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Conserved domains on  [gi|488288967|ref|WP_002360175|]
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MULTISPECIES: carbamoyl phosphate synthase small subunit [Enterococcus]

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 ...
 1-353 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: 676.74  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967   1 MKRLLILEDGTVFEGKAFGAEGNVVGEVVFTTGMTGYQEAITDQSFNGQMITFTYPLVGNYGVNRDDYESIAPTCKGVIV 80
Cdd:COG0505    3 MKALLVLEDGTVFEGKSFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVTFTYPHIGNYGVNDEDFESDRPWVAGLVV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967  81 KEHARVASNWRQQMTLDEFLKRKGIPGISGIDTRALTRKLRSAGTMKGSIIDAVDDLPHAFDQLKATVM--PKNQVAQVS 158
Cdd:COG0505   83 RELSRRPSNWRSEESLDEYLKEHGIPGISGIDTRALTRHLREKGAMKGVISTGDLDIEELLEKARAAPGmeGLDLVKEVS 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967 159 TTKPY---PSPGIGRNVVVVDFGLKHSILRELSKRQCNLTVLPYNTTAEEILELSPDGVMLTNGPGDPKDVPEAIEMIQA 235
Cdd:COG0505  163 TKEPYewtEAPGAGFHVVALDFGVKRNILRELAERGCRVTVVPATTSAEEILALNPDGVFLSNGPGDPAALDYAIETIRE 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967 236 IQGK-VPIFGICLGHQLFSLANGADTYKMKFGHRGLNHPVREIATGRIDFTSQNHGYAVDEATIDPEKLLVTHVEVNDGT 314
Cdd:COG0505  243 LLGKgIPIFGICLGHQLLALALGAKTYKLKFGHRGANHPVKDLETGRVEITSQNHGFAVDEDSLPATDLEVTHVNLNDGT 322

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 488288967 315 VEGVRHRDYPAFTVQYHPDAAPGPHDGLHLFDEFMELMD 353
Cdd:COG0505  323 VEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDRFIELME 361
 
Name Accession Description Interval E-value
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 1-353 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: 676.74  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967   1 MKRLLILEDGTVFEGKAFGAEGNVVGEVVFTTGMTGYQEAITDQSFNGQMITFTYPLVGNYGVNRDDYESIAPTCKGVIV 80
Cdd:COG0505    3 MKALLVLEDGTVFEGKSFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVTFTYPHIGNYGVNDEDFESDRPWVAGLVV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967  81 KEHARVASNWRQQMTLDEFLKRKGIPGISGIDTRALTRKLRSAGTMKGSIIDAVDDLPHAFDQLKATVM--PKNQVAQVS 158
Cdd:COG0505   83 RELSRRPSNWRSEESLDEYLKEHGIPGISGIDTRALTRHLREKGAMKGVISTGDLDIEELLEKARAAPGmeGLDLVKEVS 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967 159 TTKPY---PSPGIGRNVVVVDFGLKHSILRELSKRQCNLTVLPYNTTAEEILELSPDGVMLTNGPGDPKDVPEAIEMIQA 235
Cdd:COG0505  163 TKEPYewtEAPGAGFHVVALDFGVKRNILRELAERGCRVTVVPATTSAEEILALNPDGVFLSNGPGDPAALDYAIETIRE 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967 236 IQGK-VPIFGICLGHQLFSLANGADTYKMKFGHRGLNHPVREIATGRIDFTSQNHGYAVDEATIDPEKLLVTHVEVNDGT 314
Cdd:COG0505  243 LLGKgIPIFGICLGHQLLALALGAKTYKLKFGHRGANHPVKDLETGRVEITSQNHGFAVDEDSLPATDLEVTHVNLNDGT 322

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 488288967 315 VEGVRHRDYPAFTVQYHPDAAPGPHDGLHLFDEFMELMD 353
Cdd:COG0505  323 VEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDRFIELME 361
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
1-352 0e+00

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 672.56  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967   1 MKRLLILEDGTVFEGKAFGAEGNVVGEVVFTTGMTGYQEAITDQSFNGQMITFTYPLVGNYGVNRDDYESIAPTCKGVIV 80
Cdd:PRK12564   3 MKAYLVLEDGTVFEGKAFGAEGETVGEVVFNTSMTGYQEILTDPSYAGQIVTFTYPLIGNYGVNREDFESDRPHAKGLIV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967  81 KEHARVASNWRQQMTLDEFLKRKGIPGISGIDTRALTRKLRSAGTMKGSIIDAVDDLPHAFDQLKAT--VMPKNQVAQVS 158
Cdd:PRK12564  83 RELSDIPSNWRSEMSLDEYLKENGIPGISGIDTRALTRKLREKGAMKGVIATEDFDAEELLEKARAFpgLLGLDLVKEVS 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967 159 TTKPYPSPGIG----RNVVVVDFGLKHSILRELSKRQCNLTVLPYNTTAEEILELSPDGVMLTNGPGDPKDVPEAIEMIQ 234
Cdd:PRK12564 163 TKEPYPWPGPGgelkYKVVAIDFGVKRNILRELAERGCRVTVVPATTTAEEILALNPDGVFLSNGPGDPAALDYAIEMIR 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967 235 AIQG-KVPIFGICLGHQLFSLANGADTYKMKFGHRGLNHPVREIATGRIDFTSQNHGYAVDEATIdPEKLLVTHVEVNDG 313
Cdd:PRK12564 243 ELLEkKIPIFGICLGHQLLALALGAKTYKMKFGHRGANHPVKDLETGKVEITSQNHGFAVDEDSL-PANLEVTHVNLNDG 321

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 488288967 314 TVEGVRHRDYPAFTVQYHPDAAPGPHDGLHLFDEFMELM 352
Cdd:PRK12564 322 TVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDEFVELM 360
CPSaseIIsmall TIGR01368
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ...
 3-354 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: 564.56  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967    3 RLLILEDGTVFEGKAFGAEGNVVGEVVFTTGMTGYQEAITDQSFNGQMITFTYPLVGNYGVNRDDYESIAPTCKGVIVKE 82
Cdd:TIGR01368   1 AYLVLEDGTVFRGYSFGAEGTVAGEVVFNTGMTGYQEILTDPSYKGQIVVFTYPLIGNYGVNDEDAESKGIHVSGLVVRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967   83 HARVASNWRQQMTLDEFLKRKGIPGISGIDTRALTRKLRSAGTMKGSIidAVDDLPHAFDQLKATVMPKNQ----VAQVS 158
Cdd:TIGR01368  81 LSDRYSNWRATESLDQFLKRHGIPGIYGVDTRALVKKIREKGTMKGVI--STEDSNDEELVEKARVSPDITginlVAEVS 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967  159 TTKPYP---SPGIGRNVVVVDFGLKHSILRELSKRQCNLTVLPYNTTAEEILELSPDGVMLTNGPGDPKDVPEAIEMIQA 235
Cdd:TIGR01368 159 TKEPYTwgqRGGKGKRVVVIDFGVKRNILRRLVKRGCEVTVVPYDTDAEEIKKYNPDGIFLSNGPGDPAAVEPAIETIRK 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967  236 IQGKVPIFGICLGHQLFSLANGADTYKMKFGHRGLNHPVREIATGRIDFTSQNHGYAVDEATIDPEKLLVTHVEVNDGTV 315
Cdd:TIGR01368 239 LLEKIPIFGICLGHQLLALAFGAKTYKMKFGHRGGNHPVKDLITGRVEITSQNHGYAVDPDSLPAGDLEVTHVNLNDGTV 318

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 488288967  316 EGVRHRDYPAFTVQYHPDAAPGPHDGLHLFDEFMELMDA 354
Cdd:TIGR01368 319 EGIRHKDLPVFSVQYHPEASPGPHDTEYLFDEFIDLMKK 357
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 172-349 7.78e-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: 328.30  E-value: 7.78e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967 172 VVVVDFGLKHSILRELSKRQCNLTVLPYNTTAEEILELSPDGVMLTNGPGDPKDVPEAIEMI-QAIQGKVPIFGICLGHQ 250
Cdd:cd01744    1 VVVIDFGVKHNILRELLKRGCEVTVVPYNTDAEEILKLDPDGIFLSNGPGDPALLDEAIKTVrKLLGKKIPIFGICLGHQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967 251 LFSLANGADTYKMKFGHRGLNHPVREIATGRIDFTSQNHGYAVDEATIdPEKLLVTHVEVNDGTVEGVRHRDYPAFTVQY 330
Cdd:cd01744   81 LLALALGAKTYKMKFGHRGSNHPVKDLITGRVYITSQNHGYAVDPDSL-PGGLEVTHVNLNDGTVEGIRHKDLPVFSVQF 159

                        170
                 ....*....|....*....
gi 488288967 331 HPDAAPGPHDGLHLFDEFM 349
Cdd:cd01744  160 HPEASPGPHDTEYLFDEFL 178
CPSase_sm_chain smart01097
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 1-130 1.56e-90

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: 267.32  E-value: 1.56e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967     1 MKRLLILEDGTVFEGKAFGAEGNVVGEVVFTTGMTGYQEAITDQSFNGQMITFTYPLVGNYGVNRDDYESIAPTCKGVIV 80
Cdd:smart01097   1 MKAYLVLEDGTVFEGESFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNDEDFESDKIQVKGLVV 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 488288967    81 KEHARVASNWRQQMTLDEFLKRKGIPGISGIDTRALTRKLRSAGTMKGSI 130
Cdd:smart01097  81 RELSDEPSNWRSEQSLDEFLKENGIPGISGIDTRALTRKLREKGAMKGVI 130
CPSase_sm_chain pfam00988
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 5-130 2.10e-88

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: 261.49  E-value: 2.10e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967    5 LILEDGTVFEGKAFGAEGNVVGEVVFTTGMTGYQEAITDQSFNGQMITFTYPLVGNYGVNRDDYESIAPTCKGVIVKEHA 84
Cdd:pfam00988   1 LVLEDGTVFEGKSFGAAGSTVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNPEDFESDKIHVAGLVVREYS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 488288967   85 RVASNWRQQMTLDEFLKRKGIPGISGIDTRALTRKLRSAGTMKGSI 130
Cdd:pfam00988  81 DEPSNWRAEESLDEWLKEQGIPGISGVDTRALTRKIREKGAMKGVI 126
 
Name Accession Description Interval E-value
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 1-353 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: 676.74  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967   1 MKRLLILEDGTVFEGKAFGAEGNVVGEVVFTTGMTGYQEAITDQSFNGQMITFTYPLVGNYGVNRDDYESIAPTCKGVIV 80
Cdd:COG0505    3 MKALLVLEDGTVFEGKSFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVTFTYPHIGNYGVNDEDFESDRPWVAGLVV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967  81 KEHARVASNWRQQMTLDEFLKRKGIPGISGIDTRALTRKLRSAGTMKGSIIDAVDDLPHAFDQLKATVM--PKNQVAQVS 158
Cdd:COG0505   83 RELSRRPSNWRSEESLDEYLKEHGIPGISGIDTRALTRHLREKGAMKGVISTGDLDIEELLEKARAAPGmeGLDLVKEVS 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967 159 TTKPY---PSPGIGRNVVVVDFGLKHSILRELSKRQCNLTVLPYNTTAEEILELSPDGVMLTNGPGDPKDVPEAIEMIQA 235
Cdd:COG0505  163 TKEPYewtEAPGAGFHVVALDFGVKRNILRELAERGCRVTVVPATTSAEEILALNPDGVFLSNGPGDPAALDYAIETIRE 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967 236 IQGK-VPIFGICLGHQLFSLANGADTYKMKFGHRGLNHPVREIATGRIDFTSQNHGYAVDEATIDPEKLLVTHVEVNDGT 314
Cdd:COG0505  243 LLGKgIPIFGICLGHQLLALALGAKTYKLKFGHRGANHPVKDLETGRVEITSQNHGFAVDEDSLPATDLEVTHVNLNDGT 322

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 488288967 315 VEGVRHRDYPAFTVQYHPDAAPGPHDGLHLFDEFMELMD 353
Cdd:COG0505  323 VEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDRFIELME 361
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
1-352 0e+00

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 672.56  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967   1 MKRLLILEDGTVFEGKAFGAEGNVVGEVVFTTGMTGYQEAITDQSFNGQMITFTYPLVGNYGVNRDDYESIAPTCKGVIV 80
Cdd:PRK12564   3 MKAYLVLEDGTVFEGKAFGAEGETVGEVVFNTSMTGYQEILTDPSYAGQIVTFTYPLIGNYGVNREDFESDRPHAKGLIV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967  81 KEHARVASNWRQQMTLDEFLKRKGIPGISGIDTRALTRKLRSAGTMKGSIIDAVDDLPHAFDQLKAT--VMPKNQVAQVS 158
Cdd:PRK12564  83 RELSDIPSNWRSEMSLDEYLKENGIPGISGIDTRALTRKLREKGAMKGVIATEDFDAEELLEKARAFpgLLGLDLVKEVS 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967 159 TTKPYPSPGIG----RNVVVVDFGLKHSILRELSKRQCNLTVLPYNTTAEEILELSPDGVMLTNGPGDPKDVPEAIEMIQ 234
Cdd:PRK12564 163 TKEPYPWPGPGgelkYKVVAIDFGVKRNILRELAERGCRVTVVPATTTAEEILALNPDGVFLSNGPGDPAALDYAIEMIR 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967 235 AIQG-KVPIFGICLGHQLFSLANGADTYKMKFGHRGLNHPVREIATGRIDFTSQNHGYAVDEATIdPEKLLVTHVEVNDG 313
Cdd:PRK12564 243 ELLEkKIPIFGICLGHQLLALALGAKTYKMKFGHRGANHPVKDLETGKVEITSQNHGFAVDEDSL-PANLEVTHVNLNDG 321

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 488288967 314 TVEGVRHRDYPAFTVQYHPDAAPGPHDGLHLFDEFMELM 352
Cdd:PRK12564 322 TVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDEFVELM 360
PRK12838 PRK12838
carbamoyl phosphate synthase small subunit; Reviewed
 1-352 0e+00

carbamoyl phosphate synthase small subunit; Reviewed


Pssm-ID: 183784 [Multi-domain]  Cd Length: 354  Bit Score: 585.70  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967   1 MKRLLILEDGTVFEGKAFGAEGNVVGEVVFTTGMTGYQEAITDQSFNGQMITFTYPLVGNYGVNRDDYESIAPTCKGVIV 80
Cdd:PRK12838   1 MKAYLILEDGTVFEGELIGAPIDVTGEIVFNTGMTGYQEVLTDPSYKGQIVVFTYPLIGNYGINADDYESKQPQVKGVIV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967  81 KEHARVASNWRQQMTLDEFLKRKGIPGISGIDTRALTRKLRSAGTMKGSIIDavDDLPHAFDQLKATVMPKNQVAQVSTT 160
Cdd:PRK12838  81 YELSREGSHYRAKQSLDDFLKEWNIPGISGVDTRALVKHIREKGTMKASITT--TDDAHAFDQIKALVLPKNVVAQVSTK 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967 161 KPYPSPGIGRNVVVVDFGLKHSILRELSKRQCNLTVLPYNTTAEEILELSPDGVMLTNGPGDPKDVPEAIEMIQAIQGKV 240
Cdd:PRK12838 159 EPYTYGNGGKHVALIDFGYKKSILRSLSKRGCKVTVLPYDTSLEEIKNLNPDGIVLSNGPGDPKELQPYLPEIKKLISSY 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967 241 PIFGICLGHQLFSLANGADTYKMKFGHRGLNHPVREIATGRIDFTSQNHGYAVDEATIDPEKLLVTHVEVNDGTVEGVRH 320
Cdd:PRK12838 239 PILGICLGHQLIALALGADTEKLPFGHRGANHPVIDLTTGRVWMTSQNHGYVVDEDSLDGTPLSVRFFNVNDGSIEGLRH 318

                        330       340       350
                 ....*....|....*....|....*....|..
gi 488288967 321 RDYPAFTVQYHPDAAPGPHDGLHLFDEFMELM 352
Cdd:PRK12838 319 KKKPVLSVQFHPEAHPGPHDAEYIFDEFLEMM 350
CPSaseIIsmall TIGR01368
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ...
 3-354 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: 564.56  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967    3 RLLILEDGTVFEGKAFGAEGNVVGEVVFTTGMTGYQEAITDQSFNGQMITFTYPLVGNYGVNRDDYESIAPTCKGVIVKE 82
Cdd:TIGR01368   1 AYLVLEDGTVFRGYSFGAEGTVAGEVVFNTGMTGYQEILTDPSYKGQIVVFTYPLIGNYGVNDEDAESKGIHVSGLVVRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967   83 HARVASNWRQQMTLDEFLKRKGIPGISGIDTRALTRKLRSAGTMKGSIidAVDDLPHAFDQLKATVMPKNQ----VAQVS 158
Cdd:TIGR01368  81 LSDRYSNWRATESLDQFLKRHGIPGIYGVDTRALVKKIREKGTMKGVI--STEDSNDEELVEKARVSPDITginlVAEVS 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967  159 TTKPYP---SPGIGRNVVVVDFGLKHSILRELSKRQCNLTVLPYNTTAEEILELSPDGVMLTNGPGDPKDVPEAIEMIQA 235
Cdd:TIGR01368 159 TKEPYTwgqRGGKGKRVVVIDFGVKRNILRRLVKRGCEVTVVPYDTDAEEIKKYNPDGIFLSNGPGDPAAVEPAIETIRK 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967  236 IQGKVPIFGICLGHQLFSLANGADTYKMKFGHRGLNHPVREIATGRIDFTSQNHGYAVDEATIDPEKLLVTHVEVNDGTV 315
Cdd:TIGR01368 239 LLEKIPIFGICLGHQLLALAFGAKTYKMKFGHRGGNHPVKDLITGRVEITSQNHGYAVDPDSLPAGDLEVTHVNLNDGTV 318

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 488288967  316 EGVRHRDYPAFTVQYHPDAAPGPHDGLHLFDEFMELMDA 354
Cdd:TIGR01368 319 EGIRHKDLPVFSVQYHPEASPGPHDTEYLFDEFIDLMKK 357
carA CHL00197
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
 2-352 1.50e-131

carbamoyl-phosphate synthase arginine-specific small subunit; Provisional


Pssm-ID: 214392 [Multi-domain]  Cd Length: 382  Bit Score: 381.07  E-value: 1.50e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967   2 KRLLILEDGTVFEGKAFGAEGNVVGEVVFTTGMTGYQEAITDQSFNGQMITFTYPLVGNYGVNRDDYESIAPTCKGVIVK 81
Cdd:CHL00197   6 PAILVLEDGTYYRGWSFSNPITTIGEVVFNTGMTGYQEIITDPSYFEQIVTFTYPEIGNTGINLEDIESVKIQVKGIIAK 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967  82 EHARVASNWRQQMTLDEFLKRKGIPGISGIDTRALTRKLRSAGTMKGSIidAVDDLPHAFDQLK---ATVMPK-NQVAQV 157
Cdd:CHL00197  86 NICKSSSNWRQQESLVSYLQRHKIPFIFGIDTRALTQHLRRFGTMNGCI--SNQNLNLSYLRAKikeSPHMPSsDLIPRV 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967 158 STTKPY-----------------PSPGIGRNVVVVDFGLKHSILRELSKRQCNLTVLPYNTTAEEILELSPDGVMLTNGP 220
Cdd:CHL00197 164 TTSSYYewdekshpsfyladnkrPHSSYQLKIIVIDFGVKYNILRRLKSFGCSITVVPATSPYQDILSYQPDGILLSNGP 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967 221 GDPKDVPEAIEMIQA-IQGKVPIFGICLGHQLFSLANGADTYKMKFGHRGLNHPvreiaTG---RIDFTSQNHGYAVDEA 296
Cdd:CHL00197 244 GDPSAIHYGIKTVKKlLKYNIPIFGICMGHQILSLALEAKTFKLKFGHRGLNHP-----SGlnqQVEITSQNHGFAVNLE 318

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 488288967 297 TIDPEKLLVTHVEVNDGTVEGVRHRDYPAFTVQYHPDAAPGPHDGLHLFDEFMELM 352
Cdd:CHL00197 319 SLAKNKFYITHFNLNDGTVAGISHSPKPYFSVQYHPEASPGPHDADYLFEYFIEII 374
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 172-349 7.78e-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: 328.30  E-value: 7.78e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967 172 VVVVDFGLKHSILRELSKRQCNLTVLPYNTTAEEILELSPDGVMLTNGPGDPKDVPEAIEMI-QAIQGKVPIFGICLGHQ 250
Cdd:cd01744    1 VVVIDFGVKHNILRELLKRGCEVTVVPYNTDAEEILKLDPDGIFLSNGPGDPALLDEAIKTVrKLLGKKIPIFGICLGHQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967 251 LFSLANGADTYKMKFGHRGLNHPVREIATGRIDFTSQNHGYAVDEATIdPEKLLVTHVEVNDGTVEGVRHRDYPAFTVQY 330
Cdd:cd01744   81 LLALALGAKTYKMKFGHRGSNHPVKDLITGRVYITSQNHGYAVDPDSL-PGGLEVTHVNLNDGTVEGIRHKDLPVFSVQF 159

                        170
                 ....*....|....*....
gi 488288967 331 HPDAAPGPHDGLHLFDEFM 349
Cdd:cd01744  160 HPEASPGPHDTEYLFDEFL 178
PLN02771 PLN02771
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
 5-340 1.60e-113

carbamoyl-phosphate synthase (glutamine-hydrolyzing)


Pssm-ID: 178370 [Multi-domain]  Cd Length: 415  Bit Score: 336.57  E-value: 1.60e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967   5 LILEDGTVFEGKAFGAEGNVVGEVVFTTGMTGYQEAITDQSFNGQMITFTYPLVGNYGVNRDDYESIAPTCKGVIVKEHA 84
Cdd:PLN02771  59 LVLEDGSVWKAKSFGARGTQVGEVVFNTSLTGYQEILTDPSYAGQFVLMTNPHIGNTGVNFDDEESRQCFLAGLVIRSLS 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967  85 RVASNWRQQMTLDEFLKRKGIPGISGIDTRALTRKLRSAGTMKGSIidAVDDLPHAFDQLKAT----VMPKNQVAQVSTT 160
Cdd:PLN02771 139 ISTSNWRCTKTLGDYLAERNIMGIYDVDTRAITRRLREDGSLIGVL--STEDSKTDEELLKMSrswdIVGIDLISGVSCK 216

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967 161 KPYP---------------SPGIGRNVVVVDFGLKHSILRELSKRQCNLTVLPYNTTAEEILELSPDGVMLTNGPGDPKD 225
Cdd:PLN02771 217 SPYEwvdktnpewdfntnsRDGESYHVIAYDFGIKHNILRRLASYGCKITVVPSTWPASEALKMKPDGVLFSNGPGDPSA 296

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967 226 VPEAIEMIQAIQGKVPIFGICLGHQLFSLANGADTYKMKFGHRGLNHPVREIATGRIDFTSQNHGYAVDEATIdPEKLLV 305
Cdd:PLN02771 297 VPYAVETVKELLGKVPVFGICMGHQLLGQALGGKTFKMKFGHHGGNHPVRNNRTGRVEISAQNHNYAVDPASL-PEGVEV 375

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 488288967 306 THVEVNDGTVEGVrhrDYPAFTV---QYHPDAAPGPHD 340
Cdd:PLN02771 376 THVNLNDGSCAGL---AFPALNVmslQYHPEASPGPHD 410
CPSase_sm_chain smart01097
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 1-130 1.56e-90

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: 267.32  E-value: 1.56e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967     1 MKRLLILEDGTVFEGKAFGAEGNVVGEVVFTTGMTGYQEAITDQSFNGQMITFTYPLVGNYGVNRDDYESIAPTCKGVIV 80
Cdd:smart01097   1 MKAYLVLEDGTVFEGESFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNDEDFESDKIQVKGLVV 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 488288967    81 KEHARVASNWRQQMTLDEFLKRKGIPGISGIDTRALTRKLRSAGTMKGSI 130
Cdd:smart01097  81 RELSDEPSNWRSEQSLDEFLKENGIPGISGIDTRALTRKLREKGAMKGVI 130
CPSase_sm_chain pfam00988
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 5-130 2.10e-88

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: 261.49  E-value: 2.10e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967    5 LILEDGTVFEGKAFGAEGNVVGEVVFTTGMTGYQEAITDQSFNGQMITFTYPLVGNYGVNRDDYESIAPTCKGVIVKEHA 84
Cdd:pfam00988   1 LVLEDGTVFEGKSFGAAGSTVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNPEDFESDKIHVAGLVVREYS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 488288967   85 RVASNWRQQMTLDEFLKRKGIPGISGIDTRALTRKLRSAGTMKGSI 130
Cdd:pfam00988  81 DEPSNWRAEESLDEWLKEQGIPGISGVDTRALTRKIREKGAMKGVI 126
GATase pfam00117
Glutamine amidotransferase class-I;
173-351 6.68e-64

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 201.31  E-value: 6.68e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967  173 VVVDFGL--KHSILRELSKRQCNLTVLPYNTTAEEILELSPDGVMLTNGPGDPKDVPEAIEMIQ-AIQGKVPIFGICLGH 249
Cdd:pfam00117   1 LLIDNGDsfTYNLARALRELGVEVTVVPNDTPAEEILEENPDGIILSGGPGSPGAAGGAIEAIReARELKIPILGICLGH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967  250 QLFSLANGADTYKMK-FGHRGLNHPVRE------IATGRIDFTSQNHGYAVDEATIdPEKLLVTHVEVNDGTVEGVRHRD 322
Cdd:pfam00117  81 QLLALAFGGKVVKAKkFGHHGKNSPVGDdgcglfYGLPNVFIVRRYHSYAVDPDTL-PDGLEVTATSENDGTIMGIRHKK 159

                         170       180
                  ....*....|....*....|....*....
gi 488288967  323 YPAFTVQYHPDAAPGPHDGLHLFDEFMEL 351
Cdd:pfam00117 160 LPIFGVQFHPESILTPHGPEILFNFFIKA 188
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 184-349 2.45e-28

Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase (ASase). This group contains proteins similar to para-aminobenzoate (PABA) synthase and ASase. These enzymes catalyze similar reactions and produce similar products, PABA and ortho-aminobenzoate (anthranilate). Each enzyme is composed of non-identical subunits: a glutamine amidotransferase subunit (component II) and a subunit that produces an aminobenzoate products (component I). ASase catalyses the synthesis of anthranilate from chorismate and glutamine and is a tetrameric protein comprising two copies each of components I and II. Component II of ASase belongs to the family of triad GTases which hydrolyze glutamine and transfer nascent ammonia between the active sites. In some bacteria, such as Escherichia coli, component II can be much larger than in other organisms, due to the presence of phosphoribosyl-anthranilate transferase (PRTase) activity. PRTase catalyses the second step in tryptophan biosynthesis and results in the addition of 5-phosphoribosyl-1-pyrophosphate to anthranilate to create N-5'-phosphoribosyl-anthranilate. In E.coli, the first step in the conversion of chorismate to PABA involves two proteins: PabA and PabB which co-operate to transfer the amide nitrogen of glutamine to chorismate forming 4-amino-4 deoxychorismate (ADC). PabA acts as a glutamine amidotransferase, supplying an amino group to PabB, which carries out the amination reaction. A third protein PabC then mediates elimination of pyruvate and aromatization to give PABA. Several organisms have bipartite proteins containing fused domains homologous to PabA and PabB commonly called PABA synthases. These hybrid PABA synthases may produce ADC and not PABA.


Pssm-ID: 153214 [Multi-domain]  Cd Length: 184  Bit Score: 108.78  E-value: 2.45e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967 184 LRELskrQCNLTVLPYN-TTAEEILELSPDGVMLTNGPGDPKDVPEAIEMIQAIQGKVPIFGICLGHQLFSLANGADTYK 262
Cdd:cd01743   18 LREL---GAEVVVVRNDeITLEELELLNPDAIVISPGPGHPEDAGISLEIIRALAGKVPILGVCLGHQAIAEAFGGKVVR 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967 263 MKFGHRGLnhpVREIATGRIDFTSQN---------HGYAVDEATidPEKLLVTHVEVNDGTVEGVRHRDYPAFTVQYHPD 333
Cdd:cd01743   95 APEPMHGK---TSEIHHDGSGLFKGLpqpftvgryHSLVVDPDP--LPDLLEVTASTEDGVIMALRHRDLPIYGVQFHPE 169

                        170
                 ....*....|....*.
gi 488288967 334 AAPGPHdGLHLFDEFM 349
Cdd:cd01743  170 SILTEY-GLRLLENFL 184
PRK14607 PRK14607
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
201-349 4.51e-25

bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;


Pssm-ID: 237764 [Multi-domain]  Cd Length: 534  Bit Score: 105.95  E-value: 4.51e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967 201 TTAEEILELSPDGVMLTNGPGDPKDVPEAIEMIQAIQGKVPIFGICLGHQLFSLANGADTYKMKFGHRGLNHPVR----- 275
Cdd:PRK14607  35 ITIEEIEALNPSHIVISPGPGRPEEAGISVEVIRHFSGKVPILGVCLGHQAIGYAFGGKIVHAKRILHGKTSPIDhngkg 114

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488288967 276 --EIATGRIDFTsQNHGYAVDEATIdPEKLLVThVEVNDGTVEGVRHRDYPAFTVQYHPDAApGPHDGLHLFDEFM 349
Cdd:PRK14607 115 lfRGIPNPTVAT-RYHSLVVEEASL-PECLEVT-AKSDDGEIMGIRHKEHPIFGVQFHPESI-LTEEGKRILKNFL 186
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 184-332 5.38e-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: 97.42  E-value: 5.38e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967 184 LRELSkrqCNLTVLPYN-TTAEEILELSPDGVMLTNGPGDPKDVPEAIEMIQAIQGKVPIFGICLGHQLFSLANGADTYK 262
Cdd:COG0512   18 LGELG---AEVVVVRNDeITLEEIEALAPDGIVLSPGPGTPEEAGISLEVIRAFAGKIPILGVCLGHQAIGEAFGGKVVR 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967 263 MK-----------------FghRGLNHPVReiaTGRidftsqnhgY---AVDEATIdPEKLLVThVEVNDGTVEGVRHRD 322
Cdd:COG0512   95 APepmhgktspithdgsglF--AGLPNPFT---ATR---------YhslVVDRETL-PDELEVT-AWTEDGEIMGIRHRE 158

                        170
                 ....*....|
gi 488288967 323 YPAFTVQYHP 332
Cdd:COG0512  159 LPIEGVQFHP 168
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 202-351 5.41e-23

anthranilate synthase component II; Provisional


Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 94.43  E-value: 5.41e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967 202 TAEEILELSPDGVMLTNGPGDPKDVPEAIEMIQAIQGKVPIFGICLGHQLFSLANGAdtykmKFGHrglnhpVREIATGR 281
Cdd:PRK05670  35 TLEEIEALNPDAIVLSPGPGTPAEAGISLELIREFAGKVPILGVCLGHQAIGEAFGG-----KVVR------AKEIMHGK 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967 282 IDFTSQN-----------------HGYAVDEATIdPEKLLVThVEVNDGTVEGVRHRDYPAFTVQYHPDAApGPHDGLHL 344
Cdd:PRK05670 104 TSPIEHDgsgifaglpnpftvtryHSLVVDRESL-PDCLEVT-AWTDDGEIMGVRHKELPIYGVQFHPESI-LTEHGHKL 180


                 ....*..
gi 488288967 345 FDEFMEL 351
Cdd:PRK05670 181 LENFLEL 187
trpG_papA TIGR00566
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ...
 202-334 4.94e-19

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: 83.68  E-value: 4.94e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967  202 TAEEILELSPDGVMLTNGPGDPKDVPEAIEMIQAIQGKVPIFGICLGHQLFSLANGADTYKMKFGHRGLNHPVREIATGR 281
Cdd:TIGR00566  35 TLQEIEALLPLLIVISPGPCTPNEAGISLEAIRHFAGKLPILGVCLGHQAMGQAFGGDVVRANTVMHGKTSEIEHNGAGI 114

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 488288967  282 ID-----FTS-QNHGYAVDEATIdPEKLLVTHVEVNDGTVEGVRHRDYPAFTVQYHPDA 334
Cdd:TIGR00566 115 FRglfnpLTAtRYHSLVVEPETL-PTCFPVTAWEEENIEIMAIRHRDLPLEGVQFHPES 172
GATase1_GMP_Synthase cd01742
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ...
 172-348 5.63e-17

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: 77.96  E-value: 5.63e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967 172 VVVVDFGLK--HSILRELskRQCNLT--VLPYNTTAEEILELSPDGVMLTNGP------GDPKDVPEAIEMiqaiqgKVP 241
Cdd:cd01742    1 ILILDFGSQytHLIARRV--RELGVYseILPNTTPLEEIKLKNPKGIILSGGPssvyeeDAPRVDPEIFEL------GVP 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967 242 IFGICLGHQLFSLANGADTYKMK---FGHRGLNHPVREIATGRIDFTSQ---NHGyavDEATIDPEKLLVTHVEVNDGtV 315
Cdd:cd01742   73 VLGICYGMQLIAKALGGKVERGDkreYGKAEIEIDDSSPLFEGLPDEQTvwmSHG---DEVVKLPEGFKVIASSDNCP-V 148

                        170       180       190
                 ....*....|....*....|....*....|...
gi 488288967 316 EGVRHRDYPAFTVQYHPDAAPGPHdGLHLFDEF 348
Cdd:cd01742  149 AAIANEEKKIYGVQFHPEVTHTEK-GKEILKNF 180
guaA_Nterm TIGR00888
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ...
 172-348 1.16e-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: 76.97  E-value: 1.16e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967  172 VVVVDFGLK--HSILRELSKRQCNLTVLPYNTTAEEILELSPDGVMLTNGPGD--PKDVPEAIEMIqaIQGKVPIFGICL 247
Cdd:TIGR00888   1 ILVLDFGSQytQLIARRLRELGVYSELVPNTTPLEEIREKNPKGIILSGGPSSvyAENAPRADEKI--FELGVPVLGICY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967  248 GHQLFSLANG---ADTYKMKFG------------HRGLNhpvreiatgrIDFTS-QNHGyavDEATIDPEKLLVthVEVN 311
Cdd:TIGR00888  79 GMQLMAKQLGgevGRAEKREYGkaeleildeddlFRGLP----------DESTVwMSHG---DKVKELPEGFKV--LATS 143

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 488288967  312 DGT-VEGVRHRDYPAFTVQYHPDAAPGPHdGLHLFDEF 348
Cdd:TIGR00888 144 DNCpVAAMAHEEKPIYGVQFHPEVTHTEY-GNELLENF 180
PRK07649 PRK07649
aminodeoxychorismate/anthranilate synthase component II;
202-350 3.67e-16

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181066 [Multi-domain]  Cd Length: 195  Bit Score: 76.00  E-value: 3.67e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967 202 TAEEILELSPDGVMLTNGPGDPKDVPEAIEMIQAIQGKVPIFGICLGHQLFSLANGADTYK----MKFGHRGLNHPVREI 277
Cdd:PRK07649  35 TISDIENMKPDFLMISPGPCSPNEAGISMEVIRYFAGKIPIFGVCLGHQSIAQVFGGEVVRaerlMHGKTSLMHHDGKTI 114

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488288967 278 ATGRID-FT-SQNHGYAVDEATIdPEKLLVThVEVNDGTVEGVRHRDYPAFTVQYHPDAAPGPHdGLHLFDEFME 350
Cdd:PRK07649 115 FSDIPNpFTaTRYHSLIVKKETL-PDCLEVT-SWTEEGEIMAIRHKTLPIEGVQFHPESIMTSH-GKELLQNFIR 186
PLN02335 PLN02335
anthranilate synthase
 202-359 7.43e-16

anthranilate synthase


Pssm-ID: 177969 [Multi-domain]  Cd Length: 222  Bit Score: 75.60  E-value: 7.43e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967 202 TAEEILELSPDGVMLTNGPGDPKDVPEAIEMIQAIQGKVPIFGICLGHQLFSLANGADTYKMKFG--HrGLNHPVR---E 276
Cdd:PLN02335  54 TVEELKRKNPRGVLISPGPGTPQDSGISLQTVLELGPLVPLFGVCMGLQCIGEAFGGKIVRSPFGvmH-GKSSPVHydeK 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967 277 IATGRID-----FTS-QNHGYAVDEATIDPEKLLVThVEVNDGTVEGVRHRDYPAFT-VQYHPDAAPGPhDGLHLFDEFM 349
Cdd:PLN02335 133 GEEGLFSglpnpFTAgRYHSLVIEKDTFPSDELEVT-AWTEDGLIMAARHRKYKHIQgVQFHPESIITT-EGKTIVRNFI 210

                        170
                 ....*....|
gi 488288967 350 ELMDAWKEQN 359
Cdd:PLN02335 211 KIIEKKESEK 220
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 172-332 2.85e-14

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: 71.13  E-value: 2.85e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967 172 VVVVDFGLKHS-----ILRELSKRQCNLTV--------LPYNTTAEEilelsPDGVMLTNGPGDPKD----VPEAIEMI- 233
Cdd:COG0518    2 ILILDHDPFGGqypglIARRLREAGIELDVlrvyageiLPYDPDLED-----PDGLILSGGPMSVYDedpwLEDEPALIr 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967 234 QAIQGKVPIFGICLGHQLFSLANGADTYKmkfghrglnHPVREIATGRIDFTSQN---------------HGYAVDEAti 298
Cdd:COG0518   77 EAFELGKPVLGICYGAQLLAHALGGKVEP---------GPGREIGWAPVELTEADplfaglpdeftvwmsHGDTVTEL-- 145

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 488288967 299 dPE--KLLVThvevNDGT-VEGVRHRDyPAFTVQYHP 332
Cdd:COG0518  146 -PEgaEVLAS----SDNCpNQAFRYGR-RVYGVQFHP 176
PRK06774 PRK06774
aminodeoxychorismate synthase component II;
204-350 3.12e-14

aminodeoxychorismate synthase component II;


Pssm-ID: 180689 [Multi-domain]  Cd Length: 191  Bit Score: 70.28  E-value: 3.12e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967 204 EEILELSPDGVMLTNGPGDPKDVPEAIEMIQAIQGKVPIFGICLGHQLFSLANGADTYKMK---------FGH------R 268
Cdd:PRK06774  37 TDIEQLAPSHLVISPGPCTPNEAGISLAVIRHFADKLPILGVCLGHQALGQAFGARVVRARqvmhgktsaICHsgqgvfR 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967 269 GLNHPVReiatgridfTSQNHGYAVDEATIdPEKLLVTHVEVNDGTVE---GVRHRDYPAFTVQYHPDAAPGpHDGLHLF 345
Cdd:PRK06774 117 GLNQPLT---------VTRYHSLVIAADSL-PGCFELTAWSERGGEMDeimGIRHRTLPLEGVQFHPESILS-EQGHQLL 185


                 ....*
gi 488288967 346 DEFME 350
Cdd:PRK06774 186 DNFLK 190
PRK07765 PRK07765
aminodeoxychorismate/anthranilate synthase component II;
212-333 4.58e-14

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181107 [Multi-domain]  Cd Length: 214  Bit Score: 70.46  E-value: 4.58e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967 212 DGVMLTNGPGDPKDVPEAIEMIQAI-QGKVPIFGICLGHQLFSLANGADTYKMKFGHRGLNHPVREIATGRID-----FT 285
Cdd:PRK07765  48 DGVLLSPGPGTPERAGASIDMVRACaAAGTPLLGVCLGHQAIGVAFGATVDRAPELLHGKTSSVHHTGVGVLAglpdpFT 127

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 488288967 286 -SQNHGYAVDEATIdPEKLLVThVEVNDGTVEGVRHRDYPAFTVQYHPD 333
Cdd:PRK07765 128 aTRYHSLTILPETL-PAELEVT-ARTDSGVIMAVRHRELPIHGVQFHPE 174
PRK08007 PRK08007
aminodeoxychorismate synthase component 2;
202-334 6.09e-13

aminodeoxychorismate synthase component 2;


Pssm-ID: 181194 [Multi-domain]  Cd Length: 187  Bit Score: 66.48  E-value: 6.09e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967 202 TAEEILELSPDGVMLTNGPGDPKDVPEAIEMIQAIQGKVPIFGICLGHQLFSLANGADTYKMKFGHRGLNHPVREIATGR 281
Cdd:PRK08007  35 TLADIDALKPQKIVISPGPCTPDEAGISLDVIRHYAGRLPILGVCLGHQAMAQAFGGKVVRAAKVMHGKTSPITHNGEGV 114

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 488288967 282 ID------FTSQNHGYAVDEATIdPEKLLVThVEVNDGTVEGVRHRDYPAFTVQYHPDA 334
Cdd:PRK08007 115 FRglanplTVTRYHSLVVEPDSL-PACFEVT-AWSETREIMGIRHRQWDLEGVQFHPES 171
PRK13566 PRK13566
anthranilate synthase component I;
143-332 1.89e-12

anthranilate synthase component I;


Pssm-ID: 237429 [Multi-domain]  Cd Length: 720  Bit Score: 68.40  E-value: 1.89e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967 143 QLKATVM--------PKNQVAQVsttKPYPSPGIGRNVVVVDFglKHSILRELSK--RQCNLTVlpynTT-----AEEIL 207
Cdd:PRK13566 495 ELKASALlqalrgakPKNLSAEE---PDAAAVGEGKRVLLVDH--EDSFVHTLANyfRQTGAEV----TTvrygfAEEML 565

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967 208 -ELSPDGVMLTNGPGDPKD--VPEAIEmiQAIQGKVPIFGICLGHQ---------LFSLANGADTYKMKFGHRG----LN 271
Cdd:PRK13566 566 dRVNPDLVVLSPGPGRPSDfdCKATID--AALARNLPIFGVCLGLQaiveafggeLGQLAYPMHGKPSRIRVRGpgrlFS 643

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488288967 272 HPVREIATGRIdftsqnHGYAVDEATIdPEKLLVThVEVNDGTVEGVRHRDYPAFTVQYHP 332
Cdd:PRK13566 644 GLPEEFTVGRY------HSLFADPETL-PDELLVT-AETEDGVIMAIEHKTLPVAAVQFHP 696
PRK08857 PRK08857
aminodeoxychorismate/anthranilate synthase component II;
206-334 2.48e-12

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181566 [Multi-domain]  Cd Length: 193  Bit Score: 64.90  E-value: 2.48e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967 206 ILELSPDGVMLTNGPGDPKDVPEAIEMIQAIQGKVPIFGICLGHQLFSLANGADTYKMKFGHRGLNHPVREiaTGRIDFT 285
Cdd:PRK08857  39 IEALNPTHLVISPGPCTPNEAGISLQAIEHFAGKLPILGVCLGHQAIAQVFGGQVVRARQVMHGKTSPIRH--TGRSVFK 116

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488288967 286 SQN--------HGYAVDEATIdPEKLLVTH-VEVNDGTVE---GVRHRDYPAFTVQYHPDA 334
Cdd:PRK08857 117 GLNnpltvtryHSLVVKNDTL-PECFELTAwTELEDGSMDeimGFQHKTLPIEAVQFHPES 176
trpG CHL00101
anthranilate synthase component 2
 205-351 2.73e-12

anthranilate synthase component 2


Pssm-ID: 214365 [Multi-domain]  Cd Length: 190  Bit Score: 64.75  E-value: 2.73e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967 205 EILELSPDGVMLTNGPGDPKDVPEAIEMIQAIQGKVPIFGICLGHQLFSLANGADTYKM---------------KFGHRG 269
Cdd:CHL00101  38 KIKNLNIRHIIISPGPGHPRDSGISLDVISSYAPYIPILGVCLGHQSIGYLFGGKIIKApkpmhgktskiyhnhDDLFQG 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967 270 LNHPVreIATgridftsQNHGYAVDEATIdPEKLLVThVEVNDGTVEGVRHRDYPA-FTVQYHPDAAPGPHdGLHLFDEF 348
Cdd:CHL00101 118 LPNPF--TAT-------RYHSLIIDPLNL-PSPLEIT-AWTEDGLIMACRHKKYKMlRGIQFHPESLLTTH-GQQILRNF 185


                 ...
gi 488288967 349 MEL 351
Cdd:CHL00101 186 LSL 188
PRK05637 PRK05637
anthranilate synthase component II; Provisional
 193-338 2.48e-11

anthranilate synthase component II; Provisional


Pssm-ID: 180178 [Multi-domain]  Cd Length: 208  Bit Score: 62.55  E-value: 2.48e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967 193 NLTVLPYNTTAEEILELSPDGVMLTNGPGDPKDVPEAIEMIQAIQGKVPIFGICLGHQLFSLANGAD----------TYK 262
Cdd:PRK05637  27 KCTVFRNTVPVEEILAANPDLICLSPGPGHPRDAGNMMALIDRTLGQIPLLGICLGFQALLEHHGGKvepcgpvhgtTDN 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967 263 MKFGHRGLNHPV-----------REIATGRIDFTSQNHGYAVDEATIDPEKLLVTHVEVNDGTVeGVRHRDYPAFTVQYH 331
Cdd:PRK05637 107 MILTDAGVQSPVfaglatdvepdHPEIPGRKVPIARYHSLGCVVAPDGMESLGTCSSEIGPVIM-AAETTDGKAIGLQFH 185


                 ....*..
gi 488288967 332 PDAAPGP 338
Cdd:PRK05637 186 PESVLSP 192
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 196-348 7.85e-11

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


Pssm-ID: 153216 [Multi-domain]  Cd Length: 189  Bit Score: 60.67  E-value: 7.85e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967 196 VLPYNTTAEEILELSP--DGVMLT-----------------NGPGDPK-DVPEaIEMIQ-AIQGKVPIFGICLGHQLFSL 254
Cdd:cd01745   37 LLPPVDDEEDLEQYLEllDGLLLTgggdvdpplygeephpeLGPIDPErDAFE-LALLRaALERGKPILGICRGMQLLNV 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967 255 ANGADTYkmkfghrglnhpvREIATGRIdftsqnHGYAVDEAtidPEKLLVTHVEvNDGTVEGVRHRDYP-AFTVQYHPD 333
Cdd:cd01745  116 ALGGTLY-------------QDIRVNSL------HHQAIKRL---ADGLRVEARA-PDGVIEAIESPDRPfVLGVQWHPE 172

                        170
                 ....*....|....*.
gi 488288967 334 -AAPGPHDGLHLFDEF 348
Cdd:cd01745  173 wLADTDPDSLKLFEAF 188
PRK00758 PRK00758
GMP synthase subunit A; Validated
 172-351 1.87e-10

GMP synthase subunit A; Validated


Pssm-ID: 179112 [Multi-domain]  Cd Length: 184  Bit Score: 59.48  E-value: 1.87e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967 172 VVVVDFG--LKHSILRELSKRQCNLTVLPYNTTAEEILELsPDGVMLTNGPgDPKDVPEAIEMIQAIqgKVPIFGICLGH 249
Cdd:PRK00758   2 IVVVDNGgqYNHLIHRTLRYLGVDAKIIPNTTPVEEIKAF-EDGLILSGGP-DIERAGNCPEYLKEL--DVPILGICLGH 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967 250 QLFSLANGADTYKMKFGhrglnhpvrEIATGRIDFTSQN---HGYA---------VDEATIDPEKLLVT-HVEVNDgtVE 316
Cdd:PRK00758  78 QLIAKAFGGEVGRGEYG---------EYALVEVEILDEDdilKGLPpeirvwashADEVKELPDGFEILaRSDICE--VE 146

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 488288967 317 GVRHRDYPAFTVQYHPDAAPGPHdGLHLFDEFMEL 351
Cdd:PRK00758 147 AMKHKEKPIYGVQFHPEVAHTEY-GEEIFKNFLEI 180
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 184-335 3.25e-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: 58.80  E-value: 3.25e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967 184 LRELSKRQCNLTVlpYNTTAEEILE--LSPDGVMLTNGPGDPKD-----VPEAIEMI-QAIQGKVPIFGICLGHQLFSLA 255
Cdd:cd01741   20 LREAGAETIEIDV--VDVYAGELLPdlDDYDGLVILGGPMSVDEddypwLKKLKELIrQALAAGKPVLGICLGHQLLARA 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967 256 NGADTYKMKFGhrglnhpvREIATGRIDFTSQNHGYAVDEATIDPEKLLVTH----VEVNDGTV----------EGVRHR 321
Cdd:cd01741   98 LGGKVGRNPKG--------WEIGWFPVTLTEAGKADPLFAGLPDEFPVFHWHgdtvVELPPGAVllasseacpnQAFRYG 169

                        170
                 ....*....|....
gi 488288967 322 DYpAFTVQYHPDAA 335
Cdd:cd01741  170 DR-ALGLQFHPEER 182
guaA PRK00074
GMP synthase; Reviewed
 172-251 1.54e-09

GMP synthase; Reviewed


Pssm-ID: 234614 [Multi-domain]  Cd Length: 511  Bit Score: 59.29  E-value: 1.54e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967 172 VVVVDFGLKHSIL-----REL---SKrqcnltVLPYNTTAEEILELSPDGVMLTNGP------GDPKdVPEAIemiqaIQ 237
Cdd:PRK00074   6 ILILDFGSQYTQLiarrvRELgvySE------IVPYDISAEEIRAFNPKGIILSGGPasvyeeGAPR-ADPEI-----FE 73

                         90
                 ....*....|....
gi 488288967 238 GKVPIFGICLGHQL 251
Cdd:PRK00074  74 LGVPVLGICYGMQL 87
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 172-251 3.06e-09

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: 54.14  E-value: 3.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967 172 VVVVDFG-----LKHSILRELSKRQCNLTVLPYNTTAEEILELS--PDGVMLTNGPGDPKDVPEAIEMIQAIQ----GKV 240
Cdd:cd01653    1 VAVLLFPgfeelELASPLDALREAGAEVDVVSPDGGPVESDVDLddYDGLILPGGPGTPDDLARDEALLALLReaaaAGK 80

                         90
                 ....*....|.
gi 488288967 241 PIFGICLGHQL 251
Cdd:cd01653   81 PILGICLGAQL 91
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 196-332 4.74e-09

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: 55.73  E-value: 4.74e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967  196 VLPYNT---TAEEILELSpDGVMLTNGP--------------GDPKDVP-EAIEMI---QAIQGKVPIFGICLGHQLFSL 254
Cdd:pfam07722  42 LLPILGdpeDAAAILDRL-DGLLLTGGPnvdphfygeepsesGGPYDPArDAYELAlirAALARGKPILGICRGFQLLNV 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967  255 ANGADTY---KMKFGHRGLNHPVREIatgrIDFTSQN-----------------------HGYAVDEAtidPEKLLVTHV 308
Cdd:pfam07722 121 ALGGTLYqdiQEQPGFTDHREHCQVA----PYAPSHAvnvepgsllasllgseefrvnslHHQAIDRL---APGLRVEAV 193

                         170       180
                  ....*....|....*....|....*.
gi 488288967  309 EvNDGTVEGVRHRDYPAFT--VQYHP 332
Cdd:pfam07722 194 A-PDGTIEAIESPNAKGFAlgVQWHP 218
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 172-251 6.14e-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: 52.59  E-value: 6.14e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967 172 VVVVDFGLK-----HSILRELSKRQCNLTVLPYNTTAEEILEL--SPDGVMLTNGPGDPKDVPEAIEMIQAIQ----GKV 240
Cdd:cd03128    1 VAVLLFGGSeelelASPLDALREAGAEVDVVSPDGGPVESDVDldDYDGLILPGGPGTPDDLAWDEALLALLReaaaAGK 80

                         90
                 ....*....|.
gi 488288967 241 PIFGICLGHQL 251
Cdd:cd03128   81 PVLGICLGAQL 91
PRK09522 PRK09522
bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate ...
 197-334 1.92e-08

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


Pssm-ID: 181927 [Multi-domain]  Cd Length: 531  Bit Score: 55.80  E-value: 1.92e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967 197 LPYNTTAEEILELSPDGVMLTNGPGDPKDVPEAIEMIQAIQGKVPIFGICLGHQLFslangADTYKMKFGHRGlnhpvrE 276
Cdd:PRK09522  35 IPAQTLIERLATMSNPVLMLSPGPGVPSEAGCMPELLTRLRGKLPIIGICLGHQAI-----VEAYGGYVGQAG------E 103

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488288967 277 IATGRIDFTSQNhGYAVDEATIDPEKLLVTH----------VEVN---DGTVEGVRHRDYPAFTVQYHPDA 334
Cdd:PRK09522 104 ILHGKASSIEHD-GQAMFAGLTNPLPVARYHslvgsnipagLTINahfNGMVMAVRHDADRVCGFQFHPES 173
PuuD COG2071
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ...
 196-350 9.67e-08

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: 52.09  E-value: 9.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967 196 VLPYNTTAEEILELSP--DGVMLT-----------------NGPGDPK-DVPEaIEMIQ-AIQGKVPIFGICLGHQLFSL 254
Cdd:COG2071   33 LLPPVGDEEDLDELLDrlDGLVLTggadvdpalygeephpeLGPIDPErDAFE-LALIRaALERGKPVLGICRGMQLLNV 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967 255 ANGadtykmkfghrGLNHP-VREIATGRIDFTSQNHGYAVD-EATIDPEKLL-----VTHVEVN---------------- 311
Cdd:COG2071  112 ALG-----------GTLYQdLPDQVPGALDHRQPAPRYAPRhTVEIEPGSRLarilgEEEIRVNslhhqavkrlgpglrv 180

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 488288967 312 -----DGTVEGVRHRDYPaFT--VQYHP--DAAPGPHDgLHLFDEFME 350
Cdd:COG2071  181 sarapDGVIEAIESPGAP-FVlgVQWHPewLAASDPLS-RRLFEAFVE 226
PRK06895 PRK06895
anthranilate synthase component II;
214-334 7.84e-07

anthranilate synthase component II;


Pssm-ID: 235882 [Multi-domain]  Cd Length: 190  Bit Score: 48.97  E-value: 7.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967 214 VMLTNGPGDPKDVPEAIEMIQAIQGKVPIFGICLGHQLFSLANGADTYKMKFGHRGLNHPVREIATGRIDF---TSQN-- 288
Cdd:PRK06895  47 ILISPGPDVPRAYPQLFAMLERYHQHKSILGVCLGHQTLCEFFGGELYNLNNVRHGQQRPLKVRSNSPLFDglpEEFNig 126

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 488288967 289 --HGYAVDEATIdPEKLLVThVEVNDGTVEGVRHRDYPAFTVQYHPDA 334
Cdd:PRK06895 127 lyHSWAVSEENF-PTPLEIT-AVCDENVVMAMQHKTLPIYGVQFHPES 172
PLN02347 PLN02347
GMP synthetase
 172-359 7.29e-06

GMP synthetase


Pssm-ID: 215197 [Multi-domain]  Cd Length: 536  Bit Score: 47.76  E-value: 7.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967 172 VVVVDFGLK--HSILRELskRQCNL--TVLPYNTTAEEILELSPDGVMLTNGP------GDPKDVPEAIEMIQAiqGKVP 241
Cdd:PLN02347  13 VLILDYGSQytHLITRRV--RELGVysLLLSGTASLDRIASLNPRVVILSGGPhsvhveGAPTVPEGFFDYCRE--RGVP 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967 242 IFGICLGHQLFSLANGAdtyKMKFGHRGL--NHPVREIATGRI-----DFTSQN----HGyavDEATIDPEKLLVTHVEV 310
Cdd:PLN02347  89 VLGICYGMQLIVQKLGG---EVKPGEKQEygRMEIRVVCGSQLfgdlpSGETQTvwmsHG---DEAVKLPEGFEVVAKSV 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 488288967 311 NdGTVEGVRHRDYPAFTVQYHPDAAPGPHdGLHLFDEFM----ELMDAWKEQN 359
Cdd:PLN02347 163 Q-GAVVAIENRERRIYGLQYHPEVTHSPK-GMETLRHFLfdvcGVTADWKMQD 213
GATase1_Glutamyl_Hydrolase cd01747
Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase; Type 1 ...
 196-336 1.19e-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: 43.08  E-value: 1.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967 196 VLP--YNTTAEEILEL--SPDGVMLTNGPGDPKDVP--EAIEMI--QAIQ-----GKVPIFGICLGHQLFS-LANGADTY 261
Cdd:cd01747   36 VVPiwINESEEYYDKLfkSINGILFPGGAVDIDTSGyaRTAKIIynLALErndagDYFPVWGTCLGFELLTyLTSGETLL 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288967 262 KMKFGHRGLNHPV--REIAT-----GRID-----------FTSQNHGYAV-------DEATIDPEKLLVTHVEVNDGT-V 315
Cdd:cd01747  116 LEATEATNSALPLnfTEDALqsrlfKRFPpdllkslatepLTMNNHRYGIspenfteNGLLSDFFNVLTTNDDWNGVEfI 195

                        170       180
                 ....*....|....*....|.
gi 488288967 316 EGVRHRDYPAFTVQYHPDAAP 336
Cdd:cd01747  196 STVEAYKYPIYGVQWHPEKNA 216
 
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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