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: 75.65  E-value: 3.63e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156 194 VVAYDFGAKRN--ILRMLVDRGCRLTIVPAQTSAEDVLKMNPDGIFLSNGP----GDPAP-CDYAItaiqkfLETDIPVF 266
Cdd:cd01742     1 ILILDFGSQYThlIARRVRELGVYSEILPNTTPLEEIKLKNPKGIILSGGPssvyEEDAPrVDPEI------FELGVPVL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156 267 GICLGHQLLALASGAK---TVKMKFGHH-----GGNHPVKDVEK--NVVMitaqNHGFAVDEatLPANLRVTHKSLfDGT 336
Cdd:cd01742    75 GICYGMQLIAKALGGKverGDKREYGKAeieidDSSPLFEGLPDeqTVWM----SHGDEVVK--LPEGFKVIASSD-NCP 147

                         170
                  ....*....|....*....
gi 1234979156 337 LQGIHRTDKPAFSFQGHPE 355
Cdd:cd01742   148 VAAIANEEKKIYGVQFHPE 166
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 193-356 8.09e-15

Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group contains a subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain. GATase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. Glutamine amidotransferases (GATase) includes the triad family of amidotransferases which have a conserved Cys-His-Glu catalytic triad in the glutaminase active site. In this subgroup this triad is conserved. GATase activity can be found in a range of biosynthetic enzymes, including: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase , anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. Glutamine amidotransferase (GATase) domains can occur either as single polypeptides, as in glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.


Pssm-ID: 153212 [Multi-domain]  Cd Length: 188  Bit Score: 72.28  E-value: 8.09e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156 193 HVVAYDFGAKRNILRMLVDRGCRLTIVPAQTSAEDVLKMNPDGIFLSNGPGDPAPCDYA-----ITAIQKFLETDIPVFG 267
Cdd:cd01741     7 HDTPEGPGLFEDLLREAGAETIEIDVVDVYAGELLPDLDDYDGLVILGGPMSVDEDDYPwlkklKELIRQALAAGKPVLG 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156 268 ICLGHQLLALASGAKTVKMKFGHHGGNHPVKDVEKNVVMITAQN----------HGFAVDEatLPANLRVTHKSLFDGTl 337
Cdd:cd01741    87 ICLGHQLLARALGGKVGRNPKGWEIGWFPVTLTEAGKADPLFAGlpdefpvfhwHGDTVVE--LPPGAVLLASSEACPN- 163

                         170
                  ....*....|....*....
gi 1234979156 338 QGIhRTDKPAFSFQGHPEA 356
Cdd:cd01741   164 QAF-RYGDRALGLQFHPEE 181
trpG CHL00101
anthranilate synthase component 2
 230-356 6.68e-14

anthranilate synthase component 2


Pssm-ID: 214365 [Multi-domain]  Cd Length: 190  Bit Score: 69.76  E-value: 6.68e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156 230 KMNPDGIFLSNGPGDPAPCDYAITAIQKFLETdIPVFGICLGHQLLALASGAKTVKMKFGHHGGN----HPVKDVEKNVV 305
Cdd:CHL00101   41 NLNIRHIIISPGPGHPRDSGISLDVISSYAPY-IPILGVCLGHQSIGYLFGGKIIKAPKPMHGKTskiyHNHDDLFQGLP 119

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1234979156 306 --MITAQNHGFAVDEATLPANLRVTHKSlFDGTLQGI-HRTDKPAFSFQGHPEA 356
Cdd:CHL00101  120 npFTATRYHSLIIDPLNLPSPLEITAWT-EDGLIMACrHKKYKMLRGIQFHPES 172
trpG_papA TIGR00566
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ...
 227-373 8.59e-14

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: 69.05  E-value: 8.59e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156 227 DVLKMNPDGIFLSNGPGDPAPCDYAITAIQKFlETDIPVFGICLGHQLLALASGAKTVKMKFGHHGGNHPVKDVEKNVV- 305
Cdd:TIGR00566  38 EIEALLPLLIVISPGPCTPNEAGISLEAIRHF-AGKLPILGVCLGHQAMGQAFGGDVVRANTVMHGKTSEIEHNGAGIFr 116

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1234979156 306 -----MITAQNHGFAVDEATLPANLRVTHKSLFDGTLQGIHRTDKPAFSFQGHPEaSPGPHDAAPLFDHFIEL 373
Cdd:TIGR00566 117 glfnpLTATRYHSLVVEPETLPTCFPVTAWEEENIEIMAIRHRDLPLEGVQFHPE-SILSEQGHQLLANFLHR 188
PRK06774 PRK06774
aminodeoxychorismate synthase component II;
226-372 1.17e-13

aminodeoxychorismate synthase component II;


Pssm-ID: 180689 [Multi-domain]  Cd Length: 191  Bit Score: 69.12  E-value: 1.17e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156 226 EDVLKMNPDGIFLSNGPGDPAPCDYAITAIQKFLEtDIPVFGICLGHQLLALASGAKTVKMKFGHHGGNHPVKDVEKNVV 305
Cdd:PRK06774   37 TDIEQLAPSHLVISPGPCTPNEAGISLAVIRHFAD-KLPILGVCLGHQALGQAFGARVVRARQVMHGKTSAICHSGQGVF 115

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1234979156 306 ------MITAQNHGFAVDEATLPANLRVTHKSLFDGTLQGI----HRTdKPAFSFQGHPEA--SPGPHDaapLFDHFIE 372
Cdd:PRK06774  116 rglnqpLTVTRYHSLVIAADSLPGCFELTAWSERGGEMDEImgirHRT-LPLEGVQFHPESilSEQGHQ---LLDNFLK 190
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 203-371 1.30e-13

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: 68.76  E-value: 1.30e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156 203 RNILRMLVDRGCRLTIVPAQTSAEDVLKM--NPDGIFLSNGP--------GDPAPCD---------YAITAIQKFLETDI 263
Cdd:cd01745    22 QYYVDAVRKAGGLPVLLPPVDDEEDLEQYleLLDGLLLTGGGdvdpplygEEPHPELgpidperdaFELALLRAALERGK 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156 264 PVFGICLGHQLLALAsgaktvkmkfghHGGN-HPvkDVEKNvvmitaQNHGFAVDEatLPANLRVTHKSLfDGTLQGIHR 342
Cdd:cd01745   102 PILGICRGMQLLNVA------------LGGTlYQ--DIRVN------SLHHQAIKR--LADGLRVEARAP-DGVIEAIES 158

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1234979156 343 TDKP-AFSFQGHPE-ASPGPHDAAPLFDHFI 371
Cdd:cd01745   159 PDRPfVLGVQWHPEwLADTDPDSLKLFEAFV 189
PLN02335 PLN02335
anthranilate synthase
 204-377 1.32e-13

anthranilate synthase


Pssm-ID: 177969 [Multi-domain]  Cd Length: 222  Bit Score: 69.44  E-value: 1.32e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156 204 NILRMLVDRGCRLTIVPA-QTSAEDVLKMNPDGIFLSNGPGDPAPCDYAITAIQKfLETDIPVFGICLGHQLLALASGAK 282
Cdd:PLN02335   33 NLCQYMGELGCHFEVYRNdELTVEELKRKNPRGVLISPGPGTPQDSGISLQTVLE-LGPLVPLFGVCMGLQCIGEAFGGK 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156 283 TVKMKFG-HHGGNHPVKDVEKNVVMI---------TAQNHGFAVDEATLPAN-LRVTHKSLfDGTLQGI-HRTDKPAFSF 350
Cdd:PLN02335  112 IVRSPFGvMHGKSSPVHYDEKGEEGLfsglpnpftAGRYHSLVIEKDTFPSDeLEVTAWTE-DGLIMAArHRKYKHIQGV 190

                         170       180       190
                  ....*....|....*....|....*....|
gi 1234979156 351 QGHPEA---SPGPHdaapLFDHFIELIEQY 377
Cdd:PLN02335  191 QFHPESiitTEGKT----IVRNFIKIIEKK 216
guaA PRK00074
GMP synthase; Reviewed
 218-355 3.06e-13

GMP synthase; Reviewed


Pssm-ID: 234614 [Multi-domain]  Cd Length: 511  Bit Score: 70.85  E-value: 3.06e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156 218 IVPAQTSAEDVLKMNPDGIFLSNGP----GDPAPcdyaiTAIQKFLETDIPVFGICLGHQLLALASGAKTVKMK---FGH 290
Cdd:PRK00074   32 IVPYDISAEEIRAFNPKGIILSGGPasvyEEGAP-----RADPEIFELGVPVLGICYGMQLMAHQLGGKVERAGkreYGR 106

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1234979156 291 -----HGGNHPVKDVEKN--VVMitaqNHGFAVDEatLPANLRVTHKSlfDGT-LQGIHRTDKPAFSFQGHPE 355
Cdd:PRK00074  107 aelevDNDSPLFKGLPEEqdVWM----SHGDKVTE--LPEGFKVIAST--ENCpIAAIANEERKFYGVQFHPE 171
PRK07649 PRK07649
aminodeoxychorismate/anthranilate synthase component II;
222-381 4.86e-13

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181066 [Multi-domain]  Cd Length: 195  Bit Score: 67.14  E-value: 4.86e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156 222 QTSAEDVLKMNPDGIFLSNGPGDPAPCDYAITAIQKFlETDIPVFGICLGHQLLALASGAKTVKMKFGHHGGNHPVKDVE 301
Cdd:PRK07649   33 EVTISDIENMKPDFLMISPGPCSPNEAGISMEVIRYF-AGKIPIFGVCLGHQSIAQVFGGEVVRAERLMHGKTSLMHHDG 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156 302 KNVV------MITAQNHGFAVDEATLPANLRVTHKSLfDGTLQGIHRTDKPAFSFQGHPEASPGPHdAAPLFDHFielIE 375
Cdd:PRK07649  112 KTIFsdipnpFTATRYHSLIVKKETLPDCLEVTSWTE-EGEIMAIRHKTLPIEGVQFHPESIMTSH-GKELLQNF---IR 186


                  ....*.
gi 1234979156 376 QYRKTA 381
Cdd:PRK07649  187 KYSPSV 192
PRK07765 PRK07765
aminodeoxychorismate/anthranilate synthase component II;
222-355 9.68e-13

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181107 [Multi-domain]  Cd Length: 214  Bit Score: 66.61  E-value: 9.68e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156 222 QTSAEDVLKMNPDGIFLSNGPGDPAPCDYAITAIQKFLETDIPVFGICLGHQLLALASGAKTVKMKFGHHGGNHPVKDVE 301
Cdd:PRK07765   36 RLADEAAVAAQFDGVLLSPGPGTPERAGASIDMVRACAAAGTPLLGVCLGHQAIGVAFGATVDRAPELLHGKTSSVHHTG 115

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156 302 KNVVM-----ITA-QNHGFAVDEATLPANLRVTHKSLfDGTLQGIHRTDKPAFSFQGHPE 355
Cdd:PRK07765  116 VGVLAglpdpFTAtRYHSLTILPETLPAELEVTARTD-SGVIMAVRHRELPIHGVQFHPE 174
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 194-280 5.13e-12

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: 62.23  E-value: 5.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156 194 VVAYDF--GAKRNILRMLVDRGCRLTIVPAQTSAE--DVLKMNPDGIFLSNGPGDPAPCDY---AITAIQKFLETDIPVF 266
Cdd:cd01653     4 LLFPGFeeLELASPLDALREAGAEVDVVSPDGGPVesDVDLDDYDGLILPGGPGTPDDLARdeaLLALLREAAAAGKPIL 83

                          90
                  ....*....|....
gi 1234979156 267 GICLGHQLLALASG 280
Cdd:cd01653    84 GICLGAQLLVLGVQ 97
PRK13566 PRK13566
anthranilate synthase component I;
225-355 1.03e-11

anthranilate synthase component I;


Pssm-ID: 237429 [Multi-domain]  Cd Length: 720  Bit Score: 66.48  E-value: 1.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156 225 AEDVLK-MNPDGIFLSNGPGDPApcDYAITA-IQKFLETDIPVFGICLGHQLLALASGAKTVKMKFGHHGGNHPVKDVEK 302
Cdd:PRK13566  561 AEEMLDrVNPDLVVLSPGPGRPS--DFDCKAtIDAALARNLPIFGVCLGLQAIVEAFGGELGQLAYPMHGKPSRIRVRGP 638

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156 303 NVVM------ITA-QNHGFAVDEATLPANLRVTHKSLfDGTLQGIHRTDKPAFSFQGHPE 355
Cdd:PRK13566  639 GRLFsglpeeFTVgRYHSLFADPETLPDELLVTAETE-DGVIMAIEHKTLPVAAVQFHPE 697
PuuD COG2071
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ...
 191-372 2.29e-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: 62.88  E-value: 2.29e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156 191 PFHVVAydfgakRNILRMLVDRGCR---LTIVPAQTSAEDVLKMnPDGIFLSNGP--------GDPAPC---------DY 250
Cdd:COG2071    12 PAHYLP------EDYVRAVRAAGGLpvlLPPVGDEEDLDELLDR-LDGLVLTGGAdvdpalygEEPHPElgpidperdAF 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156 251 AITAIQKFLETDIPVFGICLGHQLLALASG-------AKTVKMKFGH---HGGNHPVKDVE------------KNVVMIt 308
Cdd:COG2071    85 ELALIRAALERGKPVLGICRGMQLLNVALGgtlyqdlPDQVPGALDHrqpAPRYAPRHTVEiepgsrlarilgEEEIRV- 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1234979156 309 aqN--HGFAVDEatLPANLRVTHKSLfDGTLQGIHRTDKP-AFSFQGHPEASPGPHDA-APLFDHFIE 372
Cdd:COG2071   164 --NslHHQAVKR--LGPGLRVSARAP-DGVIEAIESPGAPfVLGVQWHPEWLAASDPLsRRLFEAFVE 226
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 203-275 3.31e-11

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: 59.14  E-value: 3.31e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1234979156 203 RNILRMLVDRGCRLTIVPAQTSAE--DVLKMNPDGIFLSNGPGDPAPCDY---AITAIQKFLETDIPVFGICLGHQLL 275
Cdd:cd03128    15 ASPLDALREAGAEVDVVSPDGGPVesDVDLDDYDGLILPGGPGTPDDLAWdeaLLALLREAAAAGKPVLGICLGAQLL 92
PRK08007 PRK08007
aminodeoxychorismate synthase component 2;
224-356 8.34e-11

aminodeoxychorismate synthase component 2;


Pssm-ID: 181194 [Multi-domain]  Cd Length: 187  Bit Score: 60.70  E-value: 8.34e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156 224 SAEDVLKMNPDGIFLSNGPGDPAPCDYAITAIQKFlETDIPVFGICLGHQLLALASGAKTVKMKFGHHGGNHPVKDVEKN 303
Cdd:PRK08007   35 TLADIDALKPQKIVISPGPCTPDEAGISLDVIRHY-AGRLPILGVCLGHQAMAQAFGGKVVRAAKVMHGKTSPITHNGEG 113

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1234979156 304 VV------MITAQNHGFAVDEATLPANLRVTHKSLfDGTLQGIHRTDKPAFSFQGHPEA 356
Cdd:PRK08007  114 VFrglanpLTVTRYHSLVVEPDSLPACFEVTAWSE-TREIMGIRHRQWDLEGVQFHPES 171
PRK08857 PRK08857
aminodeoxychorismate/anthranilate synthase component II;
231-356 2.76e-10

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181566 [Multi-domain]  Cd Length: 193  Bit Score: 59.12  E-value: 2.76e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156 231 MNPDGIFLSNGPGDPAPCDYAITAIQKFLeTDIPVFGICLGHQLLALASGAKTVKMKFGHHGGNHPVKDVEKNVV----- 305
Cdd:PRK08857   42 LNPTHLVISPGPCTPNEAGISLQAIEHFA-GKLPILGVCLGHQAIAQVFGGQVVRARQVMHGKTSPIRHTGRSVFkglnn 120

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1234979156 306 -MITAQNHGFAVDEATLPANLRVTH-KSLFDGTLQGI----HRTdKPAFSFQGHPEA 356
Cdd:PRK08857  121 pLTVTRYHSLVVKNDTLPECFELTAwTELEDGSMDEImgfqHKT-LPIEAVQFHPES 176
PRK05637 PRK05637
anthranilate synthase component II; Provisional
 209-360 3.32e-09

anthranilate synthase component II; Provisional


Pssm-ID: 180178 [Multi-domain]  Cd Length: 208  Bit Score: 56.39  E-value: 3.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156 209 LVDR----GCRLTIVPAQTSAEDVLKMNPDGIFLSNGPGDPAPCDYAITAIQKFLETdIPVFGICLGHQLLALASGAK-- 282
Cdd:PRK05637   17 LVDAfavaGYKCTVFRNTVPVEEILAANPDLICLSPGPGHPRDAGNMMALIDRTLGQ-IPLLGICLGFQALLEHHGGKve 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156 283 --------TVKMKFGHHGGNHPV-----KDVEKNVVMI------TAQNHGFAVDEAtlPANLRV--THKSLFDGTLQGIH 341
Cdd:PRK05637   96 pcgpvhgtTDNMILTDAGVQSPVfaglaTDVEPDHPEIpgrkvpIARYHSLGCVVA--PDGMESlgTCSSEIGPVIMAAE 173

                         170       180
                  ....*....|....*....|..
gi 1234979156 342 RTDKPAFSFQGHPEA--SP-GP 360
Cdd:PRK05637  174 TTDGKAIGLQFHPESvlSPtGP 195
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 239-355 2.35e-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: 53.80  E-value: 2.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156 239 SNGPGDPAPCDYAITAIQKFLETDIPVFGICLGHQLLALASGAKT---VKMKFGHH-----------GGNHPVkDVEKNV 304
Cdd:pfam07722  82 SGGPYDPARDAYELALIRAALARGKPILGICRGFQLLNVALGGTLyqdIQEQPGFTdhrehcqvapyAPSHAV-NVEPGS 160

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1234979156 305 VM-------ITAQN--HGFAVDEatLPANLRVTHKSLfDGTLQGIHRTDKPAFSF--QGHPE 355
Cdd:pfam07722 161 LLasllgseEFRVNslHHQAIDR--LAPGLRVEAVAP-DGTIEAIESPNAKGFALgvQWHPE 219
PLN02347 PLN02347
GMP synthetase
 181-361 1.45e-07

GMP synthetase


Pssm-ID: 215197 [Multi-domain]  Cd Length: 536  Bit Score: 53.15  E-value: 1.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156 181 MPEAKKEDElpfhVVAYDFGAKRN--ILRMLVDRGCRLTIVPAQTSAEDVLKMNPDGIFLSNGP------GDPAPCDYAI 252
Cdd:PLN02347    4 EAAKSYLDV----VLILDYGSQYThlITRRVRELGVYSLLLSGTASLDRIASLNPRVVILSGGPhsvhveGAPTVPEGFF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156 253 TAIQkflETDIPVFGICLGHQLLALASGAKtVKMKFGHHGGNHPV-----------KDVEKNVVMITAqnHGfavDEAT- 320
Cdd:PLN02347   80 DYCR---ERGVPVLGICYGMQLIVQKLGGE-VKPGEKQEYGRMEIrvvcgsqlfgdLPSGETQTVWMS--HG---DEAVk 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1234979156 321 LPANLRVTHKSLfDGTLQGIHRTDKPAFSFQGHPEASPGPH 361
Cdd:PLN02347  151 LPEGFEVVAKSV-QGAVVAIENRERRIYGLQYHPEVTHSPK 190
PLN02889 PLN02889
oxo-acid-lyase/anthranilate synthase
 234-337 6.16e-07

oxo-acid-lyase/anthranilate synthase


Pssm-ID: 215481 [Multi-domain]  Cd Length: 918  Bit Score: 51.39  E-value: 6.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156 234 DGIFLSNGPGDPA-PCDYAItAIQKFLET-DIPVFGICLGHQLLALASGAKTVKMKFGHHG--------GNHPVKDVE-- 301
Cdd:PLN02889  133 DNIVISPGPGSPTcPADIGI-CLRLLLECrDIPILGVCLGHQALGYVHGARIVHAPEPVHGrlseiehnGCRLFDDIPsg 211

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1234979156 302 KNVVMITAQNHGFAVDEATLPANLRVTHKSLFDGTL 337
Cdd:PLN02889  212 RNSGFKVVRYHSLVIDAESLPKELVPIAWTSSSDTL 247
PRK09522 PRK09522
bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate ...
 219-356 5.56e-06

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


Pssm-ID: 181927 [Multi-domain]  Cd Length: 531  Bit Score: 48.10  E-value: 5.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156 219 VPAQTSAEDVLKMNPDGIFLSNGPGDP--APCdyaITAIQKFLETDIPVFGICLGHQLLALASGAKTVKMKFGHHGGNHP 296
Cdd:PRK09522   35 IPAQTLIERLATMSNPVLMLSPGPGVPseAGC---MPELLTRLRGKLPIIGICLGHQAIVEAYGGYVGQAGEILHGKASS 111

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1234979156 297 VKDVEKNVV------MITAQNHGFAvdEATLPANLRVThkSLFDGTLQGI-HRTDKpAFSFQGHPEA 356
Cdd:PRK09522  112 IEHDGQAMFagltnpLPVARYHSLV--GSNIPAGLTIN--AHFNGMVMAVrHDADR-VCGFQFHPES 173
GATase1_Glutamyl_Hydrolase cd01747
Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase; Type 1 ...
 235-358 3.73e-04

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: 41.92  E-value: 3.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156 235 GIFLSNGPGDPAPCDYAITA---IQKFLETDI-----PVFGICLGHQLLA-LASGAKTVKMKFGHHGGNHPVKDVEKN-- 303
Cdd:cd01747    57 GILFPGGAVDIDTSGYARTAkiiYNLALERNDagdyfPVWGTCLGFELLTyLTSGETLLLEATEATNSALPLNFTEDAlq 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156 304 ----------VVM------ITAQNHGFAVDEATLPAN--LRVTHKSL----------FDGTLQGIhrtDKPAFSFQGHPE 355
Cdd:cd01747   137 srlfkrfppdLLKslatepLTMNNHRYGISPENFTENglLSDFFNVLttnddwngveFISTVEAY---KYPIYGVQWHPE 213


                  ...
gi 1234979156 356 ASP 358
Cdd:cd01747   214 KNA 216
PRK05665 PRK05665
amidotransferase; Provisional
 267-355 4.36e-04

amidotransferase; Provisional


Pssm-ID: 168162 [Multi-domain]  Cd Length: 240  Bit Score: 41.34  E-value: 4.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156 267 GICLGHQLLALASGAKTVKMKFGHHGGNHPVK----------DVEKNVVMITAQnhgfavDEAT-LPANLRVTHKSLFdg 335
Cdd:PRK05665   96 GVCFGHQLLALLLGGKAERASQGWGVGIHRYQlaahapwmspAVTELTLLISHQ------DQVTaLPEGATVIASSDF-- 167

                          90       100
                  ....*....|....*....|
gi 1234979156 336 TLQGIHRTDKPAFSFQGHPE 355
Cdd:PRK05665  168 CPFAAYHIGDQVLCFQGHPE 187
PRK06895 PRK06895
anthranilate synthase component II;
236-356 6.53e-04

anthranilate synthase component II;


Pssm-ID: 235882 [Multi-domain]  Cd Length: 190  Bit Score: 40.49  E-value: 6.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156 236 IFLSNGPGDPAPCDYAITAIQKFLETDiPVFGICLGHQLLALASGAKTVKMKFGHHGGNHPVKDVEKNVVMitaQN---- 311
Cdd:PRK06895   47 ILISPGPDVPRAYPQLFAMLERYHQHK-SILGVCLGHQTLCEFFGGELYNLNNVRHGQQRPLKVRSNSPLF---DGlpee 122

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1234979156 312 ------HGFAVDEATLPANLRVTHKSLFDGTLQGIHRTdKPAFSFQGHPEA 356
Cdd:PRK06895  123 fniglyHSWAVSEENFPTPLEITAVCDENVVMAMQHKT-LPIYGVQFHPES 172
PRK07053 PRK07053
glutamine amidotransferase; Provisional
 252-282 2.07e-03

glutamine amidotransferase; Provisional


Pssm-ID: 235919 [Multi-domain]  Cd Length: 234  Bit Score: 39.16  E-value: 2.07e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1234979156 252 ITAIQKFLETDIPVFGICLGHQLLALASGAK 282
Cdd:PRK07053   73 IALLRQRLAAGLPTLGICLGAQLIARALGAR 103
GATase1_IGP_Synthase cd01748
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ...
 252-276 2.35e-03

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: 38.63  E-value: 2.35e-03
                          10        20
                  ....*....|....*....|....*
gi 1234979156 252 ITAIQKFLETDIPVFGICLGHQLLA 276
Cdd:cd01748    61 IEALKEAIASGKPFLGICLGMQLLF 85
PRK09065 PRK09065
glutamine amidotransferase; Provisional
 260-282 2.49e-03

glutamine amidotransferase; Provisional


Pssm-ID: 181635 [Multi-domain]  Cd Length: 237  Bit Score: 39.17  E-value: 2.49e-03
                          10        20
                  ....*....|....*....|...
gi 1234979156 260 ETDIPVFGICLGHQLLALASGAK 282
Cdd:PRK09065   86 AAGMPLLGICYGHQLLAHALGGE 108
HisH COG0118
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ...
 252-276 3.18e-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: 38.48  E-value: 3.18e-03
                          10        20
                  ....*....|....*....|....*
gi 1234979156 252 ITAIQKFLETDIPVFGICLGHQLLA 276
Cdd:COG0118    63 DEAIREAVAGGKPVLGICLGMQLLF 87
PRK08250 PRK08250
glutamine amidotransferase; Provisional
 225-282 4.60e-03

glutamine amidotransferase; Provisional


Pssm-ID: 181323 [Multi-domain]  Cd Length: 235  Bit Score: 38.41  E-value: 4.60e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234979156 225 AEDVLKMNPDGI-FL--SNGPGDPAP----CDY-----AITAIQKFLETDIPVFGICLGHQLLALASGAK 282
Cdd:PRK08250   35 AGEALPENADGFdLLivMGGPQSPRTtreeCPYfdskaEQRLINQAIKAGKAVIGVCLGAQLIGEALGAK 104
hisH PRK13141
imidazole glycerol phosphate synthase subunit HisH; Provisional
 252-275 5.82e-03

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237288 [Multi-domain]  Cd Length: 205  Bit Score: 37.80  E-value: 5.82e-03
                          10        20
                  ....*....|....*....|....
gi 1234979156 252 ITAIQKFLETDIPVFGICLGHQLL 275
Cdd:PRK13141   62 DEVIKEAVASGKPLLGICLGMQLL 85
 
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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