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Conserved domains on  [gi|500275449|ref|WP_011922320|]
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carbamoyl phosphate synthase small subunit [Streptococcus suis]

Protein Classification

carbamoyl-phosphate synthase small subunit( domain architecture ID 11486002)

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

EC:  6.3.5.5
Gene Ontology:  GO:0016874
PubMed:  9636022|10587438|8752005

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
1-352 0e+00

carbamoyl-phosphate synthase small subunit;


:

Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 662.54  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449   1 MSKRRLILENGTIFEGEAFGADIDVTGELVFSTGMTGYQESITDQSYNGQILTFTYPLVGNYGINRDDFESIKPTCKGVV 80
Cdd:PRK12564   2 MMKAYLVLEDGTVFEGKAFGAEGETVGEVVFNTSMTGYQEILTDPSYAGQIVTFTYPLIGNYGVNREDFESDRPHAKGLI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449  81 VSEWARRASNWRNQMTLDEFLKAKKIPAISGIDTRALTKIIRQHGTMKATLANVGDSVEHLTDQLRAT--ILPTNNIQQV 158
Cdd:PRK12564  82 VRELSDIPSNWRSEMSLDEYLKENGIPGISGIDTRALTRKLREKGAMKGVIATEDFDAEELLEKARAFpgLLGLDLVKEV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449 159 STKTAYPAPGVG----RSVVLVDFGLKHSILRELAKRDCNVTVVPYDTTAEEILALNPDGVMLSNGPGNPDDVPEALDMI 234
Cdd:PRK12564 162 STKEPYPWPGPGgelkYKVVAIDFGVKRNILRELAERGCRVTVVPATTTAEEILALNPDGVFLSNGPGDPAALDYAIEMI 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449 235 RGILG-KIPIFGICMGHQLFAKANGATTYKMKFGHRGFNHAVREIATGRVDFTSQNHGYAVAREDLPECLMITHEEINDK 313
Cdd:PRK12564 242 RELLEkKIPIFGICLGHQLLALALGAKTYKMKFGHRGANHPVKDLETGKVEITSQNHGFAVDEDSLPANLEVTHVNLNDG 321

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 500275449 314 SVEGVRHKYYPGFSVQFHPDAAPGPHDASYLFDEFMELM 352
Cdd:PRK12564 322 TVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDEFVELM 360
 
Name Accession Description Interval E-value
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
1-352 0e+00

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 662.54  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449   1 MSKRRLILENGTIFEGEAFGADIDVTGELVFSTGMTGYQESITDQSYNGQILTFTYPLVGNYGINRDDFESIKPTCKGVV 80
Cdd:PRK12564   2 MMKAYLVLEDGTVFEGKAFGAEGETVGEVVFNTSMTGYQEILTDPSYAGQIVTFTYPLIGNYGVNREDFESDRPHAKGLI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449  81 VSEWARRASNWRNQMTLDEFLKAKKIPAISGIDTRALTKIIRQHGTMKATLANVGDSVEHLTDQLRAT--ILPTNNIQQV 158
Cdd:PRK12564  82 VRELSDIPSNWRSEMSLDEYLKENGIPGISGIDTRALTRKLREKGAMKGVIATEDFDAEELLEKARAFpgLLGLDLVKEV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449 159 STKTAYPAPGVG----RSVVLVDFGLKHSILRELAKRDCNVTVVPYDTTAEEILALNPDGVMLSNGPGNPDDVPEALDMI 234
Cdd:PRK12564 162 STKEPYPWPGPGgelkYKVVAIDFGVKRNILRELAERGCRVTVVPATTTAEEILALNPDGVFLSNGPGDPAALDYAIEMI 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449 235 RGILG-KIPIFGICMGHQLFAKANGATTYKMKFGHRGFNHAVREIATGRVDFTSQNHGYAVAREDLPECLMITHEEINDK 313
Cdd:PRK12564 242 RELLEkKIPIFGICLGHQLLALALGAKTYKMKFGHRGANHPVKDLETGKVEITSQNHGFAVDEDSLPANLEVTHVNLNDG 321

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 500275449 314 SVEGVRHKYYPGFSVQFHPDAAPGPHDASYLFDEFMELM 352
Cdd:PRK12564 322 TVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDEFVELM 360
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 1-353 0e+00

Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase small subunit is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440271 [Multi-domain]  Cd Length: 361  Bit Score: 653.63  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449   1 MSKRRLILENGTIFEGEAFGADIDVTGELVFSTGMTGYQESITDQSYNGQILTFTYPLVGNYGINRDDFESIKPTCKGVV 80
Cdd:COG0505    2 MMKALLVLEDGTVFEGKSFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVTFTYPHIGNYGVNDEDFESDRPWVAGLV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449  81 VSEWARRASNWRNQMTLDEFLKAKKIPAISGIDTRALTKIIRQHGTMKATLANVGDSVEHLTDQLRAT--ILPTNNIQQV 158
Cdd:COG0505   82 VRELSRRPSNWRSEESLDEYLKEHGIPGISGIDTRALTRHLREKGAMKGVISTGDLDIEELLEKARAApgMEGLDLVKEV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449 159 STKTAY---PAPGVGRSVVLVDFGLKHSILRELAKRDCNVTVVPYDTTAEEILALNPDGVMLSNGPGNPDDVPEALDMIR 235
Cdd:COG0505  162 STKEPYewtEAPGAGFHVVALDFGVKRNILRELAERGCRVTVVPATTSAEEILALNPDGVFLSNGPGDPAALDYAIETIR 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449 236 GILGK-IPIFGICMGHQLFAKANGATTYKMKFGHRGFNHAVREIATGRVDFTSQNHGYAVAREDLPE-CLMITHEEINDK 313
Cdd:COG0505  242 ELLGKgIPIFGICLGHQLLALALGAKTYKLKFGHRGANHPVKDLETGRVEITSQNHGFAVDEDSLPAtDLEVTHVNLNDG 321

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 500275449 314 SVEGVRHKYYPGFSVQFHPDAAPGPHDASYLFDEFMELMD 353
Cdd:COG0505  322 TVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDRFIELME 361
CPSaseIIsmall TIGR01368
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ...
 4-353 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: 548.77  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449    4 RRLILENGTIFEGEAFGADIDVTGELVFSTGMTGYQESITDQSYNGQILTFTYPLVGNYGINRDDFESIKPTCKGVVVSE 83
Cdd:TIGR01368   1 AYLVLEDGTVFRGYSFGAEGTVAGEVVFNTGMTGYQEILTDPSYKGQIVVFTYPLIGNYGVNDEDAESKGIHVSGLVVRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449   84 WARRASNWRNQMTLDEFLKAKKIPAISGIDTRALTKIIRQHGTMKATLANVGDSVEHLTDQLRAT--ILPTNNIQQVSTK 161
Cdd:TIGR01368  81 LSDRYSNWRATESLDQFLKRHGIPGIYGVDTRALVKKIREKGTMKGVISTEDSNDEELVEKARVSpdITGINLVAEVSTK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449  162 TAYP---APGVGRSVVLVDFGLKHSILRELAKRDCNVTVVPYDTTAEEILALNPDGVMLSNGPGNPDDVPEALDMIRGIL 238
Cdd:TIGR01368 161 EPYTwgqRGGKGKRVVVIDFGVKRNILRRLVKRGCEVTVVPYDTDAEEIKKYNPDGIFLSNGPGDPAAVEPAIETIRKLL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449  239 GKIPIFGICMGHQLFAKANGATTYKMKFGHRGFNHAVREIATGRVDFTSQNHGYAVAREDLP-ECLMITHEEINDKSVEG 317
Cdd:TIGR01368 241 EKIPIFGICLGHQLLALAFGAKTYKMKFGHRGGNHPVKDLITGRVEITSQNHGYAVDPDSLPaGDLEVTHVNLNDGTVEG 320

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 500275449  318 VRHKYYPGFSVQFHPDAAPGPHDASYLFDEFMELMD 353
Cdd:TIGR01368 321 IRHKDLPVFSVQYHPEASPGPHDTEYLFDEFIDLMK 356
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 173-349 1.36e-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: 327.53  E-value: 1.36e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449 173 VVLVDFGLKHSILRELAKRDCNVTVVPYDTTAEEILALNPDGVMLSNGPGNPDDVPEALDMIRGILGK-IPIFGICMGHQ 251
Cdd:cd01744    1 VVVIDFGVKHNILRELLKRGCEVTVVPYNTDAEEILKLDPDGIFLSNGPGDPALLDEAIKTVRKLLGKkIPIFGICLGHQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449 252 LFAKANGATTYKMKFGHRGFNHAVREIATGRVDFTSQNHGYAVAREDLPECLMITHEEINDKSVEGVRHKYYPGFSVQFH 331
Cdd:cd01744   81 LLALALGAKTYKMKFGHRGSNHPVKDLITGRVYITSQNHGYAVDPDSLPGGLEVTHVNLNDGTVEGIRHKDLPVFSVQFH 160

                        170
                 ....*....|....*...
gi 500275449 332 PDAAPGPHDASYLFDEFM 349
Cdd:cd01744  161 PEASPGPHDTEYLFDEFL 178
CPSase_sm_chain smart01097
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 3-131 8.18e-87

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


Pssm-ID: 198165 [Multi-domain]  Cd Length: 130  Bit Score: 257.69  E-value: 8.18e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449     3 KRRLILENGTIFEGEAFGADIDVTGELVFSTGMTGYQESITDQSYNGQILTFTYPLVGNYGINRDDFESIKPTCKGVVVS 82
Cdd:smart01097   2 KAYLVLEDGTVFEGESFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNDEDFESDKIQVKGLVVR 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 500275449    83 EWARRASNWRNQMTLDEFLKAKKIPAISGIDTRALTKIIRQHGTMKATL 131
Cdd:smart01097  82 ELSDEPSNWRSEQSLDEFLKENGIPGISGIDTRALTRKLREKGAMKGVI 130
CPSase_sm_chain pfam00988
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 6-131 9.83e-87

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: 257.25  E-value: 9.83e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449    6 LILENGTIFEGEAFGADIDVTGELVFSTGMTGYQESITDQSYNGQILTFTYPLVGNYGINRDDFESIKPTCKGVVVSEWA 85
Cdd:pfam00988   1 LVLEDGTVFEGKSFGAAGSTVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNPEDFESDKIHVAGLVVREYS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 500275449   86 RRASNWRNQMTLDEFLKAKKIPAISGIDTRALTKIIRQHGTMKATL 131
Cdd:pfam00988  81 DEPSNWRAEESLDEWLKEQGIPGISGVDTRALTRKIREKGAMKGVI 126
 
Name Accession Description Interval E-value
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
1-352 0e+00

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 662.54  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449   1 MSKRRLILENGTIFEGEAFGADIDVTGELVFSTGMTGYQESITDQSYNGQILTFTYPLVGNYGINRDDFESIKPTCKGVV 80
Cdd:PRK12564   2 MMKAYLVLEDGTVFEGKAFGAEGETVGEVVFNTSMTGYQEILTDPSYAGQIVTFTYPLIGNYGVNREDFESDRPHAKGLI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449  81 VSEWARRASNWRNQMTLDEFLKAKKIPAISGIDTRALTKIIRQHGTMKATLANVGDSVEHLTDQLRAT--ILPTNNIQQV 158
Cdd:PRK12564  82 VRELSDIPSNWRSEMSLDEYLKENGIPGISGIDTRALTRKLREKGAMKGVIATEDFDAEELLEKARAFpgLLGLDLVKEV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449 159 STKTAYPAPGVG----RSVVLVDFGLKHSILRELAKRDCNVTVVPYDTTAEEILALNPDGVMLSNGPGNPDDVPEALDMI 234
Cdd:PRK12564 162 STKEPYPWPGPGgelkYKVVAIDFGVKRNILRELAERGCRVTVVPATTTAEEILALNPDGVFLSNGPGDPAALDYAIEMI 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449 235 RGILG-KIPIFGICMGHQLFAKANGATTYKMKFGHRGFNHAVREIATGRVDFTSQNHGYAVAREDLPECLMITHEEINDK 313
Cdd:PRK12564 242 RELLEkKIPIFGICLGHQLLALALGAKTYKMKFGHRGANHPVKDLETGKVEITSQNHGFAVDEDSLPANLEVTHVNLNDG 321

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 500275449 314 SVEGVRHKYYPGFSVQFHPDAAPGPHDASYLFDEFMELM 352
Cdd:PRK12564 322 TVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDEFVELM 360
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 1-353 0e+00

Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase small subunit is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440271 [Multi-domain]  Cd Length: 361  Bit Score: 653.63  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449   1 MSKRRLILENGTIFEGEAFGADIDVTGELVFSTGMTGYQESITDQSYNGQILTFTYPLVGNYGINRDDFESIKPTCKGVV 80
Cdd:COG0505    2 MMKALLVLEDGTVFEGKSFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVTFTYPHIGNYGVNDEDFESDRPWVAGLV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449  81 VSEWARRASNWRNQMTLDEFLKAKKIPAISGIDTRALTKIIRQHGTMKATLANVGDSVEHLTDQLRAT--ILPTNNIQQV 158
Cdd:COG0505   82 VRELSRRPSNWRSEESLDEYLKEHGIPGISGIDTRALTRHLREKGAMKGVISTGDLDIEELLEKARAApgMEGLDLVKEV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449 159 STKTAY---PAPGVGRSVVLVDFGLKHSILRELAKRDCNVTVVPYDTTAEEILALNPDGVMLSNGPGNPDDVPEALDMIR 235
Cdd:COG0505  162 STKEPYewtEAPGAGFHVVALDFGVKRNILRELAERGCRVTVVPATTSAEEILALNPDGVFLSNGPGDPAALDYAIETIR 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449 236 GILGK-IPIFGICMGHQLFAKANGATTYKMKFGHRGFNHAVREIATGRVDFTSQNHGYAVAREDLPE-CLMITHEEINDK 313
Cdd:COG0505  242 ELLGKgIPIFGICLGHQLLALALGAKTYKLKFGHRGANHPVKDLETGRVEITSQNHGFAVDEDSLPAtDLEVTHVNLNDG 321

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 500275449 314 SVEGVRHKYYPGFSVQFHPDAAPGPHDASYLFDEFMELMD 353
Cdd:COG0505  322 TVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDRFIELME 361
PRK12838 PRK12838
carbamoyl phosphate synthase small subunit; Reviewed
 3-352 0e+00

carbamoyl phosphate synthase small subunit; Reviewed


Pssm-ID: 183784 [Multi-domain]  Cd Length: 354  Bit Score: 568.37  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449   3 KRRLILENGTIFEGEAFGADIDVTGELVFSTGMTGYQESITDQSYNGQILTFTYPLVGNYGINRDDFESIKPTCKGVVVS 82
Cdd:PRK12838   2 KAYLILEDGTVFEGELIGAPIDVTGEIVFNTGMTGYQEVLTDPSYKGQIVVFTYPLIGNYGINADDYESKQPQVKGVIVY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449  83 EWARRASNWRNQMTLDEFLKAKKIPAISGIDTRALTKIIRQHGTMKATLANVGDsvEHLTDQLRATILPTNNIQQVSTKT 162
Cdd:PRK12838  82 ELSREGSHYRAKQSLDDFLKEWNIPGISGVDTRALVKHIREKGTMKASITTTDD--AHAFDQIKALVLPKNVVAQVSTKE 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449 163 AYPAPGVGRSVVLVDFGLKHSILRELAKRDCNVTVVPYDTTAEEILALNPDGVMLSNGPGNPDDVPEALDMIRGILGKIP 242
Cdd:PRK12838 160 PYTYGNGGKHVALIDFGYKKSILRSLSKRGCKVTVLPYDTSLEEIKNLNPDGIVLSNGPGDPKELQPYLPEIKKLISSYP 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449 243 IFGICMGHQLFAKANGATTYKMKFGHRGFNHAVREIATGRVDFTSQNHGYAVAREDLPEC-LMITHEEINDKSVEGVRHK 321
Cdd:PRK12838 240 ILGICLGHQLIALALGADTEKLPFGHRGANHPVIDLTTGRVWMTSQNHGYVVDEDSLDGTpLSVRFFNVNDGSIEGLRHK 319

                        330       340       350
                 ....*....|....*....|....*....|.
gi 500275449 322 YYPGFSVQFHPDAAPGPHDASYLFDEFMELM 352
Cdd:PRK12838 320 KKPVLSVQFHPEAHPGPHDAEYIFDEFLEMM 350
CPSaseIIsmall TIGR01368
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ...
 4-353 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: 548.77  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449    4 RRLILENGTIFEGEAFGADIDVTGELVFSTGMTGYQESITDQSYNGQILTFTYPLVGNYGINRDDFESIKPTCKGVVVSE 83
Cdd:TIGR01368   1 AYLVLEDGTVFRGYSFGAEGTVAGEVVFNTGMTGYQEILTDPSYKGQIVVFTYPLIGNYGVNDEDAESKGIHVSGLVVRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449   84 WARRASNWRNQMTLDEFLKAKKIPAISGIDTRALTKIIRQHGTMKATLANVGDSVEHLTDQLRAT--ILPTNNIQQVSTK 161
Cdd:TIGR01368  81 LSDRYSNWRATESLDQFLKRHGIPGIYGVDTRALVKKIREKGTMKGVISTEDSNDEELVEKARVSpdITGINLVAEVSTK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449  162 TAYP---APGVGRSVVLVDFGLKHSILRELAKRDCNVTVVPYDTTAEEILALNPDGVMLSNGPGNPDDVPEALDMIRGIL 238
Cdd:TIGR01368 161 EPYTwgqRGGKGKRVVVIDFGVKRNILRRLVKRGCEVTVVPYDTDAEEIKKYNPDGIFLSNGPGDPAAVEPAIETIRKLL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449  239 GKIPIFGICMGHQLFAKANGATTYKMKFGHRGFNHAVREIATGRVDFTSQNHGYAVAREDLP-ECLMITHEEINDKSVEG 317
Cdd:TIGR01368 241 EKIPIFGICLGHQLLALAFGAKTYKMKFGHRGGNHPVKDLITGRVEITSQNHGYAVDPDSLPaGDLEVTHVNLNDGTVEG 320

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 500275449  318 VRHKYYPGFSVQFHPDAAPGPHDASYLFDEFMELMD 353
Cdd:TIGR01368 321 IRHKDLPVFSVQYHPEASPGPHDTEYLFDEFIDLMK 356
carA CHL00197
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
 6-357 1.21e-126

carbamoyl-phosphate synthase arginine-specific small subunit; Provisional


Pssm-ID: 214392 [Multi-domain]  Cd Length: 382  Bit Score: 368.74  E-value: 1.21e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449   6 LILENGTIFEGEAFGADIDVTGELVFSTGMTGYQESITDQSYNGQILTFTYPLVGNYGINRDDFESIKPTCKGVVVSEWA 85
Cdd:CHL00197   9 LVLEDGTYYRGWSFSNPITTIGEVVFNTGMTGYQEIITDPSYFEQIVTFTYPEIGNTGINLEDIESVKIQVKGIIAKNIC 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449  86 RRASNWRNQMTLDEFLKAKKIPAISGIDTRALTKIIRQHGTMKATLANvgDSVEHltDQLRATI------LPTNNIQQVS 159
Cdd:CHL00197  89 KSSSNWRQQESLVSYLQRHKIPFIFGIDTRALTQHLRRFGTMNGCISN--QNLNL--SYLRAKIkesphmPSSDLIPRVT 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449 160 TKTAY-----------------PAPGVGRSVVLVDFGLKHSILRELAKRDCNVTVVPYDTTAEEILALNPDGVMLSNGPG 222
Cdd:CHL00197 165 TSSYYewdekshpsfyladnkrPHSSYQLKIIVIDFGVKYNILRRLKSFGCSITVVPATSPYQDILSYQPDGILLSNGPG 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449 223 NPDDVPEALDMIRGILG-KIPIFGICMGHQLFAKANGATTYKMKFGHRGFNHavreiATG---RVDFTSQNHGYAVARED 298
Cdd:CHL00197 245 DPSAIHYGIKTVKKLLKyNIPIFGICMGHQILSLALEAKTFKLKFGHRGLNH-----PSGlnqQVEITSQNHGFAVNLES 319

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449 299 LPE-CLMITHEEINDKSVEGVRHKYYPGFSVQFHPDAAPGPHDASYLFDEFMELMDSFKK 357
Cdd:CHL00197 320 LAKnKFYITHFNLNDGTVAGISHSPKPYFSVQYHPEASPGPHDADYLFEYFIEIIKHSKS 379
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 173-349 1.36e-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: 327.53  E-value: 1.36e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449 173 VVLVDFGLKHSILRELAKRDCNVTVVPYDTTAEEILALNPDGVMLSNGPGNPDDVPEALDMIRGILGK-IPIFGICMGHQ 251
Cdd:cd01744    1 VVVIDFGVKHNILRELLKRGCEVTVVPYNTDAEEILKLDPDGIFLSNGPGDPALLDEAIKTVRKLLGKkIPIFGICLGHQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449 252 LFAKANGATTYKMKFGHRGFNHAVREIATGRVDFTSQNHGYAVAREDLPECLMITHEEINDKSVEGVRHKYYPGFSVQFH 331
Cdd:cd01744   81 LLALALGAKTYKMKFGHRGSNHPVKDLITGRVYITSQNHGYAVDPDSLPGGLEVTHVNLNDGTVEGIRHKDLPVFSVQFH 160

                        170
                 ....*....|....*...
gi 500275449 332 PDAAPGPHDASYLFDEFM 349
Cdd:cd01744  161 PEASPGPHDTEYLFDEFL 178
PLN02771 PLN02771
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
 2-345 1.45e-105

carbamoyl-phosphate synthase (glutamine-hydrolyzing)


Pssm-ID: 178370 [Multi-domain]  Cd Length: 415  Bit Score: 316.15  E-value: 1.45e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449   2 SKRRLILENGTIFEGEAFGADIDVTGELVFSTGMTGYQESITDQSYNGQILTFTYPLVGNYGINRDDFESIKPTCKGVVV 81
Cdd:PLN02771  55 SDARLVLEDGSVWKAKSFGARGTQVGEVVFNTSLTGYQEILTDPSYAGQFVLMTNPHIGNTGVNFDDEESRQCFLAGLVI 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449  82 SEWARRASNWRNQMTLDEFLKAKKIPAISGIDTRALTKIIRQHGTMKATLANVGDSV-EHLTDQLRA-TILPTNNIQQVS 159
Cdd:PLN02771 135 RSLSISTSNWRCTKTLGDYLAERNIMGIYDVDTRAITRRLREDGSLIGVLSTEDSKTdEELLKMSRSwDIVGIDLISGVS 214

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449 160 TKTAYP---------------APGVGRSVVLVDFGLKHSILRELAKRDCNVTVVPYDTTAEEILALNPDGVMLSNGPGNP 224
Cdd:PLN02771 215 CKSPYEwvdktnpewdfntnsRDGESYHVIAYDFGIKHNILRRLASYGCKITVVPSTWPASEALKMKPDGVLFSNGPGDP 294

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449 225 DDVPEALDMIRGILGKIPIFGICMGHQLFAKANGATTYKMKFGHRGFNHAVREIATGRVDFTSQNHGYAVAREDLPECLM 304
Cdd:PLN02771 295 SAVPYAVETVKELLGKVPVFGICMGHQLLGQALGGKTFKMKFGHHGGNHPVRNNRTGRVEISAQNHNYAVDPASLPEGVE 374

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 500275449 305 ITHEEINDKSVEGVRHKYYPGFSVQFHPDAAPGPHDASYLF 345
Cdd:PLN02771 375 VTHVNLNDGSCAGLAFPALNVMSLQYHPEASPGPHDSDNAF 415
CPSase_sm_chain smart01097
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 3-131 8.18e-87

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


Pssm-ID: 198165 [Multi-domain]  Cd Length: 130  Bit Score: 257.69  E-value: 8.18e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449     3 KRRLILENGTIFEGEAFGADIDVTGELVFSTGMTGYQESITDQSYNGQILTFTYPLVGNYGINRDDFESIKPTCKGVVVS 82
Cdd:smart01097   2 KAYLVLEDGTVFEGESFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNDEDFESDKIQVKGLVVR 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 500275449    83 EWARRASNWRNQMTLDEFLKAKKIPAISGIDTRALTKIIRQHGTMKATL 131
Cdd:smart01097  82 ELSDEPSNWRSEQSLDEFLKENGIPGISGIDTRALTRKLREKGAMKGVI 130
CPSase_sm_chain pfam00988
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 6-131 9.83e-87

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: 257.25  E-value: 9.83e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449    6 LILENGTIFEGEAFGADIDVTGELVFSTGMTGYQESITDQSYNGQILTFTYPLVGNYGINRDDFESIKPTCKGVVVSEWA 85
Cdd:pfam00988   1 LVLEDGTVFEGKSFGAAGSTVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNPEDFESDKIHVAGLVVREYS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 500275449   86 RRASNWRNQMTLDEFLKAKKIPAISGIDTRALTKIIRQHGTMKATL 131
Cdd:pfam00988  81 DEPSNWRAEESLDEWLKEQGIPGISGVDTRALTRKIREKGAMKGVI 126
GATase pfam00117
Glutamine amidotransferase class-I;
174-351 7.47e-68

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 211.71  E-value: 7.47e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449  174 VLVDFGL--KHSILRELAKRDCNVTVVPYDTTAEEILALNPDGVMLSNGPGNPDDVPEALDMIRGILG-KIPIFGICMGH 250
Cdd:pfam00117   1 LLIDNGDsfTYNLARALRELGVEVTVVPNDTPAEEILEENPDGIILSGGPGSPGAAGGAIEAIREARElKIPILGICLGH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449  251 QLFAKANGATTYKMK-FGHRGFNHAVRE------IATGRVDFTSQNHGYAVAREDLPECLMITHEEINDKSVEGVRHKYY 323
Cdd:pfam00117  81 QLLALAFGGKVVKAKkFGHHGKNSPVGDdgcglfYGLPNVFIVRRYHSYAVDPDTLPDGLEVTATSENDGTIMGIRHKKL 160

                         170       180
                  ....*....|....*....|....*...
gi 500275449  324 PGFSVQFHPDAAPGPHDASYLFDEFMEL 351
Cdd:pfam00117 161 PIFGVQFHPESILTPHGPEILFNFFIKA 188
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 182-332 2.65e-31

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: 116.87  E-value: 2.65e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449 182 HSILRELAKRDCNVTVVPYD-TTAEEILALNPDGVMLSNGPGNPDDVPEALDMIRGILGKIPIFGICMGHQLFAKANGAT 260
Cdd:cd01743   12 YNLVQYLRELGAEVVVVRNDeITLEELELLNPDAIVISPGPGHPEDAGISLEIIRALAGKVPILGVCLGHQAIAEAFGGK 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449 261 TYKMKFGHRGfnhAVREIATGRVDFTSQN---------HGYAVAREDLPECLMITHEEiNDKSVEGVRHKYYPGFSVQFH 331
Cdd:cd01743   92 VVRAPEPMHG---KTSEIHHDGSGLFKGLpqpftvgryHSLVVDPDPLPDLLEVTAST-EDGVIMALRHRDLPIYGVQFH 167


                 .
gi 500275449 332 P 332
Cdd:cd01743  168 P 168
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 185-332 2.52e-30

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: 114.36  E-value: 2.52e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449 185 LRELakrDCNVTVVPYD-TTAEEILALNPDGVMLSNGPGNPDDVPEALDMIRGILGKIPIFGICMGHQLFAKANGATTYK 263
Cdd:COG0512   18 LGEL---GAEVVVVRNDeITLEEIEALAPDGIVLSPGPGTPEEAGISLEVIRAFAGKIPILGVCLGHQAIGEAFGGKVVR 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449 264 MKF---G------HRG---FNHAVREIATGRvdftsqnhgY---AVAREDLPECLMIT-HEEinDKSVEGVRHKYYPGFS 327
Cdd:COG0512   95 APEpmhGktspitHDGsglFAGLPNPFTATR---------YhslVVDRETLPDELEVTaWTE--DGEIMGIRHRELPIEG 163


                 ....*
gi 500275449 328 VQFHP 332
Cdd:COG0512  164 VQFHP 168
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 185-332 2.45e-28

anthranilate synthase component II; Provisional


Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 109.06  E-value: 2.45e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449 185 LRELakrDCNVTVVPYDT-TAEEILALNPDGVMLSNGPGNPDDVPEALDMIRGILGKIPIFGICMGHQLFAKANGAttyk 263
Cdd:PRK05670  19 LGEL---GAEVVVYRNDEiTLEEIEALNPDAIVLSPGPGTPAEAGISLELIREFAGKVPILGVCLGHQAIGEAFGG---- 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449 264 mKFGHrgfnhaVREIATGRVDFTSQN-----------------HGYAVAREDLPECLMIThEEINDKSVEGVRHKYYPGF 326
Cdd:PRK05670  92 -KVVR------AKEIMHGKTSPIEHDgsgifaglpnpftvtryHSLVVDRESLPDCLEVT-AWTDDGEIMGVRHKELPIY 163


                 ....*.
gi 500275449 327 SVQFHP 332
Cdd:PRK05670 164 GVQFHP 169
PRK14607 PRK14607
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
192-334 1.21e-24

bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;


Pssm-ID: 237764 [Multi-domain]  Cd Length: 534  Bit Score: 104.80  E-value: 1.21e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449 192 DCNVTVVPYDTTAEEILALNPDGVMLSNGPGNPDDVPEALDMIRGILGKIPIFGICMGHQLFAKANGATTYKMKFGHRG- 270
Cdd:PRK14607  25 EEIEVVRNDEITIEEIEALNPSHIVISPGPGRPEEAGISVEVIRHFSGKVPILGVCLGHQAIGYAFGGKIVHAKRILHGk 104

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449 271 ---FNHAVREI---ATGRVDFTsQNHGYAVAREDLPECLMITHEEiNDKSVEGVRHKYYPGFSVQFHPDA 334
Cdd:PRK14607 105 tspIDHNGKGLfrgIPNPTVAT-RYHSLVVEEASLPECLEVTAKS-DDGEIMGIRHKEHPIFGVQFHPES 172
GATase1_GMP_Synthase cd01742
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ...
 173-332 3.35e-21

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: 89.52  E-value: 3.35e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449 173 VVLVDFGLK--HSILRELakRDCNVT--VVPYDTTAEEILALNPDGVMLSNGP------GNPDDVPEALDMirgilgKIP 242
Cdd:cd01742    1 ILILDFGSQytHLIARRV--RELGVYseILPNTTPLEEIKLKNPKGIILSGGPssvyeeDAPRVDPEIFEL------GVP 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449 243 IFGICMGHQLFAKANGATTYKMKfgHRGFNHAVREIATGRVDFTSQ--------NHGYAVARedLPECLMITHEEINDKs 314
Cdd:cd01742   73 VLGICYGMQLIAKALGGKVERGD--KREYGKAEIEIDDSSPLFEGLpdeqtvwmSHGDEVVK--LPEGFKVIASSDNCP- 147

                        170
                 ....*....|....*...
gi 500275449 315 VEGVRHKYYPGFSVQFHP 332
Cdd:cd01742  148 VAAIANEEKKIYGVQFHP 165
trpG_papA TIGR00566
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ...
 203-334 2.10e-20

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: 87.54  E-value: 2.10e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449  203 TAEEILALNPDGVMLSNGPGNPDDVPEALDMIRGILGKIPIFGICMGHQLFAKANGATTYKMKFGHRGFNHAVREIATGR 282
Cdd:TIGR00566  35 TLQEIEALLPLLIVISPGPCTPNEAGISLEAIRHFAGKLPILGVCLGHQAMGQAFGGDVVRANTVMHGKTSEIEHNGAGI 114

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 500275449  283 VD-----FTS-QNHGYAVAREDLPECLMITHEEINDKSVEGVRHKYYPGFSVQFHPDA 334
Cdd:TIGR00566 115 FRglfnpLTAtRYHSLVVEPETLPTCFPVTAWEEENIEIMAIRHRDLPLEGVQFHPES 172
PRK07649 PRK07649
aminodeoxychorismate/anthranilate synthase component II;
201-355 3.01e-20

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181066 [Multi-domain]  Cd Length: 195  Bit Score: 87.17  E-value: 3.01e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449 201 DTTAEEILALNPDGVMLSNGPGNPDDVPEALDMIRGILGKIPIFGICMGHQLFAKANGATTYK----MKFGHRGFNHAVR 276
Cdd:PRK07649  33 EVTISDIENMKPDFLMISPGPCSPNEAGISMEVIRYFAGKIPIFGVCLGHQSIAQVFGGEVVRaerlMHGKTSLMHHDGK 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449 277 EIATGRVD-FT-SQNHGYAVAREDLPECLMITHEEINDKsVEGVRHKYYPGFSVQFHPDaapgphdaSYLFDEFMELMDS 354
Cdd:PRK07649 113 TIFSDIPNpFTaTRYHSLIVKKETLPDCLEVTSWTEEGE-IMAIRHKTLPIEGVQFHPE--------SIMTSHGKELLQN 183


                 .
gi 500275449 355 F 355
Cdd:PRK07649 184 F 184
guaA_Nterm TIGR00888
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ...
 173-333 5.32e-19

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: 83.52  E-value: 5.32e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449  173 VVLVDFGLK--HSILRELakRDCNV--TVVPYDTTAEEILALNPDGVMLSNGPG--NPDDVPEALDMIRGIlgKIPIFGI 246
Cdd:TIGR00888   1 ILVLDFGSQytQLIARRL--RELGVysELVPNTTPLEEIREKNPKGIILSGGPSsvYAENAPRADEKIFEL--GVPVLGI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449  247 CMGHQLFAKANGATTYKMKfgHRGFNHAVREIATGRVDFTSQN--------HGYAVARedLPECLMITHEEINDKsVEGV 318
Cdd:TIGR00888  77 CYGMQLMAKQLGGEVGRAE--KREYGKAELEILDEDDLFRGLPdestvwmsHGDKVKE--LPEGFKVLATSDNCP-VAAM 151

                         170
                  ....*....|....*
gi 500275449  319 RHKYYPGFSVQFHPD 333
Cdd:TIGR00888 152 AHEEKPIYGVQFHPE 166
PRK06774 PRK06774
aminodeoxychorismate synthase component II;
205-357 2.72e-18

aminodeoxychorismate synthase component II;


Pssm-ID: 180689 [Multi-domain]  Cd Length: 191  Bit Score: 81.83  E-value: 2.72e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449 205 EEILALNPDGVMLSNGPGNPDDVPEALDMIRGILGKIPIFGICMGHQLFAKANGATTYKMKFGHRGFNHAVREIATG--- 281
Cdd:PRK06774  37 TDIEQLAPSHLVISPGPCTPNEAGISLAVIRHFADKLPILGVCLGHQALGQAFGARVVRARQVMHGKTSAICHSGQGvfr 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449 282 ---RVDFTSQNHGYAVAREDLPECLMITHEEINDKSVE---GVRHKYYPGFSVQFHPDaapgphdaSYLFDEFMELMDSF 355
Cdd:PRK06774 117 glnQPLTVTRYHSLVIAADSLPGCFELTAWSERGGEMDeimGIRHRTLPLEGVQFHPE--------SILSEQGHQLLDNF 188


                 ..
gi 500275449 356 KK 357
Cdd:PRK06774 189 LK 190
PRK08007 PRK08007
aminodeoxychorismate synthase component 2;
201-334 4.54e-18

aminodeoxychorismate synthase component 2;


Pssm-ID: 181194 [Multi-domain]  Cd Length: 187  Bit Score: 81.12  E-value: 4.54e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449 201 DTTAEEILALNPDGVMLSNGPGNPDDVPEALDMIRGILGKIPIFGICMGHQLFAKANGATTYKMKFGHRGFNHAVREIAT 280
Cdd:PRK08007  33 ALTLADIDALKPQKIVISPGPCTPDEAGISLDVIRHYAGRLPILGVCLGHQAMAQAFGGKVVRAAKVMHGKTSPITHNGE 112

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500275449 281 GRvdFTSQNHGYAVAR--------EDLPECLMITHEEiNDKSVEGVRHKYYPGFSVQFHPDA 334
Cdd:PRK08007 113 GV--FRGLANPLTVTRyhslvvepDSLPACFEVTAWS-ETREIMGIRHRQWDLEGVQFHPES 171
PRK08857 PRK08857
aminodeoxychorismate/anthranilate synthase component II;
207-334 3.09e-17

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181566 [Multi-domain]  Cd Length: 193  Bit Score: 78.77  E-value: 3.09e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449 207 ILALNPDGVMLSNGPGNPDDVPEALDMIRGILGKIPIFGICMGHQLFAKANGATTYKMKFGHRGFNHAVREiaTGRVDFT 286
Cdd:PRK08857  39 IEALNPTHLVISPGPCTPNEAGISLQAIEHFAGKLPILGVCLGHQAIAQVFGGQVVRARQVMHGKTSPIRH--TGRSVFK 116

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449 287 SQN--------HGYAVAREDLPECLMIT----HEEINDKSVEGVRHKYYPGFSVQFHPDA 334
Cdd:PRK08857 117 GLNnpltvtryHSLVVKNDTLPECFELTawteLEDGSMDEIMGFQHKTLPIEAVQFHPES 176
PRK13566 PRK13566
anthranilate synthase component I;
165-332 6.40e-17

anthranilate synthase component I;


Pssm-ID: 237429 [Multi-domain]  Cd Length: 720  Bit Score: 81.89  E-value: 6.40e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449 165 PAPGVGRSVVLVDfglkH--SILRELA----KRDCNVTVVPYDTtAEEILA-LNPDGVMLSNGPGNPDD--VPEALDMIR 235
Cdd:PRK13566 521 AAVGEGKRVLLVD----HedSFVHTLAnyfrQTGAEVTTVRYGF-AEEMLDrVNPDLVVLSPGPGRPSDfdCKATIDAAL 595

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449 236 GilGKIPIFGICMGHQLFAKANGAT-------------TYKMKFGHRGFNHAVREIATGRVdftsqnHGYAVAREDLPEC 302
Cdd:PRK13566 596 A--RNLPIFGVCLGLQAIVEAFGGElgqlaypmhgkpsRIRVRGPGRLFSGLPEEFTVGRY------HSLFADPETLPDE 667

                        170       180       190
                 ....*....|....*....|....*....|
gi 500275449 303 LMITHEEiNDKSVEGVRHKYYPGFSVQFHP 332
Cdd:PRK13566 668 LLVTAET-EDGVIMAIEHKTLPVAAVQFHP 696
trpG CHL00101
anthranilate synthase component 2
 206-334 1.87e-16

anthranilate synthase component 2


Pssm-ID: 214365 [Multi-domain]  Cd Length: 190  Bit Score: 76.69  E-value: 1.87e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449 206 EILALNPDGVMLSNGPGNPDDVPEALDMIRGILGKIPIFGICMGHQLFAKANGATTYKmkfghrgfnhaVREIATGRV-- 283
Cdd:CHL00101  38 KIKNLNIRHIIISPGPGHPRDSGISLDVISSYAPYIPILGVCLGHQSIGYLFGGKIIK-----------APKPMHGKTsk 106

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500275449 284 -----DFTSQN----------HGYAVAREDLPECLMIT-HEEinDKSVEGVRHKYYPG-FSVQFHPDA 334
Cdd:CHL00101 107 iyhnhDDLFQGlpnpftatryHSLIIDPLNLPSPLEITaWTE--DGLIMACRHKKYKMlRGIQFHPES 172
PLN02335 PLN02335
anthranilate synthase
 193-334 4.13e-16

anthranilate synthase


Pssm-ID: 177969 [Multi-domain]  Cd Length: 222  Bit Score: 76.37  E-value: 4.13e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449 193 CNVTVVPYD-TTAEEILALNPDGVMLSNGPGNPDDVPEALDMIRGILGKIPIFGICMGHQLFAKANGATTYKMKFG--Hr 269
Cdd:PLN02335  43 CHFEVYRNDeLTVEELKRKNPRGVLISPGPGTPQDSGISLQTVLELGPLVPLFGVCMGLQCIGEAFGGKIVRSPFGvmH- 121

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 500275449 270 GFNHAVR---EIATGRVD-----FTS-QNHGYAVAREDLPECLMITHEEINDKSVEGVRHKYYPGFS-VQFHPDA 334
Cdd:PLN02335 122 GKSSPVHydeKGEEGLFSglpnpFTAgRYHSLVIEKDTFPSDELEVTAWTEDGLIMAARHRKYKHIQgVQFHPES 196
PRK00758 PRK00758
GMP synthase subunit A; Validated
 173-351 1.53e-15

GMP synthase subunit A; Validated


Pssm-ID: 179112 [Multi-domain]  Cd Length: 184  Bit Score: 73.73  E-value: 1.53e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449 173 VVLVDFG--LKHSILRELAKRDCNVTVVPYDTTAEEILAlNPDGVMLSNGP-----GNPDDVPEALDmirgilgkIPIFG 245
Cdd:PRK00758   2 IVVVDNGgqYNHLIHRTLRYLGVDAKIIPNTTPVEEIKA-FEDGLILSGGPdieraGNCPEYLKELD--------VPILG 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449 246 ICMGHQLFAKANGATTYKMKFGhrgfnhavrEIATGRVDFTSQN---------------HGYAVARedLPECLMIT-HEE 309
Cdd:PRK00758  73 ICLGHQLIAKAFGGEVGRGEYG---------EYALVEVEILDEDdilkglppeirvwasHADEVKE--LPDGFEILaRSD 141

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 500275449 310 INDksVEGVRHKYYPGFSVQFHPDAAPGPHdASYLFDEFMEL 351
Cdd:PRK00758 142 ICE--VEAMKHKEKPIYGVQFHPEVAHTEY-GEEIFKNFLEI 180
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 182-332 3.05e-14

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


Pssm-ID: 440284 [Multi-domain]  Cd Length: 225  Bit Score: 71.13  E-value: 3.05e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449 182 HSILRELAKRDCNVTVV--------PYDTTAEeilalNPDGVMLSNGPGNPDD----VPEALDMIRGIL-GKIPIFGICM 248
Cdd:COG0518   16 GLIARRLREAGIELDVLrvyageilPYDPDLE-----DPDGLILSGGPMSVYDedpwLEDEPALIREAFeLGKPVLGICY 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449 249 GHQLFAKANGATTYKmkfghrgfnHAVREIATGRVDFTSQN---------------HGYAVARedLPE---CLMITHEEI 310
Cdd:COG0518   91 GAQLLAHALGGKVEP---------GPGREIGWAPVELTEADplfaglpdeftvwmsHGDTVTE--LPEgaeVLASSDNCP 159

                        170       180
                 ....*....|....*....|..
gi 500275449 311 NdksvEGVRHKyYPGFSVQFHP 332
Cdd:COG0518  160 N----QAFRYG-RRVYGVQFHP 176
guaA PRK00074
GMP synthase; Reviewed
 171-332 5.82e-14

GMP synthase; Reviewed


Pssm-ID: 234614 [Multi-domain]  Cd Length: 511  Bit Score: 72.77  E-value: 5.82e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449 171 RSVVLVDFG-----LkhsILRELakRDCNV--TVVPYDTTAEEILALNPDGVMLSNGP------GNPDDVPEALDMirgi 237
Cdd:PRK00074   4 DKILILDFGsqytqL---IARRV--RELGVysEIVPYDISAEEIRAFNPKGIILSGGPasvyeeGAPRADPEIFEL---- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449 238 lgKIPIFGICMGHQLFAKANGATTYKMkfGHRGFNHAVREIATGRVDFTSQN--------HGYAVARedLPE-------- 301
Cdd:PRK00074  75 --GVPVLGICYGMQLMAHQLGGKVERA--GKREYGRAELEVDNDSPLFKGLPeeqdvwmsHGDKVTE--LPEgfkviast 148

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 500275449 302 ----CLMITHEEindksvegvrHKYYpgfSVQFHP 332
Cdd:PRK00074 149 encpIAAIANEE----------RKFY---GVQFHP 170
PRK07765 PRK07765
aminodeoxychorismate/anthranilate synthase component II;
201-333 2.96e-13

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181107 [Multi-domain]  Cd Length: 214  Bit Score: 68.15  E-value: 2.96e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449 201 DTTAEEILALNPDGVMLSNGPGNPDDVPEALDMIRGILG-KIPIFGICMGHQLFAKANGATTYKMKFGHRGFNHAVREIA 279
Cdd:PRK07765  36 RLADEAAVAAQFDGVLLSPGPGTPERAGASIDMVRACAAaGTPLLGVCLGHQAIGVAFGATVDRAPELLHGKTSSVHHTG 115

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449 280 TGRVD-----FT-SQNHGYAVAREDLPECLMIThEEINDKSVEGVRHKYYPGFSVQFHPD 333
Cdd:PRK07765 116 VGVLAglpdpFTaTRYHSLTILPETLPAELEVT-ARTDSGVIMAVRHRELPIHGVQFHPE 174
PRK05637 PRK05637
anthranilate synthase component II; Provisional
 194-275 9.89e-12

anthranilate synthase component II; Provisional


Pssm-ID: 180178 [Multi-domain]  Cd Length: 208  Bit Score: 63.71  E-value: 9.89e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449 194 NVTVVPYDTTAEEILALNPDGVMLSNGPGNPDDVPEALDMIRGILGKIPIFGICMGHQLFAKANG----------ATTYK 263
Cdd:PRK05637  27 KCTVFRNTVPVEEILAANPDLICLSPGPGHPRDAGNMMALIDRTLGQIPLLGICLGFQALLEHHGgkvepcgpvhGTTDN 106

                         90
                 ....*....|..
gi 500275449 264 MKFGHRGFNHAV 275
Cdd:PRK05637 107 MILTDAGVQSPV 118
PRK06895 PRK06895
anthranilate synthase component II;
198-334 1.36e-11

anthranilate synthase component II;


Pssm-ID: 235882 [Multi-domain]  Cd Length: 190  Bit Score: 62.83  E-value: 1.36e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449 198 VPYDTTAEEILALNP----DGVMLSNGPGNPDDVPEALDMIRGILGKIPIFGICMGHQLFAKANGATTYKMKfghrgfnh 273
Cdd:PRK06895  26 VPMQVVNVEDLDLDEvenfSHILISPGPDVPRAYPQLFAMLERYHQHKSILGVCLGHQTLCEFFGGELYNLN-------- 97

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500275449 274 AVREIATGRVDFTSQN---------------HGYAVAREDLPECLMIThEEINDKSVEGVRHKYYPGFSVQFHPDA 334
Cdd:PRK06895  98 NVRHGQQRPLKVRSNSplfdglpeefniglyHSWAVSEENFPTPLEIT-AVCDENVVMAMQHKTLPIYGVQFHPES 172
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 173-252 1.08e-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: 58.38  E-value: 1.08e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449 173 VVLVDFG-----LKHSILRELAKRDCNVTVVPYDTTAE--EILALNPDGVMLSNGPGNPDDVPEALDMIRGIL----GKI 241
Cdd:cd01653    1 VAVLLFPgfeelELASPLDALREAGAEVDVVSPDGGPVesDVDLDDYDGLILPGGPGTPDDLARDEALLALLReaaaAGK 80

                         90
                 ....*....|.
gi 500275449 242 PIFGICMGHQL 252
Cdd:cd01653   81 PILGICLGAQL 91
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 173-252 1.84e-10

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: 56.83  E-value: 1.84e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449 173 VVLVDFGLK-----HSILRELAKRDCNVTVVPYDTTAE--EILALNPDGVMLSNGPGNPDDVPEALDMIRGIL----GKI 241
Cdd:cd03128    1 VAVLLFGGSeelelASPLDALREAGAEVDVVSPDGGPVesDVDLDDYDGLILPGGPGTPDDLAWDEALLALLReaaaAGK 80

                         90
                 ....*....|.
gi 500275449 242 PIFGICMGHQL 252
Cdd:cd03128   81 PVLGICLGAQL 91
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 185-335 4.37e-10

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


Pssm-ID: 153212 [Multi-domain]  Cd Length: 188  Bit Score: 58.41  E-value: 4.37e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449 185 LRELAKRDCNVTVVPYDTTAEEILALNPDGVMLSNGPGNPDD-----VPEALDMIRGIL-GKIPIFGICMGHQLFAKANG 258
Cdd:cd01741   20 LREAGAETIEIDVVDVYAGELLPDLDDYDGLVILGGPMSVDEddypwLKKLKELIRQALaAGKPVLGICLGHQLLARALG 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449 259 ATTYKmkfghrgfNHAVREIATGRVDFTSQNHGYAVAReDLPECLMI--THEEI-------------NDKS-VEGVRhky 322
Cdd:cd01741  100 GKVGR--------NPKGWEIGWFPVTLTEAGKADPLFA-GLPDEFPVfhWHGDTvvelppgavllasSEACpNQAFR--- 167

                        170
                 ....*....|....*
gi 500275449 323 YPG--FSVQFHPDAA 335
Cdd:cd01741  168 YGDraLGLQFHPEER 182
PRK09522 PRK09522
bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate ...
 198-334 5.49e-09

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


Pssm-ID: 181927 [Multi-domain]  Cd Length: 531  Bit Score: 57.34  E-value: 5.49e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449 198 VPYDTTAEEILALNPDGVMLSNGPGNPDD---VPEALDMIRGilgKIPIFGICMGHQLFAKANGAttYKMKFGHRGFNHA 274
Cdd:PRK09522  35 IPAQTLIERLATMSNPVLMLSPGPGVPSEagcMPELLTRLRG---KLPIIGICLGHQAIVEAYGG--YVGQAGEILHGKA 109

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500275449 275 VREIATGRVDFTSQNHGYAVAR------EDLPECLMITHEeiNDKSVEGVRHKYYPGFSVQFHPDA 334
Cdd:PRK09522 110 SSIEHDGQAMFAGLTNPLPVARyhslvgSNIPAGLTINAH--FNGMVMAVRHDADRVCGFQFHPES 173
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 197-348 1.75e-08

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


Pssm-ID: 153216 [Multi-domain]  Cd Length: 189  Bit Score: 53.73  E-value: 1.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449 197 VVPYDTTAEEILAL--NPDGVMLSNGP--------GNPDDVPEALD---------MIRGIL-GKIPIFGICMGHQLFAKA 256
Cdd:cd01745   37 LLPPVDDEEDLEQYleLLDGLLLTGGGdvdpplygEEPHPELGPIDperdafelaLLRAALeRGKPILGICRGMQLLNVA 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449 257 NGATTYkmkfghrgfnhavREIATGRVdftsqnHGYAVARedLPECLMIT-HEEinDKSVEGVRHKYYP-GFSVQFHPD- 333
Cdd:cd01745  117 LGGTLY-------------QDIRVNSL------HHQAIKR--LADGLRVEaRAP--DGVIEAIESPDRPfVLGVQWHPEw 173

                        170
                 ....*....|....*
gi 500275449 334 AAPGPHDASYLFDEF 348
Cdd:cd01745  174 LADTDPDSLKLFEAF 188
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 218-332 5.21e-06

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


Pssm-ID: 429620 [Multi-domain]  Cd Length: 219  Bit Score: 46.87  E-value: 5.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449  218 SNGPGNPD-DVPEaLDMIRGILG-KIPIFGICMGHQLFAKANGATTY---KMKFG---HR--------GFNHAVReIATG 281
Cdd:pfam07722  82 SGGPYDPArDAYE-LALIRAALArGKPILGICRGFQLLNVALGGTLYqdiQEQPGftdHRehcqvapyAPSHAVN-VEPG 159

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500275449  282 RV-------DFTSQN--HGYAVARedLPECLMIT-HEEinDKSVEGVRHKYYPGF--SVQFHP 332
Cdd:pfam07722 160 SLlasllgsEEFRVNslHHQAIDR--LAPGLRVEaVAP--DGTIEAIESPNAKGFalGVQWHP 218
PLN02347 PLN02347
GMP synthetase
 173-258 2.29e-05

GMP synthetase


Pssm-ID: 215197 [Multi-domain]  Cd Length: 536  Bit Score: 46.22  E-value: 2.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449 173 VVLVDFGLK--HSILRELakRDCNV--TVVPYDTTAEEILALNPDGVMLSNGP------GNPDDVPEALDMIRGilGKIP 242
Cdd:PLN02347  13 VLILDYGSQytHLITRRV--RELGVysLLLSGTASLDRIASLNPRVVILSGGPhsvhveGAPTVPEGFFDYCRE--RGVP 88

                         90
                 ....*....|....*.
gi 500275449 243 IFGICMGHQLFAKANG 258
Cdd:PLN02347  89 VLGICYGMQLIVQKLG 104
PRK09065 PRK09065
glutamine amidotransferase; Provisional
 242-344 1.58e-03

glutamine amidotransferase; Provisional


Pssm-ID: 181635 [Multi-domain]  Cd Length: 237  Bit Score: 39.56  E-value: 1.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449 242 PIFGICMGHQLFAKANGattykmkfGHRGFNHAVREIATGRVDFTSQnhgyavARED-----LPECL--MITHEEindkS 314
Cdd:PRK09065  90 PLLGICYGHQLLAHALG--------GEVGYNPAGRESGTVTVELHPA------AADDplfagLPAQFpaHLTHLQ----S 151

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 500275449 315 V----EGVRH------------KYYPG-FSVQFHPDAAPgPHDASYL 344
Cdd:PRK09065 152 VlrlpPGAVVlarsaqdphqafRYGPHaWGVQFHPEFTA-HIMRAYL 197
hisH PRK13143
imidazole glycerol phosphate synthase subunit HisH; Provisional
 173-252 4.28e-03

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237289 [Multi-domain]  Cd Length: 200  Bit Score: 37.93  E-value: 4.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500275449 173 VVLVDFGLKH--SILRELAKRDCNVTVVpydTTAEEILALnpDGVMLSnGPGNPDDVPEALDMIRGILGK-----IPIFG 245
Cdd:PRK13143   3 IVIIDYGVGNlrSVSKALERAGAEVVIT---SDPEEILDA--DGIVLP-GVGAFGAAMENLSPLRDVILEaarsgKPFLG 76


                 ....*..
gi 500275449 246 ICMGHQL 252
Cdd:PRK13143  77 ICLGMQL 83
 
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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