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Conserved domains on  [gi|1080876380|gb|OFQ39134|]
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carbamoyl phosphate synthase small subunit [Staphylococcus sp. HMSC073C12]

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 ...
 1-355 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: 642.07  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380   1 MLERRYLVLEDGTFYEGYKLGSDELSIGEIVFNTAMTGYQETISDPSYTGQIITFTYPLIGNYGINRDDFEALTPTLNGV 80
Cdd:COG0505     1 MMMKALLVLEDGTVFEGKSFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVTFTYPHIGNYGVNDEDFESDRPWVAGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380  81 VVKEASTHPSNFRQQKTLHEVLVQYKIPGISGVDTRSITRKIRQHGVLRAAFTDCRENIDELINKLKSTE--LPRDEVMT 158
Cdd:COG0505    81 VVRELSRRPSNWRSEESLDEYLKEHGIPGISGIDTRALTRHLREKGAMKGVISTGDLDIEELLEKARAAPgmEGLDLVKE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380 159 VSTKTPYVST---GSNLSVVLLDFGKKQNIVRELNLRGCNVTVVPYDTTAEEILAMSPDGIMLSNGPGDPDVVEVAINMI 235
Cdd:COG0505   161 VSTKEPYEWTeapGAGFHVVALDFGVKRNILRELAERGCRVTVVPATTSAEEILALNPDGVFLSNGPGDPAALDYAIETI 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380 236 KGILGK-IPFFGICLGHQLFALSQGASSFKMKFGHRGANHPVKDLRTGKVDITSQNHGYAIDKDSLAQTDLEITHIALND 314
Cdd:COG0505   241 RELLGKgIPIFGICLGHQLLALALGAKTYKLKFGHRGANHPVKDLETGRVEITSQNHGFAVDEDSLPATDLEVTHVNLND 320

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1080876380 315 DTVEGLRHKTLPAFSVQYHPEARPGPSDSNYLFDDFIAMIN 355
Cdd:COG0505   321 GTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDRFIELME 361
 
Name Accession Description Interval E-value
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 1-355 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: 642.07  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380   1 MLERRYLVLEDGTFYEGYKLGSDELSIGEIVFNTAMTGYQETISDPSYTGQIITFTYPLIGNYGINRDDFEALTPTLNGV 80
Cdd:COG0505     1 MMMKALLVLEDGTVFEGKSFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVTFTYPHIGNYGVNDEDFESDRPWVAGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380  81 VVKEASTHPSNFRQQKTLHEVLVQYKIPGISGVDTRSITRKIRQHGVLRAAFTDCRENIDELINKLKSTE--LPRDEVMT 158
Cdd:COG0505    81 VVRELSRRPSNWRSEESLDEYLKEHGIPGISGIDTRALTRHLREKGAMKGVISTGDLDIEELLEKARAAPgmEGLDLVKE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380 159 VSTKTPYVST---GSNLSVVLLDFGKKQNIVRELNLRGCNVTVVPYDTTAEEILAMSPDGIMLSNGPGDPDVVEVAINMI 235
Cdd:COG0505   161 VSTKEPYEWTeapGAGFHVVALDFGVKRNILRELAERGCRVTVVPATTSAEEILALNPDGVFLSNGPGDPAALDYAIETI 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380 236 KGILGK-IPFFGICLGHQLFALSQGASSFKMKFGHRGANHPVKDLRTGKVDITSQNHGYAIDKDSLAQTDLEITHIALND 314
Cdd:COG0505   241 RELLGKgIPIFGICLGHQLLALALGAKTYKLKFGHRGANHPVKDLETGRVEITSQNHGFAVDEDSLPATDLEVTHVNLND 320

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1080876380 315 DTVEGLRHKTLPAFSVQYHPEARPGPSDSNYLFDDFIAMIN 355
Cdd:COG0505   321 GTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDRFIELME 361
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
1-354 0e+00

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 634.04  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380   1 MLERRYLVLEDGTFYEGYKLGSDELSIGEIVFNTAMTGYQETISDPSYTGQIITFTYPLIGNYGINRDDFEALTPTLNGV 80
Cdd:PRK12564    1 MMMKAYLVLEDGTVFEGKAFGAEGETVGEVVFNTSMTGYQEILTDPSYAGQIVTFTYPLIGNYGVNREDFESDRPHAKGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380  81 VVKEASTHPSNFRQQKTLHEVLVQYKIPGISGVDTRSITRKIRQHGVLRAAFTDCRENIDELINKLKSTE--LPRDEVMT 158
Cdd:PRK12564   81 IVRELSDIPSNWRSEMSLDEYLKENGIPGISGIDTRALTRKLREKGAMKGVIATEDFDAEELLEKARAFPglLGLDLVKE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380 159 VSTKTPYVSTGSN----LSVVLLDFGKKQNIVRELNLRGCNVTVVPYDTTAEEILAMSPDGIMLSNGPGDPDVVEVAINM 234
Cdd:PRK12564  161 VSTKEPYPWPGPGgelkYKVVAIDFGVKRNILRELAERGCRVTVVPATTTAEEILALNPDGVFLSNGPGDPAALDYAIEM 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380 235 IKGILG-KIPFFGICLGHQLFALSQGASSFKMKFGHRGANHPVKDLRTGKVDITSQNHGYAIDKDSLAqTDLEITHIALN 313
Cdd:PRK12564  241 IRELLEkKIPIFGICLGHQLLALALGAKTYKMKFGHRGANHPVKDLETGKVEITSQNHGFAVDEDSLP-ANLEVTHVNLN 319

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1080876380 314 DDTVEGLRHKTLPAFSVQYHPEARPGPSDSNYLFDDFIAMI 354
Cdd:PRK12564  320 DGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDEFVELM 360
CPSaseIIsmall TIGR01368
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ...
 5-356 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: 544.14  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380   5 RYLVLEDGTFYEGYKLGSDELSIGEIVFNTAMTGYQETISDPSYTGQIITFTYPLIGNYGINRDDFEALTPTLNGVVVKE 84
Cdd:TIGR01368   1 AYLVLEDGTVFRGYSFGAEGTVAGEVVFNTGMTGYQEILTDPSYKGQIVVFTYPLIGNYGVNDEDAESKGIHVSGLVVRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380  85 ASTHPSNFRQQKTLHEVLVQYKIPGISGVDTRSITRKIRQHGVLRAAFTDCRENIDELinKLKSTELPR----DEVMTVS 160
Cdd:TIGR01368  81 LSDRYSNWRATESLDQFLKRHGIPGIYGVDTRALVKKIREKGTMKGVISTEDSNDEEL--VEKARVSPDitgiNLVAEVS 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380 161 TKTPYV---STGSNLSVVLLDFGKKQNIVRELNLRGCNVTVVPYDTTAEEILAMSPDGIMLSNGPGDPDVVEVAINMIKG 237
Cdd:TIGR01368 159 TKEPYTwgqRGGKGKRVVVIDFGVKRNILRRLVKRGCEVTVVPYDTDAEEIKKYNPDGIFLSNGPGDPAAVEPAIETIRK 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380 238 ILGKIPFFGICLGHQLFALSQGASSFKMKFGHRGANHPVKDLRTGKVDITSQNHGYAIDKDSLAQTDLEITHIALNDDTV 317
Cdd:TIGR01368 239 LLEKIPIFGICLGHQLLALAFGAKTYKMKFGHRGGNHPVKDLITGRVEITSQNHGYAVDPDSLPAGDLEVTHVNLNDGTV 318

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1080876380 318 EGLRHKTLPAFSVQYHPEARPGPSDSNYLFDDFIAMINE 356
Cdd:TIGR01368 319 EGIRHKDLPVFSVQYHPEASPGPHDTEYLFDEFIDLMKK 357
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 174-351 8.03e-113

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: 325.99  E-value: 8.03e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380 174 VVLLDFGKKQNIVRELNLRGCNVTVVPYDTTAEEILAMSPDGIMLSNGPGDPDVVEVAINMIKGILGK-IPFFGICLGHQ 252
Cdd:cd01744     1 VVVIDFGVKHNILRELLKRGCEVTVVPYNTDAEEILKLDPDGIFLSNGPGDPALLDEAIKTVRKLLGKkIPIFGICLGHQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380 253 LFALSQGASSFKMKFGHRGANHPVKDLRTGKVDITSQNHGYAIDKDSLAQtDLEITHIALNDDTVEGLRHKTLPAFSVQY 332
Cdd:cd01744    81 LLALALGAKTYKMKFGHRGSNHPVKDLITGRVYITSQNHGYAVDPDSLPG-GLEVTHVNLNDGTVEGIRHKDLPVFSVQF 159

                         170
                  ....*....|....*....
gi 1080876380 333 HPEARPGPSDSNYLFDDFI 351
Cdd:cd01744   160 HPEASPGPHDTEYLFDEFL 178
CPSase_sm_chain smart01097
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 4-131 5.11e-77

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: 233.04  E-value: 5.11e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380    4 RRYLVLEDGTFYEGYKLGSDELSIGEIVFNTAMTGYQETISDPSYTGQIITFTYPLIGNYGINRDDFEALTPTLNGVVVK 83
Cdd:smart01097   2 KAYLVLEDGTVFEGESFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNDEDFESDKIQVKGLVVR 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1080876380   84 EASTHPSNFRQQKTLHEVLVQYKIPGISGVDTRSITRKIRQHGVLRAA 131
Cdd:smart01097  82 ELSDEPSNWRSEQSLDEFLKENGIPGISGIDTRALTRKLREKGAMKGV 129
CPSase_sm_chain pfam00988
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 7-131 2.10e-76

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: 231.45  E-value: 2.10e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380   7 LVLEDGTFYEGYKLGSDELSIGEIVFNTAMTGYQETISDPSYTGQIITFTYPLIGNYGINRDDFEALTPTLNGVVVKEAS 86
Cdd:pfam00988   1 LVLEDGTVFEGKSFGAAGSTVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNPEDFESDKIHVAGLVVREYS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1080876380  87 THPSNFRQQKTLHEVLVQYKIPGISGVDTRSITRKIRQHGVLRAA 131
Cdd:pfam00988  81 DEPSNWRAEESLDEWLKEQGIPGISGVDTRALTRKIREKGAMKGV 125
 
Name Accession Description Interval E-value
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 1-355 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: 642.07  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380   1 MLERRYLVLEDGTFYEGYKLGSDELSIGEIVFNTAMTGYQETISDPSYTGQIITFTYPLIGNYGINRDDFEALTPTLNGV 80
Cdd:COG0505     1 MMMKALLVLEDGTVFEGKSFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVTFTYPHIGNYGVNDEDFESDRPWVAGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380  81 VVKEASTHPSNFRQQKTLHEVLVQYKIPGISGVDTRSITRKIRQHGVLRAAFTDCRENIDELINKLKSTE--LPRDEVMT 158
Cdd:COG0505    81 VVRELSRRPSNWRSEESLDEYLKEHGIPGISGIDTRALTRHLREKGAMKGVISTGDLDIEELLEKARAAPgmEGLDLVKE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380 159 VSTKTPYVST---GSNLSVVLLDFGKKQNIVRELNLRGCNVTVVPYDTTAEEILAMSPDGIMLSNGPGDPDVVEVAINMI 235
Cdd:COG0505   161 VSTKEPYEWTeapGAGFHVVALDFGVKRNILRELAERGCRVTVVPATTSAEEILALNPDGVFLSNGPGDPAALDYAIETI 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380 236 KGILGK-IPFFGICLGHQLFALSQGASSFKMKFGHRGANHPVKDLRTGKVDITSQNHGYAIDKDSLAQTDLEITHIALND 314
Cdd:COG0505   241 RELLGKgIPIFGICLGHQLLALALGAKTYKLKFGHRGANHPVKDLETGRVEITSQNHGFAVDEDSLPATDLEVTHVNLND 320

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1080876380 315 DTVEGLRHKTLPAFSVQYHPEARPGPSDSNYLFDDFIAMIN 355
Cdd:COG0505   321 GTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDRFIELME 361
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
1-354 0e+00

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 634.04  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380   1 MLERRYLVLEDGTFYEGYKLGSDELSIGEIVFNTAMTGYQETISDPSYTGQIITFTYPLIGNYGINRDDFEALTPTLNGV 80
Cdd:PRK12564    1 MMMKAYLVLEDGTVFEGKAFGAEGETVGEVVFNTSMTGYQEILTDPSYAGQIVTFTYPLIGNYGVNREDFESDRPHAKGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380  81 VVKEASTHPSNFRQQKTLHEVLVQYKIPGISGVDTRSITRKIRQHGVLRAAFTDCRENIDELINKLKSTE--LPRDEVMT 158
Cdd:PRK12564   81 IVRELSDIPSNWRSEMSLDEYLKENGIPGISGIDTRALTRKLREKGAMKGVIATEDFDAEELLEKARAFPglLGLDLVKE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380 159 VSTKTPYVSTGSN----LSVVLLDFGKKQNIVRELNLRGCNVTVVPYDTTAEEILAMSPDGIMLSNGPGDPDVVEVAINM 234
Cdd:PRK12564  161 VSTKEPYPWPGPGgelkYKVVAIDFGVKRNILRELAERGCRVTVVPATTTAEEILALNPDGVFLSNGPGDPAALDYAIEM 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380 235 IKGILG-KIPFFGICLGHQLFALSQGASSFKMKFGHRGANHPVKDLRTGKVDITSQNHGYAIDKDSLAqTDLEITHIALN 313
Cdd:PRK12564  241 IRELLEkKIPIFGICLGHQLLALALGAKTYKMKFGHRGANHPVKDLETGKVEITSQNHGFAVDEDSLP-ANLEVTHVNLN 319

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1080876380 314 DDTVEGLRHKTLPAFSVQYHPEARPGPSDSNYLFDDFIAMI 354
Cdd:PRK12564  320 DGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDEFVELM 360
CPSaseIIsmall TIGR01368
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ...
 5-356 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: 544.14  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380   5 RYLVLEDGTFYEGYKLGSDELSIGEIVFNTAMTGYQETISDPSYTGQIITFTYPLIGNYGINRDDFEALTPTLNGVVVKE 84
Cdd:TIGR01368   1 AYLVLEDGTVFRGYSFGAEGTVAGEVVFNTGMTGYQEILTDPSYKGQIVVFTYPLIGNYGVNDEDAESKGIHVSGLVVRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380  85 ASTHPSNFRQQKTLHEVLVQYKIPGISGVDTRSITRKIRQHGVLRAAFTDCRENIDELinKLKSTELPR----DEVMTVS 160
Cdd:TIGR01368  81 LSDRYSNWRATESLDQFLKRHGIPGIYGVDTRALVKKIREKGTMKGVISTEDSNDEEL--VEKARVSPDitgiNLVAEVS 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380 161 TKTPYV---STGSNLSVVLLDFGKKQNIVRELNLRGCNVTVVPYDTTAEEILAMSPDGIMLSNGPGDPDVVEVAINMIKG 237
Cdd:TIGR01368 159 TKEPYTwgqRGGKGKRVVVIDFGVKRNILRRLVKRGCEVTVVPYDTDAEEIKKYNPDGIFLSNGPGDPAAVEPAIETIRK 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380 238 ILGKIPFFGICLGHQLFALSQGASSFKMKFGHRGANHPVKDLRTGKVDITSQNHGYAIDKDSLAQTDLEITHIALNDDTV 317
Cdd:TIGR01368 239 LLEKIPIFGICLGHQLLALAFGAKTYKMKFGHRGGNHPVKDLITGRVEITSQNHGYAVDPDSLPAGDLEVTHVNLNDGTV 318

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1080876380 318 EGLRHKTLPAFSVQYHPEARPGPSDSNYLFDDFIAMINE 356
Cdd:TIGR01368 319 EGIRHKDLPVFSVQYHPEASPGPHDTEYLFDEFIDLMKK 357
PRK12838 PRK12838
carbamoyl phosphate synthase small subunit; Reviewed
 5-356 0e+00

carbamoyl phosphate synthase small subunit; Reviewed


Pssm-ID: 183784 [Multi-domain]  Cd Length: 354  Bit Score: 521.37  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380   5 RYLVLEDGTFYEGYKLGSDELSIGEIVFNTAMTGYQETISDPSYTGQIITFTYPLIGNYGINRDDFEALTPTLNGVVVKE 84
Cdd:PRK12838    3 AYLILEDGTVFEGELIGAPIDVTGEIVFNTGMTGYQEVLTDPSYKGQIVVFTYPLIGNYGINADDYESKQPQVKGVIVYE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380  85 ASTHPSNFRQQKTLHEVLVQYKIPGISGVDTRSITRKIRQHGVLRAAFTDcrENIDELINKLKSTELPRDEVMTVSTKTP 164
Cdd:PRK12838   83 LSREGSHYRAKQSLDDFLKEWNIPGISGVDTRALVKHIREKGTMKASITT--TDDAHAFDQIKALVLPKNVVAQVSTKEP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380 165 YVSTGSNLSVVLLDFGKKQNIVRELNLRGCNVTVVPYDTTAEEILAMSPDGIMLSNGPGDPDVVEVAINMIKGILGKIPF 244
Cdd:PRK12838  161 YTYGNGGKHVALIDFGYKKSILRSLSKRGCKVTVLPYDTSLEEIKNLNPDGIVLSNGPGDPKELQPYLPEIKKLISSYPI 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380 245 FGICLGHQLFALSQGASSFKMKFGHRGANHPVKDLRTGKVDITSQNHGYAIDKDSLAQTDLEITHIALNDDTVEGLRHKT 324
Cdd:PRK12838  241 LGICLGHQLIALALGADTEKLPFGHRGANHPVIDLTTGRVWMTSQNHGYVVDEDSLDGTPLSVRFFNVNDGSIEGLRHKK 320

                         330       340       350
                  ....*....|....*....|....*....|..
gi 1080876380 325 LPAFSVQYHPEARPGPSDSNYLFDDFIAMINE 356
Cdd:PRK12838  321 KPVLSVQFHPEAHPGPHDAEYIFDEFLEMMEK 352
carA CHL00197
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
 7-360 4.83e-134

carbamoyl-phosphate synthase arginine-specific small subunit; Provisional


Pssm-ID: 214392 [Multi-domain]  Cd Length: 382  Bit Score: 387.62  E-value: 4.83e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380   7 LVLEDGTFYEGYKLGSDELSIGEIVFNTAMTGYQETISDPSYTGQIITFTYPLIGNYGINRDDFEALTPTLNGVVVKEAS 86
Cdd:CHL00197    9 LVLEDGTYYRGWSFSNPITTIGEVVFNTGMTGYQEIITDPSYFEQIVTFTYPEIGNTGINLEDIESVKIQVKGIIAKNIC 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380  87 THPSNFRQQKTLHEVLVQYKIPGISGVDTRSITRKIRQHGVLRAAFTDCRENIDELINKLKS--TELPRDEVMTVSTKTP 164
Cdd:CHL00197   89 KSSSNWRQQESLVSYLQRHKIPFIFGIDTRALTQHLRRFGTMNGCISNQNLNLSYLRAKIKEspHMPSSDLIPRVTTSSY 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380 165 Y-----------------VSTGSNLSVVLLDFGKKQNIVRELNLRGCNVTVVPYDTTAEEILAMSPDGIMLSNGPGDPDV 227
Cdd:CHL00197  169 YewdekshpsfyladnkrPHSSYQLKIIVIDFGVKYNILRRLKSFGCSITVVPATSPYQDILSYQPDGILLSNGPGDPSA 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380 228 VEVAINMIKGILG-KIPFFGICLGHQLFALSQGASSFKMKFGHRGANHPVKDLRtgKVDITSQNHGYAIDKDSLAQTDLE 306
Cdd:CHL00197  249 IHYGIKTVKKLLKyNIPIFGICMGHQILSLALEAKTFKLKFGHRGLNHPSGLNQ--QVEITSQNHGFAVNLESLAKNKFY 326

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1080876380 307 ITHIALNDDTVEGLRHKTLPAFSVQYHPEARPGPSDSNYLFDDFIAMINEFKEK 360
Cdd:CHL00197  327 ITHFNLNDGTVAGISHSPKPYFSVQYHPEASPGPHDADYLFEYFIEIIKHSKSS 380
PLN02771 PLN02771
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
 7-347 5.01e-115

carbamoyl-phosphate synthase (glutamine-hydrolyzing)


Pssm-ID: 178370 [Multi-domain]  Cd Length: 415  Bit Score: 340.42  E-value: 5.01e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380   7 LVLEDGTFYEGYKLGSDELSIGEIVFNTAMTGYQETISDPSYTGQIITFTYPLIGNYGINRDDFEALTPTLNGVVVKEAS 86
Cdd:PLN02771   59 LVLEDGSVWKAKSFGARGTQVGEVVFNTSLTGYQEILTDPSYAGQFVLMTNPHIGNTGVNFDDEESRQCFLAGLVIRSLS 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380  87 THPSNFRQQKTLHEVLVQYKIPGISGVDTRSITRKIRQHGVLRAAF-TDCRENIDELINKLKSTELPR-DEVMTVSTKTP 164
Cdd:PLN02771  139 ISTSNWRCTKTLGDYLAERNIMGIYDVDTRAITRRLREDGSLIGVLsTEDSKTDEELLKMSRSWDIVGiDLISGVSCKSP 218

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380 165 YV---------------STGSNLSVVLLDFGKKQNIVRELNLRGCNVTVVPYDTTAEEILAMSPDGIMLSNGPGDPDVVE 229
Cdd:PLN02771  219 YEwvdktnpewdfntnsRDGESYHVIAYDFGIKHNILRRLASYGCKITVVPSTWPASEALKMKPDGVLFSNGPGDPSAVP 298

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380 230 VAINMIKGILGKIPFFGICLGHQLFALSQGASSFKMKFGHRGANHPVKDLRTGKVDITSQNHGYAIDKDSLAQtDLEITH 309
Cdd:PLN02771  299 YAVETVKELLGKVPVFGICMGHQLLGQALGGKTFKMKFGHHGGNHPVRNNRTGRVEISAQNHNYAVDPASLPE-GVEVTH 377

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1080876380 310 IALNDDTVEGLRHKTLPAFSVQYHPEARPGPSDSNYLF 347
Cdd:PLN02771  378 VNLNDGSCAGLAFPALNVMSLQYHPEASPGPHDSDNAF 415
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 174-351 8.03e-113

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: 325.99  E-value: 8.03e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380 174 VVLLDFGKKQNIVRELNLRGCNVTVVPYDTTAEEILAMSPDGIMLSNGPGDPDVVEVAINMIKGILGK-IPFFGICLGHQ 252
Cdd:cd01744     1 VVVIDFGVKHNILRELLKRGCEVTVVPYNTDAEEILKLDPDGIFLSNGPGDPALLDEAIKTVRKLLGKkIPIFGICLGHQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380 253 LFALSQGASSFKMKFGHRGANHPVKDLRTGKVDITSQNHGYAIDKDSLAQtDLEITHIALNDDTVEGLRHKTLPAFSVQY 332
Cdd:cd01744    81 LLALALGAKTYKMKFGHRGSNHPVKDLITGRVYITSQNHGYAVDPDSLPG-GLEVTHVNLNDGTVEGIRHKDLPVFSVQF 159

                         170
                  ....*....|....*....
gi 1080876380 333 HPEARPGPSDSNYLFDDFI 351
Cdd:cd01744   160 HPEASPGPHDTEYLFDEFL 178
CPSase_sm_chain smart01097
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 4-131 5.11e-77

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: 233.04  E-value: 5.11e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380    4 RRYLVLEDGTFYEGYKLGSDELSIGEIVFNTAMTGYQETISDPSYTGQIITFTYPLIGNYGINRDDFEALTPTLNGVVVK 83
Cdd:smart01097   2 KAYLVLEDGTVFEGESFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNDEDFESDKIQVKGLVVR 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1080876380   84 EASTHPSNFRQQKTLHEVLVQYKIPGISGVDTRSITRKIRQHGVLRAA 131
Cdd:smart01097  82 ELSDEPSNWRSEQSLDEFLKENGIPGISGIDTRALTRKLREKGAMKGV 129
CPSase_sm_chain pfam00988
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 7-131 2.10e-76

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: 231.45  E-value: 2.10e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380   7 LVLEDGTFYEGYKLGSDELSIGEIVFNTAMTGYQETISDPSYTGQIITFTYPLIGNYGINRDDFEALTPTLNGVVVKEAS 86
Cdd:pfam00988   1 LVLEDGTVFEGKSFGAAGSTVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNPEDFESDKIHVAGLVVREYS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1080876380  87 THPSNFRQQKTLHEVLVQYKIPGISGVDTRSITRKIRQHGVLRAA 131
Cdd:pfam00988  81 DEPSNWRAEESLDEWLKEQGIPGISGVDTRALTRKIREKGAMKGV 125
GATase pfam00117
Glutamine amidotransferase class-I;
175-353 4.36e-69

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 214.79  E-value: 4.36e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380 175 VLLDFGK--KQNIVRELNLRGCNVTVVPYDTTAEEILAMSPDGIMLSNGPGDPDVVEVAINMIKGILG-KIPFFGICLGH 251
Cdd:pfam00117   1 LLIDNGDsfTYNLARALRELGVEVTVVPNDTPAEEILEENPDGIILSGGPGSPGAAGGAIEAIREARElKIPILGICLGH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380 252 QLFALSQGASSFKMK-FGHRGANHPVKD------LRTGKVDITSQNHGYAIDKDSLaQTDLEITHIALNDDTVEGLRHKT 324
Cdd:pfam00117  81 QLLALAFGGKVVKAKkFGHHGKNSPVGDdgcglfYGLPNVFIVRRYHSYAVDPDTL-PDGLEVTATSENDGTIMGIRHKK 159

                         170       180
                  ....*....|....*....|....*....
gi 1080876380 325 LPAFSVQYHPEARPGPSDSNYLFDDFIAM 353
Cdd:pfam00117 160 LPIFGVQFHPESILTPHGPEILFNFFIKA 188
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 184-335 3.43e-30

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: 113.78  E-value: 3.43e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380 184 NIVRELNLRGCNVTVVPYD-TTAEEILAMSPDGIMLSNGPGDPDVVEVAINMIKGILGKIPFFGICLGHQLFALSQGASS 262
Cdd:cd01743    13 NLVQYLRELGAEVVVVRNDeITLEELELLNPDAIVISPGPGHPEDAGISLEIIRALAGKVPILGVCLGHQAIAEAFGGKV 92

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1080876380 263 FKMKFGHRGANHPVKDLRTGKVDITSQN------HGYAIDKDSLaqTDLEITHIALNDDTVEGLRHKTLPAFSVQYHPE 335
Cdd:cd01743    93 VRAPEPMHGKTSEIHHDGSGLFKGLPQPftvgryHSLVVDPDPL--PDLLEVTASTEDGVIMALRHRDLPIYGVQFHPE 169
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 184-335 2.10e-27

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: 106.66  E-value: 2.10e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380 184 NIV---RELnlrGCNVTVVPYD-TTAEEILAMSPDGIMLSNGPGDPDVVEVAINMIKGILGKIPFFGICLGHQLFALSQG 259
Cdd:COG0512    13 NLVqylGEL---GAEVVVVRNDeITLEEIEALAPDGIVLSPGPGTPEEAGISLEVIRAFAGKIPILGVCLGHQAIGEAFG 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380 260 AssfkmKFGHrgANHPVKdlrtGKVD-ITSQNHG-------------Y---AIDKDSLAqTDLEIThiALNDD-TVEGLR 321
Cdd:COG0512    90 G-----KVVR--APEPMH----GKTSpITHDGSGlfaglpnpftatrYhslVVDRETLP-DELEVT--AWTEDgEIMGIR 155

                         170
                  ....*....|....
gi 1080876380 322 HKTLPAFSVQYHPE 335
Cdd:COG0512   156 HRELPIEGVQFHPE 169
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 184-335 1.45e-25

anthranilate synthase component II; Provisional


Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 101.74  E-value: 1.45e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380 184 NIVRELNLRGCNVTVVPYDT-TAEEILAMSPDGIMLSNGPGDPDVVEVAINMIKGILGKIPFFGICLGHQLFALSQGass 262
Cdd:PRK05670   14 NLVQYLGELGAEVVVYRNDEiTLEEIEALNPDAIVLSPGPGTPAEAGISLELIREFAGKVPILGVCLGHQAIGEAFG--- 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380 263 fkmkfGH-RGANHPVKdlrtGKVD-ITSQNHG-------------Y---AIDKDSLAQtDLEITHIAlNDDTVEGLRHKT 324
Cdd:PRK05670   91 -----GKvVRAKEIMH----GKTSpIEHDGSGifaglpnpftvtrYhslVVDRESLPD-CLEVTAWT-DDGEIMGVRHKE 159

                         170
                  ....*....|.
gi 1080876380 325 LPAFSVQYHPE 335
Cdd:PRK05670  160 LPIYGVQFHPE 170
PRK14607 PRK14607
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
198-336 2.22e-20

bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;


Pssm-ID: 237764 [Multi-domain]  Cd Length: 534  Bit Score: 92.47  E-value: 2.22e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380 198 VVPYDTTAEEILAMSPDGIMLSNGPGDPDVVEVAINMIKGILGKIPFFGICLGHQLFALSQGASSFKMKFGHRGANHPV- 276
Cdd:PRK14607   30 VRNDEITIEEIEALNPSHIVISPGPGRPEEAGISVEVIRHFSGKVPILGVCLGHQAIGYAFGGKIVHAKRILHGKTSPId 109

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1080876380 277 ---KDL-RT-GKVDITSQNHGYAIDKDSLAQtDLEITHIAlNDDTVEGLRHKTLPAFSVQYHPEA 336
Cdd:PRK14607  110 hngKGLfRGiPNPTVATRYHSLVVEEASLPE-CLEVTAKS-DDGEIMGIRHKEHPIFGVQFHPES 172
trpG_papA TIGR00566
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ...
 184-336 8.66e-18

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: 80.22  E-value: 8.66e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380 184 NIVRELNLRGCNVTVVPYDT-TAEEILAMSPDGIMLSNGPGDPDVVEVAINMIKGILGKIPFFGICLGHQLFALSQGAS- 261
Cdd:TIGR00566  14 NLVQYFCELGAEVVVKRNDSlTLQEIEALLPLLIVISPGPCTPNEAGISLEAIRHFAGKLPILGVCLGHQAMGQAFGGDv 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380 262 SFKMKFGH--------------RGANHPVKDLRTgkvditsqnHGYAIDKDSLAQTdLEITHIALNDDTVEGLRHKTLPA 327
Cdd:TIGR00566  94 VRANTVMHgktseiehngagifRGLFNPLTATRY---------HSLVVEPETLPTC-FPVTAWEEENIEIMAIRHRDLPL 163


                  ....*....
gi 1080876380 328 FSVQYHPEA 336
Cdd:TIGR00566 164 EGVQFHPES 172
PRK07649 PRK07649
aminodeoxychorismate/anthranilate synthase component II;
184-336 1.41e-16

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181066 [Multi-domain]  Cd Length: 195  Bit Score: 77.15  E-value: 1.41e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380 184 NIVRELNLRGCNVTVVPYD-TTAEEILAMSPDGIMLSNGPGDPDVVEVAINMIKGILGKIPFFGICLGHQLFALSQGASS 262
Cdd:PRK07649   14 NLVQFLGELGQELVVKRNDeVTISDIENMKPDFLMISPGPCSPNEAGISMEVIRYFAGKIPIFGVCLGHQSIAQVFGGEV 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380 263 FKMKFGHRGANHPVK-DLRTGKVDITS-----QNHGYAIDKDSLAQTdLEITHiALNDDTVEGLRHKTLPAFSVQYHPEA 336
Cdd:PRK07649   94 VRAERLMHGKTSLMHhDGKTIFSDIPNpftatRYHSLIVKKETLPDC-LEVTS-WTEEGEIMAIRHKTLPIEGVQFHPES 171
GATase1_GMP_Synthase cd01742
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ...
 174-335 2.03e-16

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: 76.42  E-value: 2.03e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380 174 VVLLDFGKK--QNIVRelNLRGCNVT--VVPYDTTAEEILAMSPDGIMLSNGPG----------DPDVVEVainmikgil 239
Cdd:cd01742     1 ILILDFGSQytHLIAR--RVRELGVYseILPNTTPLEEIKLKNPKGIILSGGPSsvyeedaprvDPEIFEL--------- 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380 240 gKIPFFGICLGHQLFALSQGA---SSFKMKFGHRGANHPVKDLRTGKVDITSQ---NHGYAIDK-----DSLAQTDleit 308
Cdd:cd01742    70 -GVPVLGICYGMQLIAKALGGkveRGDKREYGKAEIEIDDSSPLFEGLPDEQTvwmSHGDEVVKlpegfKVIASSD---- 144

                         170       180
                  ....*....|....*....|....*..
gi 1080876380 309 hialnDDTVEGLRHKTLPAFSVQYHPE 335
Cdd:cd01742   145 -----NCPVAAIANEEKKIYGVQFHPE 166
PLN02335 PLN02335
anthranilate synthase
 193-364 2.11e-15

anthranilate synthase


Pssm-ID: 177969 [Multi-domain]  Cd Length: 222  Bit Score: 74.45  E-value: 2.11e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380 193 GCNVTVVPYD-TTAEEILAMSPDGIMLSNGPGDPDVVEVAINMIKGILGKIPFFGICLGHQLFALSQGASSFKMKFG--H 269
Cdd:PLN02335   42 GCHFEVYRNDeLTVEELKRKNPRGVLISPGPGTPQDSGISLQTVLELGPLVPLFGVCMGLQCIGEAFGGKIVRSPFGvmH 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380 270 rGANHPV---KDLRTGKVD------ITSQNHGYAIDKDSLAQTDLEIThiALNDD-TVEGLRHKTLPAFS-VQYHPEARP 338
Cdd:PLN02335  122 -GKSSPVhydEKGEEGLFSglpnpfTAGRYHSLVIEKDTFPSDELEVT--AWTEDgLIMAARHRKYKHIQgVQFHPESII 198

                         170       180
                  ....*....|....*....|....*.
gi 1080876380 339 gPSDSNYLFDDFIAMINEfKEKERNT 364
Cdd:PLN02335  199 -TTEGKTIVRNFIKIIEK-KESEKLT 222
guaA_Nterm TIGR00888
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ...
 174-337 3.93e-15

GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine de novo biosynthesis is well-conserved. However, it appears to split into two separate polypeptide chains in most of the Archaea. This N-terminal region would be the smaller subunit. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 129966 [Multi-domain]  Cd Length: 188  Bit Score: 72.73  E-value: 3.93e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380 174 VVLLDFGKK--QNIVRELNLRGCNVTVVPYDTTAEEILAMSPDGIMLSNGPgDPDVVEVAINMIKGILG-KIPFFGICLG 250
Cdd:TIGR00888   1 ILVLDFGSQytQLIARRLRELGVYSELVPNTTPLEEIREKNPKGIILSGGP-SSVYAENAPRADEKIFElGVPVLGICYG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380 251 HQLFAlsqgassfkMKFGhrganhpvkdlrtGKVDITS-QNHGYA---IDKDSLAQTDLEI------TH----------- 309
Cdd:TIGR00888  80 MQLMA---------KQLG-------------GEVGRAEkREYGKAeleILDEDDLFRGLPDestvwmSHgdkvkelpegf 137

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1080876380 310 --IALNDDT-VEGLRHKTLPAFSVQYHPEAR 337
Cdd:TIGR00888 138 kvLATSDNCpVAAMAHEEKPIYGVQFHPEVT 168
PRK06774 PRK06774
aminodeoxychorismate synthase component II;
193-336 4.47e-15

aminodeoxychorismate synthase component II;


Pssm-ID: 180689 [Multi-domain]  Cd Length: 191  Bit Score: 72.97  E-value: 4.47e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380 193 GCNVTVVPYDT-TAEEILAMSPDGIMLSNGPGDPDVVEVAINMIKGILGKIPFFGICLGHQLFALSQGASSFKMKFGHRG 271
Cdd:PRK06774   23 GTEVMVKRNDElQLTDIEQLAPSHLVISPGPCTPNEAGISLAVIRHFADKLPILGVCLGHQALGQAFGARVVRARQVMHG 102

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1080876380 272 ANHPVKDLRTGKVD------ITSQNHGYAIDKDSLAQTdLEITHIALND---DTVEGLRHKTLPAFSVQYHPEA 336
Cdd:PRK06774  103 KTSAICHSGQGVFRglnqplTVTRYHSLVIAADSLPGC-FELTAWSERGgemDEIMGIRHRTLPLEGVQFHPES 175
PRK00758 PRK00758
GMP synthase subunit A; Validated
 174-335 2.37e-13

GMP synthase subunit A; Validated


Pssm-ID: 179112 [Multi-domain]  Cd Length: 184  Bit Score: 67.57  E-value: 2.37e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380 174 VVLLDFGKKQN--IVRELNLRGCNVTVVPYDTTAEEILAMsPDGIMLSNGPgDPDVVEVAINMIKGIlgKIPFFGICLGH 251
Cdd:PRK00758    2 IVVVDNGGQYNhlIHRTLRYLGVDAKIIPNTTPVEEIKAF-EDGLILSGGP-DIERAGNCPEYLKEL--DVPILGICLGH 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380 252 QLFALSQGASSFKMKFGHRGANhpvkdlrtgKVDITSQN---HGY-------AIDKDSLAQTDLEITHIAlNDDT--VEG 319
Cdd:PRK00758   78 QLIAKAFGGEVGRGEYGEYALV---------EVEILDEDdilKGLppeirvwASHADEVKELPDGFEILA-RSDIceVEA 147

                         170
                  ....*....|....*.
gi 1080876380 320 LRHKTLPAFSVQYHPE 335
Cdd:PRK00758  148 MKHKEKPIYGVQFHPE 163
PRK08857 PRK08857
aminodeoxychorismate/anthranilate synthase component II;
193-336 2.49e-13

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181566 [Multi-domain]  Cd Length: 193  Bit Score: 67.98  E-value: 2.49e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380 193 GCNVTVVPYDTT-AEEILAMSPDGIMLSNGPGDPDVVEVAINMIKGILGKIPFFGICLGHQLFALSQGASSFKMKFGHRG 271
Cdd:PRK08857   23 GAQVKVVRNDEIdIDGIEALNPTHLVISPGPCTPNEAGISLQAIEHFAGKLPILGVCLGHQAIAQVFGGQVVRARQVMHG 102

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1080876380 272 ANHPVKdlRTGKVDITSQN--------HGYAIDKDSLAQTdLEITHIALND----DTVEGLRHKTLPAFSVQYHPEA 336
Cdd:PRK08857  103 KTSPIR--HTGRSVFKGLNnpltvtryHSLVVKNDTLPEC-FELTAWTELEdgsmDEIMGFQHKTLPIEAVQFHPES 176
PRK08007 PRK08007
aminodeoxychorismate synthase component 2;
202-336 4.39e-13

aminodeoxychorismate synthase component 2;


Pssm-ID: 181194 [Multi-domain]  Cd Length: 187  Bit Score: 67.25  E-value: 4.39e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380 202 DTTAEEILAMSPDGIMLSNGPGDPDVVEVAINMIKGILGKIPFFGICLGHQLFALSQGASSFKMKFGHRGANHPVKDLRT 281
Cdd:PRK08007   33 ALTLADIDALKPQKIVISPGPCTPDEAGISLDVIRHYAGRLPILGVCLGHQAMAQAFGGKVVRAAKVMHGKTSPITHNGE 112

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1080876380 282 GKVD------ITSQNHGYAIDKDSLAQTdLEITHIALNDDtVEGLRHKTLPAFSVQYHPEA 336
Cdd:PRK08007  113 GVFRglanplTVTRYHSLVVEPDSLPAC-FEVTAWSETRE-IMGIRHRQWDLEGVQFHPES 171
PRK05637 PRK05637
anthranilate synthase component II; Provisional
 174-341 5.40e-13

anthranilate synthase component II; Provisional


Pssm-ID: 180178 [Multi-domain]  Cd Length: 208  Bit Score: 67.18  E-value: 5.40e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380 174 VVLLDFGKK--QNIVRELNLRGCNVTVVPYDTTAEEILAMSPDGIMLSNGPGDPDVVEVAINMIKGILGKIPFFGICLGH 251
Cdd:PRK05637    4 VVLIDNHDSfvYNLVDAFAVAGYKCTVFRNTVPVEEILAANPDLICLSPGPGHPRDAGNMMALIDRTLGQIPLLGICLGF 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380 252 QLFALSQG----------ASSFKMKFGHRGANHPVKDLRTGKVDITSQN-HGYAI---------------DKDSLAQTDL 305
Cdd:PRK05637   84 QALLEHHGgkvepcgpvhGTTDNMILTDAGVQSPVFAGLATDVEPDHPEiPGRKVpiaryhslgcvvapdGMESLGTCSS 163

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1080876380 306 EITHIALNDDTVEGLrhktlpAFSVQYHPEARPGPS 341
Cdd:PRK05637  164 EIGPVIMAAETTDGK------AIGLQFHPESVLSPT 193
PRK07765 PRK07765
aminodeoxychorismate/anthranilate synthase component II;
184-335 9.92e-13

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181107 [Multi-domain]  Cd Length: 214  Bit Score: 66.61  E-value: 9.92e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380 184 NIVRELNLRGCNVTVVPYD---TTAEEILAMSPDGIMLSNGPGDPDVVEVAINMIKGILG-KIPFFGICLGHQLFALSQG 259
Cdd:PRK07765   15 NLVQYLGQLGVEAEVWRNDdprLADEAAVAAQFDGVLLSPGPGTPERAGASIDMVRACAAaGTPLLGVCLGHQAIGVAFG 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380 260 ASSFKMKFGHRGANHPVKDLRTGKVD------ITSQNHGYAIDKDSLAQtDLEIThiALNDD-TVEGLRHKTLPAFSVQY 332
Cdd:PRK07765   95 ATVDRAPELLHGKTSSVHHTGVGVLAglpdpfTATRYHSLTILPETLPA-ELEVT--ARTDSgVIMAVRHRELPIHGVQF 171


                  ...
gi 1080876380 333 HPE 335
Cdd:PRK07765  172 HPE 174
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 183-351 1.05e-11

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


Pssm-ID: 153216 [Multi-domain]  Cd Length: 189  Bit Score: 62.98  E-value: 1.05e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380 183 QNIVRELNLRGCNVTVVPYDTTAEEILAMSP--DGIMLS-----------------NGPGDP--DVVEVAInmIKGIL-G 240
Cdd:cd01745    22 QYYVDAVRKAGGLPVLLPPVDDEEDLEQYLEllDGLLLTgggdvdpplygeephpeLGPIDPerDAFELAL--LRAALeR 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380 241 KIPFFGICLGHQLFALSQGASSFkmkfghrganhpvKDLRtgkvdITSqNHGYAIDKdsLAQtDLEITHIAlNDDTVEGL 320
Cdd:cd01745   100 GKPILGICRGMQLLNVALGGTLY-------------QDIR-----VNS-LHHQAIKR--LAD-GLRVEARA-PDGVIEAI 156

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1080876380 321 RHKTLP-AFSVQYHPE-ARPGPSDSNYLFDDFI 351
Cdd:cd01745   157 ESPDRPfVLGVQWHPEwLADTDPDSLKLFEAFV 189
trpG CHL00101
anthranilate synthase component 2
 183-336 1.72e-11

anthranilate synthase component 2


Pssm-ID: 214365 [Multi-domain]  Cd Length: 190  Bit Score: 62.44  E-value: 1.72e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380 183 QNIVRELNLRGCNVTVVPYDT-TAEEILAMSPDGIMLSNGPGDPDVVEVAINMIKGILGKIPFFGICLGHQLFALSQGAS 261
Cdd:CHL00101   13 YNLVQSLGELNSDVLVCRNDEiDLSKIKNLNIRHIIISPGPGHPRDSGISLDVISSYAPYIPILGVCLGHQSIGYLFGGK 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380 262 SFKM-KFGHRGAN---HPVKDLRTGKVD--ITSQNHGYAIDKDSLaQTDLEITHIAlNDDTVEGLRHKTLPA-FSVQYHP 334
Cdd:CHL00101   93 IIKApKPMHGKTSkiyHNHDDLFQGLPNpfTATRYHSLIIDPLNL-PSPLEITAWT-EDGLIMACRHKKYKMlRGIQFHP 170


                  ..
gi 1080876380 335 EA 336
Cdd:CHL00101  171 ES 172
guaA PRK00074
GMP synthase; Reviewed
 173-255 9.37e-11

GMP synthase; Reviewed


Pssm-ID: 234614 [Multi-domain]  Cd Length: 511  Bit Score: 63.14  E-value: 9.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380 173 SVVLLDFGKK--QNIVRELnlRGCNV--TVVPYDTTAEEILAMSPDGIMLSNGP------GDPDVVEVAINMikgilgKI 242
Cdd:PRK00074    5 KILILDFGSQytQLIARRV--RELGVysEIVPYDISAEEIRAFNPKGIILSGGPasvyeeGAPRADPEIFEL------GV 76

                          90
                  ....*....|...
gi 1080876380 243 PFFGICLGHQLFA 255
Cdd:PRK00074   77 PVLGICYGMQLMA 89
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 183-338 1.77e-10

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: 60.34  E-value: 1.77e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380 183 QNIVRELNLRGCNVTVV--------PYDTTAEEilamsPDGIMLSNGPG----DPDVVEVAINMIKGIL-GKIPFFGICL 249
Cdd:COG0518    16 GLIARRLREAGIELDVLrvyageilPYDPDLED-----PDGLILSGGPMsvydEDPWLEDEPALIREAFeLGKPVLGICY 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380 250 GHQLFALSQGASSFKMK---FGHrganHPVKdlRTGKVDITS---------QNHGYAIDK-----DSLAQTDleithial 312
Cdd:COG0518    91 GAQLLAHALGGKVEPGPgreIGW----APVE--LTEADPLFAglpdeftvwMSHGDTVTElpegaEVLASSD-------- 156

                         170       180
                  ....*....|....*....|....*.
gi 1080876380 313 nDDTVEGLRHKTlPAFSVQYHPEARP 338
Cdd:COG0518   157 -NCPNQAFRYGR-RVYGVQFHPEVTH 180
PRK13566 PRK13566
anthranilate synthase component I;
168-335 3.99e-10

anthranilate synthase component I;


Pssm-ID: 237429 [Multi-domain]  Cd Length: 720  Bit Score: 61.09  E-value: 3.99e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380 168 TGSNLSVVLLDFGKK-----QNIVRELnlrGCNVTVVPYDTtAEEILA-MSPDGIMLSNGPGDPDVVEVAiNMIKGILGK 241
Cdd:PRK13566  523 VGEGKRVLLVDHEDSfvhtlANYFRQT---GAEVTTVRYGF-AEEMLDrVNPDLVVLSPGPGRPSDFDCK-ATIDAALAR 597

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380 242 -IPFFGICLGHQ---------LFALSQGASSFKMKFGHRGANHPVKDL----RTGKVditsqnHGYAIDKDSLAQtDLEI 307
Cdd:PRK13566  598 nLPIFGVCLGLQaiveafggeLGQLAYPMHGKPSRIRVRGPGRLFSGLpeefTVGRY------HSLFADPETLPD-ELLV 670

                         170       180
                  ....*....|....*....|....*...
gi 1080876380 308 THIAlNDDTVEGLRHKTLPAFSVQYHPE 335
Cdd:PRK13566  671 TAET-EDGVIMAIEHKTLPVAAVQFHPE 697
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 174-263 4.98e-10

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


Pssm-ID: 153210 [Multi-domain]  Cd Length: 115  Bit Score: 56.45  E-value: 4.98e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380 174 VVLLDFGKK-----QNIVRELNLRGCNVTVVPYDTTAE--EILAMSPDGIMLSNGPGDPDVVEVAINMIKGIL----GKI 242
Cdd:cd01653     1 VAVLLFPGFeelelASPLDALREAGAEVDVVSPDGGPVesDVDLDDYDGLILPGGPGTPDDLARDEALLALLReaaaAGK 80

                          90       100
                  ....*....|....*....|..
gi 1080876380 243 PFFGICLGHQLFAL-SQGASSF 263
Cdd:cd01653    81 PILGICLGAQLLVLgVQFHPEA 102
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 174-253 2.02e-09

Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group contains proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA, the A4 beta-galactosidase middle domain and peptidase E. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase (CPSase), cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. Peptidase E is believed to be a serine peptidase having a Ser-His-Glu catalytic triad which differs from the Cys-His-Glu catalytic triad of typical GATase1 domains, by having a Ser in place of the reactive Cys at the nucleophile elbow. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase. Peptidase E has a circular permutation in the common core of a typical GTAse1 domain.


Pssm-ID: 153222 [Multi-domain]  Cd Length: 92  Bit Score: 54.13  E-value: 2.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380 174 VVLLDFGKK-----QNIVRELNLRGCNVTVVPYDTTAE--EILAMSPDGIMLSNGPGDPDVVEVAINMIKGIL----GKI 242
Cdd:cd03128     1 VAVLLFGGSeelelASPLDALREAGAEVDVVSPDGGPVesDVDLDDYDGLILPGGPGTPDDLAWDEALLALLReaaaAGK 80

                          90
                  ....*....|.
gi 1080876380 243 PFFGICLGHQL 253
Cdd:cd03128    81 PVLGICLGAQL 91
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 219-335 1.60e-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: 1.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380 219 SNGPGDP--DVVEVAinMIKGILG-KIPFFGICLGHQLFA------LSQGASSFKMKFGHRGANHPVKDLRTGKVDITSQ 289
Cdd:pfam07722  82 SGGPYDParDAYELA--LIRAALArGKPILGICRGFQLLNvalggtLYQDIQEQPGFTDHREHCQVAPYAPSHAVNVEPG 159

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1080876380 290 N----------------HGYAIDKdsLAqTDLEITHIAlNDDTVEGLRHKTLPAF--SVQYHPE 335
Cdd:pfam07722 160 SllasllgseefrvnslHHQAIDR--LA-PGLRVEAVA-PDGTIEAIESPNAKGFalGVQWHPE 219
PRK06895 PRK06895
anthranilate synthase component II;
216-336 1.06e-07

anthranilate synthase component II;


Pssm-ID: 235882 [Multi-domain]  Cd Length: 190  Bit Score: 51.66  E-value: 1.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380 216 IMLSNGPGDPDVVEVAINMIKGILGKIPFFGICLGHQ---------LFALSQGASSFKMKFGHRGANHPVKDLRTgKVDI 286
Cdd:PRK06895   47 ILISPGPDVPRAYPQLFAMLERYHQHKSILGVCLGHQtlceffggeLYNLNNVRHGQQRPLKVRSNSPLFDGLPE-EFNI 125

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1080876380 287 tSQNHGYAIDKDSLaQTDLEITHIAlNDDTVEGLRHKTLPAFSVQYHPEA 336
Cdd:PRK06895  126 -GLYHSWAVSEENF-PTPLEITAVC-DENVVMAMQHKTLPIYGVQFHPES 172
PRK09522 PRK09522
bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate ...
 184-336 2.08e-07

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


Pssm-ID: 181927 [Multi-domain]  Cd Length: 531  Bit Score: 52.72  E-value: 2.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380 184 NIVRELNLRGCNVTV----VPYDTTAEEILAMSPDGIMLSNGPGDPDVVEVAINMIKGILGKIPFFGICLGHQLFALSQG 259
Cdd:PRK09522   16 NLADQLRSNGHNVVIyrnhIPAQTLIERLATMSNPVLMLSPGPGVPSEAGCMPELLTRLRGKLPIIGICLGHQAIVEAYG 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380 260 assfkmkfGHRGAnhpVKDLRTGKVDITSQNhGYAI-----------DKDSLAQTDL--EITHIALNDDTVEGLRHKTLP 326
Cdd:PRK09522   96 --------GYVGQ---AGEILHGKASSIEHD-GQAMfagltnplpvaRYHSLVGSNIpaGLTINAHFNGMVMAVRHDADR 163

                         170
                  ....*....|
gi 1080876380 327 AFSVQYHPEA 336
Cdd:PRK09522  164 VCGFQFHPES 173
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 184-337 2.93e-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: 153212 [Multi-domain]  Cd Length: 188  Bit Score: 47.24  E-value: 2.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380 184 NIVRELNLRGCNVTVVPYDTTAEEILAMSPDGIMLSNGP------GDPDVVEVaINMIKGIL-GKIPFFGICLGHQLFAL 256
Cdd:cd01741    18 DLLREAGAETIEIDVVDVYAGELLPDLDDYDGLVILGGPmsvdedDYPWLKKL-KELIRQALaAGKPVLGICLGHQLLAR 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380 257 SQGASSFKMKFGHRGANHPVKDLRTGKVDITSQNHGYAID-----KDSLAQTDLEITHIALNDDT-VEGLRhKTLPAFSV 330
Cdd:cd01741    97 ALGGKVGRNPKGWEIGWFPVTLTEAGKADPLFAGLPDEFPvfhwhGDTVVELPPGAVLLASSEACpNQAFR-YGDRALGL 175


                  ....*..
gi 1080876380 331 QYHPEAR 337
Cdd:cd01741   176 QFHPEER 182
pyrG PRK05380
CTP synthetase; Validated
 241-361 5.87e-05

CTP synthetase; Validated


Pssm-ID: 235437 [Multi-domain]  Cd Length: 533  Bit Score: 45.01  E-value: 5.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380 241 KIPFFGICLGHQL----FALS----QGASSFKMKfghRGANHPVKDLRTGKVDITsqNHG-------Y--AIDKDSLAQT 303
Cdd:PRK05380  372 NIPFLGICLGMQLavieFARNvlglEDANSTEFD---PDTPHPVIDLMPEQKDVS--DLGgtmrlgaYpcKLKPGTLAAE 446

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380 304 -----------------------DLE-----ITHIALNDDTVEGLRHKTLPAF-SVQYHPEARPGPSDSNYLFDDFIAMI 354
Cdd:PRK05380  447 iygkeeiyerhrhryevnnkyreQLEkaglvFSGTSPDGRLVEIVELPDHPWFvGVQFHPEFKSRPRRPHPLFAGFVKAA 526


                  ....*..
gi 1080876380 355 NEFKEKE 361
Cdd:PRK05380  527 LENKKRK 533
PLN02347 PLN02347
GMP synthetase
 167-259 4.73e-04

GMP synthetase


Pssm-ID: 215197 [Multi-domain]  Cd Length: 536  Bit Score: 41.98  E-value: 4.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380 167 STGSNLSVVL-LDFGKK--QNI---VRELNLrgCNVtVVPYDTTAEEILAMSPDGIMLSNGP------GDPDVVEVAINM 234
Cdd:PLN02347    5 AAKSYLDVVLiLDYGSQytHLItrrVRELGV--YSL-LLSGTASLDRIASLNPRVVILSGGPhsvhveGAPTVPEGFFDY 81

                          90       100
                  ....*....|....*....|....*
gi 1080876380 235 IKGilGKIPFFGICLGHQLFALSQG 259
Cdd:PLN02347   82 CRE--RGVPVLGICYGMQLIVQKLG 104
PyrG COG0504
CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase ...
 241-362 7.28e-04

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: 41.53  E-value: 7.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380 241 KIPFFGICLGHQL----FALS----QGASSFKMKfghRGANHPVKDLRTGKVDITsqNHG-------YA--IDKDSLA-- 301
Cdd:COG0504   373 KIPFLGICLGMQLavieFARNvlglEDANSTEFD---PNTPHPVIDLMPEQKDVS--DLGgtmrlgaYPckLKPGTLAae 447

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380 302 --------------------------QTDLEITHIALNDDTVEGLRHKTLPAF-SVQYHPEARPGPSDSNYLFDDFIAMI 354
Cdd:COG0504   448 aygkeeiserhrhryefnneyreqleKAGLVFSGTSPDGRLVEIVELPDHPWFvGVQFHPEFKSRPNRPHPLFRGFVKAA 527


                  ....*...
gi 1080876380 355 NEFKEKER 362
Cdd:COG0504   528 LEYKKKKK 535
hisH PRK13143
imidazole glycerol phosphate synthase subunit HisH; Provisional
 174-335 3.90e-03

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237289 [Multi-domain]  Cd Length: 200  Bit Score: 37.93  E-value: 3.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380 174 VVLLDF--GKKQNIVRELNLRGCNVTVVpydTTAEEILamSPDGIMLsngPGD---PDVVEVAINMIKGILG----KIPF 244
Cdd:PRK13143    3 IVIIDYgvGNLRSVSKALERAGAEVVIT---SDPEEIL--DADGIVL---PGVgafGAAMENLSPLRDVILEaarsGKPF 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080876380 245 FGICLGHQ-LF------ALSQGASSFK---------MKFGHRGANhpvkdlrtgKVDITSQN--------------HGYA 294
Cdd:PRK13143   75 LGICLGMQlLFesseegGGVRGLGLFPgrvvrfpagVKVPHMGWN---------TVKVVKDCplfegidgeyvyfvHSYY 145

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1080876380 295 IDKDS----LAQTDLEITHIA-LNDDTVeglrhktlpaFSVQYHPE 335
Cdd:PRK13143  146 AYPDDedyvVATTDYGIEFPAaVCNDNV----------FGTQFHPE 181
 
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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