NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1180570996|ref|WP_084057965|]
View 

glutamine-hydrolyzing carbamoyl-phosphate synthase small subunit [Desulfacinum hydrothermale]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 7-376 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: 697.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996   7 RPRALLVLEDGTVFKGYAFASAeqGRALGEVVFNTAMTGYQEVLTDPSYKGQIVTMTYPLTGNYGINDEDMESAAIQVEA 86
Cdd:COG0505     2 MMKALLVLEDGTVFEGKSFGAE--GETVGEVVFNTGMTGYQEILTDPSYAGQIVTFTYPHIGNYGVNDEDFESDRPWVAG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996  87 FIIKEYQDFPSNWRSRKSLAQFLEEHRVLGIEGIDTRRLTRHIRLAGALRGVIATDTDDVGALLDQVRDFPGLKGVDMVR 166
Cdd:COG0505    80 LVVRELSRRPSNWRSEESLDEYLKEHGIPGISGIDTRALTRHLREKGAMKGVISTGDLDIEELLEKARAAPGMEGLDLVK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 167 RVTCSRPYRWEKGPqpdaawredKPDFRVAALDFGVKYNILRNLERCGCQVLVFPATASPEEILATQPDGIFLSNGPGDP 246
Cdd:COG0505   160 EVSTKEPYEWTEAP---------GAGFHVVALDFGVKRNILRELAERGCRVTVVPATTSAEEILALNPDGVFLSNGPGDP 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 247 AAVTYGIETVRKLLGT-KPMFGICLGHQLMGLALGGRTFKLKFGHRGANQPVKDLSTGRVEVTSQNHGFCVDLESMQDIP 325
Cdd:COG0505   231 AALDYAIETIRELLGKgIPIFGICLGHQLLALALGAKTYKLKFGHRGANHPVKDLETGRVEITSQNHGFAVDEDSLPATD 310

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1180570996 326 VRLTHINLNDNTLEGMEHLEMPAFSVQYHPEAAPGPHDATYLFERFVNLIR 376
Cdd:COG0505   311 LEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDRFIELME 361
 
Name Accession Description Interval E-value
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 7-376 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: 697.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996   7 RPRALLVLEDGTVFKGYAFASAeqGRALGEVVFNTAMTGYQEVLTDPSYKGQIVTMTYPLTGNYGINDEDMESAAIQVEA 86
Cdd:COG0505     2 MMKALLVLEDGTVFEGKSFGAE--GETVGEVVFNTGMTGYQEILTDPSYAGQIVTFTYPHIGNYGVNDEDFESDRPWVAG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996  87 FIIKEYQDFPSNWRSRKSLAQFLEEHRVLGIEGIDTRRLTRHIRLAGALRGVIATDTDDVGALLDQVRDFPGLKGVDMVR 166
Cdd:COG0505    80 LVVRELSRRPSNWRSEESLDEYLKEHGIPGISGIDTRALTRHLREKGAMKGVISTGDLDIEELLEKARAAPGMEGLDLVK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 167 RVTCSRPYRWEKGPqpdaawredKPDFRVAALDFGVKYNILRNLERCGCQVLVFPATASPEEILATQPDGIFLSNGPGDP 246
Cdd:COG0505   160 EVSTKEPYEWTEAP---------GAGFHVVALDFGVKRNILRELAERGCRVTVVPATTSAEEILALNPDGVFLSNGPGDP 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 247 AAVTYGIETVRKLLGT-KPMFGICLGHQLMGLALGGRTFKLKFGHRGANQPVKDLSTGRVEVTSQNHGFCVDLESMQDIP 325
Cdd:COG0505   231 AALDYAIETIRELLGKgIPIFGICLGHQLLALALGAKTYKLKFGHRGANHPVKDLETGRVEITSQNHGFAVDEDSLPATD 310

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1180570996 326 VRLTHINLNDNTLEGMEHLEMPAFSVQYHPEAAPGPHDATYLFERFVNLIR 376
Cdd:COG0505   311 LEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDRFIELME 361
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
7-375 0e+00

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 670.63  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996   7 RPRALLVLEDGTVFKGYAFASaeQGRALGEVVFNTAMTGYQEVLTDPSYKGQIVTMTYPLTGNYGINDEDMESAAIQVEA 86
Cdd:PRK12564    2 MMKAYLVLEDGTVFEGKAFGA--EGETVGEVVFNTSMTGYQEILTDPSYAGQIVTFTYPLIGNYGVNREDFESDRPHAKG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996  87 FIIKEYQDFPSNWRSRKSLAQFLEEHRVLGIEGIDTRRLTRHIRLAGALRGVIATDTDDVGALLDQVRDFPGLKGVDMVR 166
Cdd:PRK12564   80 LIVRELSDIPSNWRSEMSLDEYLKENGIPGISGIDTRALTRKLREKGAMKGVIATEDFDAEELLEKARAFPGLLGLDLVK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 167 RVTCSRPYRWEKGPqpdaawreDKPDFRVAALDFGVKYNILRNLERCGCQVLVFPATASPEEILATQPDGIFLSNGPGDP 246
Cdd:PRK12564  160 EVSTKEPYPWPGPG--------GELKYKVVAIDFGVKRNILRELAERGCRVTVVPATTTAEEILALNPDGVFLSNGPGDP 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 247 AAVTYGIETVRKLLGT-KPMFGICLGHQLMGLALGGRTFKLKFGHRGANQPVKDLSTGRVEVTSQNHGFCVDLESMQDiP 325
Cdd:PRK12564  232 AALDYAIEMIRELLEKkIPIFGICLGHQLLALALGAKTYKMKFGHRGANHPVKDLETGKVEITSQNHGFAVDEDSLPA-N 310

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1180570996 326 VRLTHINLNDNTLEGMEHLEMPAFSVQYHPEAAPGPHDATYLFERFVNLI 375
Cdd:PRK12564  311 LEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDEFVELM 360
CPSaseIIsmall TIGR01368
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ...
 10-377 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: 581.89  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996  10 ALLVLEDGTVFKGYAFASaeQGRALGEVVFNTAMTGYQEVLTDPSYKGQIVTMTYPLTGNYGINDEDMESAAIQVEAFII 89
Cdd:TIGR01368   1 AYLVLEDGTVFRGYSFGA--EGTVAGEVVFNTGMTGYQEILTDPSYKGQIVVFTYPLIGNYGVNDEDAESKGIHVSGLVV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996  90 KEYQDFPSNWRSRKSLAQFLEEHRVLGIEGIDTRRLTRHIRLAGALRGVIATDTDDVGALLDQVRDFPGLKGVDMVRRVT 169
Cdd:TIGR01368  79 RELSDRYSNWRATESLDQFLKRHGIPGIYGVDTRALVKKIREKGTMKGVISTEDSNDEELVEKARVSPDITGINLVAEVS 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 170 CSRPYRWekgpqpdaaWREDKPDFRVAALDFGVKYNILRNLERCGCQVLVFPATASPEEILATQPDGIFLSNGPGDPAAV 249
Cdd:TIGR01368 159 TKEPYTW---------GQRGGKGKRVVVIDFGVKRNILRRLVKRGCEVTVVPYDTDAEEIKKYNPDGIFLSNGPGDPAAV 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 250 TYGIETVRKLLGTKPMFGICLGHQLMGLALGGRTFKLKFGHRGANQPVKDLSTGRVEVTSQNHGFCVDLESMQDIPVRLT 329
Cdd:TIGR01368 230 EPAIETIRKLLEKIPIFGICLGHQLLALAFGAKTYKMKFGHRGGNHPVKDLITGRVEITSQNHGYAVDPDSLPAGDLEVT 309

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1180570996 330 HINLNDNTLEGMEHLEMPAFSVQYHPEAAPGPHDATYLFERFVNLIRK 377
Cdd:TIGR01368 310 HVNLNDGTVEGIRHKDLPVFSVQYHPEASPGPHDTEYLFDEFIDLMKK 357
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 195-372 2.14e-117

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: 338.32  E-value: 2.14e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 195 VAALDFGVKYNILRNLERCGCQVLVFPATASPEEILATQPDGIFLSNGPGDPAAVTYGIETVRKLLGT-KPMFGICLGHQ 273
Cdd:cd01744     1 VVVIDFGVKHNILRELLKRGCEVTVVPYNTDAEEILKLDPDGIFLSNGPGDPALLDEAIKTVRKLLGKkIPIFGICLGHQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 274 LMGLALGGRTFKLKFGHRGANQPVKDLSTGRVEVTSQNHGFCVDLESMQDiPVRLTHINLNDNTLEGMEHLEMPAFSVQY 353
Cdd:cd01744    81 LLALALGAKTYKMKFGHRGSNHPVKDLITGRVYITSQNHGYAVDPDSLPG-GLEVTHVNLNDGTVEGIRHKDLPVFSVQF 159

                         170
                  ....*....|....*....
gi 1180570996 354 HPEAAPGPHDATYLFERFV 372
Cdd:cd01744   160 HPEASPGPHDTEYLFDEFL 178
CPSase_sm_chain pfam00988
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 12-139 5.62e-85

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: 253.79  E-value: 5.62e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996  12 LVLEDGTVFKGYAFASAeqGRALGEVVFNTAMTGYQEVLTDPSYKGQIVTMTYPLTGNYGINDEDMESAAIQVEAFIIKE 91
Cdd:pfam00988   1 LVLEDGTVFEGKSFGAA--GSTVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNPEDFESDKIHVAGLVVRE 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1180570996  92 YQDFPSNWRSRKSLAQFLEEHRVLGIEGIDTRRLTRHIRLAGALRGVI 139
Cdd:pfam00988  79 YSDEPSNWRAEESLDEWLKEQGIPGISGVDTRALTRKIREKGAMKGVI 126
CPSase_sm_chain smart01097
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 8-139 3.14e-84

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: 251.91  E-value: 3.14e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996    8 PRALLVLEDGTVFKGYAFASaeQGRALGEVVFNTAMTGYQEVLTDPSYKGQIVTMTYPLTGNYGINDEDMESAAIQVEAF 87
Cdd:smart01097   1 MKAYLVLEDGTVFEGESFGA--EGETVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNDEDFESDKIQVKGL 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1180570996   88 IIKEYQDFPSNWRSRKSLAQFLEEHRVLGIEGIDTRRLTRHIRLAGALRGVI 139
Cdd:smart01097  79 VVRELSDEPSNWRSEQSLDEFLKENGIPGISGIDTRALTRKLREKGAMKGVI 130
 
Name Accession Description Interval E-value
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 7-376 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: 697.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996   7 RPRALLVLEDGTVFKGYAFASAeqGRALGEVVFNTAMTGYQEVLTDPSYKGQIVTMTYPLTGNYGINDEDMESAAIQVEA 86
Cdd:COG0505     2 MMKALLVLEDGTVFEGKSFGAE--GETVGEVVFNTGMTGYQEILTDPSYAGQIVTFTYPHIGNYGVNDEDFESDRPWVAG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996  87 FIIKEYQDFPSNWRSRKSLAQFLEEHRVLGIEGIDTRRLTRHIRLAGALRGVIATDTDDVGALLDQVRDFPGLKGVDMVR 166
Cdd:COG0505    80 LVVRELSRRPSNWRSEESLDEYLKEHGIPGISGIDTRALTRHLREKGAMKGVISTGDLDIEELLEKARAAPGMEGLDLVK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 167 RVTCSRPYRWEKGPqpdaawredKPDFRVAALDFGVKYNILRNLERCGCQVLVFPATASPEEILATQPDGIFLSNGPGDP 246
Cdd:COG0505   160 EVSTKEPYEWTEAP---------GAGFHVVALDFGVKRNILRELAERGCRVTVVPATTSAEEILALNPDGVFLSNGPGDP 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 247 AAVTYGIETVRKLLGT-KPMFGICLGHQLMGLALGGRTFKLKFGHRGANQPVKDLSTGRVEVTSQNHGFCVDLESMQDIP 325
Cdd:COG0505   231 AALDYAIETIRELLGKgIPIFGICLGHQLLALALGAKTYKLKFGHRGANHPVKDLETGRVEITSQNHGFAVDEDSLPATD 310

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1180570996 326 VRLTHINLNDNTLEGMEHLEMPAFSVQYHPEAAPGPHDATYLFERFVNLIR 376
Cdd:COG0505   311 LEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDRFIELME 361
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
7-375 0e+00

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 670.63  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996   7 RPRALLVLEDGTVFKGYAFASaeQGRALGEVVFNTAMTGYQEVLTDPSYKGQIVTMTYPLTGNYGINDEDMESAAIQVEA 86
Cdd:PRK12564    2 MMKAYLVLEDGTVFEGKAFGA--EGETVGEVVFNTSMTGYQEILTDPSYAGQIVTFTYPLIGNYGVNREDFESDRPHAKG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996  87 FIIKEYQDFPSNWRSRKSLAQFLEEHRVLGIEGIDTRRLTRHIRLAGALRGVIATDTDDVGALLDQVRDFPGLKGVDMVR 166
Cdd:PRK12564   80 LIVRELSDIPSNWRSEMSLDEYLKENGIPGISGIDTRALTRKLREKGAMKGVIATEDFDAEELLEKARAFPGLLGLDLVK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 167 RVTCSRPYRWEKGPqpdaawreDKPDFRVAALDFGVKYNILRNLERCGCQVLVFPATASPEEILATQPDGIFLSNGPGDP 246
Cdd:PRK12564  160 EVSTKEPYPWPGPG--------GELKYKVVAIDFGVKRNILRELAERGCRVTVVPATTTAEEILALNPDGVFLSNGPGDP 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 247 AAVTYGIETVRKLLGT-KPMFGICLGHQLMGLALGGRTFKLKFGHRGANQPVKDLSTGRVEVTSQNHGFCVDLESMQDiP 325
Cdd:PRK12564  232 AALDYAIEMIRELLEKkIPIFGICLGHQLLALALGAKTYKMKFGHRGANHPVKDLETGKVEITSQNHGFAVDEDSLPA-N 310

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1180570996 326 VRLTHINLNDNTLEGMEHLEMPAFSVQYHPEAAPGPHDATYLFERFVNLI 375
Cdd:PRK12564  311 LEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDEFVELM 360
CPSaseIIsmall TIGR01368
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ...
 10-377 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: 581.89  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996  10 ALLVLEDGTVFKGYAFASaeQGRALGEVVFNTAMTGYQEVLTDPSYKGQIVTMTYPLTGNYGINDEDMESAAIQVEAFII 89
Cdd:TIGR01368   1 AYLVLEDGTVFRGYSFGA--EGTVAGEVVFNTGMTGYQEILTDPSYKGQIVVFTYPLIGNYGVNDEDAESKGIHVSGLVV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996  90 KEYQDFPSNWRSRKSLAQFLEEHRVLGIEGIDTRRLTRHIRLAGALRGVIATDTDDVGALLDQVRDFPGLKGVDMVRRVT 169
Cdd:TIGR01368  79 RELSDRYSNWRATESLDQFLKRHGIPGIYGVDTRALVKKIREKGTMKGVISTEDSNDEELVEKARVSPDITGINLVAEVS 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 170 CSRPYRWekgpqpdaaWREDKPDFRVAALDFGVKYNILRNLERCGCQVLVFPATASPEEILATQPDGIFLSNGPGDPAAV 249
Cdd:TIGR01368 159 TKEPYTW---------GQRGGKGKRVVVIDFGVKRNILRRLVKRGCEVTVVPYDTDAEEIKKYNPDGIFLSNGPGDPAAV 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 250 TYGIETVRKLLGTKPMFGICLGHQLMGLALGGRTFKLKFGHRGANQPVKDLSTGRVEVTSQNHGFCVDLESMQDIPVRLT 329
Cdd:TIGR01368 230 EPAIETIRKLLEKIPIFGICLGHQLLALAFGAKTYKMKFGHRGGNHPVKDLITGRVEITSQNHGYAVDPDSLPAGDLEVT 309

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1180570996 330 HINLNDNTLEGMEHLEMPAFSVQYHPEAAPGPHDATYLFERFVNLIRK 377
Cdd:TIGR01368 310 HVNLNDGTVEGIRHKDLPVFSVQYHPEASPGPHDTEYLFDEFIDLMKK 357
PRK12838 PRK12838
carbamoyl phosphate synthase small subunit; Reviewed
 10-379 1.00e-173

carbamoyl phosphate synthase small subunit; Reviewed


Pssm-ID: 183784 [Multi-domain]  Cd Length: 354  Bit Score: 487.86  E-value: 1.00e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996  10 ALLVLEDGTVFKGYAFASaeQGRALGEVVFNTAMTGYQEVLTDPSYKGQIVTMTYPLTGNYGINDEDMESAAIQVEAFII 89
Cdd:PRK12838    3 AYLILEDGTVFEGELIGA--PIDVTGEIVFNTGMTGYQEVLTDPSYKGQIVVFTYPLIGNYGINADDYESKQPQVKGVIV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996  90 KEYQDFPSNWRSRKSLAQFLEEHRVLGIEGIDTRRLTRHIRLAGALRGVIATDTDDVGAllDQVRDFPGLKGVdmVRRVT 169
Cdd:PRK12838   81 YELSREGSHYRAKQSLDDFLKEWNIPGISGVDTRALVKHIREKGTMKASITTTDDAHAF--DQIKALVLPKNV--VAQVS 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 170 CSRPYRWEKGpqpdaawredkpDFRVAALDFGVKYNILRNLERCGCQVLVFPATASPEEILATQPDGIFLSNGPGDPAAV 249
Cdd:PRK12838  157 TKEPYTYGNG------------GKHVALIDFGYKKSILRSLSKRGCKVTVLPYDTSLEEIKNLNPDGIVLSNGPGDPKEL 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 250 TYGIETVRKLLGTKPMFGICLGHQLMGLALGGRTFKLKFGHRGANQPVKDLSTGRVEVTSQNHGFCVDLESMQDIPVRLT 329
Cdd:PRK12838  225 QPYLPEIKKLISSYPILGICLGHQLIALALGADTEKLPFGHRGANHPVIDLTTGRVWMTSQNHGYVVDEDSLDGTPLSVR 304

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1180570996 330 HINLNDNTLEGMEHLEMPAFSVQYHPEAAPGPHDATYLFERFVNLIRKDK 379
Cdd:PRK12838  305 FFNVNDGSIEGLRHKKKPVLSVQFHPEAHPGPHDAEYIFDEFLEMMEKAR 354
carA CHL00197
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
 6-379 2.26e-157

carbamoyl-phosphate synthase arginine-specific small subunit; Provisional


Pssm-ID: 214392 [Multi-domain]  Cd Length: 382  Bit Score: 447.71  E-value: 2.26e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996   6 KRPRALLVLEDGTVFKGYAFASAEQgrALGEVVFNTAMTGYQEVLTDPSYKGQIVTMTYPLTGNYGINDEDMESAAIQVE 85
Cdd:CHL00197    3 KMIPAILVLEDGTYYRGWSFSNPIT--TIGEVVFNTGMTGYQEIITDPSYFEQIVTFTYPEIGNTGINLEDIESVKIQVK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996  86 AFIIKEYQDFPSNWRSRKSLAQFLEEHRVLGIEGIDTRRLTRHIRLAGALRGVIATDTDDVGALLDQVRDFPGLKGVDMV 165
Cdd:CHL00197   81 GIIAKNICKSSSNWRQQESLVSYLQRHKIPFIFGIDTRALTQHLRRFGTMNGCISNQNLNLSYLRAKIKESPHMPSSDLI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 166 RRVTCSRPYRWEKGPQP--DAAWREDKP---DFRVAALDFGVKYNILRNLERCGCQVLVFPATASPEEILATQPDGIFLS 240
Cdd:CHL00197  161 PRVTTSSYYEWDEKSHPsfYLADNKRPHssyQLKIIVIDFGVKYNILRRLKSFGCSITVVPATSPYQDILSYQPDGILLS 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 241 NGPGDPAAVTYGIETVRKLLGTK-PMFGICLGHQLMGLALGGRTFKLKFGHRGANQPvkdlsTG---RVEVTSQNHGFCV 316
Cdd:CHL00197  241 NGPGDPSAIHYGIKTVKKLLKYNiPIFGICMGHQILSLALEAKTFKLKFGHRGLNHP-----SGlnqQVEITSQNHGFAV 315

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1180570996 317 DLESMQDIPVRLTHINLNDNTLEGMEHLEMPAFSVQYHPEAAPGPHDATYLFERFVNLIRKDK 379
Cdd:CHL00197  316 NLESLAKNKFYITHFNLNDGTVAGISHSPKPYFSVQYHPEASPGPHDADYLFEYFIEIIKHSK 378
PLN02771 PLN02771
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
 4-368 1.42e-133

carbamoyl-phosphate synthase (glutamine-hydrolyzing)


Pssm-ID: 178370 [Multi-domain]  Cd Length: 415  Bit Score: 388.57  E-value: 1.42e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996   4 PWKRPRALLVLEDGTVFKGYAFASaeQGRALGEVVFNTAMTGYQEVLTDPSYKGQIVTMTYPLTGNYGINDEDMESAAIQ 83
Cdd:PLN02771   51 PWKTSDARLVLEDGSVWKAKSFGA--RGTQVGEVVFNTSLTGYQEILTDPSYAGQFVLMTNPHIGNTGVNFDDEESRQCF 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996  84 VEAFIIKEYQDFPSNWRSRKSLAQFLEEHRVLGIEGIDTRRLTRHIRLAGALRGVIATD---TDDvgALLDQVRDFpGLK 160
Cdd:PLN02771  129 LAGLVIRSLSISTSNWRCTKTLGDYLAERNIMGIYDVDTRAITRRLREDGSLIGVLSTEdskTDE--ELLKMSRSW-DIV 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 161 GVDMVRRVTCSRPYRWEKgpQPDAAWR-----EDKPDFRVAALDFGVKYNILRNLERCGCQVLVFPATASPEEILATQPD 235
Cdd:PLN02771  206 GIDLISGVSCKSPYEWVD--KTNPEWDfntnsRDGESYHVIAYDFGIKHNILRRLASYGCKITVVPSTWPASEALKMKPD 283

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 236 GIFLSNGPGDPAAVTYGIETVRKLLGTKPMFGICLGHQLMGLALGGRTFKLKFGHRGANQPVKDLSTGRVEVTSQNHGFC 315
Cdd:PLN02771  284 GVLFSNGPGDPSAVPYAVETVKELLGKVPVFGICMGHQLLGQALGGKTFKMKFGHHGGNHPVRNNRTGRVEISAQNHNYA 363

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1180570996 316 VDLESMQDiPVRLTHINLNDNTLEGMEHLEMPAFSVQYHPEAAPGPHDATYLF 368
Cdd:PLN02771  364 VDPASLPE-GVEVTHVNLNDGSCAGLAFPALNVMSLQYHPEASPGPHDSDNAF 415
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 195-372 2.14e-117

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: 338.32  E-value: 2.14e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 195 VAALDFGVKYNILRNLERCGCQVLVFPATASPEEILATQPDGIFLSNGPGDPAAVTYGIETVRKLLGT-KPMFGICLGHQ 273
Cdd:cd01744     1 VVVIDFGVKHNILRELLKRGCEVTVVPYNTDAEEILKLDPDGIFLSNGPGDPALLDEAIKTVRKLLGKkIPIFGICLGHQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 274 LMGLALGGRTFKLKFGHRGANQPVKDLSTGRVEVTSQNHGFCVDLESMQDiPVRLTHINLNDNTLEGMEHLEMPAFSVQY 353
Cdd:cd01744    81 LLALALGAKTYKMKFGHRGSNHPVKDLITGRVYITSQNHGYAVDPDSLPG-GLEVTHVNLNDGTVEGIRHKDLPVFSVQF 159

                         170
                  ....*....|....*....
gi 1180570996 354 HPEAAPGPHDATYLFERFV 372
Cdd:cd01744   160 HPEASPGPHDTEYLFDEFL 178
CPSase_sm_chain pfam00988
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 12-139 5.62e-85

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: 253.79  E-value: 5.62e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996  12 LVLEDGTVFKGYAFASAeqGRALGEVVFNTAMTGYQEVLTDPSYKGQIVTMTYPLTGNYGINDEDMESAAIQVEAFIIKE 91
Cdd:pfam00988   1 LVLEDGTVFEGKSFGAA--GSTVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNPEDFESDKIHVAGLVVRE 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1180570996  92 YQDFPSNWRSRKSLAQFLEEHRVLGIEGIDTRRLTRHIRLAGALRGVI 139
Cdd:pfam00988  79 YSDEPSNWRAEESLDEWLKEQGIPGISGVDTRALTRKIREKGAMKGVI 126
CPSase_sm_chain smart01097
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 8-139 3.14e-84

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: 251.91  E-value: 3.14e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996    8 PRALLVLEDGTVFKGYAFASaeQGRALGEVVFNTAMTGYQEVLTDPSYKGQIVTMTYPLTGNYGINDEDMESAAIQVEAF 87
Cdd:smart01097   1 MKAYLVLEDGTVFEGESFGA--EGETVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNDEDFESDKIQVKGL 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1180570996   88 IIKEYQDFPSNWRSRKSLAQFLEEHRVLGIEGIDTRRLTRHIRLAGALRGVI 139
Cdd:smart01097  79 VVRELSDEPSNWRSEQSLDEFLKENGIPGISGIDTRALTRKLREKGAMKGVI 130
GATase pfam00117
Glutamine amidotransferase class-I;
196-374 5.30e-63

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 199.77  E-value: 5.30e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 196 AALDFG--VKYNILRNLERCGCQVLVFPATASPEEILATQPDGIFLSNGPGDPAAVTYGIETVRKLLGTK-PMFGICLGH 272
Cdd:pfam00117   1 LLIDNGdsFTYNLARALRELGVEVTVVPNDTPAEEILEENPDGIILSGGPGSPGAAGGAIEAIREARELKiPILGICLGH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 273 QLMGLALGGRTFKLK-FGHRGANQPVKDLS------TGRVEVTSQNHGFCVDLESMQDiPVRLTHINLNDNTLEGMEHLE 345
Cdd:pfam00117  81 QLLALAFGGKVVKAKkFGHHGKNSPVGDDGcglfygLPNVFIVRRYHSYAVDPDTLPD-GLEVTATSENDGTIMGIRHKK 159

                         170       180
                  ....*....|....*....|....*....
gi 1180570996 346 MPAFSVQYHPEAAPGPHDATYLFERFVNL 374
Cdd:pfam00117 160 LPIFGVQFHPESILTPHGPEILFNFFIKA 188
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 204-372 3.36e-26

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: 103.38  E-value: 3.36e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 204 YNILRNLERCGCQVLVFPATASPEEILAT-QPDGIFLSNGPGDPAAVTYGIETVRKLLGTKPMFGICLGHQLMGLALGGR 282
Cdd:cd01743    12 YNLVQYLRELGAEVVVVRNDEITLEELELlNPDAIVISPGPGHPEDAGISLEIIRALAGKVPILGVCLGHQAIAEAFGGK 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 283 TFKLKFGHRGANQPVKDLSTGRVEVTSQN------HGFCVDLESmqdIPVRL-THINLNDNTLEGMEHLEMPAFSVQYHP 355
Cdd:cd01743    92 VVRAPEPMHGKTSEIHHDGSGLFKGLPQPftvgryHSLVVDPDP---LPDLLeVTASTEDGVIMALRHRDLPIYGVQFHP 168

                         170
                  ....*....|....*..
gi 1180570996 356 EAAPGPHDATyLFERFV 372
Cdd:cd01743   169 ESILTEYGLR-LLENFL 184
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 204-356 6.76e-23

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: 94.72  E-value: 6.76e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 204 YNILRNLERCGCQVLVFPATA-SPEEILATQPDGIFLSNGPGDPAavTYGI--ETVRKLLGTKPMFGICLGHQLMGLALG 280
Cdd:COG0512    12 YNLVQYLGELGAEVVVVRNDEiTLEEIEALAPDGIVLSPGPGTPE--EAGIslEVIRAFAGKIPILGVCLGHQAIGEAFG 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 281 GRTFKlkfghrgANQPV--KdlsTGRVEVTSQN--------------HGFCVDLESMQDipvrlthiNL------NDNTL 338
Cdd:COG0512    90 GKVVR-------APEPMhgK---TSPITHDGSGlfaglpnpftatryHSLVVDRETLPD--------ELevtawtEDGEI 151

                         170
                  ....*....|....*...
gi 1180570996 339 EGMEHLEMPAFSVQYHPE 356
Cdd:COG0512   152 MGIRHRELPIEGVQFHPE 169
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 204-376 8.69e-20

anthranilate synthase component II; Provisional


Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 85.95  E-value: 8.69e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 204 YNILRNLERCGCQVLVFP-ATASPEEILATQPDGIFLSNGPGDPAAVtyGI--ETVRKLLGTKPMFGICLGHQLMGLALG 280
Cdd:PRK05670   13 YNLVQYLGELGAEVVVYRnDEITLEEIEALNPDAIVLSPGPGTPAEA--GIslELIREFAGKVPILGVCLGHQAIGEAFG 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 281 GRTfklkfghRGANQPVKdlstGRV-EVTSQNHG-FcvdlesmQDIPVRLT----H--------------IN--LNDNTL 338
Cdd:PRK05670   91 GKV-------VRAKEIMH----GKTsPIEHDGSGiF-------AGLPNPFTvtryHslvvdreslpdcleVTawTDDGEI 152

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1180570996 339 EGMEHLEMPAFSVQYHPEAAPGPHDATyLFERFVNLIR 376
Cdd:PRK05670  153 MGVRHKELPIYGVQFHPESILTEHGHK-LLENFLELAR 189
GATase1_GMP_Synthase cd01742
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ...
 195-372 4.74e-19

Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase. GMP synthetase is a glutamine amidotransferase from the de novo purine biosynthetic pathway. Glutamine amidotransferase (GATase) activity catalyse the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. GMP synthetase catalyses the amination of the nucleotide precursor xanthosine 5'-monophosphate to form GMP. GMP synthetase belongs to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.


Pssm-ID: 153213 [Multi-domain]  Cd Length: 181  Bit Score: 83.74  E-value: 4.74e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 195 VAALDFGVKYN--ILRNLERCGCQVLVFPATASPEEILATQPDGIFLSNGPG----------DPAAVTYGIetvrkllgt 262
Cdd:cd01742     1 ILILDFGSQYThlIARRVRELGVYSEILPNTTPLEEIKLKNPKGIILSGGPSsvyeedaprvDPEIFELGV--------- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 263 kPMFGICLGHQLMGLALGGRTfklkfgHRGANQpvkdlSTGRVEVTSQNHgfCVDLESMQD-IPVRLTH----INLNDN- 336
Cdd:cd01742    72 -PVLGICYGMQLIAKALGGKV------ERGDKR-----EYGKAEIEIDDS--SPLFEGLPDeQTVWMSHgdevVKLPEGf 137

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1180570996 337 ---------TLEGMEHLEMPAFSVQYHPEAAPGPHdATYLFERFV 372
Cdd:cd01742   138 kviassdncPVAAIANEEKKIYGVQFHPEVTHTEK-GKEILKNFL 181
PRK14607 PRK14607
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
204-376 1.80e-16

bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;


Pssm-ID: 237764 [Multi-domain]  Cd Length: 534  Bit Score: 80.92  E-value: 1.80e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 204 YNILRNLERCG--CQVLVFPATASPEEILATQPDGIFLSNGPGDPAAVTYGIETVRKLLGTKPMFGICLGHQLMGLALGG 281
Cdd:PRK14607   13 YNIYQYIGELGpeEIEVVRNDEITIEEIEALNPSHIVISPGPGRPEEAGISVEVIRHFSGKVPILGVCLGHQAIGYAFGG 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 282 RTFKLKFGHRGANQPVKDLSTGRVEVTSQN------HGFCVDLESMQD---IPVRLThinlnDNTLEGMEHLEMPAFSVQ 352
Cdd:PRK14607   93 KIVHAKRILHGKTSPIDHNGKGLFRGIPNPtvatryHSLVVEEASLPEcleVTAKSD-----DGEIMGIRHKEHPIFGVQ 167

                         170       180
                  ....*....|....*....|....
gi 1180570996 353 YHPEAApGPHDATYLFERFVNLIR 376
Cdd:PRK14607  168 FHPESI-LTEEGKRILKNFLNYQR 190
guaA_Nterm TIGR00888
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ...
 198-375 7.02e-16

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: 75.04  E-value: 7.02e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 198 LDFGVKYN--ILRNLERCGCQVLVFPATASPEEILATQPDGIFLSNGP------GDPAAVTYGIEtvrklLGtKPMFGIC 269
Cdd:TIGR00888   4 LDFGSQYTqlIARRLRELGVYSELVPNTTPLEEIREKNPKGIILSGGPssvyaeNAPRADEKIFE-----LG-VPVLGIC 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 270 LGHQLMGLALGG---RTFKLKFG------------HRGAN--QPV----KDlstgrvEVTSQNHGFCVDLESmqdipvrl 328
Cdd:TIGR00888  78 YGMQLMAKQLGGevgRAEKREYGkaeleildeddlFRGLPdeSTVwmshGD------KVKELPEGFKVLATS-------- 143

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1180570996 329 thinlnDNT-LEGMEHLEMPAFSVQYHPEAAPGPHDATyLFERFVNLI 375
Cdd:TIGR00888 144 ------DNCpVAAMAHEEKPIYGVQFHPEVTHTEYGNE-LLENFVYDV 184
trpG_papA TIGR00566
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ...
 204-357 4.12e-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: 72.90  E-value: 4.12e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 204 YNILRNLERCGCQVLVFPATA-SPEEILATQPDGIFLSNGPGDPAAVTYGIETVRKLLGTKPMFGICLGHQLMGLALGGR 282
Cdd:TIGR00566  13 YNLVQYFCELGAEVVVKRNDSlTLQEIEALLPLLIVISPGPCTPNEAGISLEAIRHFAGKLPILGVCLGHQAMGQAFGGD 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 283 TFKLKFGHRGANQPVKDLSTGRVE------VTSQNHGFCVDLESMQDIpVRLTHINLNDNTLEGMEHLEMPAFSVQYHPE 356
Cdd:TIGR00566  93 VVRANTVMHGKTSEIEHNGAGIFRglfnplTATRYHSLVVEPETLPTC-FPVTAWEEENIEIMAIRHRDLPLEGVQFHPE 171


                  .
gi 1180570996 357 A 357
Cdd:TIGR00566 172 S 172
PRK00758 PRK00758
GMP synthase subunit A; Validated
 194-372 1.08e-14

GMP synthase subunit A; Validated


Pssm-ID: 179112 [Multi-domain]  Cd Length: 184  Bit Score: 71.81  E-value: 1.08e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 194 RVAALDFGVKYN--ILRNLERCGCQVLVFPATASPEEILAtQPDGIFLSNGPgDPAAVTYGIETVRKLlgTKPMFGICLG 271
Cdd:PRK00758    1 KIVVVDNGGQYNhlIHRTLRYLGVDAKIIPNTTPVEEIKA-FEDGLILSGGP-DIERAGNCPEYLKEL--DVPILGICLG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 272 HQLMGLALGGRTFKLKFGHRGAnqpVKdlstgrVEVTSQNhgfcvDL-----------ESMQD----IPVRLTHINLNDN 336
Cdd:PRK00758   77 HQLIAKAFGGEVGRGEYGEYAL---VE------VEILDED-----DIlkglppeirvwASHADevkeLPDGFEILARSDI 142

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1180570996 337 T-LEGMEHLEMPAFSVQYHPEAAPGPHdATYLFERFV 372
Cdd:PRK00758  143 CeVEAMKHKEKPIYGVQFHPEVAHTEY-GEEIFKNFL 178
PLN02335 PLN02335
anthranilate synthase
 204-357 3.32e-13

anthranilate synthase


Pssm-ID: 177969 [Multi-domain]  Cd Length: 222  Bit Score: 68.29  E-value: 3.32e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 204 YNILRNLERCGCQVLVFPATA-SPEEILATQPDGIFLSNGPGDPAAVTYGIETVRKLLGTKPMFGICLGHQLMGLALGGR 282
Cdd:PLN02335   32 YNLCQYMGELGCHFEVYRNDElTVEELKRKNPRGVLISPGPGTPQDSGISLQTVLELGPLVPLFGVCMGLQCIGEAFGGK 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 283 TFKLKFG--HrGANQPV---KDLSTGRVE------VTSQNHGFCVDLESMQDIPVRLTHINlNDNTLEGMEHLEMPAFS- 350
Cdd:PLN02335  112 IVRSPFGvmH-GKSSPVhydEKGEEGLFSglpnpfTAGRYHSLVIEKDTFPSDELEVTAWT-EDGLIMAARHRKYKHIQg 189


                  ....*..
gi 1180570996 351 VQYHPEA 357
Cdd:PLN02335  190 VQFHPES 196
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 194-359 7.62e-13

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: 67.28  E-value: 7.62e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 194 RVAALD---FGVKYN--ILRNLERCGCQVLVFPATAS---PEEILATQPDGIFLSNGPGDPAAVTYGIETVRKLLGT--- 262
Cdd:COG0518     1 KILILDhdpFGGQYPglIARRLREAGIELDVLRVYAGeilPYDPDLEDPDGLILSGGPMSVYDEDPWLEDEPALIREafe 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 263 --KPMFGICLGHQLMGLALGGRTFKlkfghrganQPVKDLSTGRVEVTSQN---------------HGFCVDlesmqDIP 325
Cdd:COG0518    81 lgKPVLGICYGAQLLAHALGGKVEP---------GPGREIGWAPVELTEADplfaglpdeftvwmsHGDTVT-----ELP 146

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1180570996 326 VRLTHINLNDNT-LEGMEHlEMPAFSVQYHPEAAP 359
Cdd:COG0518   147 EGAEVLASSDNCpNQAFRY-GRRVYGVQFHPEVTH 180
PRK05637 PRK05637
anthranilate synthase component II; Provisional
 204-361 1.56e-11

anthranilate synthase component II; Provisional


Pssm-ID: 180178 [Multi-domain]  Cd Length: 208  Bit Score: 63.32  E-value: 1.56e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 204 YNILRNLERCGCQVLVFPATASPEEILATQPDGIFLSNGPGDPAAVTYGIETVRKLLGTKPMFGICLGHQLMGLALGGR- 282
Cdd:PRK05637   15 YNLVDAFAVAGYKCTVFRNTVPVEEILAANPDLICLSPGPGHPRDAGNMMALIDRTLGQIPLLGICLGFQALLEHHGGKv 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 283 ---------TFKLKFGHRGANQPVKDLSTGRVEVTSQN-HGFCV---------------DLESMQDIPVRLTHINLNDNT 337
Cdd:PRK05637   95 epcgpvhgtTDNMILTDAGVQSPVFAGLATDVEPDHPEiPGRKVpiaryhslgcvvapdGMESLGTCSSEIGPVIMAAET 174

                         170       180
                  ....*....|....*....|....
gi 1180570996 338 LEGMehlempAFSVQYHPEAAPGP 361
Cdd:PRK05637  175 TDGK------AIGLQFHPESVLSP 192
guaA PRK00074
GMP synthase; Reviewed
 194-372 4.55e-11

GMP synthase; Reviewed


Pssm-ID: 234614 [Multi-domain]  Cd Length: 511  Bit Score: 63.91  E-value: 4.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 194 RVAALDFGVKYN--ILRNLERCGCQVLVFPATASPEEILATQPDGIFLSNGP------GDPAAVTYGIEtvrklLGtKPM 265
Cdd:PRK00074    5 KILILDFGSQYTqlIARRVRELGVYSEIVPYDISAEEIRAFNPKGIILSGGPasvyeeGAPRADPEIFE-----LG-VPV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 266 FGICLGHQLMGLALGG---RTFKLKFGH-----RGANQPVKDLSTGRV-------EVTSQNHGFCVdLESMQDIPVrlth 330
Cdd:PRK00074   79 LGICYGMQLMAHQLGGkveRAGKREYGRaelevDNDSPLFKGLPEEQDvwmshgdKVTELPEGFKV-IASTENCPI---- 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1180570996 331 inlndntlEGMEHLEMPAFSVQYHPEAAPGPHDATYLfERFV 372
Cdd:PRK00074  154 --------AAIANEERKFYGVQFHPEVTHTPQGKKLL-ENFV 186
PRK06774 PRK06774
aminodeoxychorismate synthase component II;
204-357 1.24e-10

aminodeoxychorismate synthase component II;


Pssm-ID: 180689 [Multi-domain]  Cd Length: 191  Bit Score: 60.26  E-value: 1.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 204 YNILRNLERCGCQVLVFPATA-SPEEILATQPDGIFLSNGPGDPAAVTYGIETVRKLLGTKPMFGICLGHQLMGLALGGR 282
Cdd:PRK06774   13 YNLYQYFCELGTEVMVKRNDElQLTDIEQLAPSHLVISPGPCTPNEAGISLAVIRHFADKLPILGVCLGHQALGQAFGAR 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 283 TFKLKFGHRGANQPVKDLSTG------RVEVTSQNHGFCVDLESMQDiPVRLTHINLNDNTLE---GMEHLEMPAFSVQY 353
Cdd:PRK06774   93 VVRARQVMHGKTSAICHSGQGvfrglnQPLTVTRYHSLVIAADSLPG-CFELTAWSERGGEMDeimGIRHRTLPLEGVQF 171


                  ....
gi 1180570996 354 HPEA 357
Cdd:PRK06774  172 HPES 175
PRK07649 PRK07649
aminodeoxychorismate/anthranilate synthase component II;
227-377 1.31e-10

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181066 [Multi-domain]  Cd Length: 195  Bit Score: 60.20  E-value: 1.31e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 227 EEILATQPDGIFLSNGPGDPAAVTYGIETVRKLLGTKPMFGICLGHQLMGLALGGRTFKLKFGHRGANQPV----KDLST 302
Cdd:PRK07649   37 SDIENMKPDFLMISPGPCSPNEAGISMEVIRYFAGKIPIFGVCLGHQSIAQVFGGEVVRAERLMHGKTSLMhhdgKTIFS 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 303 GRVE--VTSQNHGFCVDLESMQDIpvrlthINLNDNTLEG----MEHLEMPAFSVQYHPEAAPGPHDATyLFERFVNLIR 376
Cdd:PRK07649  117 DIPNpfTATRYHSLIVKKETLPDC------LEVTSWTEEGeimaIRHKTLPIEGVQFHPESIMTSHGKE-LLQNFIRKYS 189


                  .
gi 1180570996 377 K 377
Cdd:PRK07649  190 P 190
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 205-372 1.37e-10

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: 59.95  E-value: 1.37e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 205 NILRNLERCGCQVLVFPATASPEEILATQPDGIFLSNGPGDPAAVTYG-IETVRKLLGT-----KPMFGICLGHQLMGLA 278
Cdd:cd01741    18 DLLREAGAETIEIDVVDVYAGELLPDLDDYDGLVILGGPMSVDEDDYPwLKKLKELIRQalaagKPVLGICLGHQLLARA 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 279 LGGRTfklkfghrGANQPVKDLSTGRVEVTSQNHGFCVDLESMQDIPVRLTHinlNDN--TL-EGMEHL----------- 344
Cdd:cd01741    98 LGGKV--------GRNPKGWEIGWFPVTLTEAGKADPLFAGLPDEFPVFHWH---GDTvvELpPGAVLLasseacpnqaf 166

                         170       180       190
                  ....*....|....*....|....*....|
gi 1180570996 345 --EMPAFSVQYHPEAApgphdatyLFERFV 372
Cdd:cd01741   167 ryGDRALGLQFHPEER--------LLRNFL 188
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 195-281 5.72e-10

Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group includes proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA. and, the A4 beta-galactosidase middle domain. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.


Pssm-ID: 153210 [Multi-domain]  Cd Length: 115  Bit Score: 56.45  E-value: 5.72e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 195 VAALDFGVK-----YNILRNLERCGCQVLVFPATASPE--EILATQPDGIFLSNGPGDPAAVTYG---IETVRKLLGT-K 263
Cdd:cd01653     1 VAVLLFPGFeelelASPLDALREAGAEVDVVSPDGGPVesDVDLDDYDGLILPGGPGTPDDLARDealLALLREAAAAgK 80

                          90
                  ....*....|....*...
gi 1180570996 264 PMFGICLGHQLMGLALGG 281
Cdd:cd01653    81 PILGICLGAQLLVLGVQF 98
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 211-356 8.93e-10

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: 58.04  E-value: 8.93e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 211 ERCGCQVLVFPATASPEEI--LATQPDGIFLS-----------------NGPGDPAAVTYGIETVRKLLGT-KPMFGICL 270
Cdd:pfam07722  34 EGAGGLPVLLPILGDPEDAaaILDRLDGLLLTggpnvdphfygeepsesGGPYDPARDAYELALIRAALARgKPILGICR 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 271 GHQLMGLALGGRTF------KLKFGHRGANQPVKD-----------------LSTGRVEVTSQnHGFCVD-----LESMQ 322
Cdd:pfam07722 114 GFQLLNVALGGTLYqdiqeqPGFTDHREHCQVAPYapshavnvepgsllaslLGSEEFRVNSL-HHQAIDrlapgLRVEA 192

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1180570996 323 DIPvrlthinlnDNTLEGMEHLEMPAF--SVQYHPE 356
Cdd:pfam07722 193 VAP---------DGTIEAIESPNAKGFalGVQWHPE 219
PRK08007 PRK08007
aminodeoxychorismate synthase component 2;
204-357 9.54e-10

aminodeoxychorismate synthase component 2;


Pssm-ID: 181194 [Multi-domain]  Cd Length: 187  Bit Score: 57.62  E-value: 9.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 204 YNILRNLERCGCQVLVFPATA-SPEEILATQPDGIFLSNGPGDPAAVTYGIETVRKLLGTKPMFGICLGHQLMGLALGGR 282
Cdd:PRK08007   13 WNLYQYFCELGADVLVKRNDAlTLADIDALKPQKIVISPGPCTPDEAGISLDVIRHYAGRLPILGVCLGHQAMAQAFGGK 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 283 TFKLKFGHRGANQPVKDLSTGRVE------VTSQNHGFCVDLESMQDIpvrlTHINLNDNTLE--GMEHLEMPAFSVQYH 354
Cdd:PRK08007   93 VVRAAKVMHGKTSPITHNGEGVFRglanplTVTRYHSLVVEPDSLPAC----FEVTAWSETREimGIRHRQWDLEGVQFH 168


                  ...
gi 1180570996 355 PEA 357
Cdd:PRK08007  169 PES 171
PRK07765 PRK07765
aminodeoxychorismate/anthranilate synthase component II;
201-356 1.26e-09

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181107 [Multi-domain]  Cd Length: 214  Bit Score: 57.75  E-value: 1.26e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 201 GVKYNILRNLErcgcqvlvfPATASPEEIlATQPDGIFLSNGPGDPAAVTYGIETVRKLLGTK-PMFGICLGHQLMGLAL 279
Cdd:PRK07765   24 GVEAEVWRNDD---------PRLADEAAV-AAQFDGVLLSPGPGTPERAGASIDMVRACAAAGtPLLGVCLGHQAIGVAF 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 280 G-----------GRTFKLKFGHRGANQPVKDLSTGrvevtSQNHGFCVDLESMQDIPVRLTHInlNDNTLEGMEHLEMPA 348
Cdd:PRK07765   94 GatvdrapellhGKTSSVHHTGVGVLAGLPDPFTA-----TRYHSLTILPETLPAELEVTART--DSGVIMAVRHRELPI 166


                  ....*...
gi 1180570996 349 FSVQYHPE 356
Cdd:PRK07765  167 HGVQFHPE 174
PRK13566 PRK13566
anthranilate synthase component I;
226-356 1.60e-09

anthranilate synthase component I;


Pssm-ID: 237429 [Multi-domain]  Cd Length: 720  Bit Score: 59.55  E-value: 1.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 226 PEEILATQ-PDGIFLSNGPGDPAavTYGI-ETVRKLLGTK-PMFGICLGHQLMGLALGGRTFKLKFGHRGANQPVKDLST 302
Cdd:PRK13566  561 AEEMLDRVnPDLVVLSPGPGRPS--DFDCkATIDAALARNlPIFGVCLGLQAIVEAFGGELGQLAYPMHGKPSRIRVRGP 638

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1180570996 303 GRV------EVT-SQNHGFCVDLESMQDiPVRLTHINlNDNTLEGMEHLEMPAFSVQYHPE 356
Cdd:PRK13566  639 GRLfsglpeEFTvGRYHSLFADPETLPD-ELLVTAET-EDGVIMAIEHKTLPVAAVQFHPE 697
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 195-275 2.40e-09

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: 54.13  E-value: 2.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 195 VAALDFGVK-----YNILRNLERCGCQVLVFPATASPE--EILATQPDGIFLSNGPGDPAAVTYG---IETVRKLLGT-K 263
Cdd:cd03128     1 VAVLLFGGSeelelASPLDALREAGAEVDVVSPDGGPVesDVDLDDYDGLILPGGPGTPDDLAWDealLALLREAAAAgK 80

                          90
                  ....*....|..
gi 1180570996 264 PMFGICLGHQLM 275
Cdd:cd03128    81 PVLGICLGAQLL 92
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 205-372 1.50e-08

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


Pssm-ID: 153216 [Multi-domain]  Cd Length: 189  Bit Score: 54.12  E-value: 1.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 205 NILRNLERCGCQVLVFPATaSPEEILATQP---DGIFLS-----------------NGPGDPAAVTYGIETVRKLL-GTK 263
Cdd:cd01745    23 YYVDAVRKAGGLPVLLPPV-DDEEDLEQYLellDGLLLTgggdvdpplygeephpeLGPIDPERDAFELALLRAALeRGK 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 264 PMFGICLGHQLMGLALGGRTFKlkfgHRGAN----QPVKDLSTG-RVEVTSqnhgfcvdlesmqdipvrlthinlNDNTL 338
Cdd:cd01745   102 PILGICRGMQLLNVALGGTLYQ----DIRVNslhhQAIKRLADGlRVEARA------------------------PDGVI 153

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1180570996 339 EGMEHLEMP-AFSVQYHPE-AAPGPHDATYLFERFV 372
Cdd:cd01745   154 EAIESPDRPfVLGVQWHPEwLADTDPDSLKLFEAFV 189
PLN02347 PLN02347
GMP synthetase
 195-362 3.84e-08

GMP synthetase


Pssm-ID: 215197 [Multi-domain]  Cd Length: 536  Bit Score: 55.08  E-value: 3.84e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 195 VAALDFGVKYN--ILRNLERCGCQVLVFPATASPEEILATQPDGIFLSNGP------GDPAAVTYGIETVRKllGTKPMF 266
Cdd:PLN02347   13 VLILDYGSQYThlITRRVRELGVYSLLLSGTASLDRIASLNPRVVILSGGPhsvhveGAPTVPEGFFDYCRE--RGVPVL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 267 GICLGHQLMGLALGGRtfkLKFGHRGanqpvkdlSTGRVEV-TSQNHGFCVDLESMQDIPVRLTHINLNDNTLEG----- 340
Cdd:PLN02347   91 GICYGMQLIVQKLGGE---VKPGEKQ--------EYGRMEIrVVCGSQLFGDLPSGETQTVWMSHGDEAVKLPEGfevva 159

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1180570996 341 ---------MEHLEMPAFSVQYHPEAAPGPH 362
Cdd:PLN02347  160 ksvqgavvaIENRERRIYGLQYHPEVTHSPK 190
HisH COG0118
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ...
 194-275 3.98e-08

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: 52.73  E-value: 3.98e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 194 RVAALDFGVK--YNILRNLERCGCQVLVfpaTASPEEILATqpDGIFLsngPGD---PAAVTY-----GIETVRKLL-GT 262
Cdd:COG0118     2 MIAIIDYGMGnlRSVAKALERLGAEVVV---TSDPDEIRAA--DRLVL---PGVgafGDAMENlrergLDEAIREAVaGG 73

                          90
                  ....*....|...
gi 1180570996 263 KPMFGICLGHQLM 275
Cdd:COG0118    74 KPVLGICLGMQLL 86
PRK06895 PRK06895
anthranilate synthase component II;
237-357 7.99e-08

anthranilate synthase component II;


Pssm-ID: 235882 [Multi-domain]  Cd Length: 190  Bit Score: 52.05  E-value: 7.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 237 IFLSNGPGDPAAVTYGIETVRKLLGTKPMFGICLGHQLMGLALGGRTFKLKFGHRGANQPVKDLSTGRVevtSQN----- 311
Cdd:PRK06895   47 ILISPGPDVPRAYPQLFAMLERYHQHKSILGVCLGHQTLCEFFGGELYNLNNVRHGQQRPLKVRSNSPL---FDGlpeef 123

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1180570996 312 -----HGFCVDLESMQDiPVRLTHInLNDNTLEGMEHLEMPAFSVQYHPEA 357
Cdd:PRK06895  124 niglyHSWAVSEENFPT-PLEITAV-CDENVVMAMQHKTLPIYGVQFHPES 172
GATase1_Glutamyl_Hydrolase cd01747
Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase; Type 1 ...
 264-377 1.26e-07

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: 52.32  E-value: 1.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 264 PMFGICLGHQL-MGLALGGRTFKLKFGHRGANQPVK---DLSTGRVE---------------VTSQNHGFCVDLESMQD- 323
Cdd:cd01747    94 PVWGTCLGFELlTYLTSGETLLLEATEATNSALPLNfteDALQSRLFkrfppdllkslatepLTMNNHRYGISPENFTEn 173

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1180570996 324 ------IPVRLTHINLNDNT-LEGMEHLEMPAFSVQYHPEAAP--------GPHD------ATYLFERFVNLIRK 377
Cdd:cd01747   174 gllsdfFNVLTTNDDWNGVEfISTVEAYKYPIYGVQWHPEKNAfewkksssIPHSeeairlTQYFANFFVNEARK 248
PuuD COG2071
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ...
 205-377 1.65e-07

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: 51.71  E-value: 1.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 205 NILRNLERCGCQVLVFPATASPEEI--LATQPDGIFLSNGPgDPAAVTYGiETVRKLLGT-------------------- 262
Cdd:COG2071    19 DYVRAVRAAGGLPVLLPPVGDEEDLdeLLDRLDGLVLTGGA-DVDPALYG-EEPHPELGPidperdafelaliraalerg 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 263 KPMFGICLGHQLMGLALGGR-------TFKLKFGHRGA---NQPVKD------------LSTGRVEVTSQnHGFCVDles 320
Cdd:COG2071    97 KPVLGICRGMQLLNVALGGTlyqdlpdQVPGALDHRQPaprYAPRHTveiepgsrlariLGEEEIRVNSL-HHQAVK--- 172

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1180570996 321 mqDIPVRLT-----HinlnDNTLEGMEHLEMP-AFSVQYHPE--AAPGPHDATyLFERFVNLIRK 377
Cdd:COG2071   173 --RLGPGLRvsaraP----DGVIEAIESPGAPfVLGVQWHPEwlAASDPLSRR-LFEAFVEAARA 230
PRK08857 PRK08857
aminodeoxychorismate/anthranilate synthase component II;
229-357 1.75e-07

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181566 [Multi-domain]  Cd Length: 193  Bit Score: 51.03  E-value: 1.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 229 ILATQPDGIFLSNGPGDPAAVTYGIETVRKLLGTKPMFGICLGHQLMGLALGGRTFKLKFGHRGANQPVKdlSTGRVEVT 308
Cdd:PRK08857   39 IEALNPTHLVISPGPCTPNEAGISLQAIEHFAGKLPILGVCLGHQAIAQVFGGQVVRARQVMHGKTSPIR--HTGRSVFK 116

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 309 SQN--------HGFCVDLESMQDIPVRLTHINLNDNTLE---GMEHLEMPAFSVQYHPEA 357
Cdd:PRK08857  117 GLNnpltvtryHSLVVKNDTLPECFELTAWTELEDGSMDeimGFQHKTLPIEAVQFHPES 176
hisH PRK13143
imidazole glycerol phosphate synthase subunit HisH; Provisional
 194-275 2.69e-07

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237289 [Multi-domain]  Cd Length: 200  Bit Score: 50.64  E-value: 2.69e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 194 RVAALDFGVK--YNILRNLERCGCQVLVfpaTASPEEILATqpDGIFLsngPGD---PAAVTYgIETVRKLLGT-----K 263
Cdd:PRK13143    2 MIVIIDYGVGnlRSVSKALERAGAEVVI---TSDPEEILDA--DGIVL---PGVgafGAAMEN-LSPLRDVILEaarsgK 72

                          90
                  ....*....|..
gi 1180570996 264 PMFGICLGHQLM 275
Cdd:PRK13143   73 PFLGICLGMQLL 84
trpG CHL00101
anthranilate synthase component 2
 234-286 5.82e-07

anthranilate synthase component 2


Pssm-ID: 214365 [Multi-domain]  Cd Length: 190  Bit Score: 49.34  E-value: 5.82e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1180570996 234 PDGIFLSNGPGDPAAVTYGIETVRKLLGTKPMFGICLGHQLMGLALGGRTFKL 286
Cdd:CHL00101   44 IRHIIISPGPGHPRDSGISLDVISSYAPYIPILGVCLGHQSIGYLFGGKIIKA 96
PRK09522 PRK09522
bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate ...
 204-281 3.93e-06

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


Pssm-ID: 181927 [Multi-domain]  Cd Length: 531  Bit Score: 48.87  E-value: 3.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 204 YNILRNLERCGCQVLVF----PATASPEEILATQPDGIFLSNGPGDPAAVTYGIETVRKLLGTKPMFGICLGHQLMGLAL 279
Cdd:PRK09522   15 YNLADQLRSNGHNVVIYrnhiPAQTLIERLATMSNPVLMLSPGPGVPSEAGCMPELLTRLRGKLPIIGICLGHQAIVEAY 94


                  ..
gi 1180570996 280 GG 281
Cdd:PRK09522   95 GG 96
hisH PRK13146
imidazole glycerol phosphate synthase subunit HisH; Provisional
 194-275 3.75e-05

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237290 [Multi-domain]  Cd Length: 209  Bit Score: 44.39  E-value: 3.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 194 RVAALDFGVKyNIL---RNLERCG--CQVLVfpaTASPEEILATqpDGIFLsngPGDPA---------AVTYG---IETV 256
Cdd:PRK13146    3 TVAIIDYGSG-NLRsaaKALERAGagADVVV---TADPDAVAAA--DRVVL---PGVGAfadcmrglrAVGLGeavIEAV 73

                          90
                  ....*....|....*....
gi 1180570996 257 RKllGTKPMFGICLGHQLM 275
Cdd:PRK13146   74 LA--AGRPFLGICVGMQLL 90
GATase1_IGP_Synthase cd01748
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ...
 195-275 9.83e-05

Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate synthase (IGPS); Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate synthase (IGPS). IGPS incorporates ammonia derived from glutamine into N1-[(5'-phosphoribulosyl)-formimino]-5-aminoimidazole-4-carboxamide ribonucleotide (PRFAR) to form 5'-(5-aminoimidazole-4-carboxamide) ribonucleotide (AICAR) and imidazole glycerol phosphate (IGP). The glutamine amidotransferase domain generates the ammonia nucleophile which is channeled from the glutaminase active site to the PRFAR active site. IGPS belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.


Pssm-ID: 153219 [Multi-domain]  Cd Length: 198  Bit Score: 42.87  E-value: 9.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 195 VAALDFGVK--YNILRNLERCGCQVLVfpaTASPEEILATqpDGIFLsngPGD---PAAV-----TYGIETVRKLLGT-K 263
Cdd:cd01748     1 IAIIDYGMGnlRSVANALERLGAEVII---TSDPEEILSA--DKLIL---PGVgafGDAManlreRGLIEALKEAIASgK 72

                          90
                  ....*....|..
gi 1180570996 264 PMFGICLGHQLM 275
Cdd:cd01748    73 PFLGICLGMQLL 84
hisH PRK13170
imidazole glycerol phosphate synthase subunit HisH; Provisional
 202-276 2.19e-04

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 183877 [Multi-domain]  Cd Length: 196  Bit Score: 41.77  E-value: 2.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 202 VKYNIlrnlERCGCQVLVfpaTASPEEILATqpDGIFLSnGPGDPAAVTYG------IETVRKLlgTKPMFGICLGHQLM 275
Cdd:PRK13170   16 VKFAI----ERLGYEPVV---SRDPDVILAA--DKLFLP-GVGTAQAAMDQlrerelIDLIKAC--TQPVLGICLGMQLL 83


                  .
gi 1180570996 276 G 276
Cdd:PRK13170   84 G 84
PRK09065 PRK09065
glutamine amidotransferase; Provisional
 206-281 2.21e-04

glutamine amidotransferase; Provisional


Pssm-ID: 181635 [Multi-domain]  Cd Length: 237  Bit Score: 42.26  E-value: 2.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 206 ILRNLERCGCQVLVFPATA-----SPEEIlatqpDGIFLSngpGDPAAVT-------YGIETVRKLLGTK-PMFGICLGH 272
Cdd:PRK09065   27 IRVALGLAEQPVVVVRVFAgeplpAPDDF-----AGVIIT---GSWAMVTdrldwseRTADWLRQAAAAGmPLLGICYGH 98


                  ....*....
gi 1180570996 273 QLMGLALGG 281
Cdd:PRK09065   99 QLLAHALGG 107
hisH PRK13141
imidazole glycerol phosphate synthase subunit HisH; Provisional
 204-275 5.68e-04

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237288 [Multi-domain]  Cd Length: 205  Bit Score: 40.88  E-value: 5.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 204 YNILRNLERCGCQVLVfpaTASPEEILATqpDGIFLsngPG----DPAA---VTYG-IETVRKLLGT-KPMFGICLGHQL 274
Cdd:PRK13141   13 RSVEKALERLGAEAVI---TSDPEEILAA--DGVIL---PGvgafPDAManlRERGlDEVIKEAVASgKPLLGICLGMQL 84


                  .
gi 1180570996 275 M 275
Cdd:PRK13141   85 L 85
IMP_synth_hisH TIGR01855
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model ...
 195-299 7.38e-04

imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model represents the glutamine amidotransferase subunit (or domain, in eukaryotic systems) of imidazole glycerol phosphate synthase. This subunit catalyzes step 5 of histidine biosynthesis from PRPP. The other subunit, the cyclase, catalyzes step 6. [Amino acid biosynthesis, Histidine family]


Pssm-ID: 273836 [Multi-domain]  Cd Length: 196  Bit Score: 40.39  E-value: 7.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180570996 195 VAALDFGVK--YNILRNLERCGCQVLVfpaTASPEEILatQPDGIFLsngPG---DPAAVT----YGIETVRKLL--GTK 263
Cdd:TIGR01855   1 IVIIDYGVGnlGSVKRALKRVGAEPVV---VKDSKEAE--LADKLIL---PGvgaFGAAMArlreNGLDLFVELVvrLGK 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1180570996 264 PMFGICLGHQLM-----------GLAL-GGRTFKLKFG---HRGANQ--PVKD 299
Cdd:TIGR01855  73 PVLGICLGMQLLferseegggvpGLGLiKGNVVKLEARkvpHMGWNEvhPVKE 125
PLN02889 PLN02889
oxo-acid-lyase/anthranilate synthase
 235-282 2.96e-03

oxo-acid-lyase/anthranilate synthase


Pssm-ID: 215481 [Multi-domain]  Cd Length: 918  Bit Score: 39.83  E-value: 2.96e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1180570996 235 DGIFLSNGPGDPA-AVTYGIeTVRKLLGTK--PMFGICLGHQLMGLALGGR 282
Cdd:PLN02889  133 DNIVISPGPGSPTcPADIGI-CLRLLLECRdiPILGVCLGHQALGYVHGAR 182
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH