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Conserved domains on  [gi|2090925019|gb|UAD18061|]
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glutamine-hydrolyzing carbamoyl-phosphate synthase small subunit [Klebsiella quasipneumoniae]

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: 729.90  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019   1 MIKSALLVLEDGTQFHGRAIGATGTAVGEVVFNTSMTGYQEILTDPSYSRQIVTLTYPHIGNVGTNAADEESSQVHAQGL 80
Cdd:COG0505     1 MMMKALLVLEDGTVFEGKSFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVTFTYPHIGNYGVNDEDFESDRPWVAGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019  81 VIRDLPLIASNFRSTEDLSSYLKRHNIVAIADIDTRKLTRLLREKGAQNGCIIAGDsPDAQLALEKAKAFPGLNGMDLAK 160
Cdd:COG0505    81 VVRELSRRPSNWRSEESLDEYLKEHGIPGISGIDTRALTRHLREKGAMKGVISTGD-LDIEELLEKARAAPGMEGLDLVK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019 161 EVTTAETYSWTQgswtlagdlpeakaESELPFHVVAYDFGAKRNILRMLVDRGCRLTVVPAKTSAADVLALNPDGIFLSN 240
Cdd:COG0505   160 EVSTKEPYEWTE--------------APGAGFHVVALDFGVKRNILRELAERGCRVTVVPATTSAEEILALNPDGVFLSN 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019 241 GPGDPAPCDYAIEAIEKFLETDIPVFGICLGHQLLALASGARTIKMKFGHHGGNHPVKDIDNNVVMITAQNHGFAVDEAT 320
Cdd:COG0505   226 GPGDPAALDYAIETIRELLGKGIPIFGICLGHQLLALALGAKTYKLKFGHRGANHPVKDLETGRVEITSQNHGFAVDEDS 305

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2090925019 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: 729.90  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019   1 MIKSALLVLEDGTQFHGRAIGATGTAVGEVVFNTSMTGYQEILTDPSYSRQIVTLTYPHIGNVGTNAADEESSQVHAQGL 80
Cdd:COG0505     1 MMMKALLVLEDGTVFEGKSFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVTFTYPHIGNYGVNDEDFESDRPWVAGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019  81 VIRDLPLIASNFRSTEDLSSYLKRHNIVAIADIDTRKLTRLLREKGAQNGCIIAGDsPDAQLALEKAKAFPGLNGMDLAK 160
Cdd:COG0505    81 VVRELSRRPSNWRSEESLDEYLKEHGIPGISGIDTRALTRHLREKGAMKGVISTGD-LDIEELLEKARAAPGMEGLDLVK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019 161 EVTTAETYSWTQgswtlagdlpeakaESELPFHVVAYDFGAKRNILRMLVDRGCRLTVVPAKTSAADVLALNPDGIFLSN 240
Cdd:COG0505   160 EVSTKEPYEWTE--------------APGAGFHVVALDFGVKRNILRELAERGCRVTVVPATTSAEEILALNPDGVFLSN 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019 241 GPGDPAPCDYAIEAIEKFLETDIPVFGICLGHQLLALASGARTIKMKFGHHGGNHPVKDIDNNVVMITAQNHGFAVDEAT 320
Cdd:COG0505   226 GPGDPAALDYAIETIRELLGKGIPIFGICLGHQLLALALGAKTYKLKFGHRGANHPVKDLETGRVEITSQNHGFAVDEDS 305

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2090925019 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: 707.61  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019   1 MIKSALLVLEDGTQFHGRAIGATGTAVGEVVFNTSMTGYQEILTDPSYSRQIVTLTYPHIGNVGTNAADEESSQVHAQGL 80
Cdd:PRK12564    1 MMMKAYLVLEDGTVFEGKAFGAEGETVGEVVFNTSMTGYQEILTDPSYAGQIVTFTYPLIGNYGVNREDFESDRPHAKGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019  81 VIRDLPLIASNFRSTEDLSSYLKRHNIVAIADIDTRKLTRLLREKGAQNGCIIAGDSpDAQLALEKAKAFPGLNGMDLAK 160
Cdd:PRK12564   81 IVRELSDIPSNWRSEMSLDEYLKENGIPGISGIDTRALTRKLREKGAMKGVIATEDF-DAEELLEKARAFPGLLGLDLVK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019 161 EVTTAETYSWTQGswtlagdlpeakaESELPFHVVAYDFGAKRNILRMLVDRGCRLTVVPAKTSAADVLALNPDGIFLSN 240
Cdd:PRK12564  160 EVSTKEPYPWPGP-------------GGELKYKVVAIDFGVKRNILRELAERGCRVTVVPATTTAEEILALNPDGVFLSN 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019 241 GPGDPAPCDYAIEAIEKFLETDIPVFGICLGHQLLALASGARTIKMKFGHHGGNHPVKDIDNNVVMITAQNHGFAVDEAT 320
Cdd:PRK12564  227 GPGDPAALDYAIEMIRELLEKKIPIFGICLGHQLLALALGAKTYKMKFGHRGANHPVKDLETGKVEITSQNHGFAVDEDS 306

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2090925019 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: 589.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019   5 ALLVLEDGTQFHGRAIGATGTAVGEVVFNTSMTGYQEILTDPSYSRQIVTLTYPHIGNVGTNAADEESSQVHAQGLVIRD 84
Cdd:TIGR01368   1 AYLVLEDGTVFRGYSFGAEGTVAGEVVFNTGMTGYQEILTDPSYKGQIVVFTYPLIGNYGVNDEDAESKGIHVSGLVVRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019  85 LPLIASNFRSTEDLSSYLKRHNIVAIADIDTRKLTRLLREKGAQNGCIIAGDSPDAQLaLEKAKAFPGLNGMDLAKEVTT 164
Cdd:TIGR01368  81 LSDRYSNWRATESLDQFLKRHGIPGIYGVDTRALVKKIREKGTMKGVISTEDSNDEEL-VEKARVSPDITGINLVAEVST 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019 165 AETYSWTQgswtlagdlpeakaESELPFHVVAYDFGAKRNILRMLVDRGCRLTVVPAKTSAADVLALNPDGIFLSNGPGD 244
Cdd:TIGR01368 160 KEPYTWGQ--------------RGGKGKRVVVIDFGVKRNILRRLVKRGCEVTVVPYDTDAEEIKKYNPDGIFLSNGPGD 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019 245 PAPCDYAIEAIEKFLEtDIPVFGICLGHQLLALASGARTIKMKFGHHGGNHPVKDIDNNVVMITAQNHGFAVDEATLPAN 324
Cdd:TIGR01368 226 PAAVEPAIETIRKLLE-KIPIFGICLGHQLLALAFGAKTYKMKFGHRGGNHPVKDLITGRVEITSQNHGYAVDPDSLPAG 304

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2090925019 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 1.86e-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: 330.61  E-value: 1.86e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019 194 VVAYDFGAKRNILRMLVDRGCRLTVVPAKTSAADVLALNPDGIFLSNGPGDPAPCDYAIEAIEKFLETDIPVFGICLGHQ 273
Cdd:cd01744     1 VVVIDFGVKHNILRELLKRGCEVTVVPYNTDAEEILKLDPDGIFLSNGPGDPALLDEAIKTVRKLLGKKIPIFGICLGHQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019 274 LLALASGARTIKMKFGHHGGNHPVKDIDNNVVMITAQNHGFAVDEATLPANLRVTHKSLFDGTLQGIHRTDKPAFSFQGH 353
Cdd:cd01744    81 LLALALGAKTYKMKFGHRGSNHPVKDLITGRVYITSQNHGYAVDPDSLPGGLEVTHVNLNDGTVEGIRHKDLPVFSVQFH 160

                         170
                  ....*....|....*...
gi 2090925019 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 2.03e-87

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: 260.00  E-value: 2.03e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019    3 KSALLVLEDGTQFHGRAIGATGTAVGEVVFNTSMTGYQEILTDPSYSRQIVTLTYPHIGNVGTNAADEESSQVHAQGLVI 82
Cdd:smart01097   1 MKAYLVLEDGTVFEGESFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNDEDFESDKIQVKGLVV 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 2090925019   83 RDLPLIASNFRSTEDLSSYLKRHNIVAIADIDTRKLTRLLREKGAQNGCI 132
Cdd:smart01097  81 RELSDEPSNWRSEQSLDEFLKENGIPGISGIDTRALTRKLREKGAMKGVI 130
CPSase_sm_chain pfam00988
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 7-132 1.41e-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: 257.64  E-value: 1.41e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019   7 LVLEDGTQFHGRAIGATGTAVGEVVFNTSMTGYQEILTDPSYSRQIVTLTYPHIGNVGTNAADEESSQVHAQGLVIRDLP 86
Cdd:pfam00988   1 LVLEDGTVFEGKSFGAAGSTVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNPEDFESDKIHVAGLVVREYS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2090925019  87 LIASNFRSTEDLSSYLKRHNIVAIADIDTRKLTRLLREKGAQNGCI 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: 729.90  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019   1 MIKSALLVLEDGTQFHGRAIGATGTAVGEVVFNTSMTGYQEILTDPSYSRQIVTLTYPHIGNVGTNAADEESSQVHAQGL 80
Cdd:COG0505     1 MMMKALLVLEDGTVFEGKSFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVTFTYPHIGNYGVNDEDFESDRPWVAGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019  81 VIRDLPLIASNFRSTEDLSSYLKRHNIVAIADIDTRKLTRLLREKGAQNGCIIAGDsPDAQLALEKAKAFPGLNGMDLAK 160
Cdd:COG0505    81 VVRELSRRPSNWRSEESLDEYLKEHGIPGISGIDTRALTRHLREKGAMKGVISTGD-LDIEELLEKARAAPGMEGLDLVK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019 161 EVTTAETYSWTQgswtlagdlpeakaESELPFHVVAYDFGAKRNILRMLVDRGCRLTVVPAKTSAADVLALNPDGIFLSN 240
Cdd:COG0505   160 EVSTKEPYEWTE--------------APGAGFHVVALDFGVKRNILRELAERGCRVTVVPATTSAEEILALNPDGVFLSN 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019 241 GPGDPAPCDYAIEAIEKFLETDIPVFGICLGHQLLALASGARTIKMKFGHHGGNHPVKDIDNNVVMITAQNHGFAVDEAT 320
Cdd:COG0505   226 GPGDPAALDYAIETIRELLGKGIPIFGICLGHQLLALALGAKTYKLKFGHRGANHPVKDLETGRVEITSQNHGFAVDEDS 305

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2090925019 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: 707.61  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019   1 MIKSALLVLEDGTQFHGRAIGATGTAVGEVVFNTSMTGYQEILTDPSYSRQIVTLTYPHIGNVGTNAADEESSQVHAQGL 80
Cdd:PRK12564    1 MMMKAYLVLEDGTVFEGKAFGAEGETVGEVVFNTSMTGYQEILTDPSYAGQIVTFTYPLIGNYGVNREDFESDRPHAKGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019  81 VIRDLPLIASNFRSTEDLSSYLKRHNIVAIADIDTRKLTRLLREKGAQNGCIIAGDSpDAQLALEKAKAFPGLNGMDLAK 160
Cdd:PRK12564   81 IVRELSDIPSNWRSEMSLDEYLKENGIPGISGIDTRALTRKLREKGAMKGVIATEDF-DAEELLEKARAFPGLLGLDLVK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019 161 EVTTAETYSWTQGswtlagdlpeakaESELPFHVVAYDFGAKRNILRMLVDRGCRLTVVPAKTSAADVLALNPDGIFLSN 240
Cdd:PRK12564  160 EVSTKEPYPWPGP-------------GGELKYKVVAIDFGVKRNILRELAERGCRVTVVPATTTAEEILALNPDGVFLSN 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019 241 GPGDPAPCDYAIEAIEKFLETDIPVFGICLGHQLLALASGARTIKMKFGHHGGNHPVKDIDNNVVMITAQNHGFAVDEAT 320
Cdd:PRK12564  227 GPGDPAALDYAIEMIRELLEKKIPIFGICLGHQLLALALGAKTYKMKFGHRGANHPVKDLETGKVEITSQNHGFAVDEDS 306

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2090925019 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: 589.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019   5 ALLVLEDGTQFHGRAIGATGTAVGEVVFNTSMTGYQEILTDPSYSRQIVTLTYPHIGNVGTNAADEESSQVHAQGLVIRD 84
Cdd:TIGR01368   1 AYLVLEDGTVFRGYSFGAEGTVAGEVVFNTGMTGYQEILTDPSYKGQIVVFTYPLIGNYGVNDEDAESKGIHVSGLVVRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019  85 LPLIASNFRSTEDLSSYLKRHNIVAIADIDTRKLTRLLREKGAQNGCIIAGDSPDAQLaLEKAKAFPGLNGMDLAKEVTT 164
Cdd:TIGR01368  81 LSDRYSNWRATESLDQFLKRHGIPGIYGVDTRALVKKIREKGTMKGVISTEDSNDEEL-VEKARVSPDITGINLVAEVST 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019 165 AETYSWTQgswtlagdlpeakaESELPFHVVAYDFGAKRNILRMLVDRGCRLTVVPAKTSAADVLALNPDGIFLSNGPGD 244
Cdd:TIGR01368 160 KEPYTWGQ--------------RGGKGKRVVVIDFGVKRNILRRLVKRGCEVTVVPYDTDAEEIKKYNPDGIFLSNGPGD 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019 245 PAPCDYAIEAIEKFLEtDIPVFGICLGHQLLALASGARTIKMKFGHHGGNHPVKDIDNNVVMITAQNHGFAVDEATLPAN 324
Cdd:TIGR01368 226 PAAVEPAIETIRKLLE-KIPIFGICLGHQLLALAFGAKTYKMKFGHRGGNHPVKDLITGRVEITSQNHGYAVDPDSLPAG 304

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2090925019 325 -LRVTHKSLFDGTLQGIHRTDKPAFSFQGHPEASPGPHDAAPLFDHFIELIEQ 376
Cdd:TIGR01368 305 dLEVTHVNLNDGTVEGIRHKDLPVFSVQYHPEASPGPHDTEYLFDEFIDLMKK 357
PRK12838 PRK12838
carbamoyl phosphate synthase small subunit; Reviewed
 5-378 6.49e-159

carbamoyl phosphate synthase small subunit; Reviewed


Pssm-ID: 183784 [Multi-domain]  Cd Length: 354  Bit Score: 450.50  E-value: 6.49e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019   5 ALLVLEDGTQFHGRAIGATGTAVGEVVFNTSMTGYQEILTDPSYSRQIVTLTYPHIGNVGTNAADEESSQVHAQGLVIRD 84
Cdd:PRK12838    3 AYLILEDGTVFEGELIGAPIDVTGEIVFNTGMTGYQEVLTDPSYKGQIVVFTYPLIGNYGINADDYESKQPQVKGVIVYE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019  85 LPLIASNFRSTEDLSSYLKRHNIVAIADIDTRKLTRLLREKGAQNGCIIagDSPDAQLALEKAKAFPGLNgmdLAKEVTT 164
Cdd:PRK12838   83 LSREGSHYRAKQSLDDFLKEWNIPGISGVDTRALVKHIREKGTMKASIT--TTDDAHAFDQIKALVLPKN---VVAQVST 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019 165 AETYSWTQGSwtlagdlpeakaeselpFHVVAYDFGAKRNILRMLVDRGCRLTVVPAKTSAADVLALNPDGIFLSNGPGD 244
Cdd:PRK12838  158 KEPYTYGNGG-----------------KHVALIDFGYKKSILRSLSKRGCKVTVLPYDTSLEEIKNLNPDGIVLSNGPGD 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019 245 PAPCDYAIEAIEKfLETDIPVFGICLGHQLLALASGARTIKMKFGHHGGNHPVKDIDNNVVMITAQNHGFAVDEATLPAN 324
Cdd:PRK12838  221 PKELQPYLPEIKK-LISSYPILGICLGHQLIALALGADTEKLPFGHRGANHPVIDLTTGRVWMTSQNHGYVVDEDSLDGT 299

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2090925019 325 -LRVTHKSLFDGTLQGIHRTDKPAFSFQGHPEASPGPHDAAPLFDHFIELIEQYR 378
Cdd:PRK12838  300 pLSVRFFNVNDGSIEGLRHKKKPVLSVQFHPEAHPGPHDAEYIFDEFLEMMEKAR 354
carA CHL00197
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
 3-381 7.94e-147

carbamoyl-phosphate synthase arginine-specific small subunit; Provisional


Pssm-ID: 214392 [Multi-domain]  Cd Length: 382  Bit Score: 420.74  E-value: 7.94e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019   3 KSALLVLEDGTQFHGRAIGATGTAVGEVVFNTSMTGYQEILTDPSYSRQIVTLTYPHIGNVGTNAADEESSQVHAQGLVI 82
Cdd:CHL00197    5 IPAILVLEDGTYYRGWSFSNPITTIGEVVFNTGMTGYQEIITDPSYFEQIVTFTYPEIGNTGINLEDIESVKIQVKGIIA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019  83 RDLPLIASNFRSTEDLSSYLKRHNIVAIADIDTRKLTRLLREKGAQNGCiIAGDSPDAQLALEKAKAFPGLNGMDLAKEV 162
Cdd:CHL00197   85 KNICKSSSNWRQQESLVSYLQRHKIPFIFGIDTRALTQHLRRFGTMNGC-ISNQNLNLSYLRAKIKESPHMPSSDLIPRV 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019 163 TTAETYSWTQGS---WTLAgdlPEAKAESELPFHVVAYDFGAKRNILRMLVDRGCRLTVVPAKTSAADVLALNPDGIFLS 239
Cdd:CHL00197  164 TTSSYYEWDEKShpsFYLA---DNKRPHSSYQLKIIVIDFGVKYNILRRLKSFGCSITVVPATSPYQDILSYQPDGILLS 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019 240 NGPGDPAPCDYAIEAIEKFLETDIPVFGICLGHQLLALASGARTIKMKFGHHGGNHPVKdiDNNVVMITAQNHGFAVDEA 319
Cdd:CHL00197  241 NGPGDPSAIHYGIKTVKKLLKYNIPIFGICMGHQILSLALEAKTFKLKFGHRGLNHPSG--LNQQVEITSQNHGFAVNLE 318

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2090925019 320 TLPAN-LRVTHKSLFDGTLQGIHRTDKPAFSFQGHPEASPGPHDAAPLFDHFIELIEQYRQSA 381
Cdd:CHL00197  319 SLAKNkFYITHFNLNDGTVAGISHSPKPYFSVQYHPEASPGPHDADYLFEYFIEIIKHSKSSK 381
PLN02771 PLN02771
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
 5-367 2.78e-136

carbamoyl-phosphate synthase (glutamine-hydrolyzing)


Pssm-ID: 178370 [Multi-domain]  Cd Length: 415  Bit Score: 395.12  E-value: 2.78e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019   5 ALLVLEDGTQFHGRAIGATGTAVGEVVFNTSMTGYQEILTDPSYSRQIVTLTYPHIGNVGTNAADEESSQVHAQGLVIRD 84
Cdd:PLN02771   57 ARLVLEDGSVWKAKSFGARGTQVGEVVFNTSLTGYQEILTDPSYAGQFVLMTNPHIGNTGVNFDDEESRQCFLAGLVIRS 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019  85 LPLIASNFRSTEDLSSYLKRHNIVAIADIDTRKLTRLLREKGAQNGCIIAGDSPDAQLALEKAKAFpGLNGMDLAKEVTT 164
Cdd:PLN02771  137 LSISTSNWRCTKTLGDYLAERNIMGIYDVDTRAITRRLREDGSLIGVLSTEDSKTDEELLKMSRSW-DIVGIDLISGVSC 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019 165 AETYSW---TQGSWtlagDLPEAKAESELpFHVVAYDFGAKRNILRMLVDRGCRLTVVPAKTSAADVLALNPDGIFLSNG 241
Cdd:PLN02771  216 KSPYEWvdkTNPEW----DFNTNSRDGES-YHVIAYDFGIKHNILRRLASYGCKITVVPSTWPASEALKMKPDGVLFSNG 290

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019 242 PGDPAPCDYAIEAIEKFLeTDIPVFGICLGHQLLALASGARTIKMKFGHHGGNHPVKDIDNNVVMITAQNHGFAVDEATL 321
Cdd:PLN02771  291 PGDPSAVPYAVETVKELL-GKVPVFGICMGHQLLGQALGGKTFKMKFGHHGGNHPVRNNRTGRVEISAQNHNYAVDPASL 369

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 2090925019 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 1.86e-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: 330.61  E-value: 1.86e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019 194 VVAYDFGAKRNILRMLVDRGCRLTVVPAKTSAADVLALNPDGIFLSNGPGDPAPCDYAIEAIEKFLETDIPVFGICLGHQ 273
Cdd:cd01744     1 VVVIDFGVKHNILRELLKRGCEVTVVPYNTDAEEILKLDPDGIFLSNGPGDPALLDEAIKTVRKLLGKKIPIFGICLGHQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019 274 LLALASGARTIKMKFGHHGGNHPVKDIDNNVVMITAQNHGFAVDEATLPANLRVTHKSLFDGTLQGIHRTDKPAFSFQGH 353
Cdd:cd01744    81 LLALALGAKTYKMKFGHRGSNHPVKDLITGRVYITSQNHGYAVDPDSLPGGLEVTHVNLNDGTVEGIRHKDLPVFSVQFH 160

                         170
                  ....*....|....*...
gi 2090925019 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 2.03e-87

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: 260.00  E-value: 2.03e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019    3 KSALLVLEDGTQFHGRAIGATGTAVGEVVFNTSMTGYQEILTDPSYSRQIVTLTYPHIGNVGTNAADEESSQVHAQGLVI 82
Cdd:smart01097   1 MKAYLVLEDGTVFEGESFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNDEDFESDKIQVKGLVV 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 2090925019   83 RDLPLIASNFRSTEDLSSYLKRHNIVAIADIDTRKLTRLLREKGAQNGCI 132
Cdd:smart01097  81 RELSDEPSNWRSEQSLDEFLKENGIPGISGIDTRALTRKLREKGAMKGVI 130
CPSase_sm_chain pfam00988
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 7-132 1.41e-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: 257.64  E-value: 1.41e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019   7 LVLEDGTQFHGRAIGATGTAVGEVVFNTSMTGYQEILTDPSYSRQIVTLTYPHIGNVGTNAADEESSQVHAQGLVIRDLP 86
Cdd:pfam00988   1 LVLEDGTVFEGKSFGAAGSTVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNPEDFESDKIHVAGLVVREYS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2090925019  87 LIASNFRSTEDLSSYLKRHNIVAIADIDTRKLTRLLREKGAQNGCI 132
Cdd:pfam00988  81 DEPSNWRAEESLDEWLKEQGIPGISGVDTRALTRKIREKGAMKGVI 126
GATase pfam00117
Glutamine amidotransferase class-I;
195-373 4.35e-72

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 223.27  E-value: 4.35e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019 195 VAYDFGA--KRNILRMLVDRGCRLTVVPAKTSAADVLALNPDGIFLSNGPGDPAPCDYAIEAIEKFLETDIPVFGICLGH 272
Cdd:pfam00117   1 LLIDNGDsfTYNLARALRELGVEVTVVPNDTPAEEILEENPDGIILSGGPGSPGAAGGAIEAIREARELKIPILGICLGH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019 273 QLLALASGARTIKMK-FGHHGGNHPVKDIDNNV------VMITAQNHGFAVDEATLPANLRVTHKSLFDGTLQGIHRTDK 345
Cdd:pfam00117  81 QLLALAFGGKVVKAKkFGHHGKNSPVGDDGCGLfyglpnVFIVRRYHSYAVDPDTLPDGLEVTATSENDGTIMGIRHKKL 160

                         170       180
                  ....*....|....*....|....*...
gi 2090925019 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 2.57e-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: 109.16  E-value: 2.57e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019 204 NILRMLVDRGCRLTVVPA-KTSAADVLALNPDGIFLSNGPGDPApcDYAI-EAIEKFLETDIPVFGICLGHQLLALASGA 281
Cdd:cd01743    13 NLVQYLRELGAEVVVVRNdEITLEELELLNPDAIVISPGPGHPE--DAGIsLEIIRALAGKVPILGVCLGHQAIAEAFGG 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019 282 RTIKMKFGHHGGNHPVKDIDNNVVMITAQN------HGFAVDEATLPANLRVTHKSlFDGTLQGIHRTDKPAFSFQGHPE 355
Cdd:cd01743    91 KVVRAPEPMHGKTSEIHHDGSGLFKGLPQPftvgryHSLVVDPDPLPDLLEVTAST-EDGVIMALRHRDLPIYGVQFHPE 169
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 206-355 4.43e-24

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: 97.80  E-value: 4.43e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019 206 LRMLvdrGCRLTVVPA-KTSAADVLALNPDGIFLSNGPGDPAPCDYAIEAIEKFlETDIPVFGICLGHQLLALASGARTI 284
Cdd:COG0512    18 LGEL---GAEVVVVRNdEITLEEIEALAPDGIVLSPGPGTPEEAGISLEVIRAF-AGKIPILGVCLGHQAIGEAFGGKVV 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019 285 KMKFGHHGGNHPVKdIDNNVVMitaQN----------HGFAVDEATLPANLRVTHKSLfDGTLQGIHRTDKPAFSFQGHP 354
Cdd:COG0512    94 RAPEPMHGKTSPIT-HDGSGLF---AGlpnpftatryHSLVVDRETLPDELEVTAWTE-DGEIMGIRHRELPIEGVQFHP 168


                  .
gi 2090925019 355 E 355
Cdd:COG0512   169 E 169
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 206-355 1.08e-21

anthranilate synthase component II; Provisional


Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 91.34  E-value: 1.08e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019 206 LRMLvdrGCRLTVVP-AKTSAADVLALNPDGIFLSNGPGDPAPCDYAIEAIEKFLETdIPVFGICLGHQLLALASGARTI 284
Cdd:PRK05670   19 LGEL---GAEVVVYRnDEITLEEIEALNPDAIVLSPGPGTPAEAGISLELIREFAGK-VPILGVCLGHQAIGEAFGGKVV 94

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2090925019 285 KMKFGHHG-------GNHPV-KDIDNNvvMITAQNHGFAVDEATLPANLRVTHKSlFDGTLQGIHRTDKPAFSFQGHPE 355
Cdd:PRK05670   95 RAKEIMHGktspiehDGSGIfAGLPNP--FTVTRYHSLVVDRESLPDCLEVTAWT-DDGEIMGVRHKELPIYGVQFHPE 170
PRK14607 PRK14607
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
204-371 7.27e-21

bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;


Pssm-ID: 237764 [Multi-domain]  Cd Length: 534  Bit Score: 94.01  E-value: 7.27e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019 204 NILRMLVDRG--CRLTVVPAKTSAADVLALNPDGIFLSNGPGDPAPCDYAIEAIEKFlETDIPVFGICLGHQLLALASGA 281
Cdd:PRK14607   14 NIYQYIGELGpeEIEVVRNDEITIEEIEALNPSHIVISPGPGRPEEAGISVEVIRHF-SGKVPILGVCLGHQAIGYAFGG 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019 282 RTIKMKFGHHGGNHPV----KDIDNNVV--MITAQNHGFAVDEATLPANLRVTHKSLfDGTLQGIHRTDKPAFSFQGHPE 355
Cdd:PRK14607   93 KIVHAKRILHGKTSPIdhngKGLFRGIPnpTVATRYHSLVVEEASLPECLEVTAKSD-DGEIMGIRHKEHPIFGVQFHPE 171

                         170
                  ....*....|....*.
gi 2090925019 356 aSPGPHDAAPLFDHFI 371
Cdd:PRK14607  172 -SILTEEGKRILKNFL 186
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 205-358 7.47e-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: 81.53  E-value: 7.47e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019 205 ILRMLVDRGCRLTVVPAKTSA---ADVLALNPDGIFLSNGPGDP-APCDY---AIEAIEKFLETDIPVFGICLGHQLLAL 277
Cdd:COG0518    18 IARRLREAGIELDVLRVYAGEilpYDPDLEDPDGLILSGGPMSVyDEDPWledEPALIREAFELGKPVLGICYGAQLLAH 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019 278 ASGARTIKMKfGHHGGNHPVKDIDNNVVM------ITA-QNHGFAVDEatLPANLRVTHKSLFDgTLQGIhRTDKPAFSF 350
Cdd:COG0518    98 ALGGKVEPGP-GREIGWAPVELTEADPLFaglpdeFTVwMSHGDTVTE--LPEGAEVLASSDNC-PNQAF-RYGRRVYGV 172


                  ....*...
gi 2090925019 351 QGHPEASP 358
Cdd:COG0518   173 QFHPEVTH 180
trpG_papA TIGR00566
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ...
 226-373 1.77e-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: 74.05  E-value: 1.77e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019 226 ADVLALNPDGIFLSNGPGDPAPCDYAIEAIEKFlETDIPVFGICLGHQLLALASGARTIKMKFGHHGGNHPVKDIDNNVV 305
Cdd:TIGR00566  37 QEIEALLPLLIVISPGPCTPNEAGISLEAIRHF-AGKLPILGVCLGHQAMGQAFGGDVVRANTVMHGKTSEIEHNGAGIF 115

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2090925019 306 ------MITAQNHGFAVDEATLPANLRVTHKSLFDGTLQGIHRTDKPAFSFQGHPEaSPGPHDAAPLFDHFIEL 373
Cdd:TIGR00566 116 rglfnpLTATRYHSLVVEPETLPTCFPVTAWEEENIEIMAIRHRDLPLEGVQFHPE-SILSEQGHQLLANFLHR 188
guaA_Nterm TIGR00888
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ...
 194-355 3.20e-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: 73.12  E-value: 3.20e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019 194 VVAYDFGAKRN--ILRMLVDRGCRLTVVPAKTSAADVLALNPDGIFLSNGPGDpapcDY---AIEAIEKFLETDIPVFGI 268
Cdd:TIGR00888   1 ILVLDFGSQYTqlIARRLRELGVYSELVPNTTPLEEIREKNPKGIILSGGPSS----VYaenAPRADEKIFELGVPVLGI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019 269 CLGHQLLALASGARTIKMKFGHHGgnhPVK-DIDNNVVMITAQNHGFAV-----DEAT-LPANLRVTHKSlfDGT-LQGI 340
Cdd:TIGR00888  77 CYGMQLMAKQLGGEVGRAEKREYG---KAElEILDEDDLFRGLPDESTVwmshgDKVKeLPEGFKVLATS--DNCpVAAM 151

                         170
                  ....*....|....*
gi 2090925019 341 HRTDKPAFSFQGHPE 355
Cdd:TIGR00888 152 AHEEKPIYGVQFHPE 166
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 193-356 3.82e-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: 73.05  E-value: 3.82e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019 193 HVVAYDFGAKRNILRMLVDRGCRLTVVPAKTSAADVLALNPDGIFLSNGPGDPAPCDYA-----IEAIEKFLETDIPVFG 267
Cdd:cd01741     7 HDTPEGPGLFEDLLREAGAETIEIDVVDVYAGELLPDLDDYDGLVILGGPMSVDEDDYPwlkklKELIRQALAAGKPVLG 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019 268 ICLGHQLLALASGARTIKMKFGHHGGNHPVKDIDNNVVMITAQN----------HGFAVDEatLPANLRVTHKSLFDGTl 337
Cdd:cd01741    87 ICLGHQLLARALGGKVGRNPKGWEIGWFPVTLTEAGKADPLFAGlpdefpvfhwHGDTVVE--LPPGAVLLASSEACPN- 163

                         170
                  ....*....|....*....
gi 2090925019 338 QGIhRTDKPAFSFQGHPEA 356
Cdd:cd01741   164 QAF-RYGDRALGLQFHPEE 181
PRK00758 PRK00758
GMP synthase subunit A; Validated
 205-377 1.03e-14

GMP synthase subunit A; Validated


Pssm-ID: 179112 [Multi-domain]  Cd Length: 184  Bit Score: 71.81  E-value: 1.03e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019 205 ILRMLVDRGCRLTVVPAKTSAADVLAlNPDGIFLSNGPgdpaPCDYAIEAIEKFLETDIPVFGICLGHQLLALASGARTI 284
Cdd:PRK00758   15 IHRTLRYLGVDAKIIPNTTPVEEIKA-FEDGLILSGGP----DIERAGNCPEYLKELDVPILGICLGHQLIAKAFGGEVG 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019 285 KMKFGHHGgnhpvkDIDNNVV------------MITAQNHGfavDE-ATLPANLRVTHKSLFDGtLQGIHRTDKPAFSFQ 351
Cdd:PRK00758   90 RGEYGEYA------LVEVEILdeddilkglppeIRVWASHA---DEvKELPDGFEILARSDICE-VEAMKHKEKPIYGVQ 159

                         170       180
                  ....*....|....*....|....*.
gi 2090925019 352 GHPEASPGPHDAApLFDHFIELIEQY 377
Cdd:PRK00758  160 FHPEVAHTEYGEE-IFKNFLEICGKY 184
GATase1_GMP_Synthase cd01742
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ...
 194-355 1.54e-14

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: 71.03  E-value: 1.54e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019 194 VVAYDFGAKRN--ILRMLVDRGCRLTVVPAKTSAADVLALNPDGIFLSNGP----GDPAP-CDyaieaiEKFLETDIPVF 266
Cdd:cd01742     1 ILILDFGSQYThlIARRVRELGVYSEILPNTTPLEEIKLKNPKGIILSGGPssvyEEDAPrVD------PEIFELGVPVL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019 267 GICLGHQLLALASGA---RTIKMKFGHH-----GGNHPVKDIDN--NVVMitaqNHGFAVDEatLPANLRVTHKSLfDGT 336
Cdd:cd01742    75 GICYGMQLIAKALGGkveRGDKREYGKAeieidDSSPLFEGLPDeqTVWM----SHGDEVVK--LPEGFKVIASSD-NCP 147

                         170
                  ....*....|....*....
gi 2090925019 337 LQGIHRTDKPAFSFQGHPE 355
Cdd:cd01742   148 VAAIANEEKKIYGVQFHPE 166
trpG CHL00101
anthranilate synthase component 2
 231-356 3.62e-14

anthranilate synthase component 2


Pssm-ID: 214365 [Multi-domain]  Cd Length: 190  Bit Score: 70.53  E-value: 3.62e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019 231 LNPDGIFLSNGPGDPAPCDYAIEAIEKFLETdIPVFGICLGHQLLALASGARTIKMKFGHHGGN----HPVKDIDNNVV- 305
Cdd:CHL00101   42 LNIRHIIISPGPGHPRDSGISLDVISSYAPY-IPILGVCLGHQSIGYLFGGKIIKAPKPMHGKTskiyHNHDDLFQGLPn 120

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2090925019 306 -MITAQNHGFAVDEATLPANLRVTHKSlFDGTLQGI-HRTDKPAFSFQGHPEA 356
Cdd:CHL00101  121 pFTATRYHSLIIDPLNLPSPLEITAWT-EDGLIMACrHKKYKMLRGIQFHPES 172
PRK07765 PRK07765
aminodeoxychorismate/anthranilate synthase component II;
223-355 1.51e-13

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181107 [Multi-domain]  Cd Length: 214  Bit Score: 68.92  E-value: 1.51e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019 223 TSAADVLALNPDGIFLSNGPGDPAPCDYAIEAIEKFLETDIPVFGICLGHQLLALASGARTIKMKFGHHGGNHPVKDIDN 302
Cdd:PRK07765   37 LADEAAVAAQFDGVLLSPGPGTPERAGASIDMVRACAAAGTPLLGVCLGHQAIGVAFGATVDRAPELLHGKTSSVHHTGV 116

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2090925019 303 NVVM-----ITA-QNHGFAVDEATLPANLRVTHKSLfDGTLQGIHRTDKPAFSFQGHPE 355
Cdd:PRK07765  117 GVLAglpdpFTAtRYHSLTILPETLPAELEVTARTD-SGVIMAVRHRELPIHGVQFHPE 174
PRK06774 PRK06774
aminodeoxychorismate synthase component II;
226-372 4.17e-13

aminodeoxychorismate synthase component II;


Pssm-ID: 180689 [Multi-domain]  Cd Length: 191  Bit Score: 67.19  E-value: 4.17e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019 226 ADVLALNPDGIFLSNGPGDPAPCDYAIEAIEKFLEtDIPVFGICLGHQLLALASGARTIKMKFGHHGGNHPVKDIDNNVV 305
Cdd:PRK06774   37 TDIEQLAPSHLVISPGPCTPNEAGISLAVIRHFAD-KLPILGVCLGHQALGQAFGARVVRARQVMHGKTSAICHSGQGVF 115

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2090925019 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 5.08e-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: 66.83  E-value: 5.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019 203 RNILRMLVDRGCRLTVVPAKT--SAADVLALNPDGIFLSNGP--------GDPAPCD---------YAIEAIEKFLETDI 263
Cdd:cd01745    22 QYYVDAVRKAGGLPVLLPPVDdeEDLEQYLELLDGLLLTGGGdvdpplygEEPHPELgpidperdaFELALLRAALERGK 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019 264 PVFGICLGHQLLALAsgartikmkfghHGGN-HPvkDIDNNvvmitaQNHGFAVDEatLPANLRVTHKSLfDGTLQGIHR 342
Cdd:cd01745   102 PILGICRGMQLLNVA------------LGGTlYQ--DIRVN------SLHHQAIKR--LADGLRVEARAP-DGVIEAIES 158

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2090925019 343 TDKP-AFSFQGHPE-ASPGPHDAAPLFDHFI 371
Cdd:cd01745   159 PDRPfVLGVQWHPEwLADTDPDSLKLFEAFV 189
PRK07649 PRK07649
aminodeoxychorismate/anthranilate synthase component II;
224-381 7.35e-13

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181066 [Multi-domain]  Cd Length: 195  Bit Score: 66.75  E-value: 7.35e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019 224 SAADVLALNPDGIFLSNGPGDPAPCDYAIEAIEKFlETDIPVFGICLGHQLLALASGARTIKMKFGHHGGNHPV------ 297
Cdd:PRK07649   35 TISDIENMKPDFLMISPGPCSPNEAGISMEVIRYF-AGKIPIFGVCLGHQSIAQVFGGEVVRAERLMHGKTSLMhhdgkt 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019 298 --KDIDNNVVmiTAQNHGFAVDEATLPANLRVTHKSLfDGTLQGIHRTDKPAFSFQGHPEASPGPHdAAPLFDHFielIE 375
Cdd:PRK07649  114 ifSDIPNPFT--ATRYHSLIVKKETLPDCLEVTSWTE-EGEIMAIRHKTLPIEGVQFHPESIMTSH-GKELLQNF---IR 186


                  ....*.
gi 2090925019 376 QYRQSA 381
Cdd:PRK07649  187 KYSPSV 192
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 203-280 2.23e-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: 63.39  E-value: 2.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019 203 RNILRMLVDRGCRLTVVPAKTSA--ADVLALNPDGIFLSNGPGDPAPCDY---AIEAIEKFLETDIPVFGICLGHQLLAL 277
Cdd:cd01653    15 ASPLDALREAGAEVDVVSPDGGPveSDVDLDDYDGLILPGGPGTPDDLARdeaLLALLREAAAAGKPILGICLGAQLLVL 94


                  ...
gi 2090925019 278 ASG 280
Cdd:cd01653    95 GVQ 97
PRK08857 PRK08857
aminodeoxychorismate/anthranilate synthase component II;
226-356 5.12e-12

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181566 [Multi-domain]  Cd Length: 193  Bit Score: 64.13  E-value: 5.12e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019 226 ADVLALNPDGIFLSNGPGDPAPCDYAIEAIEKFLeTDIPVFGICLGHQLLALASGARTIKMKFGHHGGNHPVKDID---- 301
Cdd:PRK08857   37 DGIEALNPTHLVISPGPCTPNEAGISLQAIEHFA-GKLPILGVCLGHQAIAQVFGGQVVRARQVMHGKTSPIRHTGrsvf 115

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2090925019 302 ---NNVVMITaQNHGFAVDEATLPANLRVTH-KSLFDGTLQGI----HRTdKPAFSFQGHPEA 356
Cdd:PRK08857  116 kglNNPLTVT-RYHSLVVKNDTLPECFELTAwTELEDGSMDEImgfqHKT-LPIEAVQFHPES 176
PLN02335 PLN02335
anthranilate synthase
 204-377 7.45e-12

anthranilate synthase


Pssm-ID: 177969 [Multi-domain]  Cd Length: 222  Bit Score: 64.43  E-value: 7.45e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019 204 NILRMLVDRGCRLTVVPA-KTSAADVLALNPDGIFLSNGPGDPAPCDYAIEAIEKfLETDIPVFGICLGHQLLALASGAR 282
Cdd:PLN02335   33 NLCQYMGELGCHFEVYRNdELTVEELKRKNPRGVLISPGPGTPQDSGISLQTVLE-LGPLVPLFGVCMGLQCIGEAFGGK 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019 283 TIKMKFG-HHGGNHPV---KDIDNNVV------MITAQNHGFAVDEATLPAN-LRVTHKSLfDGTLQGI-HRTDKPAFSF 350
Cdd:PLN02335  112 IVRSPFGvMHGKSSPVhydEKGEEGLFsglpnpFTAGRYHSLVIEKDTFPSDeLEVTAWTE-DGLIMAArHRKYKHIQGV 190

                         170       180
                  ....*....|....*....|....*..
gi 2090925019 351 QGHPEaSPGPHDAAPLFDHFIELIEQY 377
Cdd:PLN02335  191 QFHPE-SIITTEGKTIVRNFIKIIEKK 216
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 203-275 1.11e-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: 60.68  E-value: 1.11e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2090925019 203 RNILRMLVDRGCRLTVVPAKTSA--ADVLALNPDGIFLSNGPGDPAPCDY---AIEAIEKFLETDIPVFGICLGHQLL 275
Cdd:cd03128    15 ASPLDALREAGAEVDVVSPDGGPveSDVDLDDYDGLILPGGPGTPDDLAWdeaLLALLREAAAAGKPVLGICLGAQLL 92
PRK08007 PRK08007
aminodeoxychorismate synthase component 2;
224-356 1.35e-11

aminodeoxychorismate synthase component 2;


Pssm-ID: 181194 [Multi-domain]  Cd Length: 187  Bit Score: 63.01  E-value: 1.35e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019 224 SAADVLALNPDGIFLSNGPGDPAPCDYAIEAIEKFlETDIPVFGICLGHQLLALASGARTIKMKFGHHGGNHPVKDID-- 301
Cdd:PRK08007   35 TLADIDALKPQKIVISPGPCTPDEAGISLDVIRHY-AGRLPILGVCLGHQAMAQAFGGKVVRAAKVMHGKTSPITHNGeg 113

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019 302 -----NNVVMITaQNHGFAVDEATLPANLRVTHKSLfDGTLQGIHRTDKPAFSFQGHPEA 356
Cdd:PRK08007  114 vfrglANPLTVT-RYHSLVVEPDSLPACFEVTAWSE-TREIMGIRHRQWDLEGVQFHPES 171
guaA PRK00074
GMP synthase; Reviewed
 218-355 1.61e-11

GMP synthase; Reviewed


Pssm-ID: 234614 [Multi-domain]  Cd Length: 511  Bit Score: 65.45  E-value: 1.61e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019 218 VVPAKTSAADVLALNPDGIFLSNGP----GDPAPcdyaiEAIEKFLETDIPVFGICLGHQLLALASG---ARTIKMKFGH 290
Cdd:PRK00074   32 IVPYDISAEEIRAFNPKGIILSGGPasvyEEGAP-----RADPEIFELGVPVLGICYGMQLMAHQLGgkvERAGKREYGR 106

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2090925019 291 -----HGGNHPVKDIDNN--VVMitaqNHGFAVDEatLPANLRVTHKSlfDGT-LQGIHRTDKPAFSFQGHPE 355
Cdd:PRK00074  107 aelevDNDSPLFKGLPEEqdVWM----SHGDKVTE--LPEGFKVIAST--ENCpIAAIANEERKFYGVQFHPE 171
PRK13566 PRK13566
anthranilate synthase component I;
225-355 6.86e-11

anthranilate synthase component I;


Pssm-ID: 237429 [Multi-domain]  Cd Length: 720  Bit Score: 63.78  E-value: 6.86e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019 225 AADVLA-LNPDGIFLSNGPGDPApcDYAIEA-IEKFLETDIPVFGICLGHQLLALASGARTIKMKFGHHGGNHPVKDIDN 302
Cdd:PRK13566  561 AEEMLDrVNPDLVVLSPGPGRPS--DFDCKAtIDAALARNLPIFGVCLGLQAIVEAFGGELGQLAYPMHGKPSRIRVRGP 638

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019 303 NVVM------ITA-QNHGFAVDEATLPANLRVTHKSLfDGTLQGIHRTDKPAFSFQGHPE 355
Cdd:PRK13566  639 GRLFsglpeeFTVgRYHSLFADPETLPDELLVTAETE-DGVIMAIEHKTLPVAAVQFHPE 697
PuuD COG2071
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ...
 191-372 2.46e-10

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: 60.18  E-value: 2.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019 191 PFHVVAydfgakRNILRMLVDRGCR---LTVVPAKTSAADVLA-LnpDGIFLSNGP--------GDPAPCDYA------- 251
Cdd:COG2071    12 PAHYLP------EDYVRAVRAAGGLpvlLPPVGDEEDLDELLDrL--DGLVLTGGAdvdpalygEEPHPELGPidperda 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019 252 --IEAIEKFLETDIPVFGICLGHQLLALASG------ARTIKMKFGHH----GGNHPVKDIDnnvvmITAQ--------- 310
Cdd:COG2071    84 feLALIRAALERGKPVLGICRGMQLLNVALGgtlyqdLPDQVPGALDHrqpaPRYAPRHTVE-----IEPGsrlarilge 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2090925019 311 -----N--HGFAVDEatLPANLRVTHKSLfDGTLQGIHRTDKP-AFSFQGHPEASPGPHDA-APLFDHFIE 372
Cdd:COG2071   159 eeirvNslHHQAVKR--LGPGLRVSARAP-DGVIEAIESPGAPfVLGVQWHPEWLAASDPLsRRLFEAFVE 226
PRK05637 PRK05637
anthranilate synthase component II; Provisional
 209-360 3.94e-09

anthranilate synthase component II; Provisional


Pssm-ID: 180178 [Multi-domain]  Cd Length: 208  Bit Score: 56.01  E-value: 3.94e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019 209 LVDR----GCRLTVVPAKTSAADVLALNPDGIFLSNGPGDPAPCDYAIEAIEKFLETdIPVFGICLGHQLLALASGAR-- 282
Cdd:PRK05637   17 LVDAfavaGYKCTVFRNTVPVEEILAANPDLICLSPGPGHPRDAGNMMALIDRTLGQ-IPLLGICLGFQALLEHHGGKve 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019 283 --------TIKMKFGHHGGNHPV------------KDIDNNVVMItAQNHGFAVDEAtlPANLRV--THKSLFDGTLQGI 340
Cdd:PRK05637   96 pcgpvhgtTDNMILTDAGVQSPVfaglatdvepdhPEIPGRKVPI-ARYHSLGCVVA--PDGMESlgTCSSEIGPVIMAA 172

                         170       180
                  ....*....|....*....|...
gi 2090925019 341 HRTDKPAFSFQGHPEA--SP-GP 360
Cdd:PRK05637  173 ETTDGKAIGLQFHPESvlSPtGP 195
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 239-355 2.40e-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: 2.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019 239 SNGPGDPAPCDYAIEAIEKFLETDIPVFGICLGHQLLALASGART---IKMKFGHHGG-NHPVKDIDN-----NVV---- 305
Cdd:pfam07722  82 SGGPYDPARDAYELALIRAALARGKPILGICRGFQLLNVALGGTLyqdIQEQPGFTDHrEHCQVAPYApshavNVEpgsl 161

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2090925019 306 -------MITAQN--HGFAVDEatLPANLRVTHKSLfDGTLQGIHRTDKPAFSF--QGHPE 355
Cdd:pfam07722 162 lasllgsEEFRVNslHHQAIDR--LAPGLRVEAVAP-DGTIEAIESPNAKGFALgvQWHPE 219
PLN02347 PLN02347
GMP synthetase
 183-361 1.94e-07

GMP synthetase


Pssm-ID: 215197 [Multi-domain]  Cd Length: 536  Bit Score: 52.76  E-value: 1.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019 183 EAKAESELPFHVVAYDFGAKRN--ILRMLVDRGCRLTVVPAKTSAADVLALNPDGIFLSNGP------GDPAPCDYAIEA 254
Cdd:PLN02347    2 ESEAAKSYLDVVLILDYGSQYThlITRRVRELGVYSLLLSGTASLDRIASLNPRVVILSGGPhsvhveGAPTVPEGFFDY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019 255 IEkflETDIPVFGICLGHQLLALASGARtikMKFGHHG--GNHPVKDIDNNVVM-----ITAQN----HGfavDEAT-LP 322
Cdd:PLN02347   82 CR---ERGVPVLGICYGMQLIVQKLGGE---VKPGEKQeyGRMEIRVVCGSQLFgdlpsGETQTvwmsHG---DEAVkLP 152

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2090925019 323 ANLRVTHKSLfDGTLQGIHRTDKPAFSFQGHPEASPGPH 361
Cdd:PLN02347  153 EGFEVVAKSV-QGAVVAIENRERRIYGLQYHPEVTHSPK 190
PLN02889 PLN02889
oxo-acid-lyase/anthranilate synthase
 234-337 1.21e-06

oxo-acid-lyase/anthranilate synthase


Pssm-ID: 215481 [Multi-domain]  Cd Length: 918  Bit Score: 50.62  E-value: 1.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019 234 DGIFLSNGPGDPA-PCDYAIeAIEKFLET-DIPVFGICLGHQLLALASGARTIKMKFGHHG--------GNHPVKDIDN- 302
Cdd:PLN02889  133 DNIVISPGPGSPTcPADIGI-CLRLLLECrDIPILGVCLGHQALGYVHGARIVHAPEPVHGrlseiehnGCRLFDDIPSg 211

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2090925019 303 -NVVMITAQNHGFAVDEATLPANLRVTHKSLFDGTL 337
Cdd:PLN02889  212 rNSGFKVVRYHSLVIDAESLPKELVPIAWTSSSDTL 247
PRK06895 PRK06895
anthranilate synthase component II;
236-356 3.12e-05

anthranilate synthase component II;


Pssm-ID: 235882 [Multi-domain]  Cd Length: 190  Bit Score: 44.34  E-value: 3.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019 236 IFLSNGPGDPAPCDYAIEAIEKFLETDiPVFGICLGHQLLALASGARTIKMKFGHHGGNHPVKDIDNNVVMitaQN---- 311
Cdd:PRK06895   47 ILISPGPDVPRAYPQLFAMLERYHQHK-SILGVCLGHQTLCEFFGGELYNLNNVRHGQQRPLKVRSNSPLF---DGlpee 122

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2090925019 312 ------HGFAVDEATLPANLRVTHKSLFDGTLQGIHRTdKPAFSFQGHPEA 356
Cdd:PRK06895  123 fniglyHSWAVSEENFPTPLEITAVCDENVVMAMQHKT-LPIYGVQFHPES 172
GATase1_Glutamyl_Hydrolase cd01747
Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase; Type 1 ...
 235-358 3.09e-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: 3.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019 235 GIFLSNGPGDPAPCDYAiEAIEKF----LETDI-----PVFGICLGHQLLA-LASGARTIKMKFGHHGGNHPV------- 297
Cdd:cd01747    57 GILFPGGAVDIDTSGYA-RTAKIIynlaLERNDagdyfPVWGTCLGFELLTyLTSGETLLLEATEATNSALPLnftedal 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019 298 -----KDIDNNVVM------ITAQNHGFAVDEATLPAN--LRVTHKSL----------FDGTLQGIhrtDKPAFSFQGHP 354
Cdd:cd01747   136 qsrlfKRFPPDLLKslatepLTMNNHRYGISPENFTENglLSDFFNVLttnddwngveFISTVEAY---KYPIYGVQWHP 212


                  ....
gi 2090925019 355 EASP 358
Cdd:cd01747   213 EKNA 216
PRK09522 PRK09522
bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate ...
 219-356 3.83e-04

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


Pssm-ID: 181927 [Multi-domain]  Cd Length: 531  Bit Score: 42.32  E-value: 3.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019 219 VPAKTSAADVLALNPDGIFLSNGPGDPAPCDYAIEAIEKfLETDIPVFGICLGHQLLALASG-----ARTI---KMKFGH 290
Cdd:PRK09522   35 IPAQTLIERLATMSNPVLMLSPGPGVPSEAGCMPELLTR-LRGKLPIIGICLGHQAIVEAYGgyvgqAGEIlhgKASSIE 113

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2090925019 291 HGGNHPVKDIDNNvvMITAQNHGFAvdEATLPANLRVThkSLFDGTLQGI-HRTDKpAFSFQGHPEA 356
Cdd:PRK09522  114 HDGQAMFAGLTNP--LPVARYHSLV--GSNIPAGLTIN--AHFNGMVMAVrHDADR-VCGFQFHPES 173
GATase1_IGP_Synthase cd01748
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ...
 252-276 4.71e-04

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: 40.94  E-value: 4.71e-04
                          10        20
                  ....*....|....*....|....*
gi 2090925019 252 IEAIEKFLETDIPVFGICLGHQLLA 276
Cdd:cd01748    61 IEALKEAIASGKPFLGICLGMQLLF 85
HisH COG0118
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ...
 252-276 4.95e-04

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: 40.79  E-value: 4.95e-04
                          10        20
                  ....*....|....*....|....*
gi 2090925019 252 IEAIEKFLETDIPVFGICLGHQLLA 276
Cdd:COG0118    63 DEAIREAVAGGKPVLGICLGMQLLF 87
PRK07053 PRK07053
glutamine amidotransferase; Provisional
 252-282 4.97e-04

glutamine amidotransferase; Provisional


Pssm-ID: 235919 [Multi-domain]  Cd Length: 234  Bit Score: 41.08  E-value: 4.97e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2090925019 252 IEAIEKFLETDIPVFGICLGHQLLALASGAR 282
Cdd:PRK07053   73 IALLRQRLAAGLPTLGICLGAQLIARALGAR 103
PRK05665 PRK05665
amidotransferase; Provisional
 255-355 1.75e-03

amidotransferase; Provisional


Pssm-ID: 168162 [Multi-domain]  Cd Length: 240  Bit Score: 39.41  E-value: 1.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019 255 IEKFLETDIPVFGICLGHQLLALASGARTIKMKFGHHGGNHPVK----------DIDNNVVMITAQnhgfavDEAT-LPA 323
Cdd:PRK05665   84 LLKLYERGDKLLGVCFGHQLLALLLGGKAERASQGWGVGIHRYQlaahapwmspAVTELTLLISHQ------DQVTaLPE 157

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2090925019 324 NLRVTHKSLFdgTLQGIHRTDKPAFSFQGHPE 355
Cdd:PRK05665  158 GATVIASSDF--CPFAAYHIGDQVLCFQGHPE 187
hisH PRK13181
imidazole glycerol phosphate synthase subunit HisH; Provisional
 252-279 3.17e-03

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 183878 [Multi-domain]  Cd Length: 199  Bit Score: 38.31  E-value: 3.17e-03
                          10        20
                  ....*....|....*....|....*...
gi 2090925019 252 IEAIEKFLETDIPVFGICLGHQLLALAS 279
Cdd:PRK13181   62 DEALKEHVEKKQPVLGICLGMQLLFESS 89
PRK09065 PRK09065
glutamine amidotransferase; Provisional
 260-280 5.06e-03

glutamine amidotransferase; Provisional


Pssm-ID: 181635 [Multi-domain]  Cd Length: 237  Bit Score: 38.02  E-value: 5.06e-03
                          10        20
                  ....*....|....*....|.
gi 2090925019 260 ETDIPVFGICLGHQLLALASG 280
Cdd:PRK09065   86 AAGMPLLGICYGHQLLAHALG 106
hisH PRK13146
imidazole glycerol phosphate synthase subunit HisH; Provisional
 194-276 6.45e-03

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237290 [Multi-domain]  Cd Length: 209  Bit Score: 37.45  E-value: 6.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019 194 VVAYDFGAKRNILRML--VDRGCRLTVvpakTSAADVlALNPDGIFLsngPGDPA--PCDYAIEA-------IEKFLETD 262
Cdd:PRK13146    6 IIDYGSGNLRSAAKALerAGAGADVVV----TADPDA-VAAADRVVL---PGVGAfaDCMRGLRAvglgeavIEAVLAAG 77

                          90
                  ....*....|....
gi 2090925019 263 IPVFGICLGHQLLA 276
Cdd:PRK13146   78 RPFLGICVGMQLLF 91
hisH PRK13143
imidazole glycerol phosphate synthase subunit HisH; Provisional
 194-275 6.61e-03

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237289 [Multi-domain]  Cd Length: 200  Bit Score: 37.54  E-value: 6.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925019 194 VVAYDFGAKRNILRMLVDRGCRLTVV--PAKTSAADVLALNPDGIFlsngpgdPAPCDYAI---EAIEKFLETDIPVFGI 268
Cdd:PRK13143    5 IIDYGVGNLRSVSKALERAGAEVVITsdPEEILDADGIVLPGVGAF-------GAAMENLSplrDVILEAARSGKPFLGI 77


                  ....*..
gi 2090925019 269 CLGHQLL 275
Cdd:PRK13143   78 CLGMQLL 84
DJ-1_PfpI pfam01965
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ...
 219-286 8.89e-03

DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in transcriptional regulators.


Pssm-ID: 396514 [Multi-domain]  Cd Length: 165  Bit Score: 36.85  E-value: 8.89e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2090925019 219 VPAKTSAADVLALNPDGIFLSNG---PGDPAPCDYAIEAIEKFLETDIPVFGICLGHQLLALASGARTIKM 286
Cdd:pfam01965  48 VTVDASLDDVKPDDYDALVLPGGragPERLRDNEKLVEFVKDFYEKGKPVAAICHGPQVLAAAGVLKGRKV 118
hisH PRK13141
imidazole glycerol phosphate synthase subunit HisH; Provisional
 252-275 9.91e-03

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237288 [Multi-domain]  Cd Length: 205  Bit Score: 37.03  E-value: 9.91e-03
                          10        20
                  ....*....|....*....|....
gi 2090925019 252 IEAIEKFLETDIPVFGICLGHQLL 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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