NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|851012666|ref|WP_048068592|]
View 

glutamine-hydrolyzing carbamoyl-phosphate synthase small subunit [Methanoregula boonei]

Protein Classification

carbamoyl-phosphate synthase small subunit( domain architecture ID 11423442)

small subunit of carbamoyl phosphate synthetase (CPS) which plays a key role in both arginine and pyrimidine biosynthesis

CATH:  3.40.50.880|3.50.30.20
EC:  6.3.5.5
Gene Ontology:  GO:0005524|GO:0046982|GO:0004359|GO:0004088|GO:0019856|GO:0006526

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 1-350 3.22e-175

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: 490.69  E-value: 3.22e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666   1 MKAVLGFEDGDFVVGEGFGVKGECAGELVFNTQMTGYMESLTDPSYFGQILMFTFPQIGNYGVDTRNFQNPRVCALGCIA 80
Cdd:COG0505    3 MKALLVLEDGTVFEGKSFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVTFTYPHIGNYGVNDEDFESDRPWVAGLVV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666  81 KEICEKPEH---GPTLRTFFEEHSLLGMTGVDTRALTIKARVHGTMRAALVVGSDDSAYAVSLAQKSPTICDIIPIPEVS 157
Cdd:COG0505   83 RELSRRPSNwrsEESLDEYLKEHGIPGISGIDTRALTRHLREKGAMKGVISTGDLDIEELLEKARAAPGMEGLDLVKEVS 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666 158 CKEPYHI---PGSGKRIAVIDLGIKKNMLTSLSKRNGDLYVFPYNATADQVRACKPDALFVSNGPGDPKQAPDAIRCIQN 234
Cdd:COG0505  163 TKEPYEWteaPGAGFHVVALDFGVKRNILRELAERGCRVTVVPATTSAEEILALNPDGVFLSNGPGDPAALDYAIETIRE 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666 235 LLG-ELPIFGICMGNQVSALALGGDTYKLKFGHRGANQPVR-FTDGRIFITTQNHGFAVDAESLPE-GCRVTYTNVNDGT 311
Cdd:COG0505  243 LLGkGIPIFGICLGHQLLALALGAKTYKLKFGHRGANHPVKdLETGRVEITSQNHGFAVDEDSLPAtDLEVTHVNLNDGT 322

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 851012666 312 VEGFENRDMRLTTVQFHPEAHGGPRDTeAHFFDDlFRRL 350
Cdd:COG0505  323 VEGLRHKDLPAFSVQYHPEASPGPHDS-AYLFDR-FIEL 359
 
Name Accession Description Interval E-value
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 1-350 3.22e-175

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: 490.69  E-value: 3.22e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666   1 MKAVLGFEDGDFVVGEGFGVKGECAGELVFNTQMTGYMESLTDPSYFGQILMFTFPQIGNYGVDTRNFQNPRVCALGCIA 80
Cdd:COG0505    3 MKALLVLEDGTVFEGKSFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVTFTYPHIGNYGVNDEDFESDRPWVAGLVV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666  81 KEICEKPEH---GPTLRTFFEEHSLLGMTGVDTRALTIKARVHGTMRAALVVGSDDSAYAVSLAQKSPTICDIIPIPEVS 157
Cdd:COG0505   83 RELSRRPSNwrsEESLDEYLKEHGIPGISGIDTRALTRHLREKGAMKGVISTGDLDIEELLEKARAAPGMEGLDLVKEVS 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666 158 CKEPYHI---PGSGKRIAVIDLGIKKNMLTSLSKRNGDLYVFPYNATADQVRACKPDALFVSNGPGDPKQAPDAIRCIQN 234
Cdd:COG0505  163 TKEPYEWteaPGAGFHVVALDFGVKRNILRELAERGCRVTVVPATTSAEEILALNPDGVFLSNGPGDPAALDYAIETIRE 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666 235 LLG-ELPIFGICMGNQVSALALGGDTYKLKFGHRGANQPVR-FTDGRIFITTQNHGFAVDAESLPE-GCRVTYTNVNDGT 311
Cdd:COG0505  243 LLGkGIPIFGICLGHQLLALALGAKTYKLKFGHRGANHPVKdLETGRVEITSQNHGFAVDEDSLPAtDLEVTHVNLNDGT 322

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 851012666 312 VEGFENRDMRLTTVQFHPEAHGGPRDTeAHFFDDlFRRL 350
Cdd:COG0505  323 VEGLRHKDLPAFSVQYHPEASPGPHDS-AYLFDR-FIEL 359
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
1-350 6.21e-174

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 487.28  E-value: 6.21e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666   1 MKAVLGFEDGDFVVGEGFGVKGECAGELVFNTQMTGYMESLTDPSYFGQILMFTFPQIGNYGVDTRNFQNPRVCALGCIA 80
Cdd:PRK12564   3 MKAYLVLEDGTVFEGKAFGAEGETVGEVVFNTSMTGYQEILTDPSYAGQIVTFTYPLIGNYGVNREDFESDRPHAKGLIV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666  81 KEICEKPEH---GPTLRTFFEEHSLLGMTGVDTRALTIKARVHGTMRAALVVGSDDSAYAVSLAQKSPTICDIIPIPEVS 157
Cdd:PRK12564  83 RELSDIPSNwrsEMSLDEYLKENGIPGISGIDTRALTRKLREKGAMKGVIATEDFDAEELLEKARAFPGLLGLDLVKEVS 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666 158 CKEPYHIPG----SGKRIAVIDLGIKKNMLTSLSKRNGDLYVFPYNATADQVRACKPDALFVSNGPGDPKQAPDAIRCIQ 233
Cdd:PRK12564 163 TKEPYPWPGpggeLKYKVVAIDFGVKRNILRELAERGCRVTVVPATTTAEEILALNPDGVFLSNGPGDPAALDYAIEMIR 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666 234 NLLGE-LPIFGICMGNQVSALALGGDTYKLKFGHRGANQPVR-FTDGRIFITTQNHGFAVDAESLPEGCRVTYTNVNDGT 311
Cdd:PRK12564 243 ELLEKkIPIFGICLGHQLLALALGAKTYKMKFGHRGANHPVKdLETGKVEITSQNHGFAVDEDSLPANLEVTHVNLNDGT 322

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 851012666 312 VEGFENRDMRLTTVQFHPEAHGGPRDTEaHFFDDlFRRL 350
Cdd:PRK12564 323 VEGLRHKDLPAFSVQYHPEASPGPHDSA-YLFDE-FVEL 359
CPSaseIIsmall TIGR01368
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ...
 3-351 2.50e-154

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: 437.44  E-value: 2.50e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666    3 AVLGFEDGDFVVGEGFGVKGECAGELVFNTQMTGYMESLTDPSYFGQILMFTFPQIGNYGVDTRNFQNPRVCALGCIAKE 82
Cdd:TIGR01368   1 AYLVLEDGTVFRGYSFGAEGTVAGEVVFNTGMTGYQEILTDPSYKGQIVVFTYPLIGNYGVNDEDAESKGIHVSGLVVRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666   83 ICEKPEH---GPTLRTFFEEHSLLGMTGVDTRALTIKARVHGTMRAALVVGSDDSAYAVSLAQKSPTICDIIPIPEVSCK 159
Cdd:TIGR01368  81 LSDRYSNwraTESLDQFLKRHGIPGIYGVDTRALVKKIREKGTMKGVISTEDSNDEELVEKARVSPDITGINLVAEVSTK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666  160 EPYHIP---GSGKRIAVIDLGIKKNMLTSLSKRNGDLYVFPYNATADQVRACKPDALFVSNGPGDPKQAPDAIRCIQNLL 236
Cdd:TIGR01368 161 EPYTWGqrgGKGKRVVVIDFGVKRNILRRLVKRGCEVTVVPYDTDAEEIKKYNPDGIFLSNGPGDPAAVEPAIETIRKLL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666  237 GELPIFGICMGNQVSALALGGDTYKLKFGHRGANQPVR-FTDGRIFITTQNHGFAVDAESLPEGC-RVTYTNVNDGTVEG 314
Cdd:TIGR01368 241 EKIPIFGICLGHQLLALAFGAKTYKMKFGHRGGNHPVKdLITGRVEITSQNHGYAVDPDSLPAGDlEVTHVNLNDGTVEG 320

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 851012666  315 FENRDMRLTTVQFHPEAHGGPRDTEaHFFDDLFRRLA 351
Cdd:TIGR01368 321 IRHKDLPVFSVQYHPEASPGPHDTE-YLFDEFIDLMK 356
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 171-347 1.77e-98

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: 289.01  E-value: 1.77e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666 171 IAVIDLGIKKNMLTSLSKRNGDLYVFPYNATADQVRACKPDALFVSNGPGDPKQAPDAIRCIQNLLGE-LPIFGICMGNQ 249
Cdd:cd01744    1 VVVIDFGVKHNILRELLKRGCEVTVVPYNTDAEEILKLDPDGIFLSNGPGDPALLDEAIKTVRKLLGKkIPIFGICLGHQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666 250 VSALALGGDTYKLKFGHRGANQPVR-FTDGRIFITTQNHGFAVDAESLPEGCRVTYTNVNDGTVEGFENRDMRLTTVQFH 328
Cdd:cd01744   81 LLALALGAKTYKMKFGHRGSNHPVKdLITGRVYITSQNHGYAVDPDSLPGGLEVTHVNLNDGTVEGIRHKDLPVFSVQFH 160

                        170
                 ....*....|....*....
gi 851012666 329 PEAHGGPRDTEaHFFDDLF 347
Cdd:cd01744  161 PEASPGPHDTE-YLFDEFL 178
CPSase_sm_chain smart01097
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 1-127 1.06e-63

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: 198.37  E-value: 1.06e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666     1 MKAVLGFEDGDFVVGEGFGVKGECAGELVFNTQMTGYMESLTDPSYFGQILMFTFPQIGNYGVDTRNFQNPRVCALGCIA 80
Cdd:smart01097   1 MKAYLVLEDGTVFEGESFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNDEDFESDKIQVKGLVV 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 851012666    81 KEICEKPEHG---PTLRTFFEEHSLLGMTGVDTRALTIKARVHGTMRAAL 127
Cdd:smart01097  81 RELSDEPSNWrseQSLDEFLKENGIPGISGIDTRALTRKLREKGAMKGVI 130
CPSase_sm_chain pfam00988
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 5-127 6.28e-60

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: 188.69  E-value: 6.28e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666    5 LGFEDGDFVVGEGFGVKGECAGELVFNTQMTGYMESLTDPSYFGQILMFTFPQIGNYGVDTRNFQNPRVCALGCIAKEIC 84
Cdd:pfam00988   1 LVLEDGTVFEGKSFGAAGSTVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNPEDFESDKIHVAGLVVREYS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 851012666   85 EKPEH---GPTLRTFFEEHSLLGMTGVDTRALTIKARVHGTMRAAL 127
Cdd:pfam00988  81 DEPSNwraEESLDEWLKEQGIPGISGVDTRALTRKIREKGAMKGVI 126
 
Name Accession Description Interval E-value
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 1-350 3.22e-175

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: 490.69  E-value: 3.22e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666   1 MKAVLGFEDGDFVVGEGFGVKGECAGELVFNTQMTGYMESLTDPSYFGQILMFTFPQIGNYGVDTRNFQNPRVCALGCIA 80
Cdd:COG0505    3 MKALLVLEDGTVFEGKSFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVTFTYPHIGNYGVNDEDFESDRPWVAGLVV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666  81 KEICEKPEH---GPTLRTFFEEHSLLGMTGVDTRALTIKARVHGTMRAALVVGSDDSAYAVSLAQKSPTICDIIPIPEVS 157
Cdd:COG0505   83 RELSRRPSNwrsEESLDEYLKEHGIPGISGIDTRALTRHLREKGAMKGVISTGDLDIEELLEKARAAPGMEGLDLVKEVS 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666 158 CKEPYHI---PGSGKRIAVIDLGIKKNMLTSLSKRNGDLYVFPYNATADQVRACKPDALFVSNGPGDPKQAPDAIRCIQN 234
Cdd:COG0505  163 TKEPYEWteaPGAGFHVVALDFGVKRNILRELAERGCRVTVVPATTSAEEILALNPDGVFLSNGPGDPAALDYAIETIRE 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666 235 LLG-ELPIFGICMGNQVSALALGGDTYKLKFGHRGANQPVR-FTDGRIFITTQNHGFAVDAESLPE-GCRVTYTNVNDGT 311
Cdd:COG0505  243 LLGkGIPIFGICLGHQLLALALGAKTYKLKFGHRGANHPVKdLETGRVEITSQNHGFAVDEDSLPAtDLEVTHVNLNDGT 322

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 851012666 312 VEGFENRDMRLTTVQFHPEAHGGPRDTeAHFFDDlFRRL 350
Cdd:COG0505  323 VEGLRHKDLPAFSVQYHPEASPGPHDS-AYLFDR-FIEL 359
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
1-350 6.21e-174

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 487.28  E-value: 6.21e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666   1 MKAVLGFEDGDFVVGEGFGVKGECAGELVFNTQMTGYMESLTDPSYFGQILMFTFPQIGNYGVDTRNFQNPRVCALGCIA 80
Cdd:PRK12564   3 MKAYLVLEDGTVFEGKAFGAEGETVGEVVFNTSMTGYQEILTDPSYAGQIVTFTYPLIGNYGVNREDFESDRPHAKGLIV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666  81 KEICEKPEH---GPTLRTFFEEHSLLGMTGVDTRALTIKARVHGTMRAALVVGSDDSAYAVSLAQKSPTICDIIPIPEVS 157
Cdd:PRK12564  83 RELSDIPSNwrsEMSLDEYLKENGIPGISGIDTRALTRKLREKGAMKGVIATEDFDAEELLEKARAFPGLLGLDLVKEVS 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666 158 CKEPYHIPG----SGKRIAVIDLGIKKNMLTSLSKRNGDLYVFPYNATADQVRACKPDALFVSNGPGDPKQAPDAIRCIQ 233
Cdd:PRK12564 163 TKEPYPWPGpggeLKYKVVAIDFGVKRNILRELAERGCRVTVVPATTTAEEILALNPDGVFLSNGPGDPAALDYAIEMIR 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666 234 NLLGE-LPIFGICMGNQVSALALGGDTYKLKFGHRGANQPVR-FTDGRIFITTQNHGFAVDAESLPEGCRVTYTNVNDGT 311
Cdd:PRK12564 243 ELLEKkIPIFGICLGHQLLALALGAKTYKMKFGHRGANHPVKdLETGKVEITSQNHGFAVDEDSLPANLEVTHVNLNDGT 322

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 851012666 312 VEGFENRDMRLTTVQFHPEAHGGPRDTEaHFFDDlFRRL 350
Cdd:PRK12564 323 VEGLRHKDLPAFSVQYHPEASPGPHDSA-YLFDE-FVEL 359
CPSaseIIsmall TIGR01368
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ...
 3-351 2.50e-154

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: 437.44  E-value: 2.50e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666    3 AVLGFEDGDFVVGEGFGVKGECAGELVFNTQMTGYMESLTDPSYFGQILMFTFPQIGNYGVDTRNFQNPRVCALGCIAKE 82
Cdd:TIGR01368   1 AYLVLEDGTVFRGYSFGAEGTVAGEVVFNTGMTGYQEILTDPSYKGQIVVFTYPLIGNYGVNDEDAESKGIHVSGLVVRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666   83 ICEKPEH---GPTLRTFFEEHSLLGMTGVDTRALTIKARVHGTMRAALVVGSDDSAYAVSLAQKSPTICDIIPIPEVSCK 159
Cdd:TIGR01368  81 LSDRYSNwraTESLDQFLKRHGIPGIYGVDTRALVKKIREKGTMKGVISTEDSNDEELVEKARVSPDITGINLVAEVSTK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666  160 EPYHIP---GSGKRIAVIDLGIKKNMLTSLSKRNGDLYVFPYNATADQVRACKPDALFVSNGPGDPKQAPDAIRCIQNLL 236
Cdd:TIGR01368 161 EPYTWGqrgGKGKRVVVIDFGVKRNILRRLVKRGCEVTVVPYDTDAEEIKKYNPDGIFLSNGPGDPAAVEPAIETIRKLL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666  237 GELPIFGICMGNQVSALALGGDTYKLKFGHRGANQPVR-FTDGRIFITTQNHGFAVDAESLPEGC-RVTYTNVNDGTVEG 314
Cdd:TIGR01368 241 EKIPIFGICLGHQLLALAFGAKTYKMKFGHRGGNHPVKdLITGRVEITSQNHGYAVDPDSLPAGDlEVTHVNLNDGTVEG 320

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 851012666  315 FENRDMRLTTVQFHPEAHGGPRDTEaHFFDDLFRRLA 351
Cdd:TIGR01368 321 IRHKDLPVFSVQYHPEASPGPHDTE-YLFDEFIDLMK 356
PRK12838 PRK12838
carbamoyl phosphate synthase small subunit; Reviewed
 1-345 8.29e-146

carbamoyl phosphate synthase small subunit; Reviewed


Pssm-ID: 183784 [Multi-domain]  Cd Length: 354  Bit Score: 415.83  E-value: 8.29e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666   1 MKAVLGFEDGDFVVGEGFGVKGECAGELVFNTQMTGYMESLTDPSYFGQILMFTFPQIGNYGVDTRNFQNPRVCALGCIA 80
Cdd:PRK12838   1 MKAYLILEDGTVFEGELIGAPIDVTGEIVFNTGMTGYQEVLTDPSYKGQIVVFTYPLIGNYGINADDYESKQPQVKGVIV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666  81 KEICEKPEHGP---TLRTFFEEHSLLGMTGVDTRALTIKARVHGTMRAALVVGSDDSAYAVSLAQKSPTIcdiiPIPEVS 157
Cdd:PRK12838  81 YELSREGSHYRakqSLDDFLKEWNIPGISGVDTRALVKHIREKGTMKASITTTDDAHAFDQIKALVLPKN----VVAQVS 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666 158 CKEPYHIPGSGKRIAVIDLGIKKNMLTSLSKRNGDLYVFPYNATADQVRACKPDALFVSNGPGDPKQAPDAIRCIQNLLG 237
Cdd:PRK12838 157 TKEPYTYGNGGKHVALIDFGYKKSILRSLSKRGCKVTVLPYDTSLEEIKNLNPDGIVLSNGPGDPKELQPYLPEIKKLIS 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666 238 ELPIFGICMGNQVSALALGGDTYKLKFGHRGANQPVR-FTDGRIFITTQNHGFAVDAESLPE-GCRVTYTNVNDGTVEGF 315
Cdd:PRK12838 237 SYPILGICLGHQLIALALGADTEKLPFGHRGANHPVIdLTTGRVWMTSQNHGYVVDEDSLDGtPLSVRFFNVNDGSIEGL 316

                        330       340       350
                 ....*....|....*....|....*....|
gi 851012666 316 ENRDMRLTTVQFHPEAHGGPRDTEaHFFDD 345
Cdd:PRK12838 317 RHKKKPVLSVQFHPEAHPGPHDAE-YIFDE 345
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 171-347 1.77e-98

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: 289.01  E-value: 1.77e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666 171 IAVIDLGIKKNMLTSLSKRNGDLYVFPYNATADQVRACKPDALFVSNGPGDPKQAPDAIRCIQNLLGE-LPIFGICMGNQ 249
Cdd:cd01744    1 VVVIDFGVKHNILRELLKRGCEVTVVPYNTDAEEILKLDPDGIFLSNGPGDPALLDEAIKTVRKLLGKkIPIFGICLGHQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666 250 VSALALGGDTYKLKFGHRGANQPVR-FTDGRIFITTQNHGFAVDAESLPEGCRVTYTNVNDGTVEGFENRDMRLTTVQFH 328
Cdd:cd01744   81 LLALALGAKTYKMKFGHRGSNHPVKdLITGRVYITSQNHGYAVDPDSLPGGLEVTHVNLNDGTVEGIRHKDLPVFSVQFH 160

                        170
                 ....*....|....*....
gi 851012666 329 PEAHGGPRDTEaHFFDDLF 347
Cdd:cd01744  161 PEASPGPHDTE-YLFDEFL 178
carA CHL00197
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
 2-342 2.95e-89

carbamoyl-phosphate synthase arginine-specific small subunit; Provisional


Pssm-ID: 214392 [Multi-domain]  Cd Length: 382  Bit Score: 272.83  E-value: 2.95e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666   2 KAVLGFEDGDFVVGEGFGVKGECAGELVFNTQMTGYMESLTDPSYFGQILMFTFPQIGNYGVDTRNFQNPRVCALGCIAK 81
Cdd:CHL00197   6 PAILVLEDGTYYRGWSFSNPITTIGEVVFNTGMTGYQEIITDPSYFEQIVTFTYPEIGNTGINLEDIESVKIQVKGIIAK 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666  82 EICEKPEHGPTLRTF---FEEHSLLGMTGVDTRALTIKARVHGTMRAALVVGSDDSAYAVSLAQKSPTICDIIPIPEVSC 158
Cdd:CHL00197  86 NICKSSSNWRQQESLvsyLQRHKIPFIFGIDTRALTQHLRRFGTMNGCISNQNLNLSYLRAKIKESPHMPSSDLIPRVTT 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666 159 KEPY------------------HIpGSGKRIAVIDLGIKKNMLTSLSKRNGDLYVFPYNATADQVRACKPDALFVSNGPG 220
Cdd:CHL00197 166 SSYYewdekshpsfyladnkrpHS-SYQLKIIVIDFGVKYNILRRLKSFGCSITVVPATSPYQDILSYQPDGILLSNGPG 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666 221 DPKQAPDAIRCIQNLLGE-LPIFGICMGNQVSALALGGDTYKLKFGHRGANQPVRFTDgRIFITTQNHGFAVDAESLPEG 299
Cdd:CHL00197 245 DPSAIHYGIKTVKKLLKYnIPIFGICMGHQILSLALEAKTFKLKFGHRGLNHPSGLNQ-QVEITSQNHGFAVNLESLAKN 323

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 851012666 300 -CRVTYTNVNDGTVEGFENRDMRLTTVQFHPEAHGGPRDTEAHF 342
Cdd:CHL00197 324 kFYITHFNLNDGTVAGISHSPKPYFSVQYHPEASPGPHDADYLF 367
PLN02771 PLN02771
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
 3-342 2.38e-86

carbamoyl-phosphate synthase (glutamine-hydrolyzing)


Pssm-ID: 178370 [Multi-domain]  Cd Length: 415  Bit Score: 266.46  E-value: 2.38e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666   3 AVLGFEDGDFVVGEGFGVKGECAGELVFNTQMTGYMESLTDPSYFGQILMFTFPQIGNYGVdtrNF--QNPRVCAL-GCI 79
Cdd:PLN02771  57 ARLVLEDGSVWKAKSFGARGTQVGEVVFNTSLTGYQEILTDPSYAGQFVLMTNPHIGNTGV---NFddEESRQCFLaGLV 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666  80 AKEI--------CEKpehgpTLRTFFEEHSLLGMTGVDTRALTIKARVHGTMRAalVVGSDDSAYAVSLAQKSPT--ICD 149
Cdd:PLN02771 134 IRSLsistsnwrCTK-----TLGDYLAERNIMGIYDVDTRAITRRLREDGSLIG--VLSTEDSKTDEELLKMSRSwdIVG 206

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666 150 IIPIPEVSCKEPYH---------------IPGSGKRIAVIDLGIKKNMLTSLSKRNGDLYVFPYNATADQVRACKPDALF 214
Cdd:PLN02771 207 IDLISGVSCKSPYEwvdktnpewdfntnsRDGESYHVIAYDFGIKHNILRRLASYGCKITVVPSTWPASEALKMKPDGVL 286

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666 215 VSNGPGDPKQAPDAIRCIQNLLGELPIFGICMGNQVSALALGGDTYKLKFGHRGANQPVR-FTDGRIFITTQNHGFAVDA 293
Cdd:PLN02771 287 FSNGPGDPSAVPYAVETVKELLGKVPVFGICMGHQLLGQALGGKTFKMKFGHHGGNHPVRnNRTGRVEISAQNHNYAVDP 366

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 851012666 294 ESLPEGCRVTYTNVNDGTVEGFENRDMRLTTVQFHPEAHGGPRDTEAHF 342
Cdd:PLN02771 367 ASLPEGVEVTHVNLNDGSCAGLAFPALNVMSLQYHPEASPGPHDSDNAF 415
CPSase_sm_chain smart01097
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 1-127 1.06e-63

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: 198.37  E-value: 1.06e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666     1 MKAVLGFEDGDFVVGEGFGVKGECAGELVFNTQMTGYMESLTDPSYFGQILMFTFPQIGNYGVDTRNFQNPRVCALGCIA 80
Cdd:smart01097   1 MKAYLVLEDGTVFEGESFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNDEDFESDKIQVKGLVV 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 851012666    81 KEICEKPEHG---PTLRTFFEEHSLLGMTGVDTRALTIKARVHGTMRAAL 127
Cdd:smart01097  81 RELSDEPSNWrseQSLDEFLKENGIPGISGIDTRALTRKLREKGAMKGVI 130
CPSase_sm_chain pfam00988
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 5-127 6.28e-60

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: 188.69  E-value: 6.28e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666    5 LGFEDGDFVVGEGFGVKGECAGELVFNTQMTGYMESLTDPSYFGQILMFTFPQIGNYGVDTRNFQNPRVCALGCIAKEIC 84
Cdd:pfam00988   1 LVLEDGTVFEGKSFGAAGSTVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNPEDFESDKIHVAGLVVREYS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 851012666   85 EKPEH---GPTLRTFFEEHSLLGMTGVDTRALTIKARVHGTMRAAL 127
Cdd:pfam00988  81 DEPSNwraEESLDEWLKEQGIPGISGVDTRALTRKIREKGAMKGVI 126
GATase pfam00117
Glutamine amidotransferase class-I;
172-348 1.05e-50

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 167.41  E-value: 1.05e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666  172 AVIDLG--IKKNMLTSLSKRNGDLYVFPYNATADQVRACKPDALFVSNGPGDPKQAPDAIRCIQNLLG-ELPIFGICMGN 248
Cdd:pfam00117   1 LLIDNGdsFTYNLARALRELGVEVTVVPNDTPAEEILEENPDGIILSGGPGSPGAAGGAIEAIREARElKIPILGICLGH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666  249 QVSALALGGDTYKLK-FGHRGANQPVR-------FTDGRIFITTQNHGFAVDAESLPEGCRVTYTNVNDGTVEGFENRDM 320
Cdd:pfam00117  81 QLLALAFGGKVVKAKkFGHHGKNSPVGddgcglfYGLPNVFIVRRYHSYAVDPDTLPDGLEVTATSENDGTIMGIRHKKL 160

                         170       180
                  ....*....|....*....|....*...
gi 851012666  321 RLTTVQFHPEAHGGPRDTEaHFFDDLFR 348
Cdd:pfam00117 161 PIFGVQFHPESILTPHGPE-ILFNFFIK 187
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 181-330 3.73e-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: 3.73e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666 181 NMLTSLSKRNGDLYVFPYNA-TADQVRACKPDALFVSNGPGDPKQAPDAIRCIQNLLGELPIFGICMGNQVSALALGGDT 259
Cdd:cd01743   13 NLVQYLRELGAEVVVVRNDEiTLEELELLNPDAIVISPGPGHPEDAGISLEIIRALAGKVPILGVCLGHQAIAEAFGGKV 92

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 851012666 260 YKLKFGHRGANQPVRFTDGRIFITTQN-------HGFAVDAESLPEGCRVTYTNvNDGTVEGFENRDMRLTTVQFHPE 330
Cdd:cd01743   93 VRAPEPMHGKTSEIHHDGSGLFKGLPQpftvgryHSLVVDPDPLPDLLEVTAST-EDGVIMALRHRDLPIYGVQFHPE 169
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 195-330 1.70e-21

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: 90.48  E-value: 1.70e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666 195 VFPYNA-TADQVRACKPDALFVSNGPGDPKQAPDAIRCIQNLLGELPIFGICMGNQVSALALGGDTYKLKFGHRGANQPV 273
Cdd:COG0512   27 VVRNDEiTLEEIEALAPDGIVLSPGPGTPEEAGISLEVIRAFAGKIPILGVCLGHQAIGEAFGGKVVRAPEPMHGKTSPI 106

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 851012666 274 RFTDGRIFittQN----------HGFAVDAESLPEGCRVT-YTnvNDGTVEGFENRDMRLTTVQFHPE 330
Cdd:COG0512  107 THDGSGLF---AGlpnpftatryHSLVVDRETLPDELEVTaWT--EDGEIMGIRHRELPIEGVQFHPE 169
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 201-330 1.36e-20

anthranilate synthase component II; Provisional


Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 87.88  E-value: 1.36e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666 201 TADQVRACKPDALFVSNGPGDPKQA---PDAIRciqNLLGELPIFGICMGNQVSALALGGDTYKLKFGHRGANQPVRFTD 277
Cdd:PRK05670  35 TLEEIEALNPDAIVLSPGPGTPAEAgisLELIR---EFAGKVPILGVCLGHQAIGEAFGGKVVRAKEIMHGKTSPIEHDG 111

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666 278 GRIFITTQN-------HGFAVDAESLPEGCRVTYTnVNDGTVEGFENRDMRLTTVQFHPE 330
Cdd:PRK05670 112 SGIFAGLPNpftvtryHSLVVDRESLPDCLEVTAW-TDDGEIMGVRHKELPIYGVQFHPE 170
PRK14607 PRK14607
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
201-331 1.58e-19

bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;


Pssm-ID: 237764 [Multi-domain]  Cd Length: 534  Bit Score: 89.39  E-value: 1.58e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666 201 TADQVRACKPDALFVSNGPGDPKQAPDAIRCIQNLLGELPIFGICMGNQVSALALGGDTYKLKFGHRGANQPVRFtDGR- 279
Cdd:PRK14607  36 TIEEIEALNPSHIVISPGPGRPEEAGISVEVIRHFSGKVPILGVCLGHQAIGYAFGGKIVHAKRILHGKTSPIDH-NGKg 114

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 851012666 280 IF-------ITTQNHGFAVDAESLPEGCRVTyTNVNDGTVEGFENRDMRLTTVQFHPEA 331
Cdd:PRK14607 115 LFrgipnptVATRYHSLVVEEASLPECLEVT-AKSDDGEIMGIRHKEHPIFGVQFHPES 172
trpG_papA TIGR00566
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ...
 201-331 4.95e-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: 4.95e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666  201 TADQVRACKPDALFVSNGPGDPKQAPDAIRCIQNLLGELPIFGICMGNQVSALALGGDTYKLKFGHRGANQPVRFTDGRI 280
Cdd:TIGR00566  35 TLQEIEALLPLLIVISPGPCTPNEAGISLEAIRHFAGKLPILGVCLGHQAMGQAFGGDVVRANTVMHGKTSEIEHNGAGI 114

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 851012666  281 F-------ITTQNHGFAVDAESLPEGCRVTYTNVNDGTVEGFENRDMRLTTVQFHPEA 331
Cdd:TIGR00566 115 FrglfnplTATRYHSLVVEPETLPTCFPVTAWEEENIEIMAIRHRDLPLEGVQFHPES 172
PRK08857 PRK08857
aminodeoxychorismate/anthranilate synthase component II;
205-331 1.22e-18

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181566 [Multi-domain]  Cd Length: 193  Bit Score: 82.62  E-value: 1.22e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666 205 VRACKPDALFVSNGPGDPKQAPDAIRCIQNLLGELPIFGICMGNQVSALALGGDTYKLKFGHRGANQPVRFTDGRIFITT 284
Cdd:PRK08857  39 IEALNPTHLVISPGPCTPNEAGISLQAIEHFAGKLPILGVCLGHQAIAQVFGGQVVRARQVMHGKTSPIRHTGRSVFKGL 118

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 851012666 285 QN-------HGFAVDAESLPEGCRVT-YTNVNDGTVE---GFENRDMRLTTVQFHPEA 331
Cdd:PRK08857 119 NNpltvtryHSLVVKNDTLPECFELTaWTELEDGSMDeimGFQHKTLPIEAVQFHPES 176
PRK07649 PRK07649
aminodeoxychorismate/anthranilate synthase component II;
188-331 3.04e-16

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181066 [Multi-domain]  Cd Length: 195  Bit Score: 76.00  E-value: 3.04e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666 188 KRNGDLyvfpynaTADQVRACKPDALFVSNGPGDPKQAPDAIRCIQNLLGELPIFGICMGNQVSALALGGDTYKLKFGHR 267
Cdd:PRK07649  29 KRNDEV-------TISDIENMKPDFLMISPGPCSPNEAGISMEVIRYFAGKIPIFGVCLGHQSIAQVFGGEVVRAERLMH 101

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 851012666 268 GANQPVrFTDGRI--------FITTQNHGFAVDAESLPEgCRVTYTNVNDGTVEGFENRDMRLTTVQFHPEA 331
Cdd:PRK07649 102 GKTSLM-HHDGKTifsdipnpFTATRYHSLIVKKETLPD-CLEVTSWTEEGEIMAIRHKTLPIEGVQFHPES 171
PRK06774 PRK06774
aminodeoxychorismate synthase component II;
186-331 1.53e-15

aminodeoxychorismate synthase component II;


Pssm-ID: 180689 [Multi-domain]  Cd Length: 191  Bit Score: 74.13  E-value: 1.53e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666 186 LSKRNGDLyvfpynaTADQVRACKPDALFVSNGPGDPKQAPDAIRCIQNLLGELPIFGICMGNQVSALALGGDTYKLKFG 265
Cdd:PRK06774  27 MVKRNDEL-------QLTDIEQLAPSHLVISPGPCTPNEAGISLAVIRHFADKLPILGVCLGHQALGQAFGARVVRARQV 99

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 851012666 266 HRGANQPVRFTDGRIF-------ITTQNHGFAVDAESLPEGCRVTYTNVNDGTVE---GFENRDMRLTTVQFHPEA 331
Cdd:PRK06774 100 MHGKTSAICHSGQGVFrglnqplTVTRYHSLVIAADSLPGCFELTAWSERGGEMDeimGIRHRTLPLEGVQFHPES 175
PRK08007 PRK08007
aminodeoxychorismate synthase component 2;
186-331 1.10e-14

aminodeoxychorismate synthase component 2;


Pssm-ID: 181194 [Multi-domain]  Cd Length: 187  Bit Score: 71.49  E-value: 1.10e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666 186 LSKRNGDLyvfpynaTADQVRACKPDALFVSNGPGDPKQAPDAIRCIQNLLGELPIFGICMGNQVSALALGGDTYKLKFG 265
Cdd:PRK08007  27 LVKRNDAL-------TLADIDALKPQKIVISPGPCTPDEAGISLDVIRHYAGRLPILGVCLGHQAMAQAFGGKVVRAAKV 99

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 851012666 266 HRGANQPVRFTDGRIF-------ITTQNHGFAVDAESLPEGCRVTYTNvNDGTVEGFENRDMRLTTVQFHPEA 331
Cdd:PRK08007 100 MHGKTSPITHNGEGVFrglanplTVTRYHSLVVEPDSLPACFEVTAWS-ETREIMGIRHRQWDLEGVQFHPES 171
guaA_Nterm TIGR00888
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ...
 171-332 1.23e-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: 68.50  E-value: 1.23e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666  171 IAVIDLGIKKNMLTSLSKRNGDLY--VFPYNATADQVRACKPDALFVSNGPGDPKqAPDAIRCIQNLLG-ELPIFGICMG 247
Cdd:TIGR00888   1 ILVLDFGSQYTQLIARRLRELGVYseLVPNTTPLEEIREKNPKGIILSGGPSSVY-AENAPRADEKIFElGVPVLGICYG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666  248 NQVSALALGGDTYKLKFGHRG------ANQPVRFTD-GRIFITTQNHGFAVDAesLPEGCRVTYTNVNdGTVEGFENRDM 320
Cdd:TIGR00888  80 MQLMAKQLGGEVGRAEKREYGkaeleiLDEDDLFRGlPDESTVWMSHGDKVKE--LPEGFKVLATSDN-CPVAAMAHEEK 156

                         170
                  ....*....|..
gi 851012666  321 RLTTVQFHPEAH 332
Cdd:TIGR00888 157 PIYGVQFHPEVT 168
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 197-346 9.27e-13

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


Pssm-ID: 440284 [Multi-domain]  Cd Length: 225  Bit Score: 66.89  E-value: 9.27e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666 197 PYNATADQvrackPDALFVSNGPG----DPKQAPDAIRCIQNLL-GELPIFGICMGNQVSALALGGDTYKLK---FGHrg 268
Cdd:COG0518   41 PYDPDLED-----PDGLILSGGPMsvydEDPWLEDEPALIREAFeLGKPVLGICYGAQLLAHALGGKVEPGPgreIGW-- 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666 269 anQPVRFTD--------GRIFITTQNHGFAVDAesLPEGCRVTYTNVNDgTVEGFENRDmRLTTVQFHPEA-HGGPRDTE 339
Cdd:COG0518  114 --APVELTEadplfaglPDEFTVWMSHGDTVTE--LPEGAEVLASSDNC-PNQAFRYGR-RVYGVQFHPEVtHTMMEAWL 187


                 ....*..
gi 851012666 340 AHFFDDL 346
Cdd:COG0518  188 EERADEL 194
PLN02335 PLN02335
anthranilate synthase
 201-331 1.42e-12

anthranilate synthase


Pssm-ID: 177969 [Multi-domain]  Cd Length: 222  Bit Score: 66.36  E-value: 1.42e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666 201 TADQVRACKPDALFVSNGPGDPKQAPDAIRCIQNLLGELPIFGICMGNQVSALALGGDTYKLKFG--HrGANQPVRFTDG 278
Cdd:PLN02335  54 TVEELKRKNPRGVLISPGPGTPQDSGISLQTVLELGPLVPLFGVCMGLQCIGEAFGGKIVRSPFGvmH-GKSSPVHYDEK 132

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 851012666 279 ----------RIFITTQNHGFAVDAESLPEGCRVTYTNVNDGTVEGFENRDMR-LTTVQFHPEA 331
Cdd:PLN02335 133 geeglfsglpNPFTAGRYHSLVIEKDTFPSDELEVTAWTEDGLIMAARHRKYKhIQGVQFHPES 196
GATase1_GMP_Synthase cd01742
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ...
 195-330 8.63e-12

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: 62.94  E-value: 8.63e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666 195 VFPYNATADQVRACKPDALFVSNGPG---DPKqAPDAIRCIQNLlgELPIFGICMGNQVSALALGGDTYKLKFGHRGANQ 271
Cdd:cd01742   27 ILPNTTPLEEIKLKNPKGIILSGGPSsvyEED-APRVDPEIFEL--GVPVLGICYGMQLIAKALGGKVERGDKREYGKAE 103

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 851012666 272 PVRFTDGRIF----ITTQ---NHGFAVdaESLPEGCRVTYTNVNDGtVEGFENRDMRLTTVQFHPE 330
Cdd:cd01742  104 IEIDDSSPLFeglpDEQTvwmSHGDEV--VKLPEGFKVIASSDNCP-VAAIANEEKKIYGVQFHPE 166
PRK07765 PRK07765
aminodeoxychorismate/anthranilate synthase component II;
189-336 1.18e-10

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181107 [Multi-domain]  Cd Length: 214  Bit Score: 60.45  E-value: 1.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666 189 RNGDLYVfpynATADQVrACKPDALFVSNGPGDPKQAPDAIRCIQNLLG-ELPIFGICMGNQVSALALGGDTYKLKFGHR 267
Cdd:PRK07765  31 RNDDPRL----ADEAAV-AAQFDGVLLSPGPGTPERAGASIDMVRACAAaGTPLLGVCLGHQAIGVAFGATVDRAPELLH 105

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 851012666 268 GANQPVRFTDGRI-------FITTQNHGFAVDAESLPEGCRVTyTNVNDGTVEGFENRDMRLTTVQFHPEA---HGGPR 336
Cdd:PRK07765 106 GKTSSVHHTGVGVlaglpdpFTATRYHSLTILPETLPAELEVT-ARTDSGVIMAVRHRELPIHGVQFHPESvltEGGHR 183
PRK13566 PRK13566
anthranilate synthase component I;
209-330 1.71e-10

anthranilate synthase component I;


Pssm-ID: 237429 [Multi-domain]  Cd Length: 720  Bit Score: 62.24  E-value: 1.71e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666 209 KPDALFVSNGPGDPKQApDAIRCIQNLLG-ELPIFGICMGNQVSALALGGDTYKLKFGHRGANQPVRFTDGRI------- 280
Cdd:PRK13566 569 NPDLVVLSPGPGRPSDF-DCKATIDAALArNLPIFGVCLGLQAIVEAFGGELGQLAYPMHGKPSRIRVRGPGRlfsglpe 647

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 851012666 281 -FITTQNHGFAVDAESLPEGCRVTYTNvNDGTVEGFENRDMRLTTVQFHPE 330
Cdd:PRK13566 648 eFTVGRYHSLFADPETLPDELLVTAET-EDGVIMAIEHKTLPVAAVQFHPE 697
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 170-332 1.90e-10

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


Pssm-ID: 153212 [Multi-domain]  Cd Length: 188  Bit Score: 59.57  E-value: 1.90e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666 170 RIAVI------DLGIKKNMLTSLSKRNGDLYVFPYNATADQVRACKPDALFVSNGPGDPKQAPDA-----IRCIQNLL-G 237
Cdd:cd01741    1 RILILqhdtpeGPGLFEDLLREAGAETIEIDVVDVYAGELLPDLDDYDGLVILGGPMSVDEDDYPwlkklKELIRQALaA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666 238 ELPIFGICMGNQVSALALGGDTYKLKFGHRGANQPVRFTD-GRIFITTQNHGFAVDA--------ESLPEGCRVTYTNvN 308
Cdd:cd01741   81 GKPVLGICLGHQLLARALGGKVGRNPKGWEIGWFPVTLTEaGKADPLFAGLPDEFPVfhwhgdtvVELPPGAVLLASS-E 159

                        170       180
                 ....*....|....*....|....
gi 851012666 309 DGTVEGFENRDmRLTTVQFHPEAH 332
Cdd:cd01741  160 ACPNQAFRYGD-RALGLQFHPEER 182
trpG CHL00101
anthranilate synthase component 2
 181-331 2.10e-10

anthranilate synthase component 2


Pssm-ID: 214365 [Multi-domain]  Cd Length: 190  Bit Score: 59.36  E-value: 2.10e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666 181 NMLTSLSKRNGDLYVFPYNA-TADQVRACKPDALFVSNGPGDPKQAPDAIRCIQNLLGELPIFGICMGNQVSALALGGDT 259
Cdd:CHL00101  14 NLVQSLGELNSDVLVCRNDEiDLSKIKNLNIRHIIISPGPGHPRDSGISLDVISSYAPYIPILGVCLGHQSIGYLFGGKI 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666 260 YKL-KFGHRGANQPVRFTDGRI------FITTQNHGFAVDAESLPEGCRVTyTNVNDGTVEGFENRDMRLTT-VQFHPEA 331
Cdd:CHL00101  94 IKApKPMHGKTSKIYHNHDDLFqglpnpFTATRYHSLIIDPLNLPSPLEIT-AWTEDGLIMACRHKKYKMLRgIQFHPES 172
guaA PRK00074
GMP synthase; Reviewed
 195-330 2.97e-10

GMP synthase; Reviewed


Pssm-ID: 234614 [Multi-domain]  Cd Length: 511  Bit Score: 61.22  E-value: 2.97e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666 195 VFPYNATADQVRACKPDALFVSNGPgDPKQAPDAIRCIQNL--LGeLPIFGICMGNQVSALALGGD---TYKLKFGHrgA 269
Cdd:PRK00074  32 IVPYDISAEEIRAFNPKGIILSGGP-ASVYEEGAPRADPEIfeLG-VPVLGICYGMQLMAHQLGGKverAGKREYGR--A 107

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 851012666 270 NqpVRFTD-GRIF--ITTQ-----NHGFAVdaESLPEGCRVTYTNVNdGTVEGFENRDMRLTTVQFHPE 330
Cdd:PRK00074 108 E--LEVDNdSPLFkgLPEEqdvwmSHGDKV--TELPEGFKVIASTEN-CPIAAIANEERKFYGVQFHPE 171
PuuD COG2071
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ...
 239-332 1.64e-09

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: 57.49  E-value: 1.64e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666 239 LPIFGICMGNQVSALALGG-------DTYKLKFGHRGANQ------PVRFTDG----RIFITTQ---N--HGFAVDAesL 296
Cdd:COG2071   97 KPVLGICRGMQLLNVALGGtlyqdlpDQVPGALDHRQPAPryaprhTVEIEPGsrlaRILGEEEirvNslHHQAVKR--L 174

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 851012666 297 PEGCRVT-YTnvNDGTVEGFENRDMRLTT-VQFHPEAH 332
Cdd:COG2071  175 GPGLRVSaRA--PDGVIEAIESPGAPFVLgVQWHPEWL 210
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 239-330 9.94e-09

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


Pssm-ID: 153216 [Multi-domain]  Cd Length: 189  Bit Score: 54.50  E-value: 9.94e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666 239 LPIFGICMGNQVSALALGGDTYklkfghrganQPVRftdgrifiTTQNHGFAVDAesLPEGCRVTYTnVNDGTVEGFENR 318
Cdd:cd01745  101 KPILGICRGMQLLNVALGGTLY----------QDIR--------VNSLHHQAIKR--LADGLRVEAR-APDGVIEAIESP 159

                         90
                 ....*....|...
gi 851012666 319 DMRLTT-VQFHPE 330
Cdd:cd01745  160 DRPFVLgVQWHPE 172
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 240-330 1.50e-08

Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze the cleavage of the gamma-glutamyl bond in poly-gamma-glutamyl substrates. They are structurally related to pfam00117, but contain extensions in four loops and at the C terminus.


Pssm-ID: 429620 [Multi-domain]  Cd Length: 219  Bit Score: 54.57  E-value: 1.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666  240 PIFGICMGNQVSALALGGDTY------KLKFGHRGANQPVRFTD------------GRIFITTQ---N--HGFAVDAesL 296
Cdd:pfam07722 107 PILGICRGFQLLNVALGGTLYqdiqeqPGFTDHREHCQVAPYAPshavnvepgsllASLLGSEEfrvNslHHQAIDR--L 184

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 851012666  297 PEGCRVTYTNvNDGTVEGFE--NRDMRLTTVQFHPE 330
Cdd:pfam07722 185 APGLRVEAVA-PDGTIEAIEspNAKGFALGVQWHPE 219
PLN02347 PLN02347
GMP synthetase
 171-346 1.94e-07

GMP synthetase


Pssm-ID: 215197 [Multi-domain]  Cd Length: 536  Bit Score: 52.38  E-value: 1.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666 171 IAVIDLGIKKNMLtsLSKRNGDLYVF----PYNATADQVRACKPDALFVSNGP------GDPKQAPDAIRCIQNllGELP 240
Cdd:PLN02347  13 VLILDYGSQYTHL--ITRRVRELGVYslllSGTASLDRIASLNPRVVILSGGPhsvhveGAPTVPEGFFDYCRE--RGVP 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666 241 IFGICMGNQVSALALGGdtyKLKFGHRG--ANQPVRFT-DGRIF-----ITTQN----HGfaVDAESLPEGCRVTYTNVN 308
Cdd:PLN02347  89 VLGICYGMQLIVQKLGG---EVKPGEKQeyGRMEIRVVcGSQLFgdlpsGETQTvwmsHG--DEAVKLPEGFEVVAKSVQ 163

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 851012666 309 dGTVEGFENRDMRLTTVQFHPEAHGGPR--DTEAHFFDDL 346
Cdd:PLN02347 164 -GAVVAIENRERRIYGLQYHPEVTHSPKgmETLRHFLFDV 202
PRK05637 PRK05637
anthranilate synthase component II; Provisional
 195-294 2.08e-07

anthranilate synthase component II; Provisional


Pssm-ID: 180178 [Multi-domain]  Cd Length: 208  Bit Score: 51.00  E-value: 2.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666 195 VFPYNATADQVRACKPDALFVSNGPGDPKQAPDAIRCIQNLLGELPIFGICMGNQVSALALGGDTYKLKFGHrGANQPVR 274
Cdd:PRK05637  30 VFRNTVPVEEILAANPDLICLSPGPGHPRDAGNMMALIDRTLGQIPLLGICLGFQALLEHHGGKVEPCGPVH-GTTDNMI 108

                         90       100
                 ....*....|....*....|....
gi 851012666 275 FTDGR----IFittqnHGFAVDAE 294
Cdd:PRK05637 109 LTDAGvqspVF-----AGLATDVE 127
PRK06895 PRK06895
anthranilate synthase component II;
213-331 1.27e-05

anthranilate synthase component II;


Pssm-ID: 235882 [Multi-domain]  Cd Length: 190  Bit Score: 45.50  E-value: 1.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666 213 LFVSNGPGDPKQAPDAIRCIQNLLGELPIFGICMGNQVSALALGGDTYKLKFGHRGANQPV-RFTDGRIFI---TTQN-- 286
Cdd:PRK06895  47 ILISPGPDVPRAYPQLFAMLERYHQHKSILGVCLGHQTLCEFFGGELYNLNNVRHGQQRPLkVRSNSPLFDglpEEFNig 126

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 851012666 287 --HGFAVDAESLPEGCRVTYTnVNDGTVEGFENRDMRLTTVQFHPEA 331
Cdd:PRK06895 127 lyHSWAVSEENFPTPLEITAV-CDENVVMAMQHKTLPIYGVQFHPES 172
PRK09522 PRK09522
bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate ...
 197-257 6.40e-05

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


Pssm-ID: 181927 [Multi-domain]  Cd Length: 531  Bit Score: 44.63  E-value: 6.40e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 851012666 197 PYNATADQVRACKPDALFVSNGPGDPKQAPDAIRCIQNLLGELPIFGICMGNQVSALALGG 257
Cdd:PRK09522  36 PAQTLIERLATMSNPVLMLSPGPGVPSEAGCMPELLTRLRGKLPIIGICLGHQAIVEAYGG 96
GATase1_Glutamyl_Hydrolase cd01747
Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase; Type 1 ...
 240-330 7.11e-05

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: 43.85  E-value: 7.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666 240 PIFGICMG-NQVSALALGGDTYKLKFGHRGANQPVRFTD----GRIF---------------ITTQNHGFAVDAESLPEG 299
Cdd:cd01747   94 PVWGTCLGfELLTYLTSGETLLLEATEATNSALPLNFTEdalqSRLFkrfppdllkslatepLTMNNHRYGISPENFTEN 173

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 851012666 300 C------RVTYTNVNDGTVE---GFENRDMRLTTVQFHPE 330
Cdd:cd01747  174 GllsdffNVLTTNDDWNGVEfisTVEAYKYPIYGVQWHPE 213
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 171-250 7.60e-05

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: 41.82  E-value: 7.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666 171 IAVIDLGIKKNM-----LTSLSKRNGDLYVFPYNATA--DQVRACKPDALFVSNGPGDPK---QAPDAIRCIQNLLGE-L 239
Cdd:cd01653    1 VAVLLFPGFEELelaspLDALREAGAEVDVVSPDGGPveSDVDLDDYDGLILPGGPGTPDdlaRDEALLALLREAAAAgK 80

                         90
                 ....*....|.
gi 851012666 240 PIFGICMGNQV 250
Cdd:cd01653   81 PILGICLGAQL 91
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 171-250 3.65e-04

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: 39.11  E-value: 3.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851012666 171 IAVIDLGIKKNM-----LTSLSKRNGDLYVFPYNATA--DQVRACKPDALFVSNGPGDPK---QAPDAIRCIQNLLGE-L 239
Cdd:cd03128    1 VAVLLFGGSEELelaspLDALREAGAEVDVVSPDGGPveSDVDLDDYDGLILPGGPGTPDdlaWDEALLALLREAAAAgK 80

                         90
                 ....*....|.
gi 851012666 240 PIFGICMGNQV 250
Cdd:cd03128   81 PVLGICLGAQL 91
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH