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Conserved domains on  [gi|489666608|ref|WP_003570893|]
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carbamoyl phosphate synthase small subunit [Lacticaseibacillus paracasei]

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 ...
 1-351 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: 652.09  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608   1 MKRYLILEDGSVFPGVGFGAETVTTGEIVFNTGMSGYQETITDQSYNGQIITFTQPLIGNVGINRDDYESIDPTAKGIVV 80
Cdd:COG0505    3 MKALLVLEDGTVFEGKSFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVTFTYPHIGNYGVNDEDFESDRPWVAGLVV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608  81 RDVARVTGNWRSQMTLDEFLKRKHIPGISGVDTRALTKKIREVGAMKASIV--DAADEHAFDQLKAL--VLPKNQVQQVS 156
Cdd:COG0505   83 RELSRRPSNWRSEESLDEYLKEHGIPGISGIDTRALTRHLREKGAMKGVIStgDLDIEELLEKARAApgMEGLDLVKEVS 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608 157 TQQAY---PAPGTGRNVVVIDFGLKHSILRELAKRQCNVTVLPATTTASTILELAPDGVMLTNGPGDPKDVPEALDMIRG 233
Cdd:COG0505  163 TKEPYewtEAPGAGFHVVALDFGVKRNILRELAERGCRVTVVPATTSAEEILALNPDGVFLSNGPGDPAALDYAIETIRE 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608 234 VEGK-IPLFGICLGHQLFALANGANTFKMKYGHRGFNHPVREIATGRIDFTSQNHGYAVDPDSIDPDTLLITHVEINDGT 312
Cdd:COG0505  243 LLGKgIPIFGICLGHQLLALALGAKTYKLKFGHRGANHPVKDLETGRVEITSQNHGFAVDEDSLPATDLEVTHVNLNDGT 322

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 489666608 313 VEGLRHRLYPAFTVQFHPDAAPGPHDADHLFDEFMEMMD 351
Cdd:COG0505  323 VEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDRFIELME 361
 
Name Accession Description Interval E-value
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 1-351 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: 652.09  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608   1 MKRYLILEDGSVFPGVGFGAETVTTGEIVFNTGMSGYQETITDQSYNGQIITFTQPLIGNVGINRDDYESIDPTAKGIVV 80
Cdd:COG0505    3 MKALLVLEDGTVFEGKSFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVTFTYPHIGNYGVNDEDFESDRPWVAGLVV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608  81 RDVARVTGNWRSQMTLDEFLKRKHIPGISGVDTRALTKKIREVGAMKASIV--DAADEHAFDQLKAL--VLPKNQVQQVS 156
Cdd:COG0505   83 RELSRRPSNWRSEESLDEYLKEHGIPGISGIDTRALTRHLREKGAMKGVIStgDLDIEELLEKARAApgMEGLDLVKEVS 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608 157 TQQAY---PAPGTGRNVVVIDFGLKHSILRELAKRQCNVTVLPATTTASTILELAPDGVMLTNGPGDPKDVPEALDMIRG 233
Cdd:COG0505  163 TKEPYewtEAPGAGFHVVALDFGVKRNILRELAERGCRVTVVPATTSAEEILALNPDGVFLSNGPGDPAALDYAIETIRE 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608 234 VEGK-IPLFGICLGHQLFALANGANTFKMKYGHRGFNHPVREIATGRIDFTSQNHGYAVDPDSIDPDTLLITHVEINDGT 312
Cdd:COG0505  243 LLGKgIPIFGICLGHQLLALALGAKTYKLKFGHRGANHPVKDLETGRVEITSQNHGFAVDEDSLPATDLEVTHVNLNDGT 322

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 489666608 313 VEGLRHRLYPAFTVQFHPDAAPGPHDADHLFDEFMEMMD 351
Cdd:COG0505  323 VEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDRFIELME 361
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
1-350 0e+00

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 649.06  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608   1 MKRYLILEDGSVFPGVGFGAETVTTGEIVFNTGMSGYQETITDQSYNGQIITFTQPLIGNVGINRDDYESIDPTAKGIVV 80
Cdd:PRK12564   3 MKAYLVLEDGTVFEGKAFGAEGETVGEVVFNTSMTGYQEILTDPSYAGQIVTFTYPLIGNYGVNREDFESDRPHAKGLIV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608  81 RDVARVTGNWRSQMTLDEFLKRKHIPGISGVDTRALTKKIREVGAMKASIVDAAD--EHAFDQLKAL--VLPKNQVQQVS 156
Cdd:PRK12564  83 RELSDIPSNWRSEMSLDEYLKENGIPGISGIDTRALTRKLREKGAMKGVIATEDFdaEELLEKARAFpgLLGLDLVKEVS 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608 157 TQQAYPAPGTG----RNVVVIDFGLKHSILRELAKRQCNVTVLPATTTASTILELAPDGVMLTNGPGDPKDVPEALDMIR 232
Cdd:PRK12564 163 TKEPYPWPGPGgelkYKVVAIDFGVKRNILRELAERGCRVTVVPATTTAEEILALNPDGVFLSNGPGDPAALDYAIEMIR 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608 233 GV-EGKIPLFGICLGHQLFALANGANTFKMKYGHRGFNHPVREIATGRIDFTSQNHGYAVDPDSIdPDTLLITHVEINDG 311
Cdd:PRK12564 243 ELlEKKIPIFGICLGHQLLALALGAKTYKMKFGHRGANHPVKDLETGKVEITSQNHGFAVDEDSL-PANLEVTHVNLNDG 321

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 489666608 312 TVEGLRHRLYPAFTVQFHPDAAPGPHDADHLFDEFMEMM 350
Cdd:PRK12564 322 TVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDEFVELM 360
CPSaseIIsmall TIGR01368
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ...
 3-352 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: 557.24  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608    3 RYLILEDGSVFPGVGFGAETVTTGEIVFNTGMSGYQETITDQSYNGQIITFTQPLIGNVGINRDDYESIDPTAKGIVVRD 82
Cdd:TIGR01368   1 AYLVLEDGTVFRGYSFGAEGTVAGEVVFNTGMTGYQEILTDPSYKGQIVVFTYPLIGNYGVNDEDAESKGIHVSGLVVRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608   83 VARVTGNWRSQMTLDEFLKRKHIPGISGVDTRALTKKIREVGAMKASIVDAADEHAFDQLKALVLPKNQ----VQQVSTQ 158
Cdd:TIGR01368  81 LSDRYSNWRATESLDQFLKRHGIPGIYGVDTRALVKKIREKGTMKGVISTEDSNDEELVEKARVSPDITginlVAEVSTK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608  159 QAYP---APGTGRNVVVIDFGLKHSILRELAKRQCNVTVLPATTTASTILELAPDGVMLTNGPGDPKDVPEALDMIRGVE 235
Cdd:TIGR01368 161 EPYTwgqRGGKGKRVVVIDFGVKRNILRRLVKRGCEVTVVPYDTDAEEIKKYNPDGIFLSNGPGDPAAVEPAIETIRKLL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608  236 GKIPLFGICLGHQLFALANGANTFKMKYGHRGFNHPVREIATGRIDFTSQNHGYAVDPDSIDPDTLLITHVEINDGTVEG 315
Cdd:TIGR01368 241 EKIPIFGICLGHQLLALAFGAKTYKMKFGHRGGNHPVKDLITGRVEITSQNHGYAVDPDSLPAGDLEVTHVNLNDGTVEG 320

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 489666608  316 LRHRLYPAFTVQFHPDAAPGPHDADHLFDEFMEMMDA 352
Cdd:TIGR01368 321 IRHKDLPVFSVQYHPEASPGPHDTEYLFDEFIDLMKK 357
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 170-347 9.99e-111

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: 320.21  E-value: 9.99e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608 170 VVVIDFGLKHSILRELAKRQCNVTVLPATTTASTILELAPDGVMLTNGPGDPKDVPEALDMIRGV-EGKIPLFGICLGHQ 248
Cdd:cd01744    1 VVVIDFGVKHNILRELLKRGCEVTVVPYNTDAEEILKLDPDGIFLSNGPGDPALLDEAIKTVRKLlGKKIPIFGICLGHQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608 249 LFALANGANTFKMKYGHRGFNHPVREIATGRIDFTSQNHGYAVDPDSIdPDTLLITHVEINDGTVEGLRHRLYPAFTVQF 328
Cdd:cd01744   81 LLALALGAKTYKMKFGHRGSNHPVKDLITGRVYITSQNHGYAVDPDSL-PGGLEVTHVNLNDGTVEGIRHKDLPVFSVQF 159

                        170
                 ....*....|....*....
gi 489666608 329 HPDAAPGPHDADHLFDEFM 347
Cdd:cd01744  160 HPEASPGPHDTEYLFDEFL 178
CPSase_sm_chain smart01097
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 1-130 3.28e-87

Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase domain is in the amino terminus of protein. Carbamoyl-phosphate synthase catalyses the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesise carbamoyl phosphate. The small chain has a GATase domain in the carboxyl terminus.


Pssm-ID: 198165 [Multi-domain]  Cd Length: 130  Bit Score: 258.84  E-value: 3.28e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608     1 MKRYLILEDGSVFPGVGFGAETVTTGEIVFNTGMSGYQETITDQSYNGQIITFTQPLIGNVGINRDDYESIDPTAKGIVV 80
Cdd:smart01097   1 MKAYLVLEDGTVFEGESFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNDEDFESDKIQVKGLVV 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 489666608    81 RDVARVTGNWRSQMTLDEFLKRKHIPGISGVDTRALTKKIREVGAMKASI 130
Cdd:smart01097  81 RELSDEPSNWRSEQSLDEFLKENGIPGISGIDTRALTRKLREKGAMKGVI 130
CPSase_sm_chain pfam00988
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 5-130 1.11e-84

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: 252.25  E-value: 1.11e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608    5 LILEDGSVFPGVGFGAETVTTGEIVFNTGMSGYQETITDQSYNGQIITFTQPLIGNVGINRDDYESIDPTAKGIVVRDVA 84
Cdd:pfam00988   1 LVLEDGTVFEGKSFGAAGSTVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNPEDFESDKIHVAGLVVREYS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 489666608   85 RVTGNWRSQMTLDEFLKRKHIPGISGVDTRALTKKIREVGAMKASI 130
Cdd:pfam00988  81 DEPSNWRAEESLDEWLKEQGIPGISGVDTRALTRKIREKGAMKGVI 126
 
Name Accession Description Interval E-value
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 1-351 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: 652.09  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608   1 MKRYLILEDGSVFPGVGFGAETVTTGEIVFNTGMSGYQETITDQSYNGQIITFTQPLIGNVGINRDDYESIDPTAKGIVV 80
Cdd:COG0505    3 MKALLVLEDGTVFEGKSFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVTFTYPHIGNYGVNDEDFESDRPWVAGLVV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608  81 RDVARVTGNWRSQMTLDEFLKRKHIPGISGVDTRALTKKIREVGAMKASIV--DAADEHAFDQLKAL--VLPKNQVQQVS 156
Cdd:COG0505   83 RELSRRPSNWRSEESLDEYLKEHGIPGISGIDTRALTRHLREKGAMKGVIStgDLDIEELLEKARAApgMEGLDLVKEVS 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608 157 TQQAY---PAPGTGRNVVVIDFGLKHSILRELAKRQCNVTVLPATTTASTILELAPDGVMLTNGPGDPKDVPEALDMIRG 233
Cdd:COG0505  163 TKEPYewtEAPGAGFHVVALDFGVKRNILRELAERGCRVTVVPATTSAEEILALNPDGVFLSNGPGDPAALDYAIETIRE 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608 234 VEGK-IPLFGICLGHQLFALANGANTFKMKYGHRGFNHPVREIATGRIDFTSQNHGYAVDPDSIDPDTLLITHVEINDGT 312
Cdd:COG0505  243 LLGKgIPIFGICLGHQLLALALGAKTYKLKFGHRGANHPVKDLETGRVEITSQNHGFAVDEDSLPATDLEVTHVNLNDGT 322

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 489666608 313 VEGLRHRLYPAFTVQFHPDAAPGPHDADHLFDEFMEMMD 351
Cdd:COG0505  323 VEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDRFIELME 361
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
1-350 0e+00

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 649.06  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608   1 MKRYLILEDGSVFPGVGFGAETVTTGEIVFNTGMSGYQETITDQSYNGQIITFTQPLIGNVGINRDDYESIDPTAKGIVV 80
Cdd:PRK12564   3 MKAYLVLEDGTVFEGKAFGAEGETVGEVVFNTSMTGYQEILTDPSYAGQIVTFTYPLIGNYGVNREDFESDRPHAKGLIV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608  81 RDVARVTGNWRSQMTLDEFLKRKHIPGISGVDTRALTKKIREVGAMKASIVDAAD--EHAFDQLKAL--VLPKNQVQQVS 156
Cdd:PRK12564  83 RELSDIPSNWRSEMSLDEYLKENGIPGISGIDTRALTRKLREKGAMKGVIATEDFdaEELLEKARAFpgLLGLDLVKEVS 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608 157 TQQAYPAPGTG----RNVVVIDFGLKHSILRELAKRQCNVTVLPATTTASTILELAPDGVMLTNGPGDPKDVPEALDMIR 232
Cdd:PRK12564 163 TKEPYPWPGPGgelkYKVVAIDFGVKRNILRELAERGCRVTVVPATTTAEEILALNPDGVFLSNGPGDPAALDYAIEMIR 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608 233 GV-EGKIPLFGICLGHQLFALANGANTFKMKYGHRGFNHPVREIATGRIDFTSQNHGYAVDPDSIdPDTLLITHVEINDG 311
Cdd:PRK12564 243 ELlEKKIPIFGICLGHQLLALALGAKTYKMKFGHRGANHPVKDLETGKVEITSQNHGFAVDEDSL-PANLEVTHVNLNDG 321

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 489666608 312 TVEGLRHRLYPAFTVQFHPDAAPGPHDADHLFDEFMEMM 350
Cdd:PRK12564 322 TVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDEFVELM 360
PRK12838 PRK12838
carbamoyl phosphate synthase small subunit; Reviewed
 1-350 0e+00

carbamoyl phosphate synthase small subunit; Reviewed


Pssm-ID: 183784 [Multi-domain]  Cd Length: 354  Bit Score: 595.72  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608   1 MKRYLILEDGSVFPGVGFGAETVTTGEIVFNTGMSGYQETITDQSYNGQIITFTQPLIGNVGINRDDYESIDPTAKGIVV 80
Cdd:PRK12838   1 MKAYLILEDGTVFEGELIGAPIDVTGEIVFNTGMTGYQEVLTDPSYKGQIVVFTYPLIGNYGINADDYESKQPQVKGVIV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608  81 RDVARVTGNWRSQMTLDEFLKRKHIPGISGVDTRALTKKIREVGAMKASIVDAADEHAFDQLKALVLPKNQVQQVSTQQA 160
Cdd:PRK12838  81 YELSREGSHYRAKQSLDDFLKEWNIPGISGVDTRALVKHIREKGTMKASITTTDDAHAFDQIKALVLPKNVVAQVSTKEP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608 161 YPAPGTGRNVVVIDFGLKHSILRELAKRQCNVTVLPATTTASTILELAPDGVMLTNGPGDPKDVPEALDMIRGVEGKIPL 240
Cdd:PRK12838 161 YTYGNGGKHVALIDFGYKKSILRSLSKRGCKVTVLPYDTSLEEIKNLNPDGIVLSNGPGDPKELQPYLPEIKKLISSYPI 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608 241 FGICLGHQLFALANGANTFKMKYGHRGFNHPVREIATGRIDFTSQNHGYAVDPDSIDPDTLLITHVEINDGTVEGLRHRL 320
Cdd:PRK12838 241 LGICLGHQLIALALGADTEKLPFGHRGANHPVIDLTTGRVWMTSQNHGYVVDEDSLDGTPLSVRFFNVNDGSIEGLRHKK 320

                        330       340       350
                 ....*....|....*....|....*....|
gi 489666608 321 YPAFTVQFHPDAAPGPHDADHLFDEFMEMM 350
Cdd:PRK12838 321 KPVLSVQFHPEAHPGPHDAEYIFDEFLEMM 350
CPSaseIIsmall TIGR01368
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ...
 3-352 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: 557.24  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608    3 RYLILEDGSVFPGVGFGAETVTTGEIVFNTGMSGYQETITDQSYNGQIITFTQPLIGNVGINRDDYESIDPTAKGIVVRD 82
Cdd:TIGR01368   1 AYLVLEDGTVFRGYSFGAEGTVAGEVVFNTGMTGYQEILTDPSYKGQIVVFTYPLIGNYGVNDEDAESKGIHVSGLVVRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608   83 VARVTGNWRSQMTLDEFLKRKHIPGISGVDTRALTKKIREVGAMKASIVDAADEHAFDQLKALVLPKNQ----VQQVSTQ 158
Cdd:TIGR01368  81 LSDRYSNWRATESLDQFLKRHGIPGIYGVDTRALVKKIREKGTMKGVISTEDSNDEELVEKARVSPDITginlVAEVSTK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608  159 QAYP---APGTGRNVVVIDFGLKHSILRELAKRQCNVTVLPATTTASTILELAPDGVMLTNGPGDPKDVPEALDMIRGVE 235
Cdd:TIGR01368 161 EPYTwgqRGGKGKRVVVIDFGVKRNILRRLVKRGCEVTVVPYDTDAEEIKKYNPDGIFLSNGPGDPAAVEPAIETIRKLL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608  236 GKIPLFGICLGHQLFALANGANTFKMKYGHRGFNHPVREIATGRIDFTSQNHGYAVDPDSIDPDTLLITHVEINDGTVEG 315
Cdd:TIGR01368 241 EKIPIFGICLGHQLLALAFGAKTYKMKFGHRGGNHPVKDLITGRVEITSQNHGYAVDPDSLPAGDLEVTHVNLNDGTVEG 320

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 489666608  316 LRHRLYPAFTVQFHPDAAPGPHDADHLFDEFMEMMDA 352
Cdd:TIGR01368 321 IRHKDLPVFSVQYHPEASPGPHDTEYLFDEFIDLMKK 357
carA CHL00197
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
 5-355 9.43e-131

carbamoyl-phosphate synthase arginine-specific small subunit; Provisional


Pssm-ID: 214392 [Multi-domain]  Cd Length: 382  Bit Score: 379.14  E-value: 9.43e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608   5 LILEDGSVFPGVGFGAETVTTGEIVFNTGMSGYQETITDQSYNGQIITFTQPLIGNVGINRDDYESIDPTAKGIVVRDVA 84
Cdd:CHL00197   9 LVLEDGTYYRGWSFSNPITTIGEVVFNTGMTGYQEIITDPSYFEQIVTFTYPEIGNTGINLEDIESVKIQVKGIIAKNIC 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608  85 RVTGNWRSQMTLDEFLKRKHIPGISGVDTRALTKKIREVGAMKASIVDAADEHAFDQLKALVLPKNQ----VQQVSTQQA 160
Cdd:CHL00197  89 KSSSNWRQQESLVSYLQRHKIPFIFGIDTRALTQHLRRFGTMNGCISNQNLNLSYLRAKIKESPHMPssdlIPRVTTSSY 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608 161 Y-----------------PAPGTGRNVVVIDFGLKHSILRELAKRQCNVTVLPATTTASTILELAPDGVMLTNGPGDPKD 223
Cdd:CHL00197 169 YewdekshpsfyladnkrPHSSYQLKIIVIDFGVKYNILRRLKSFGCSITVVPATSPYQDILSYQPDGILLSNGPGDPSA 248

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608 224 VPEALDMIRG-VEGKIPLFGICLGHQLFALANGANTFKMKYGHRGFNHPvreiaTG---RIDFTSQNHGYAVDPDSIDPD 299
Cdd:CHL00197 249 IHYGIKTVKKlLKYNIPIFGICMGHQILSLALEAKTFKLKFGHRGLNHP-----SGlnqQVEITSQNHGFAVNLESLAKN 323

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489666608 300 TLLITHVEINDGTVEGLRHRLYPAFTVQFHPDAAPGPHDADHLFDEFMEMMDAFSN 355
Cdd:CHL00197 324 KFYITHFNLNDGTVAGISHSPKPYFSVQYHPEASPGPHDADYLFEYFIEIIKHSKS 379
PLN02771 PLN02771
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
 5-343 4.33e-112

carbamoyl-phosphate synthase (glutamine-hydrolyzing)


Pssm-ID: 178370 [Multi-domain]  Cd Length: 415  Bit Score: 332.71  E-value: 4.33e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608   5 LILEDGSVFPGVGFGAETVTTGEIVFNTGMSGYQETITDQSYNGQIITFTQPLIGNVGINRDDYESIDPTAKGIVVRDVA 84
Cdd:PLN02771  59 LVLEDGSVWKAKSFGARGTQVGEVVFNTSLTGYQEILTDPSYAGQFVLMTNPHIGNTGVNFDDEESRQCFLAGLVIRSLS 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608  85 RVTGNWRSQMTLDEFLKRKHIPGISGVDTRALTKKIREVGAMkASIVDAADEHAFDQLKAL-----VLPKNQVQQVSTQQ 159
Cdd:PLN02771 139 ISTSNWRCTKTLGDYLAERNIMGIYDVDTRAITRRLREDGSL-IGVLSTEDSKTDEELLKMsrswdIVGIDLISGVSCKS 217

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608 160 AYP---------------APGTGRNVVVIDFGLKHSILRELAKRQCNVTVLPATTTASTILELAPDGVMLTNGPGDPKDV 224
Cdd:PLN02771 218 PYEwvdktnpewdfntnsRDGESYHVIAYDFGIKHNILRRLASYGCKITVVPSTWPASEALKMKPDGVLFSNGPGDPSAV 297

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608 225 PEALDMIRGVEGKIPLFGICLGHQLFALANGANTFKMKYGHRGFNHPVREIATGRIDFTSQNHGYAVDPDSIdPDTLLIT 304
Cdd:PLN02771 298 PYAVETVKELLGKVPVFGICMGHQLLGQALGGKTFKMKFGHHGGNHPVRNNRTGRVEISAQNHNYAVDPASL-PEGVEVT 376

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 489666608 305 HVEINDGTVEGLRhrlYPAFTV---QFHPDAAPGPHDADHLF 343
Cdd:PLN02771 377 HVNLNDGSCAGLA---FPALNVmslQYHPEASPGPHDSDNAF 415
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 170-347 9.99e-111

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: 320.21  E-value: 9.99e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608 170 VVVIDFGLKHSILRELAKRQCNVTVLPATTTASTILELAPDGVMLTNGPGDPKDVPEALDMIRGV-EGKIPLFGICLGHQ 248
Cdd:cd01744    1 VVVIDFGVKHNILRELLKRGCEVTVVPYNTDAEEILKLDPDGIFLSNGPGDPALLDEAIKTVRKLlGKKIPIFGICLGHQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608 249 LFALANGANTFKMKYGHRGFNHPVREIATGRIDFTSQNHGYAVDPDSIdPDTLLITHVEINDGTVEGLRHRLYPAFTVQF 328
Cdd:cd01744   81 LLALALGAKTYKMKFGHRGSNHPVKDLITGRVYITSQNHGYAVDPDSL-PGGLEVTHVNLNDGTVEGIRHKDLPVFSVQF 159

                        170
                 ....*....|....*....
gi 489666608 329 HPDAAPGPHDADHLFDEFM 347
Cdd:cd01744  160 HPEASPGPHDTEYLFDEFL 178
CPSase_sm_chain smart01097
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 1-130 3.28e-87

Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase domain is in the amino terminus of protein. Carbamoyl-phosphate synthase catalyses the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesise carbamoyl phosphate. The small chain has a GATase domain in the carboxyl terminus.


Pssm-ID: 198165 [Multi-domain]  Cd Length: 130  Bit Score: 258.84  E-value: 3.28e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608     1 MKRYLILEDGSVFPGVGFGAETVTTGEIVFNTGMSGYQETITDQSYNGQIITFTQPLIGNVGINRDDYESIDPTAKGIVV 80
Cdd:smart01097   1 MKAYLVLEDGTVFEGESFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNDEDFESDKIQVKGLVV 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 489666608    81 RDVARVTGNWRSQMTLDEFLKRKHIPGISGVDTRALTKKIREVGAMKASI 130
Cdd:smart01097  81 RELSDEPSNWRSEQSLDEFLKENGIPGISGIDTRALTRKLREKGAMKGVI 130
CPSase_sm_chain pfam00988
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 5-130 1.11e-84

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: 252.25  E-value: 1.11e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608    5 LILEDGSVFPGVGFGAETVTTGEIVFNTGMSGYQETITDQSYNGQIITFTQPLIGNVGINRDDYESIDPTAKGIVVRDVA 84
Cdd:pfam00988   1 LVLEDGTVFEGKSFGAAGSTVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNPEDFESDKIHVAGLVVREYS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 489666608   85 RVTGNWRSQMTLDEFLKRKHIPGISGVDTRALTKKIREVGAMKASI 130
Cdd:pfam00988  81 DEPSNWRAEESLDEWLKEQGIPGISGVDTRALTRKIREKGAMKGVI 126
GATase pfam00117
Glutamine amidotransferase class-I;
171-349 5.13e-62

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 196.69  E-value: 5.13e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608  171 VVIDFGL--KHSILRELAKRQCNVTVLPATTTASTILELAPDGVMLTNGPGDPKDVPEALDMIR-GVEGKIPLFGICLGH 247
Cdd:pfam00117   1 LLIDNGDsfTYNLARALRELGVEVTVVPNDTPAEEILEENPDGIILSGGPGSPGAAGGAIEAIReARELKIPILGICLGH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608  248 QLFALANGANTFKMK-YGHRGFNHPVRE------IATGRIDFTSQNHGYAVDPDSIdPDTLLITHVEINDGTVEGLRHRL 320
Cdd:pfam00117  81 QLLALAFGGKVVKAKkFGHHGKNSPVGDdgcglfYGLPNVFIVRRYHSYAVDPDTL-PDGLEVTATSENDGTIMGIRHKK 159

                         170       180
                  ....*....|....*....|....*....
gi 489666608  321 YPAFTVQFHPDAAPGPHDADHLFDEFMEM 349
Cdd:pfam00117 160 LPIFGVQFHPESILTPHGPEILFNFFIKA 188
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 170-330 3.62e-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: 103.00  E-value: 3.62e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608 170 VVVID------FGLKHsILRELakrQCNVTVLPATTTASTILELA-PDGVMLTNGPGDPKDVPEALDMIRGVEGKIPLFG 242
Cdd:cd01743    1 ILLIDnydsftYNLVQ-YLREL---GAEVVVVRNDEITLEELELLnPDAIVISPGPGHPEDAGISLEIIRALAGKVPILG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608 243 ICLGHQLFALANGANTFKMKYGHRGFnhpVREIATGRIDFTSQN---------HGYAVDPDSiDPDTLLITHVEiNDGTV 313
Cdd:cd01743   77 VCLGHQAIAEAFGGKVVRAPEPMHGK---TSEIHHDGSGLFKGLpqpftvgryHSLVVDPDP-LPDLLEVTAST-EDGVI 151

                        170
                 ....*....|....*..
gi 489666608 314 EGLRHRLYPAFTVQFHP 330
Cdd:cd01743  152 MALRHRDLPIYGVQFHP 168
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 170-330 3.30e-24

Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 440278 [Multi-domain]  Cd Length: 189  Bit Score: 97.80  E-value: 3.30e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608 170 VVVID------FGLKHsILRELAkrqCNVTVLPAT-TTASTILELAPDGVMLTNGPGDPKDVPEALDMIRGVEGKIPLFG 242
Cdd:COG0512    1 ILLIDnydsftYNLVQ-YLGELG---AEVVVVRNDeITLEEIEALAPDGIVLSPGPGTPEEAGISLEVIRAFAGKIPILG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608 243 ICLGHQLFALANGANTFKMKYGHRGFNHPVR------------EIATGRidftsqnhgY---AVDPDSIdPDTLLIT-HV 306
Cdd:COG0512   77 VCLGHQAIGEAFGGKVVRAPEPMHGKTSPIThdgsglfaglpnPFTATR---------YhslVVDRETL-PDELEVTaWT 146

                        170       180
                 ....*....|....*....|....
gi 489666608 307 EinDGTVEGLRHRLYPAFTVQFHP 330
Cdd:COG0512  147 E--DGEIMGIRHRELPIEGVQFHP 168
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 204-330 1.84e-20

anthranilate synthase component II; Provisional


Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 87.49  E-value: 1.84e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608 204 ILELAPDGVMLTNGPGDPKDVPEALDMIRGVEGKIPLFGICLGHQLFALANGAntfkmKYGHrgfnhpVREIATGRIDFT 283
Cdd:PRK05670  39 IEALNPDAIVLSPGPGTPAEAGISLELIREFAGKVPILGVCLGHQAIGEAFGG-----KVVR------AKEIMHGKTSPI 107

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489666608 284 SQN-----------------HGYAVDPDSIdPDTLLIThVEINDGTVEGLRHRLYPAFTVQFHP 330
Cdd:PRK05670 108 EHDgsgifaglpnpftvtryHSLVVDRESL-PDCLEVT-AWTDDGEIMGVRHKELPIYGVQFHP 169
PRK14607 PRK14607
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
194-347 3.15e-19

bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;


Pssm-ID: 237764 [Multi-domain]  Cd Length: 534  Bit Score: 88.62  E-value: 3.15e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608 194 VLPATTTASTILELAPDGVMLTNGPGDPKDVPEALDMIRGVEGKIPLFGICLGHQLFALANGANTFKMKYGHRGFNHPVR 273
Cdd:PRK14607  30 VRNDEITIEEIEALNPSHIVISPGPGRPEEAGISVEVIRHFSGKVPILGVCLGHQAIGYAFGGKIVHAKRILHGKTSPID 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608 274 -------EIATGRIDFTsQNHGYAVDPDSIdPDTLLIThVEINDGTVEGLRHRLYPAFTVQFHPDAApGPHDADHLFDEF 346
Cdd:PRK14607 110 hngkglfRGIPNPTVAT-RYHSLVVEEASL-PECLEVT-AKSDDGEIMGIRHKEHPIFGVQFHPESI-LTEEGKRILKNF 185


                 .
gi 489666608 347 M 347
Cdd:PRK14607 186 L 186
trpG_papA TIGR00566
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ...
 200-332 7.23e-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: 83.30  E-value: 7.23e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608  200 TASTILELAPDGVMLTNGPGDPKDVPEALDMIRGVEGKIPLFGICLGHQLFALANGANTFKMKYGHRGFNHPVREIATGR 279
Cdd:TIGR00566  35 TLQEIEALLPLLIVISPGPCTPNEAGISLEAIRHFAGKLPILGVCLGHQAMGQAFGGDVVRANTVMHGKTSEIEHNGAGI 114

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 489666608  280 ID-----FTS-QNHGYAVDPDSIdPDTLLITHVEINDGTVEGLRHRLYPAFTVQFHPDA 332
Cdd:TIGR00566 115 FRglfnpLTAtRYHSLVVEPETL-PTCFPVTAWEEENIEIMAIRHRDLPLEGVQFHPES 172
PRK13566 PRK13566
anthranilate synthase component I;
132-330 2.31e-15

anthranilate synthase component I;


Pssm-ID: 237429 [Multi-domain]  Cd Length: 720  Bit Score: 77.26  E-value: 2.31e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608 132 DAADEHAFDQLKALVL--------PKNQVqqvSTQQAYPAPGTGRNVVVIDFglKHSILRELAK--RQ--CNVTVLPATT 199
Cdd:PRK13566 486 DPEAEEAETELKASALlqalrgakPKNLS---AEEPDAAAVGEGKRVLLVDH--EDSFVHTLANyfRQtgAEVTTVRYGF 560

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608 200 TASTILELAPDGVMLTNGPGDPKD--VPEALDmiRGVEGKIPLFGICLGHQ---------LFALANGANTFKMKYGHRG- 267
Cdd:PRK13566 561 AEEMLDRVNPDLVVLSPGPGRPSDfdCKATID--AALARNLPIFGVCLGLQaiveafggeLGQLAYPMHGKPSRIRVRGp 638

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489666608 268 ---FNHPVREIATGRIdftsqnHGYAVDPDSIdPDTLLIThVEINDGTVEGLRHRLYPAFTVQFHP 330
Cdd:PRK13566 639 grlFSGLPEEFTVGRY------HSLFADPETL-PDELLVT-AETEDGVIMAIEHKTLPVAAVQFHP 696
PRK08007 PRK08007
aminodeoxychorismate synthase component 2;
200-332 2.37e-15

aminodeoxychorismate synthase component 2;


Pssm-ID: 181194 [Multi-domain]  Cd Length: 187  Bit Score: 73.41  E-value: 2.37e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608 200 TASTILELAPDGVMLTNGPGDPKDVPEALDMIRGVEGKIPLFGICLGHQLFALANGANTFKMKYGHRGFNHPVREIATGR 279
Cdd:PRK08007  35 TLADIDALKPQKIVISPGPCTPDEAGISLDVIRHYAGRLPILGVCLGHQAMAQAFGGKVVRAAKVMHGKTSPITHNGEGV 114

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489666608 280 ID------FTSQNHGYAVDPDSIdPDTLLITHVEiNDGTVEGLRHRLYPAFTVQFHPDA 332
Cdd:PRK08007 115 FRglanplTVTRYHSLVVEPDSL-PACFEVTAWS-ETREIMGIRHRQWDLEGVQFHPES 171
PRK07765 PRK07765
aminodeoxychorismate/anthranilate synthase component II;
210-331 3.68e-15

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181107 [Multi-domain]  Cd Length: 214  Bit Score: 73.54  E-value: 3.68e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608 210 DGVMLTNGPGDPKDVPEALDMIRGVEG-KIPLFGICLGHQLFALANGANTFKMKYGHRGFNHPVREIATGRID-----FT 283
Cdd:PRK07765  48 DGVLLSPGPGTPERAGASIDMVRACAAaGTPLLGVCLGHQAIGVAFGATVDRAPELLHGKTSSVHHTGVGVLAglpdpFT 127

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 489666608 284 -SQNHGYAVDPDSIdPDTLLIThVEINDGTVEGLRHRLYPAFTVQFHPD 331
Cdd:PRK07765 128 aTRYHSLTILPETL-PAELEVT-ARTDSGVIMAVRHRELPIHGVQFHPE 174
GATase1_GMP_Synthase cd01742
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ...
 170-330 3.84e-15

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: 72.57  E-value: 3.84e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608 170 VVVIDFGLK--HSILRELakRQCNVT--VLPATTTASTILELAPDGVMLTNGP------GDPKDVPEALDMirgvegKIP 239
Cdd:cd01742    1 ILILDFGSQytHLIARRV--RELGVYseILPNTTPLEEIKLKNPKGIILSGGPssvyeeDAPRVDPEIFEL------GVP 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608 240 LFGICLGHQLFALANGANTFKMKygHRGFNHPVREIATGRIDFTSQ--------NHGyavdpDSID--PDTLLITHVEIN 309
Cdd:cd01742   73 VLGICYGMQLIAKALGGKVERGD--KREYGKAEIEIDDSSPLFEGLpdeqtvwmSHG-----DEVVklPEGFKVIASSDN 145

                        170       180
                 ....*....|....*....|.
gi 489666608 310 DGtVEGLRHRLYPAFTVQFHP 330
Cdd:cd01742  146 CP-VAAIANEEKKIYGVQFHP 165
PRK07649 PRK07649
aminodeoxychorismate/anthranilate synthase component II;
200-332 4.07e-15

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181066 [Multi-domain]  Cd Length: 195  Bit Score: 72.91  E-value: 4.07e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608 200 TASTILELAPDGVMLTNGPGDPKDVPEALDMIRGVEGKIPLFGICLGHQLFALANGANTFKMKYGHRGFNHPVREiaTGR 279
Cdd:PRK07649  35 TISDIENMKPDFLMISPGPCSPNEAGISMEVIRYFAGKIPIFGVCLGHQSIAQVFGGEVVRAERLMHGKTSLMHH--DGK 112

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489666608 280 IDFT--------SQNHGYAVDPDSIdPDTLLIThVEINDGTVEGLRHRLYPAFTVQFHPDA 332
Cdd:PRK07649 113 TIFSdipnpftaTRYHSLIVKKETL-PDCLEVT-SWTEEGEIMAIRHKTLPIEGVQFHPES 171
PRK06774 PRK06774
aminodeoxychorismate synthase component II;
204-332 3.27e-14

aminodeoxychorismate synthase component II;


Pssm-ID: 180689 [Multi-domain]  Cd Length: 191  Bit Score: 70.28  E-value: 3.27e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608 204 ILELAPDGVMLTNGPGDPKDVPEALDMIRGVEGKIPLFGICLGHQLFALANGANTFKMKYGHRGFNHPVREIATG----- 278
Cdd:PRK06774  39 IEQLAPSHLVISPGPCTPNEAGISLAVIRHFADKLPILGVCLGHQALGQAFGARVVRARQVMHGKTSAICHSGQGvfrgl 118

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 489666608 279 -RIDFTSQNHGYAVDPDSIdPDTLLITHVEINDGTVE---GLRHRLYPAFTVQFHPDA 332
Cdd:PRK06774 119 nQPLTVTRYHSLVIAADSL-PGCFELTAWSERGGEMDeimGIRHRTLPLEGVQFHPES 175
PLN02335 PLN02335
anthranilate synthase
 200-332 8.91e-14

anthranilate synthase


Pssm-ID: 177969 [Multi-domain]  Cd Length: 222  Bit Score: 69.83  E-value: 8.91e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608 200 TASTILELAPDGVMLTNGPGDPKDVPEALDMIRGVEGKIPLFGICLGHQLFALANGANTFKMKYG--HrGFNHPVR---E 274
Cdd:PLN02335  54 TVEELKRKNPRGVLISPGPGTPQDSGISLQTVLELGPLVPLFGVCMGLQCIGEAFGGKIVRSPFGvmH-GKSSPVHydeK 132

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489666608 275 IATGRID-----FTS-QNHGYAVDPDSIDPDTLLIThVEINDGTVEGLRHRLYPAFT-VQFHPDA 332
Cdd:PLN02335 133 GEEGLFSglpnpFTAgRYHSLVIEKDTFPSDELEVT-AWTEDGLIMAARHRKYKHIQgVQFHPES 196
guaA_Nterm TIGR00888
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ...
 170-331 2.21e-13

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: 67.72  E-value: 2.21e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608  170 VVVIDFGLK--HSILRELAKRQCNVTVLPATTTASTILELAPDGVMLTNGPGD--PKDVPEALDMIrgVEGKIPLFGICL 245
Cdd:TIGR00888   1 ILVLDFGSQytQLIARRLRELGVYSELVPNTTPLEEIREKNPKGIILSGGPSSvyAENAPRADEKI--FELGVPVLGICY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608  246 GHQLFALANGANTfkMKYGHRGFNHPVREIATGRIDFTSQN--------HGYAVD--PDSIDpdtlLITHVEINDgtVEG 315
Cdd:TIGR00888  79 GMQLMAKQLGGEV--GRAEKREYGKAELEILDEDDLFRGLPdestvwmsHGDKVKelPEGFK----VLATSDNCP--VAA 150

                         170
                  ....*....|....*.
gi 489666608  316 LRHRLYPAFTVQFHPD 331
Cdd:TIGR00888 151 MAHEEKPIYGVQFHPE 166
PRK08857 PRK08857
aminodeoxychorismate/anthranilate synthase component II;
204-332 2.22e-12

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181566 [Multi-domain]  Cd Length: 193  Bit Score: 65.28  E-value: 2.22e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608 204 ILELAPDGVMLTNGPGDPKDVPEALDMIRGVEGKIPLFGICLGHQLFALANGANTFKMKYGHRGFNHPVREiaTGRIDFT 283
Cdd:PRK08857  39 IEALNPTHLVISPGPCTPNEAGISLQAIEHFAGKLPILGVCLGHQAIAQVFGGQVVRARQVMHGKTSPIRH--TGRSVFK 116

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489666608 284 SQN--------HGYAVDPDSIdPDTLLITH-VEINDGTVE---GLRHRLYPAFTVQFHPDA 332
Cdd:PRK08857 117 GLNnpltvtryHSLVVKNDTL-PECFELTAwTELEDGSMDeimGFQHKTLPIEAVQFHPES 176
trpG CHL00101
anthranilate synthase component 2
 200-332 5.19e-12

anthranilate synthase component 2


Pssm-ID: 214365 [Multi-domain]  Cd Length: 190  Bit Score: 63.98  E-value: 5.19e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608 200 TASTILELAPDGVMLTNGPGDPKDVPEALDMIRGVEGKIPLFGICLGHQLFALANGANTFKmkyghrgfnhpVREIATGR 279
Cdd:CHL00101  35 DLSKIKNLNIRHIIISPGPGHPRDSGISLDVISSYAPYIPILGVCLGHQSIGYLFGGKIIK-----------APKPMHGK 103

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489666608 280 I-------DFTSQN----------HGYAVDPDSIdPDTLLIT-HVEinDGTVEGLRHRLYPA-FTVQFHPDA 332
Cdd:CHL00101 104 TskiyhnhDDLFQGlpnpftatryHSLIIDPLNL-PSPLEITaWTE--DGLIMACRHKKYKMlRGIQFHPES 172
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 170-330 9.38e-12

GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP synthase, glutamine amidotransferase domain is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 440284 [Multi-domain]  Cd Length: 225  Bit Score: 63.81  E-value: 9.38e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608 170 VVVIDFGLKHS-----ILRELAKRQCNVTV--------LPATTTAStilelAPDGVMLTNGPGDPKD----VPEALDMIR 232
Cdd:COG0518    2 ILILDHDPFGGqypglIARRLREAGIELDVlrvyageiLPYDPDLE-----DPDGLILSGGPMSVYDedpwLEDEPALIR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608 233 G-VEGKIPLFGICLGHQLFALANGANTFKmkyghrgfnHPVREIATGRIDFTSQN---------------HGYAVdpDSI 296
Cdd:COG0518   77 EaFELGKPVLGICYGAQLLAHALGGKVEP---------GPGREIGWAPVELTEADplfaglpdeftvwmsHGDTV--TEL 145

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 489666608 297 dPD--TLLIThveiNDGT-VEGLRHRLyPAFTVQFHP 330
Cdd:COG0518  146 -PEgaEVLAS----SDNCpNQAFRYGR-RVYGVQFHP 176
PRK00758 PRK00758
GMP synthase subunit A; Validated
 170-349 3.09e-10

GMP synthase subunit A; Validated


Pssm-ID: 179112 [Multi-domain]  Cd Length: 184  Bit Score: 58.71  E-value: 3.09e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608 170 VVVIDFG--LKHSILRELAKRQCNVTVLPATTTASTILELaPDGVMLTNGP-----GDPKDVPEALDmirgvegkIPLFG 242
Cdd:PRK00758   2 IVVVDNGgqYNHLIHRTLRYLGVDAKIIPNTTPVEEIKAF-EDGLILSGGPdieraGNCPEYLKELD--------VPILG 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608 243 ICLGHQLFALANGANTFKMKYGhrgfnhpvreiatgridftsqnhGYA-VDPDSIDPDTLLI----------TH----VE 307
Cdd:PRK00758  73 ICLGHQLIAKAFGGEVGRGEYG-----------------------EYAlVEVEILDEDDILKglppeirvwaSHadevKE 129

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 489666608 308 INDG----------TVEGLRHRLYPAFTVQFHPDAAPGPHDADhLFDEFMEM 349
Cdd:PRK00758 130 LPDGfeilarsdicEVEAMKHKEKPIYGVQFHPEVAHTEYGEE-IFKNFLEI 180
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 182-333 7.29e-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: 57.64  E-value: 7.29e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608 182 LRELAKRQCNVTVLPATTTASTILELAPDGVMLTNGPGDPKD-----VPEALDMIRGV-EGKIPLFGICLGHQLFALANG 255
Cdd:cd01741   20 LREAGAETIEIDVVDVYAGELLPDLDDYDGLVILGGPMSVDEddypwLKKLKELIRQAlAAGKPVLGICLGHQLLARALG 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608 256 ANTFKMKYGhrgfnhpvREIATGRIDFTSQnhGYAVDPDSIDPDTLLI------THVEINDGTV----------EGLRhr 319
Cdd:cd01741  100 GKVGRNPKG--------WEIGWFPVTLTEA--GKADPLFAGLPDEFPVfhwhgdTVVELPPGAVllasseacpnQAFR-- 167

                        170
                 ....*....|....*.
gi 489666608 320 lYP--AFTVQFHPDAA 333
Cdd:cd01741  168 -YGdrALGLQFHPEER 182
PRK05637 PRK05637
anthranilate synthase component II; Provisional
 191-272 2.96e-09

anthranilate synthase component II; Provisional


Pssm-ID: 180178 [Multi-domain]  Cd Length: 208  Bit Score: 56.39  E-value: 2.96e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608 191 NVTVLPATTTASTILELAPDGVMLTNGPGDPKDVPEALDMIRGVEGKIPLFGICLGHQLFALANGAN----------TFK 260
Cdd:PRK05637  27 KCTVFRNTVPVEEILAANPDLICLSPGPGHPRDAGNMMALIDRTLGQIPLLGICLGFQALLEHHGGKvepcgpvhgtTDN 106

                         90
                 ....*....|..
gi 489666608 261 MKYGHRGFNHPV 272
Cdd:PRK05637 107 MILTDAGVQSPV 118
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 170-253 4.19e-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: 53.76  E-value: 4.19e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608 170 VVVIDFG-----LKHSILRELAKRQCNVTVLPATTTASTILELA--PDGVMLTNGPGDPKDVPEALDMIRGV----EGKI 238
Cdd:cd01653    1 VAVLLFPgfeelELASPLDALREAGAEVDVVSPDGGPVESDVDLddYDGLILPGGPGTPDDLARDEALLALLreaaAAGK 80

                         90
                 ....*....|....*
gi 489666608 239 PLFGICLGHQLFALA 253
Cdd:cd01653   81 PILGICLGAQLLVLG 95
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 170-249 1.91e-08

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: 51.43  E-value: 1.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608 170 VVVIDFGLK-----HSILRELAKRQCNVTVLPATTTASTILELA--PDGVMLTNGPGDPKDVPEALDMIRGV----EGKI 238
Cdd:cd03128    1 VAVLLFGGSeelelASPLDALREAGAEVDVVSPDGGPVESDVDLddYDGLILPGGPGTPDDLAWDEALLALLreaaAAGK 80

                         90
                 ....*....|.
gi 489666608 239 PLFGICLGHQL 249
Cdd:cd03128   81 PVLGICLGAQL 91
guaA PRK00074
GMP synthase; Reviewed
 170-255 4.75e-08

GMP synthase; Reviewed


Pssm-ID: 234614 [Multi-domain]  Cd Length: 511  Bit Score: 54.67  E-value: 4.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608 170 VVVIDFG-----LkhsILRELakRQCNV--TVLPATTTASTILELAPDGVMLTNGP------GDPKDVPEALDMirgveg 236
Cdd:PRK00074   6 ILILDFGsqytqL---IARRV--RELGVysEIVPYDISAEEIRAFNPKGIILSGGPasvyeeGAPRADPEIFEL------ 74

                         90
                 ....*....|....*....
gi 489666608 237 KIPLFGICLGHQLFALANG 255
Cdd:PRK00074  75 GVPVLGICYGMQLMAHQLG 93
PRK09522 PRK09522
bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate ...
 191-332 2.40e-07

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


Pssm-ID: 181927 [Multi-domain]  Cd Length: 531  Bit Score: 52.34  E-value: 2.40e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608 191 NVTVLPATTTASTILE----LAPDGVMLTNGPGDPKDVPEALDMIRGVEGKIPLFGICLGHQLFALANGantfkmkyGHR 266
Cdd:PRK09522  27 NVVIYRNHIPAQTLIErlatMSNPVLMLSPGPGVPSEAGCMPELLTRLRGKLPIIGICLGHQAIVEAYG--------GYV 98

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489666608 267 GfnhPVREIATGRIDFTSQNhGYAVDPDSIDPDTLLITH----------VEIN---DGTVEGLRHRLYPAFTVQFHPDA 332
Cdd:PRK09522  99 G---QAGEILHGKASSIEHD-GQAMFAGLTNPLPVARYHslvgsnipagLTINahfNGMVMAVRHDADRVCGFQFHPES 173
PRK06895 PRK06895
anthranilate synthase component II;
212-332 3.77e-07

anthranilate synthase component II;


Pssm-ID: 235882 [Multi-domain]  Cd Length: 190  Bit Score: 49.74  E-value: 3.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608 212 VMLTNGPGDPKDVPEALDMIRGVEGKIPLFGICLGHQLFALANGANTFKMKYGHRGFNHPVREIATGRIDF---TSQN-- 286
Cdd:PRK06895  47 ILISPGPDVPRAYPQLFAMLERYHQHKSILGVCLGHQTLCEFFGGELYNLNNVRHGQQRPLKVRSNSPLFDglpEEFNig 126

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 489666608 287 --HGYAVDPDSIdPDTLLITHVeINDGTVEGLRHRLYPAFTVQFHPDA 332
Cdd:PRK06895 127 lyHSWAVSEENF-PTPLEITAV-CDENVVMAMQHKTLPIYGVQFHPES 172
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 194-346 1.36e-06

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: 48.34  E-value: 1.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608 194 VLPATTTASTILELAP--DGVMLTNGP--------GDPKDVPEALD---------MIRG-VEGKIPLFGICLGHQLFALA 253
Cdd:cd01745   37 LLPPVDDEEDLEQYLEllDGLLLTGGGdvdpplygEEPHPELGPIDperdafelaLLRAaLERGKPILGICRGMQLLNVA 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608 254 NGANTFkmkyghrgfnhpvREIATGRIdftsqnHGYAVDPdsiDPDTLLITHVEiNDGTVEGLRHR-LYPAFTVQFHPD- 331
Cdd:cd01745  117 LGGTLY-------------QDIRVNSL------HHQAIKR---LADGLRVEARA-PDGVIEAIESPdRPFVLGVQWHPEw 173

                        170
                 ....*....|....*
gi 489666608 332 AAPGPHDADHLFDEF 346
Cdd:cd01745  174 LADTDPDSLKLFEAF 188
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 194-330 5.33e-06

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: 46.87  E-value: 5.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608  194 VLPATT---TASTILELApDGVMLTNGP--------------GDPKDvPE----ALDMIRG-VEGKIPLFGICLGHQLFA 251
Cdd:pfam07722  42 LLPILGdpeDAAAILDRL-DGLLLTGGPnvdphfygeepsesGGPYD-PArdayELALIRAaLARGKPILGICRGFQLLN 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608  252 LANGANTFKMKYGHRGFNHPvREIATGRIDFTSQnhgyAVDpdsIDPDTLL-----ITHVEIN----------------- 309
Cdd:pfam07722 120 VALGGTLYQDIQEQPGFTDH-REHCQVAPYAPSH----AVN---VEPGSLLasllgSEEFRVNslhhqaidrlapglrve 191

                         170       180
                  ....*....|....*....|....*..
gi 489666608  310 ----DGTVEGLRHRLYPAFT--VQFHP 330
Cdd:pfam07722 192 avapDGTIEAIESPNAKGFAlgVQWHP 218
PLN02347 PLN02347
GMP synthetase
 170-251 2.97e-05

GMP synthetase


Pssm-ID: 215197 [Multi-domain]  Cd Length: 536  Bit Score: 45.83  E-value: 2.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608 170 VVVIDFGLK--HSILRELakRQCNV--TVLPATTTASTILELAPDGVMLTNGP------GDPKDVPEALDMIRgvEGKIP 239
Cdd:PLN02347  13 VLILDYGSQytHLITRRV--RELGVysLLLSGTASLDRIASLNPRVVILSGGPhsvhveGAPTVPEGFFDYCR--ERGVP 88

                         90
                 ....*....|..
gi 489666608 240 LFGICLGHQLFA 251
Cdd:PLN02347  89 VLGICYGMQLIV 100
pyrG PRK05380
CTP synthetase; Validated
 231-249 5.25e-03

CTP synthetase; Validated


Pssm-ID: 235437 [Multi-domain]  Cd Length: 533  Bit Score: 38.46  E-value: 5.25e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 489666608 231 IRGVEGKI-----------PLFGICLGHQL 249
Cdd:PRK05380 355 ERGIEGKIlairyarenniPFLGICLGMQL 384
PyrG COG0504
CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase ...
 231-249 5.63e-03

CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase (UTP-ammonia lyase) is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 440270 [Multi-domain]  Cd Length: 535  Bit Score: 38.45  E-value: 5.63e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 489666608 231 IRGVEGKI-----------PLFGICLGHQL 249
Cdd:COG0504  356 ERGIEGKIaairyarenkiPFLGICLGMQL 385
hisH PRK13146
imidazole glycerol phosphate synthase subunit HisH; Provisional
 170-251 6.40e-03

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237290 [Multi-domain]  Cd Length: 209  Bit Score: 37.45  E-value: 6.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608 170 VVVIDFG---LkHSILR--ELAKRQCNVTVlpaTTTASTILelAPDGVMLtngPGDP--KDVPEALDMIRGVE------- 235
Cdd:PRK13146   4 VAIIDYGsgnL-RSAAKalERAGAGADVVV---TADPDAVA--AADRVVL---PGVGafADCMRGLRAVGLGEavieavl 74

                         90
                 ....*....|....*...
gi 489666608 236 --GKiPLFGICLGHQLFA 251
Cdd:PRK13146  75 aaGR-PFLGICVGMQLLF 91
HisH COG0118
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ...
 169-251 6.61e-03

Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid transport and metabolism]; Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH is part of the Pathway/BioSystem: Histidine biosynthesis


Pssm-ID: 439888 [Multi-domain]  Cd Length: 196  Bit Score: 37.33  E-value: 6.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489666608 169 NVVVIDFG---LkHSILRELAKRQCNVTVlpaTTTASTILElApDGVMLtngPG-----------DPKDVPEALDmiRGV 234
Cdd:COG0118    2 MIAIIDYGmgnL-RSVAKALERLGAEVVV---TSDPDEIRA-A-DRLVL---PGvgafgdamenlRERGLDEAIR--EAV 70

                         90
                 ....*....|....*..
gi 489666608 235 EGKIPLFGICLGHQLFA 251
Cdd:COG0118   71 AGGKPVLGICLGMQLLF 87
 
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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