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Conserved domains on  [gi|1333889359|ref|WP_102993871|]
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glutamine-hydrolyzing carbamoyl-phosphate synthase small subunit [Laceyella tengchongensis]

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 ...
 1-352 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: 684.06  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359   1 MKARLLLEDGTLFTGTSFGAEGNSLGEVVFNTSMTGYQEILTDPSYCGQIITMTYPLIGNYGISRDDNESLRPYAQGLVV 80
Cdd:COG0505     3 MKALLVLEDGTVFEGKSFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVTFTYPHIGNYGVNDEDFESDRPWVAGLVV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359  81 REIAEYASNWRNEMPLSTFLKEYGIIGIAGIDTRMLTRKLRQNGVMKGIITTGDETIEALMEQM-GTPLM--RDQVARVS 157
Cdd:COG0505    83 RELSRRPSNWRSEESLDEYLKEHGIPGISGIDTRALTRHLREKGAMKGVISTGDLDIEELLEKArAAPGMegLDLVKEVS 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359 158 TKS---IHIAPSYGKRVVLVDFGAKHNIQRELVERGCEVISVPYNTPAEEILRFRPDGIMLSNGPGDPKDVPEAITMIGK 234
Cdd:COG0505   163 TKEpyeWTEAPGAGFHVVALDFGVKRNILRELAERGCRVTVVPATTSAEEILALNPDGVFLSNGPGDPAALDYAIETIRE 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359 235 LLGK-VPMFGICLGHQLFALACGADTVKMKFGHRGGNHPVKELATGRTVITSQNHGYAVNPESVKGTGLEISHIALNDGT 313
Cdd:COG0505   243 LLGKgIPIFGICLGHQLLALALGAKTYKLKFGHRGANHPVKDLETGRVEITSQNHGFAVDEDSLPATDLEVTHVNLNDGT 322

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1333889359 314 VEGLVHQSHPAFSVQYHPESAPGPLDSGYLFDRFVEMMD 352
Cdd:COG0505   323 VEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDRFIELME 361
 
Name Accession Description Interval E-value
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 1-352 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: 684.06  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359   1 MKARLLLEDGTLFTGTSFGAEGNSLGEVVFNTSMTGYQEILTDPSYCGQIITMTYPLIGNYGISRDDNESLRPYAQGLVV 80
Cdd:COG0505     3 MKALLVLEDGTVFEGKSFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVTFTYPHIGNYGVNDEDFESDRPWVAGLVV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359  81 REIAEYASNWRNEMPLSTFLKEYGIIGIAGIDTRMLTRKLRQNGVMKGIITTGDETIEALMEQM-GTPLM--RDQVARVS 157
Cdd:COG0505    83 RELSRRPSNWRSEESLDEYLKEHGIPGISGIDTRALTRHLREKGAMKGVISTGDLDIEELLEKArAAPGMegLDLVKEVS 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359 158 TKS---IHIAPSYGKRVVLVDFGAKHNIQRELVERGCEVISVPYNTPAEEILRFRPDGIMLSNGPGDPKDVPEAITMIGK 234
Cdd:COG0505   163 TKEpyeWTEAPGAGFHVVALDFGVKRNILRELAERGCRVTVVPATTSAEEILALNPDGVFLSNGPGDPAALDYAIETIRE 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359 235 LLGK-VPMFGICLGHQLFALACGADTVKMKFGHRGGNHPVKELATGRTVITSQNHGYAVNPESVKGTGLEISHIALNDGT 313
Cdd:COG0505   243 LLGKgIPIFGICLGHQLLALALGAKTYKLKFGHRGANHPVKDLETGRVEITSQNHGFAVDEDSLPATDLEVTHVNLNDGT 322

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1333889359 314 VEGLVHQSHPAFSVQYHPESAPGPLDSGYLFDRFVEMMD 352
Cdd:COG0505   323 VEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDRFIELME 361
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
1-351 0e+00

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 650.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359   1 MKARLLLEDGTLFTGTSFGAEGNSLGEVVFNTSMTGYQEILTDPSYCGQIITMTYPLIGNYGISRDDNESLRPYAQGLVV 80
Cdd:PRK12564    3 MKAYLVLEDGTVFEGKAFGAEGETVGEVVFNTSMTGYQEILTDPSYAGQIVTFTYPLIGNYGVNREDFESDRPHAKGLIV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359  81 REIAEYASNWRNEMPLSTFLKEYGIIGIAGIDTRMLTRKLRQNGVMKGIITTGDETIEALMEQM-GTPLM--RDQVARVS 157
Cdd:PRK12564   83 RELSDIPSNWRSEMSLDEYLKENGIPGISGIDTRALTRKLREKGAMKGVIATEDFDAEELLEKArAFPGLlgLDLVKEVS 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359 158 TKSIHI----APSYGKRVVLVDFGAKHNIQRELVERGCEVISVPYNTPAEEILRFRPDGIMLSNGPGDPKDVPEAITMIG 233
Cdd:PRK12564  163 TKEPYPwpgpGGELKYKVVAIDFGVKRNILRELAERGCRVTVVPATTTAEEILALNPDGVFLSNGPGDPAALDYAIEMIR 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359 234 KLLG-KVPMFGICLGHQLFALACGADTVKMKFGHRGGNHPVKELATGRTVITSQNHGYAVNPESVKGTgLEISHIALNDG 312
Cdd:PRK12564  243 ELLEkKIPIFGICLGHQLLALALGAKTYKMKFGHRGANHPVKDLETGKVEITSQNHGFAVDEDSLPAN-LEVTHVNLNDG 321

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1333889359 313 TVEGLVHQSHPAFSVQYHPESAPGPLDSGYLFDRFVEMM 351
Cdd:PRK12564  322 TVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDEFVELM 360
CPSaseIIsmall TIGR01368
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ...
 3-352 0e+00

carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small chain of the glutamine-dependent form (EC 6.3.5.5) of carbamoyl phosphate synthase, CPSase II. The C-terminal domain has glutamine amidotransferase activity. Note that the sequence from the mammalian urea cycle form has lost the active site Cys, resulting in an ammonia-dependent form, CPSase I (EC 6.3.4.16). CPSases of pyrimidine biosynthesis, arginine biosynthesis, and the urea cycle may be encoded by one or by several genes, depending on the species. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273580 [Multi-domain]  Cd Length: 357  Bit Score: 568.80  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359   3 ARLLLEDGTLFTGTSFGAEGNSLGEVVFNTSMTGYQEILTDPSYCGQIITMTYPLIGNYGISRDDNESLRPYAQGLVVRE 82
Cdd:TIGR01368   1 AYLVLEDGTVFRGYSFGAEGTVAGEVVFNTGMTGYQEILTDPSYKGQIVVFTYPLIGNYGVNDEDAESKGIHVSGLVVRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359  83 IAEYASNWRNEMPLSTFLKEYGIIGIAGIDTRMLTRKLRQNGVMKGIITTGDETIEALMEQMGT---PLMRDQVARVSTK 159
Cdd:TIGR01368  81 LSDRYSNWRATESLDQFLKRHGIPGIYGVDTRALVKKIREKGTMKGVISTEDSNDEELVEKARVspdITGINLVAEVSTK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359 160 SI-HIAPSYGK--RVVLVDFGAKHNIQRELVERGCEVISVPYNTPAEEILRFRPDGIMLSNGPGDPKDVPEAITMIGKLL 236
Cdd:TIGR01368 161 EPyTWGQRGGKgkRVVVIDFGVKRNILRRLVKRGCEVTVVPYDTDAEEIKKYNPDGIFLSNGPGDPAAVEPAIETIRKLL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359 237 GKVPMFGICLGHQLFALACGADTVKMKFGHRGGNHPVKELATGRTVITSQNHGYAVNPESVKGTGLEISHIALNDGTVEG 316
Cdd:TIGR01368 241 EKIPIFGICLGHQLLALAFGAKTYKMKFGHRGGNHPVKDLITGRVEITSQNHGYAVDPDSLPAGDLEVTHVNLNDGTVEG 320

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 1333889359 317 LVHQSHPAFSVQYHPESAPGPLDSGYLFDRFVEMMD 352
Cdd:TIGR01368 321 IRHKDLPVFSVQYHPEASPGPHDTEYLFDEFIDLMK 356
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 171-348 1.76e-115

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: 332.54  E-value: 1.76e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359 171 VVLVDFGAKHNIQRELVERGCEVISVPYNTPAEEILRFRPDGIMLSNGPGDPKDVPEAITMIGKLLGK-VPMFGICLGHQ 249
Cdd:cd01744     1 VVVIDFGVKHNILRELLKRGCEVTVVPYNTDAEEILKLDPDGIFLSNGPGDPALLDEAIKTVRKLLGKkIPIFGICLGHQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359 250 LFALACGADTVKMKFGHRGGNHPVKELATGRTVITSQNHGYAVNPESVKGtGLEISHIALNDGTVEGLVHQSHPAFSVQY 329
Cdd:cd01744    81 LLALALGAKTYKMKFGHRGSNHPVKDLITGRVYITSQNHGYAVDPDSLPG-GLEVTHVNLNDGTVEGIRHKDLPVFSVQF 159

                         170
                  ....*....|....*....
gi 1333889359 330 HPESAPGPLDSGYLFDRFV 348
Cdd:cd01744   160 HPEASPGPHDTEYLFDEFL 178
CPSase_sm_chain smart01097
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 1-130 3.34e-89

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: 263.85  E-value: 3.34e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359    1 MKARLLLEDGTLFTGTSFGAEGNSLGEVVFNTSMTGYQEILTDPSYCGQIITMTYPLIGNYGISRDDNESLRPYAQGLVV 80
Cdd:smart01097   1 MKAYLVLEDGTVFEGESFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNDEDFESDKIQVKGLVV 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1333889359   81 REIAEYASNWRNEMPLSTFLKEYGIIGIAGIDTRMLTRKLRQNGVMKGII 130
Cdd:smart01097  81 RELSDEPSNWRSEQSLDEFLKENGIPGISGIDTRALTRKLREKGAMKGVI 130
CPSase_sm_chain pfam00988
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 5-130 1.10e-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: 259.95  E-value: 1.10e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359   5 LLLEDGTLFTGTSFGAEGNSLGEVVFNTSMTGYQEILTDPSYCGQIITMTYPLIGNYGISRDDNESLRPYAQGLVVREIA 84
Cdd:pfam00988   1 LVLEDGTVFEGKSFGAAGSTVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNPEDFESDKIHVAGLVVREYS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1333889359  85 EYASNWRNEMPLSTFLKEYGIIGIAGIDTRMLTRKLRQNGVMKGII 130
Cdd:pfam00988  81 DEPSNWRAEESLDEWLKEQGIPGISGVDTRALTRKIREKGAMKGVI 126
 
Name Accession Description Interval E-value
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 1-352 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: 684.06  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359   1 MKARLLLEDGTLFTGTSFGAEGNSLGEVVFNTSMTGYQEILTDPSYCGQIITMTYPLIGNYGISRDDNESLRPYAQGLVV 80
Cdd:COG0505     3 MKALLVLEDGTVFEGKSFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVTFTYPHIGNYGVNDEDFESDRPWVAGLVV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359  81 REIAEYASNWRNEMPLSTFLKEYGIIGIAGIDTRMLTRKLRQNGVMKGIITTGDETIEALMEQM-GTPLM--RDQVARVS 157
Cdd:COG0505    83 RELSRRPSNWRSEESLDEYLKEHGIPGISGIDTRALTRHLREKGAMKGVISTGDLDIEELLEKArAAPGMegLDLVKEVS 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359 158 TKS---IHIAPSYGKRVVLVDFGAKHNIQRELVERGCEVISVPYNTPAEEILRFRPDGIMLSNGPGDPKDVPEAITMIGK 234
Cdd:COG0505   163 TKEpyeWTEAPGAGFHVVALDFGVKRNILRELAERGCRVTVVPATTSAEEILALNPDGVFLSNGPGDPAALDYAIETIRE 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359 235 LLGK-VPMFGICLGHQLFALACGADTVKMKFGHRGGNHPVKELATGRTVITSQNHGYAVNPESVKGTGLEISHIALNDGT 313
Cdd:COG0505   243 LLGKgIPIFGICLGHQLLALALGAKTYKLKFGHRGANHPVKDLETGRVEITSQNHGFAVDEDSLPATDLEVTHVNLNDGT 322

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1333889359 314 VEGLVHQSHPAFSVQYHPESAPGPLDSGYLFDRFVEMMD 352
Cdd:COG0505   323 VEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDRFIELME 361
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
1-351 0e+00

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 650.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359   1 MKARLLLEDGTLFTGTSFGAEGNSLGEVVFNTSMTGYQEILTDPSYCGQIITMTYPLIGNYGISRDDNESLRPYAQGLVV 80
Cdd:PRK12564    3 MKAYLVLEDGTVFEGKAFGAEGETVGEVVFNTSMTGYQEILTDPSYAGQIVTFTYPLIGNYGVNREDFESDRPHAKGLIV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359  81 REIAEYASNWRNEMPLSTFLKEYGIIGIAGIDTRMLTRKLRQNGVMKGIITTGDETIEALMEQM-GTPLM--RDQVARVS 157
Cdd:PRK12564   83 RELSDIPSNWRSEMSLDEYLKENGIPGISGIDTRALTRKLREKGAMKGVIATEDFDAEELLEKArAFPGLlgLDLVKEVS 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359 158 TKSIHI----APSYGKRVVLVDFGAKHNIQRELVERGCEVISVPYNTPAEEILRFRPDGIMLSNGPGDPKDVPEAITMIG 233
Cdd:PRK12564  163 TKEPYPwpgpGGELKYKVVAIDFGVKRNILRELAERGCRVTVVPATTTAEEILALNPDGVFLSNGPGDPAALDYAIEMIR 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359 234 KLLG-KVPMFGICLGHQLFALACGADTVKMKFGHRGGNHPVKELATGRTVITSQNHGYAVNPESVKGTgLEISHIALNDG 312
Cdd:PRK12564  243 ELLEkKIPIFGICLGHQLLALALGAKTYKMKFGHRGANHPVKDLETGKVEITSQNHGFAVDEDSLPAN-LEVTHVNLNDG 321

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1333889359 313 TVEGLVHQSHPAFSVQYHPESAPGPLDSGYLFDRFVEMM 351
Cdd:PRK12564  322 TVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDEFVELM 360
CPSaseIIsmall TIGR01368
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ...
 3-352 0e+00

carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small chain of the glutamine-dependent form (EC 6.3.5.5) of carbamoyl phosphate synthase, CPSase II. The C-terminal domain has glutamine amidotransferase activity. Note that the sequence from the mammalian urea cycle form has lost the active site Cys, resulting in an ammonia-dependent form, CPSase I (EC 6.3.4.16). CPSases of pyrimidine biosynthesis, arginine biosynthesis, and the urea cycle may be encoded by one or by several genes, depending on the species. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273580 [Multi-domain]  Cd Length: 357  Bit Score: 568.80  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359   3 ARLLLEDGTLFTGTSFGAEGNSLGEVVFNTSMTGYQEILTDPSYCGQIITMTYPLIGNYGISRDDNESLRPYAQGLVVRE 82
Cdd:TIGR01368   1 AYLVLEDGTVFRGYSFGAEGTVAGEVVFNTGMTGYQEILTDPSYKGQIVVFTYPLIGNYGVNDEDAESKGIHVSGLVVRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359  83 IAEYASNWRNEMPLSTFLKEYGIIGIAGIDTRMLTRKLRQNGVMKGIITTGDETIEALMEQMGT---PLMRDQVARVSTK 159
Cdd:TIGR01368  81 LSDRYSNWRATESLDQFLKRHGIPGIYGVDTRALVKKIREKGTMKGVISTEDSNDEELVEKARVspdITGINLVAEVSTK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359 160 SI-HIAPSYGK--RVVLVDFGAKHNIQRELVERGCEVISVPYNTPAEEILRFRPDGIMLSNGPGDPKDVPEAITMIGKLL 236
Cdd:TIGR01368 161 EPyTWGQRGGKgkRVVVIDFGVKRNILRRLVKRGCEVTVVPYDTDAEEIKKYNPDGIFLSNGPGDPAAVEPAIETIRKLL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359 237 GKVPMFGICLGHQLFALACGADTVKMKFGHRGGNHPVKELATGRTVITSQNHGYAVNPESVKGTGLEISHIALNDGTVEG 316
Cdd:TIGR01368 241 EKIPIFGICLGHQLLALAFGAKTYKMKFGHRGGNHPVKDLITGRVEITSQNHGYAVDPDSLPAGDLEVTHVNLNDGTVEG 320

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 1333889359 317 LVHQSHPAFSVQYHPESAPGPLDSGYLFDRFVEMMD 352
Cdd:TIGR01368 321 IRHKDLPVFSVQYHPEASPGPHDTEYLFDEFIDLMK 356
PRK12838 PRK12838
carbamoyl phosphate synthase small subunit; Reviewed
 1-351 0e+00

carbamoyl phosphate synthase small subunit; Reviewed


Pssm-ID: 183784 [Multi-domain]  Cd Length: 354  Bit Score: 541.02  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359   1 MKARLLLEDGTLFTGTSFGAEGNSLGEVVFNTSMTGYQEILTDPSYCGQIITMTYPLIGNYGISRDDNESLRPYAQGLVV 80
Cdd:PRK12838    1 MKAYLILEDGTVFEGELIGAPIDVTGEIVFNTGMTGYQEVLTDPSYKGQIVVFTYPLIGNYGINADDYESKQPQVKGVIV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359  81 REIAEYASNWRNEMPLSTFLKEYGIIGIAGIDTRMLTRKLRQNGVMKGIITTGDETIEALMEQMgTPLMRDQVARVSTKS 160
Cdd:PRK12838   81 YELSREGSHYRAKQSLDDFLKEWNIPGISGVDTRALVKHIREKGTMKASITTTDDAHAFDQIKA-LVLPKNVVAQVSTKE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359 161 IHIAPSYGKRVVLVDFGAKHNIQRELVERGCEVISVPYNTPAEEILRFRPDGIMLSNGPGDPKDVPEAITMIGKLLGKVP 240
Cdd:PRK12838  160 PYTYGNGGKHVALIDFGYKKSILRSLSKRGCKVTVLPYDTSLEEIKNLNPDGIVLSNGPGDPKELQPYLPEIKKLISSYP 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359 241 MFGICLGHQLFALACGADTVKMKFGHRGGNHPVKELATGRTVITSQNHGYAVNPESVKGTGLEISHIALNDGTVEGLVHQ 320
Cdd:PRK12838  240 ILGICLGHQLIALALGADTEKLPFGHRGANHPVIDLTTGRVWMTSQNHGYVVDEDSLDGTPLSVRFFNVNDGSIEGLRHK 319

                         330       340       350
                  ....*....|....*....|....*....|.
gi 1333889359 321 SHPAFSVQYHPESAPGPLDSGYLFDRFVEMM 351
Cdd:PRK12838  320 KKPVLSVQFHPEAHPGPHDAEYIFDEFLEMM 350
carA CHL00197
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
 2-358 9.34e-136

carbamoyl-phosphate synthase arginine-specific small subunit; Provisional


Pssm-ID: 214392 [Multi-domain]  Cd Length: 382  Bit Score: 391.85  E-value: 9.34e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359   2 KARLLLEDGTLFTGTSFGAEGNSLGEVVFNTSMTGYQEILTDPSYCGQIITMTYPLIGNYGISRDDNESLRPYAQGLVVR 81
Cdd:CHL00197    6 PAILVLEDGTYYRGWSFSNPITTIGEVVFNTGMTGYQEIITDPSYFEQIVTFTYPEIGNTGINLEDIESVKIQVKGIIAK 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359  82 EIAEYASNWRNEMPLSTFLKEYGIIGIAGIDTRMLTRKLRQNGVMKGIITTGD---ETIEALMEQMGTPLMRDQVARVST 158
Cdd:CHL00197   86 NICKSSSNWRQQESLVSYLQRHKIPFIFGIDTRALTQHLRRFGTMNGCISNQNlnlSYLRAKIKESPHMPSSDLIPRVTT 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359 159 KS---------------IHIAPSYGK--RVVLVDFGAKHNIQRELVERGCEVISVPYNTPAEEILRFRPDGIMLSNGPGD 221
Cdd:CHL00197  166 SSyyewdekshpsfylaDNKRPHSSYqlKIIVIDFGVKYNILRRLKSFGCSITVVPATSPYQDILSYQPDGILLSNGPGD 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359 222 PKDVPEAITMIGKLLG-KVPMFGICLGHQLFALACGADTVKMKFGHRGGNHPV--KELATgrtvITSQNHGYAVNPESVK 298
Cdd:CHL00197  246 PSAIHYGIKTVKKLLKyNIPIFGICMGHQILSLALEAKTFKLKFGHRGLNHPSglNQQVE----ITSQNHGFAVNLESLA 321

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359 299 GTGLEISHIALNDGTVEGLVHQSHPAFSVQYHPESAPGPLDSGYLFDRFVEMMDTFAARK 358
Cdd:CHL00197  322 KNKFYITHFNLNDGTVAGISHSPKPYFSVQYHPEASPGPHDADYLFEYFIEIIKHSKSSK 381
PLN02771 PLN02771
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
 3-344 1.40e-126

carbamoyl-phosphate synthase (glutamine-hydrolyzing)


Pssm-ID: 178370 [Multi-domain]  Cd Length: 415  Bit Score: 369.69  E-value: 1.40e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359   3 ARLLLEDGTLFTGTSFGAEGNSLGEVVFNTSMTGYQEILTDPSYCGQIITMTYPLIGNYGISRDDNESLRPYAQGLVVRE 82
Cdd:PLN02771   57 ARLVLEDGSVWKAKSFGARGTQVGEVVFNTSLTGYQEILTDPSYAGQFVLMTNPHIGNTGVNFDDEESRQCFLAGLVIRS 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359  83 IAEYASNWRNEMPLSTFLKEYGIIGIAGIDTRMLTRKLRQNGVMKGIITTGDETIEALMEQMGTP---LMRDQVARVSTK 159
Cdd:PLN02771  137 LSISTSNWRCTKTLGDYLAERNIMGIYDVDTRAITRRLREDGSLIGVLSTEDSKTDEELLKMSRSwdiVGIDLISGVSCK 216

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359 160 SI-----------------HIAPSYgkRVVLVDFGAKHNIQRELVERGCEVISVPYNTPAEEILRFRPDGIMLSNGPGDP 222
Cdd:PLN02771  217 SPyewvdktnpewdfntnsRDGESY--HVIAYDFGIKHNILRRLASYGCKITVVPSTWPASEALKMKPDGVLFSNGPGDP 294

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359 223 KDVPEAITMIGKLLGKVPMFGICLGHQLFALACGADTVKMKFGHRGGNHPVKELATGRTVITSQNHGYAVNPESVKGtGL 302
Cdd:PLN02771  295 SAVPYAVETVKELLGKVPVFGICMGHQLLGQALGGKTFKMKFGHHGGNHPVRNNRTGRVEISAQNHNYAVDPASLPE-GV 373

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1333889359 303 EISHIALNDGTVEGLVHQSHPAFSVQYHPESAPGPLDSGYLF 344
Cdd:PLN02771  374 EVTHVNLNDGSCAGLAFPALNVMSLQYHPEASPGPHDSDNAF 415
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 171-348 1.76e-115

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: 332.54  E-value: 1.76e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359 171 VVLVDFGAKHNIQRELVERGCEVISVPYNTPAEEILRFRPDGIMLSNGPGDPKDVPEAITMIGKLLGK-VPMFGICLGHQ 249
Cdd:cd01744     1 VVVIDFGVKHNILRELLKRGCEVTVVPYNTDAEEILKLDPDGIFLSNGPGDPALLDEAIKTVRKLLGKkIPIFGICLGHQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359 250 LFALACGADTVKMKFGHRGGNHPVKELATGRTVITSQNHGYAVNPESVKGtGLEISHIALNDGTVEGLVHQSHPAFSVQY 329
Cdd:cd01744    81 LLALALGAKTYKMKFGHRGSNHPVKDLITGRVYITSQNHGYAVDPDSLPG-GLEVTHVNLNDGTVEGIRHKDLPVFSVQF 159

                         170
                  ....*....|....*....
gi 1333889359 330 HPESAPGPLDSGYLFDRFV 348
Cdd:cd01744   160 HPEASPGPHDTEYLFDEFL 178
CPSase_sm_chain smart01097
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 1-130 3.34e-89

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: 263.85  E-value: 3.34e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359    1 MKARLLLEDGTLFTGTSFGAEGNSLGEVVFNTSMTGYQEILTDPSYCGQIITMTYPLIGNYGISRDDNESLRPYAQGLVV 80
Cdd:smart01097   1 MKAYLVLEDGTVFEGESFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNDEDFESDKIQVKGLVV 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1333889359   81 REIAEYASNWRNEMPLSTFLKEYGIIGIAGIDTRMLTRKLRQNGVMKGII 130
Cdd:smart01097  81 RELSDEPSNWRSEQSLDEFLKENGIPGISGIDTRALTRKLREKGAMKGVI 130
CPSase_sm_chain pfam00988
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 5-130 1.10e-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: 259.95  E-value: 1.10e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359   5 LLLEDGTLFTGTSFGAEGNSLGEVVFNTSMTGYQEILTDPSYCGQIITMTYPLIGNYGISRDDNESLRPYAQGLVVREIA 84
Cdd:pfam00988   1 LVLEDGTVFEGKSFGAAGSTVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNPEDFESDKIHVAGLVVREYS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1333889359  85 EYASNWRNEMPLSTFLKEYGIIGIAGIDTRMLTRKLRQNGVMKGII 130
Cdd:pfam00988  81 DEPSNWRAEESLDEWLKEQGIPGISGVDTRALTRKIREKGAMKGVI 126
GATase pfam00117
Glutamine amidotransferase class-I;
172-350 1.06e-68

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 214.02  E-value: 1.06e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359 172 VLVDFGA--KHNIQRELVERGCEVISVPYNTPAEEILRFRPDGIMLSNGPGDPKDVPEAITMIGKLLG-KVPMFGICLGH 248
Cdd:pfam00117   1 LLIDNGDsfTYNLARALRELGVEVTVVPNDTPAEEILEENPDGIILSGGPGSPGAAGGAIEAIREARElKIPILGICLGH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359 249 QLFALACGADTVKMK-FGHRGGNHPVKE------LATGRTVITSQNHGYAVNPESVKgTGLEISHIALNDGTVEGLVHQS 321
Cdd:pfam00117  81 QLLALAFGGKVVKAKkFGHHGKNSPVGDdgcglfYGLPNVFIVRRYHSYAVDPDTLP-DGLEVTATSENDGTIMGIRHKK 159

                         170       180
                  ....*....|....*....|....*....
gi 1333889359 322 HPAFSVQYHPESAPGPLDSGYLFDRFVEM 350
Cdd:pfam00117 160 LPIFGVQFHPESILTPHGPEILFNFFIKA 188
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 180-333 6.50e-28

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


Pssm-ID: 153214 [Multi-domain]  Cd Length: 184  Bit Score: 107.62  E-value: 6.50e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359 180 HNIQRELVERGCEVISVPYNTPA-EEILRFRPDGIMLSNGPGDPKDVPEAITMIGKLLGKVPMFGICLGHQLFALACGAD 258
Cdd:cd01743    12 YNLVQYLRELGAEVVVVRNDEITlEELELLNPDAIVISPGPGHPEDAGISLEIIRALAGKVPILGVCLGHQAIAEAFGGK 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359 259 TVKMKFGHRGGNHPVKELATGRTVITSQN------HGYAVNPESVkGTGLEIShIALNDGTVEGLVHQSHPAFSVQYHPE 332
Cdd:cd01743    92 VVRAPEPMHGKTSEIHHDGSGLFKGLPQPftvgryHSLVVDPDPL-PDLLEVT-ASTEDGVIMALRHRDLPIYGVQFHPE 169


                  .
gi 1333889359 333 S 333
Cdd:cd01743   170 S 170
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 180-333 2.85e-24

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


Pssm-ID: 440278 [Multi-domain]  Cd Length: 189  Bit Score: 98.19  E-value: 2.85e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359 180 HNIQRELVERGCEVISVPYN-TPAEEILRFRPDGIMLSNGPGDPKDVPEAITMIGKLLGKVPMFGICLGHQLFALACGAD 258
Cdd:COG0512    12 YNLVQYLGELGAEVVVVRNDeITLEEIEALAPDGIVLSPGPGTPEEAGISLEVIRAFAGKIPILGVCLGHQAIGEAFGGK 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359 259 TVKMkfghrggnhpvKELATGRT-VITSQNHG-------------Y---AVNPESVKgTGLEIshIALN-DGTVEGLVHQ 320
Cdd:COG0512    92 VVRA-----------PEPMHGKTsPITHDGSGlfaglpnpftatrYhslVVDRETLP-DELEV--TAWTeDGEIMGIRHR 157

                         170
                  ....*....|...
gi 1333889359 321 SHPAFSVQYHPES 333
Cdd:COG0512   158 ELPIEGVQFHPES 170
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 181-333 1.50e-21

anthranilate synthase component II; Provisional


Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 90.57  E-value: 1.50e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359 181 NIQRELVERGCEVISVPYNTPA-EEILRFRPDGIMLSNGPGDPKDVPEAITMIGKLLGKVPMFGICLGHQLFALACGADT 259
Cdd:PRK05670   14 NLVQYLGELGAEVVVYRNDEITlEEIEALNPDAIVLSPGPGTPAEAGISLELIREFAGKVPILGVCLGHQAIGEAFGGKV 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359 260 VKmkfghrggnhpVKELATGRT-VITSQNHG-------------Y---AVNPESVKgTGLEISHIAlNDGTVEGLVHQSH 322
Cdd:PRK05670   94 VR-----------AKEIMHGKTsPIEHDGSGifaglpnpftvtrYhslVVDRESLP-DCLEVTAWT-DDGEIMGVRHKEL 160

                         170
                  ....*....|.
gi 1333889359 323 PAFSVQYHPES 333
Cdd:PRK05670  161 PIYGVQFHPES 171
PRK14607 PRK14607
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
170-333 4.88e-21

bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;


Pssm-ID: 237764 [Multi-domain]  Cd Length: 534  Bit Score: 94.40  E-value: 4.88e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359 170 RVVLVD----FgaKHNIQRELVERGCEVISVPYN--TPAEEILRFRPDGIMLSNGPGDPKDVPEAITMIGKLLGKVPMFG 243
Cdd:PRK14607    1 MIILIDnydsF--TYNIYQYIGELGPEEIEVVRNdeITIEEIEALNPSHIVISPGPGRPEEAGISVEVIRHFSGKVPILG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359 244 ICLGHQLFALACGADTVKMKFGHRGGNHPVKELATG--RTV----ITSQNHGYAVNPESVKGTgLEISHIAlNDGTVEGL 317
Cdd:PRK14607   79 VCLGHQAIGYAFGGKIVHAKRILHGKTSPIDHNGKGlfRGIpnptVATRYHSLVVEEASLPEC-LEVTAKS-DDGEIMGI 156

                         170
                  ....*....|....*.
gi 1333889359 318 VHQSHPAFSVQYHPES 333
Cdd:PRK14607  157 RHKEHPIFGVQFHPES 172
guaA_Nterm TIGR00888
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ...
 171-332 6.14e-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: 6.14e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359 171 VVLVDFGAKHN--IQRELVERG--CEVisVPYNTPAEEILRFRPDGIMLSNGPGD--PKDVPEAITMIGKLlgKVPMFGI 244
Cdd:TIGR00888   1 ILVLDFGSQYTqlIARRLRELGvySEL--VPNTTPLEEIREKNPKGIILSGGPSSvyAENAPRADEKIFEL--GVPVLGI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359 245 CLGHQLFALACGADTVKmkfGHRGGNHPVKELATGRTVITS---------QNHGYAVN--PEsvkgtGLEIshIALNDGT 313
Cdd:TIGR00888  77 CYGMQLMAKQLGGEVGR---AEKREYGKAELEILDEDDLFRglpdestvwMSHGDKVKelPE-----GFKV--LATSDNC 146

                         170       180
                  ....*....|....*....|
gi 1333889359 314 -VEGLVHQSHPAFSVQYHPE 332
Cdd:TIGR00888 147 pVAAMAHEEKPIYGVQFHPE 166
trpG_papA TIGR00566
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ...
 180-333 1.20e-17

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: 79.83  E-value: 1.20e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359 180 HNIQRELVERGCEVIsVPYNTPA--EEILRFRPDGIMLSNGPGDPKDVPEAITMIGKLLGKVPMFGICLGHQLFALACGA 257
Cdd:TIGR00566  13 YNLVQYFCELGAEVV-VKRNDSLtlQEIEALLPLLIVISPGPCTPNEAGISLEAIRHFAGKLPILGVCLGHQAMGQAFGG 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359 258 DTVKMKFGHRGGNHPVKELATGR------TVITSQNHGYAVNPESVKGTgLEISHIALNDGTVEGLVHQSHPAFSVQYHP 331
Cdd:TIGR00566  92 DVVRANTVMHGKTSEIEHNGAGIfrglfnPLTATRYHSLVVEPETLPTC-FPVTAWEEENIEIMAIRHRDLPLEGVQFHP 170


                  ..
gi 1333889359 332 ES 333
Cdd:TIGR00566 171 ES 172
PabB-fungal TIGR01823
aminodeoxychorismate synthase, fungal clade; This model represents the fungal clade of a ...
 193-361 2.75e-17

aminodeoxychorismate synthase, fungal clade; This model represents the fungal clade of a para-aminobenzoate synthesis enzyme, aminodeoxychorismate synthase, which acts on chorismate in a pathway that yields PABA, a precursor of folate.


Pssm-ID: 273821 [Multi-domain]  Cd Length: 742  Bit Score: 83.42  E-value: 2.75e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359 193 VISVPYNTPAEEILRFRP--DGIMLSNGPGDPkDVPEAITMIGKL-----LGKVPMFGICLGHQLFALACGADTVKMKFG 265
Cdd:TIGR01823  35 VTTVHSDTFQDQLLELLPlfDAIVVGPGPGNP-NNAQDMGIISELwelanLDEVPVLGICLGFQSLCLAQGADISRLPTP 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359 266 HRGGNHPVKELATGR-----TVITSQNHGYAVNPESVKGTGLEISHIALNDGTVEGLVHQSHPAFSVQYHPESAPGPLDS 340
Cdd:TIGR01823 114 KHGQVYEMHTNDAAIfcglfSVKSTRYHSLYANPEGIDTLLPLCLTEDEEGIILMSAQTKKKPWFGVQYHPESCCSELGS 193

                         170       180
                  ....*....|....*....|.
gi 1333889359 341 GYLFDRFVEMMDTFAARKGEG 361
Cdd:TIGR01823 194 GKLVSNFLKLAFINNVKTGRW 214
GATase1_GMP_Synthase cd01742
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ...
 171-332 2.20e-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: 76.04  E-value: 2.20e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359 171 VVLVDFGAK--HNIQRELVERG--CEVIsvPYNTPAEEILRFRPDGIMLSNGP------GDPKDVPEAITMigkllgKVP 240
Cdd:cd01742     1 ILILDFGSQytHLIARRVRELGvySEIL--PNTTPLEEIKLKNPKGIILSGGPssvyeeDAPRVDPEIFEL------GVP 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359 241 MFGICLGHQLFALACGAdTVKmKFGHRGGnhpvkelatGRTVITSQNHGyavnpESVKGTGLEI----SH----IALNDG 312
Cdd:cd01742    73 VLGICYGMQLIAKALGG-KVE-RGDKREY---------GKAEIEIDDSS-----PLFEGLPDEQtvwmSHgdevVKLPEG 136

                         170       180       190
                  ....*....|....*....|....*....|
gi 1333889359 313 ----------TVEGLVHQSHPAFSVQYHPE 332
Cdd:cd01742   137 fkviassdncPVAAIANEEKKIYGVQFHPE 166
guaA PRK00074
GMP synthase; Reviewed
 170-332 4.33e-14

GMP synthase; Reviewed


Pssm-ID: 234614 [Multi-domain]  Cd Length: 511  Bit Score: 73.16  E-value: 4.33e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359 170 RVVLVDFGAKHN--IQRELVERG--CEVisVPYNTPAEEILRFRPDGIMLSNGP------GDPKdVPEAITMIGkllgkV 239
Cdd:PRK00074    5 KILILDFGSQYTqlIARRVRELGvySEI--VPYDISAEEIRAFNPKGIILSGGPasvyeeGAPR-ADPEIFELG-----V 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359 240 PMFGICLGHQLFALACGADTVKMK---FGH-----RGGNHPVKELATGRTVITSqnHGYAVN--PEsvkgtGLEIshIAL 309
Cdd:PRK00074   77 PVLGICYGMQLMAHQLGGKVERAGkreYGRaelevDNDSPLFKGLPEEQDVWMS--HGDKVTelPE-----GFKV--IAS 147

                         170       180
                  ....*....|....*....|....
gi 1333889359 310 NDGT-VEGLVHQSHPAFSVQYHPE 332
Cdd:PRK00074  148 TENCpIAAIANEERKFYGVQFHPE 171
PRK07649 PRK07649
aminodeoxychorismate/anthranilate synthase component II;
203-333 1.15e-13

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181066 [Multi-domain]  Cd Length: 195  Bit Score: 69.06  E-value: 1.15e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359 203 EEILRFRPDGIMLSNGPGDPKDVPEAITMIGKLLGKVPMFGICLGHQLFALACGADTVKMKFGHRGGNHPVKElaTGRTV 282
Cdd:PRK07649   37 SDIENMKPDFLMISPGPCSPNEAGISMEVIRYFAGKIPIFGVCLGHQSIAQVFGGEVVRAERLMHGKTSLMHH--DGKTI 114

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1333889359 283 IT--------SQNHGYAVNPESVKGTgLEISHiALNDGTVEGLVHQSHPAFSVQYHPES 333
Cdd:PRK07649  115 FSdipnpftaTRYHSLIVKKETLPDC-LEVTS-WTEEGEIMAIRHKTLPIEGVQFHPES 171
PRK00758 PRK00758
GMP synthase subunit A; Validated
 170-332 3.19e-13

GMP synthase subunit A; Validated


Pssm-ID: 179112 [Multi-domain]  Cd Length: 184  Bit Score: 67.18  E-value: 3.19e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359 170 RVVLVDFGAK--HNIQRELVERGCEVISVPYNTPAEEILRFrPDGIMLSNGPgDPKDVPEAITMIGKLlgKVPMFGICLG 247
Cdd:PRK00758    1 KIVVVDNGGQynHLIHRTLRYLGVDAKIIPNTTPVEEIKAF-EDGLILSGGP-DIERAGNCPEYLKEL--DVPILGICLG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359 248 HQLFALACGADTVKMKFGHRGG--------NHPVKELATGRTVITSQNhgyavnpESVKGTGLEISHIALNDGT-VEGLV 318
Cdd:PRK00758   77 HQLIAKAFGGEVGRGEYGEYALveveildeDDILKGLPPEIRVWASHA-------DEVKELPDGFEILARSDICeVEAMK 149

                         170
                  ....*....|....
gi 1333889359 319 HQSHPAFSVQYHPE 332
Cdd:PRK00758  150 HKEKPIYGVQFHPE 163
PRK05637 PRK05637
anthranilate synthase component II; Provisional
 201-337 3.23e-13

anthranilate synthase component II; Provisional


Pssm-ID: 180178 [Multi-domain]  Cd Length: 208  Bit Score: 67.95  E-value: 3.23e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359 201 PAEEILRFRPDGIMLSNGPGDPKDVPEAITMIGKLLGKVPMFGICLGHQlfAL---------ACG---ADTVKMKFGHRG 268
Cdd:PRK05637   36 PVEEILAANPDLICLSPGPGHPRDAGNMMALIDRTLGQIPLLGICLGFQ--ALlehhggkvePCGpvhGTTDNMILTDAG 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359 269 GNHPV-KELAT----------GRTVITSQNH--GYAVNP---ESVKGTGLEISHIALNDGTVEGLvhqshpAFSVQYHPE 332
Cdd:PRK05637  114 VQSPVfAGLATdvepdhpeipGRKVPIARYHslGCVVAPdgmESLGTCSSEIGPVIMAAETTDGK------AIGLQFHPE 187


                  ....*
gi 1333889359 333 SAPGP 337
Cdd:PRK05637  188 SVLSP 192
PLN02335 PLN02335
anthranilate synthase
 203-333 5.32e-13

anthranilate synthase


Pssm-ID: 177969 [Multi-domain]  Cd Length: 222  Bit Score: 67.51  E-value: 5.32e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359 203 EEILRFRPDGIMLSNGPGDPKDVPEAITMIGKLLGKVPMFGICLGHQLFALACGADTVKMKFG--HrGGNHPV---KELA 277
Cdd:PLN02335   56 EELKRKNPRGVLISPGPGTPQDSGISLQTVLELGPLVPLFGVCMGLQCIGEAFGGKIVRSPFGvmH-GKSSPVhydEKGE 134

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1333889359 278 TG------RTVITSQNHGYAVNPESVKGTGLEISHIAlNDGTVEGLVHQSHPAFS-VQYHPES 333
Cdd:PLN02335  135 EGlfsglpNPFTAGRYHSLVIEKDTFPSDELEVTAWT-EDGLIMAARHRKYKHIQgVQFHPES 196
PRK06774 PRK06774
aminodeoxychorismate synthase component II;
180-333 1.21e-12

aminodeoxychorismate synthase component II;


Pssm-ID: 180689 [Multi-domain]  Cd Length: 191  Bit Score: 66.04  E-value: 1.21e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359 180 HNIQRELVERGCEVIsVPYNTPA--EEILRFRPDGIMLSNGPGDPKDVPEAITMIGKLLGKVPMFGICLGHQLFALACGA 257
Cdd:PRK06774   13 YNLYQYFCELGTEVM-VKRNDELqlTDIEQLAPSHLVISPGPCTPNEAGISLAVIRHFADKLPILGVCLGHQALGQAFGA 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359 258 DTVKMKFGHRGGNHPVKELATG------RTVITSQNHGYAVNPESVKGTgLEISHIALNDGTVE---GLVHQSHPAFSVQ 328
Cdd:PRK06774   92 RVVRARQVMHGKTSAICHSGQGvfrglnQPLTVTRYHSLVIAADSLPGC-FELTAWSERGGEMDeimGIRHRTLPLEGVQ 170


                  ....*
gi 1333889359 329 YHPES 333
Cdd:PRK06774  171 FHPES 175
PRK13566 PRK13566
anthranilate synthase component I;
154-333 2.86e-12

anthranilate synthase component I;


Pssm-ID: 237429 [Multi-domain]  Cd Length: 720  Bit Score: 68.02  E-value: 2.86e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359 154 ARVSTKSIHIAPSYGKRVVLVDfgakH---------NIQRELverGCEVISVPYNTPAEEILRFRPDGIMLSNGPGDPKD 224
Cdd:PRK13566  512 NLSAEEPDAAAVGEGKRVLLVD----HedsfvhtlaNYFRQT---GAEVTTVRYGFAEEMLDRVNPDLVVLSPGPGRPSD 584

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359 225 --VPEaitMIGKLLGK-VPMFGICLGHQ---------LFALACGADTVKMKFGHRGGNHPVKELATGRTVitSQNHGYAV 292
Cdd:PRK13566  585 fdCKA---TIDAALARnLPIFGVCLGLQaiveafggeLGQLAYPMHGKPSRIRVRGPGRLFSGLPEEFTV--GRYHSLFA 659

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1333889359 293 NPESVkGTGLEISHIAlNDGTVEGLVHQSHPAFSVQYHPES 333
Cdd:PRK13566  660 DPETL-PDELLVTAET-EDGVIMAIEHKTLPVAAVQFHPES 698
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 170-332 3.30e-12

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


Pssm-ID: 440284 [Multi-domain]  Cd Length: 225  Bit Score: 65.35  E-value: 3.30e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359 170 RVVLVDFGA-----KHNIQRELVERGCEVISV--------PYNTPAEEilrfrPDGIMLSNGPGDPKD----VPEAITMI 232
Cdd:COG0518     1 KILILDHDPfggqyPGLIARRLREAGIELDVLrvyageilPYDPDLED-----PDGLILSGGPMSVYDedpwLEDEPALI 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359 233 GKLL-GKVPMFGICLGHQLFALACGADTVKMkfGHRG-GNHPV---------KELATGRTVItsQNHGYAVN--PEsvkg 299
Cdd:COG0518    76 REAFeLGKPVLGICYGAQLLAHALGGKVEPG--PGREiGWAPVelteadplfAGLPDEFTVW--MSHGDTVTelPE---- 147

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1333889359 300 tGLEisHIALNDGT-VEGLVHqSHPAFSVQYHPE 332
Cdd:COG0518   148 -GAE--VLASSDNCpNQAFRY-GRRVYGVQFHPE 177
PRK08857 PRK08857
aminodeoxychorismate/anthranilate synthase component II;
205-333 2.22e-11

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181566 [Multi-domain]  Cd Length: 193  Bit Score: 62.20  E-value: 2.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359 205 ILRFRPDGIMLSNGPGDPKDVPEAITMIGKLLGKVPMFGICLGHQLFALACGADTVKMKFGHRGGNHPVKElaTGRTVIT 284
Cdd:PRK08857   39 IEALNPTHLVISPGPCTPNEAGISLQAIEHFAGKLPILGVCLGHQAIAQVFGGQVVRARQVMHGKTSPIRH--TGRSVFK 116

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359 285 SQN--------HGYAVNPESVKGTGLEISHIALNDGTVE---GLVHQSHPAFSVQYHPES 333
Cdd:PRK08857  117 GLNnpltvtryHSLVVKNDTLPECFELTAWTELEDGSMDeimGFQHKTLPIEAVQFHPES 176
PRK08007 PRK08007
aminodeoxychorismate synthase component 2;
181-333 3.34e-11

aminodeoxychorismate synthase component 2;


Pssm-ID: 181194 [Multi-domain]  Cd Length: 187  Bit Score: 61.86  E-value: 3.34e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359 181 NIQRELVERGCEVIsVPYNTPA--EEILRFRPDGIMLSNGPGDPKDVPEAITMIGKLLGKVPMFGICLGHQLFALACGAD 258
Cdd:PRK08007   14 NLYQYFCELGADVL-VKRNDALtlADIDALKPQKIVISPGPCTPDEAGISLDVIRHYAGRLPILGVCLGHQAMAQAFGGK 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359 259 TVKMKFGHRGGNHPVKELATG------RTVITSQNHGYAVNPESVKGTgLEISHIAlNDGTVEGLVHQSHPAFSVQYHPE 332
Cdd:PRK08007   93 VVRAAKVMHGKTSPITHNGEGvfrglaNPLTVTRYHSLVVEPDSLPAC-FEVTAWS-ETREIMGIRHRQWDLEGVQFHPE 170


                  .
gi 1333889359 333 S 333
Cdd:PRK08007  171 S 171
PRK07765 PRK07765
aminodeoxychorismate/anthranilate synthase component II;
211-333 8.32e-11

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181107 [Multi-domain]  Cd Length: 214  Bit Score: 60.83  E-value: 8.32e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359 211 DGIMLSNGPGDPKDVPEAITMIGKLLG-KVPMFGICLGHQLFALACGAdTVkmkfghrgGNHPvkELATGRT-VITSQN- 287
Cdd:PRK07765   48 DGVLLSPGPGTPERAGASIDMVRACAAaGTPLLGVCLGHQAIGVAFGA-TV--------DRAP--ELLHGKTsSVHHTGv 116

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1333889359 288 ---------------HGYAVNPESVKGtglEISHIALND-GTVEGLVHQSHPAFSVQYHPES 333
Cdd:PRK07765  117 gvlaglpdpftatryHSLTILPETLPA---ELEVTARTDsGVIMAVRHRELPIHGVQFHPES 175
trpG CHL00101
anthranilate synthase component 2
 204-333 2.29e-09

anthranilate synthase component 2


Pssm-ID: 214365 [Multi-domain]  Cd Length: 190  Bit Score: 56.28  E-value: 2.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359 204 EILRFRPDGIMLSNGPGDPKDVPEAITMIGKLLGKVPMFGICLGHQLFALACGADTVKMKFGHRGGN----HPVKELATG 279
Cdd:CHL00101   38 KIKNLNIRHIIISPGPGHPRDSGISLDVISSYAPYIPILGVCLGHQSIGYLFGGKIIKAPKPMHGKTskiyHNHDDLFQG 117

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1333889359 280 --RTVITSQNHGYAVNPESVKgTGLEISHIAlNDGTVEGLVHQSHPA-FSVQYHPES 333
Cdd:CHL00101  118 lpNPFTATRYHSLIIDPLNLP-SPLEITAWT-EDGLIMACRHKKYKMlRGIQFHPES 172
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 192-348 1.25e-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: 153212 [Multi-domain]  Cd Length: 188  Bit Score: 54.17  E-value: 1.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359 192 EVISVPYNTPAEEILRFrpDGIMLSNGPGDPKD-----VPEAITMIGKLL-GKVPMFGICLGHQLFALACGADTVKMKFG 265
Cdd:cd01741    31 DVVDVYAGELLPDLDDY--DGLVILGGPMSVDEddypwLKKLKELIRQALaAGKPVLGICLGHQLLARALGGKVGRNPKG 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359 266 HRGGNHPVKELATGRTVITSQN----------HGYAV--NPESVKgtgleisHIALNDGT-VEGLVHQSHpAFSVQYHPE 332
Cdd:cd01741   109 WEIGWFPVTLTEAGKADPLFAGlpdefpvfhwHGDTVveLPPGAV-------LLASSEACpNQAFRYGDR-ALGLQFHPE 180

                         170
                  ....*....|....*.
gi 1333889359 333 SApgpldsgyLFDRFV 348
Cdd:cd01741   181 ER--------LLRNFL 188
PRK09522 PRK09522
bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate ...
 180-333 5.71e-08

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


Pssm-ID: 181927 [Multi-domain]  Cd Length: 531  Bit Score: 54.26  E-value: 5.71e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359 180 HNIQRELVERGCEVI----SVPYNTPAEEILRFRPDGIMLSNGPGDPKD---VPEAITmigKLLGKVPMFGICLGHQLFA 252
Cdd:PRK09522   15 YNLADQLRSNGHNVViyrnHIPAQTLIERLATMSNPVLMLSPGPGVPSEagcMPELLT---RLRGKLPIIGICLGHQAIV 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359 253 LACGadtvkmkfGHRGgnhPVKELATGRTVITSQNhGYA-----VNP------ESVKGT----GLEIShiALNDGTVEGL 317
Cdd:PRK09522   92 EAYG--------GYVG---QAGEILHGKASSIEHD-GQAmfaglTNPlpvaryHSLVGSnipaGLTIN--AHFNGMVMAV 157

                         170
                  ....*....|....*.
gi 1333889359 318 VHQSHPAFSVQYHPES 333
Cdd:PRK09522  158 RHDADRVCGFQFHPES 173
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 180-348 6.75e-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: 52.19  E-value: 6.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359 180 HNIQRELVERGCEVISVPYNTPAEEILR--FRPDGIMLS-----------------NGPGDPK-DVPEAITMIGKLLGKV 239
Cdd:cd01745    22 QYYVDAVRKAGGLPVLLPPVDDEEDLEQylELLDGLLLTgggdvdpplygeephpeLGPIDPErDAFELALLRAALERGK 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359 240 PMFGICLGHQLFALACGadtvkmkfghrGGNHPVkelatgrtVITSQNHGYAVNPesvKGTGLEISHIAlNDGTVEGLVH 319
Cdd:cd01745   102 PILGICRGMQLLNVALG-----------GTLYQD--------IRVNSLHHQAIKR---LADGLRVEARA-PDGVIEAIES 158

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1333889359 320 QSHP-AFSVQYHPES-APGPLDSGYLFDRFV 348
Cdd:cd01745   159 PDRPfVLGVQWHPEWlADTDPDSLKLFEAFV 189
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 171-256 7.57e-08

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: 50.29  E-value: 7.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359 171 VVLVDFGAK-----HNIQRELVERGCEVISVPYNTPAEEILRF--RPDGIMLSNGPGDPKDVPEAITMIGKLL----GKV 239
Cdd:cd01653     1 VAVLLFPGFeelelASPLDALREAGAEVDVVSPDGGPVESDVDldDYDGLILPGGPGTPDDLARDEALLALLReaaaAGK 80

                          90
                  ....*....|....*..
gi 1333889359 240 PMFGICLGHQLFALACG 256
Cdd:cd01653    81 PILGICLGAQLLVLGVQ 97
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 171-250 3.85e-07

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: 47.58  E-value: 3.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359 171 VVLVDFGAK-----HNIQRELVERGCEVISVPYNTPAEEILRF--RPDGIMLSNGPGDPKDVPEAITMIGKLL----GKV 239
Cdd:cd03128     1 VAVLLFGGSeelelASPLDALREAGAEVDVVSPDGGPVESDVDldDYDGLILPGGPGTPDDLAWDEALLALLReaaaAGK 80

                          90
                  ....*....|.
gi 1333889359 240 PMFGICLGHQL 250
Cdd:cd03128    81 PVLGICLGAQL 91
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 238-332 3.22e-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: 47.64  E-value: 3.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359 238 KVPMFGICLGHQLFALACG-----------------ADTVKMKFGHRggnHPVK-----ELA----TGRTVITSQNHgya 291
Cdd:pfam07722 105 GKPILGICRGFQLLNVALGgtlyqdiqeqpgftdhrEHCQVAPYAPS---HAVNvepgsLLAsllgSEEFRVNSLHH--- 178

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1333889359 292 vnpESVK--GTGLEISHIAlNDGTVEGLVHQSHPAF--SVQYHPE 332
Cdd:pfam07722 179 ---QAIDrlAPGLRVEAVA-PDGTIEAIESPNAKGFalGVQWHPE 219
GATase1_CTP_Synthase cd01746
Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase; ...
 238-336 1.08e-05

Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase; Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase (CTP). CTP is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. CTPs produce CTP from UTP and glutamine and regulate intracellular CTP levels through interactions with four ribonucleotide triphosphates. The enzyme exists as a dimer of identical chains that aggregates as a tetramer. CTP is derived form UTP in three separate steps involving two active sites. In one active site, the UTP O4 oxygen is activated by Mg-ATP-dependent phosphorylation, followed by displacement of the resulting 4-phosphate moiety by ammonia. At a separate site, ammonia is generated via rate limiting glutamine hydrolysis (glutaminase) activity. A gated channel that spans between the glutamine hydrolysis and amidoligase active sites provides a path for ammonia diffusion. CTPs belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.


Pssm-ID: 153217 [Multi-domain]  Cd Length: 235  Bit Score: 46.01  E-value: 1.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359 238 KVPMFGICLGHQL----FA-------------------------LACGADTVKMKFGHRGGNHPVK-------ELATGRT 281
Cdd:cd01746    84 NIPFLGICLGMQLavieFArnvlglpdanstefdpdtphpvvdlMPEQKGVKDLGGTMRLGAYPVIlkpgtlaHKYYGKD 163

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1333889359 282 VITSQ-NHGYAVNPESVK---GTGLEISHIALNDGTVEGLVHQSHPAF-SVQYHPE--SAPG 336
Cdd:cd01746   164 EVEERhRHRYEVNPEYVDeleEAGLRFSGTDPDGGLVEIVELPDHPFFvGTQFHPEfkSRPL 225
PLN02347 PLN02347
GMP synthetase
 164-332 5.66e-05

GMP synthetase


Pssm-ID: 215197 [Multi-domain]  Cd Length: 536  Bit Score: 45.06  E-value: 5.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359 164 APSYGKRVVLVDFGAK--HNIQRELVERGCEVISVPYNTPAEEILRFRPDGIMLSNGP------GDPKDVPEAITMIGKl 235
Cdd:PLN02347    6 AKSYLDVVLILDYGSQytHLITRRVRELGVYSLLLSGTASLDRIASLNPRVVILSGGPhsvhveGAPTVPEGFFDYCRE- 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359 236 lGKVPMFGICLGHQLFALACGADtVKMKFGHRGGNHPVK---------ELATGRTVITSQNHGYAVN--PESVKGTGlei 304
Cdd:PLN02347   85 -RGVPVLGICYGMQLIVQKLGGE-VKPGEKQEYGRMEIRvvcgsqlfgDLPSGETQTVWMSHGDEAVklPEGFEVVA--- 159

                         170       180
                  ....*....|....*....|....*...
gi 1333889359 305 shiALNDGTVEGLVHQSHPAFSVQYHPE 332
Cdd:PLN02347  160 ---KSVQGAVVAIENRERRIYGLQYHPE 184
PRK09065 PRK09065
glutamine amidotransferase; Provisional
 239-335 5.68e-04

glutamine amidotransferase; Provisional


Pssm-ID: 181635 [Multi-domain]  Cd Length: 237  Bit Score: 41.10  E-value: 5.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359 239 VPMFGICLGHQLFALACGADTVKMKFGHRGGNHPVKELATGRT-----VITSQNHGYAVNPESVkgtgleishIALNDGT 313
Cdd:PRK09065   89 MPLLGICYGHQLLAHALGGEVGYNPAGRESGTVTVELHPAAADdplfaGLPAQFPAHLTHLQSV---------LRLPPGA 159

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1333889359 314 V--EGLVHQSHPAF-------SVQYHPESAP 335
Cdd:PRK09065  160 VvlARSAQDPHQAFrygphawGVQFHPEFTA 190
GATase1_Glutamyl_Hydrolase cd01747
Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase; Type 1 ...
 190-358 6.27e-04

Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase; Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase. gamma-Glutamyl Hydrolase catalyzes the cleavage of the gamma-glutamyl chain of folylpoly-gamma-glutamyl substrates and is a central enzyme in folyl and antifolyl poly-gamma-glutamate metabolism. GATase activity involves the removal of the ammonia group from a glutamate molecule and its subsequent transfer to a specific substrate, thus creating a new carbon-nitrogen group on the substrate. gamma-Glutamyl hydrolases belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.


Pssm-ID: 153218 [Multi-domain]  Cd Length: 273  Bit Score: 41.15  E-value: 6.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359 190 GCEVISVPYNTPAEEILR-FRP-DGIMLSNGPGDPKDVP--EAITMIGKLLGKV-------PMFGICLGHQLFA-LACGA 257
Cdd:cd01747    33 GARVVPIWINESEEYYDKlFKSiNGILFPGGAVDIDTSGyaRTAKIIYNLALERndagdyfPVWGTCLGFELLTyLTSGE 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359 258 DTVKMKFGHRGGNHPV--------------------KELATgrTVITSQNHGYAVNPESVKGTGL--EISHIALNDGTVE 315
Cdd:cd01747   113 TLLLEATEATNSALPLnftedalqsrlfkrfppdllKSLAT--EPLTMNNHRYGISPENFTENGLlsDFFNVLTTNDDWN 190

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1333889359 316 GLV------HQSHPAFSVQYHPESAP--------------GPLDSGYLFDRFVEmmdtfAARK 358
Cdd:cd01747   191 GVEfistveAYKYPIYGVQWHPEKNAfewkksssiphseeAIRLTQYFANFFVN-----EARK 248
PLN02889 PLN02889
oxo-acid-lyase/anthranilate synthase
 211-260 5.84e-03

oxo-acid-lyase/anthranilate synthase


Pssm-ID: 215481 [Multi-domain]  Cd Length: 918  Bit Score: 38.68  E-value: 5.84e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1333889359 211 DGIMLSNGPGDPKdVPEAITMIGKLLGK---VPMFGICLGHQLFALACGADTV 260
Cdd:PLN02889  133 DNIVISPGPGSPT-CPADIGICLRLLLEcrdIPILGVCLGHQALGYVHGARIV 184
hisH PRK13143
imidazole glycerol phosphate synthase subunit HisH; Provisional
 169-250 5.96e-03

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237289 [Multi-domain]  Cd Length: 200  Bit Score: 37.54  E-value: 5.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333889359 169 KRVVLVDFGAKH--NIQRELVERGCEVISVpyNTPaEEILRFrpDGIMLsngPGdpkdV---PEAITMIGKLLGK----- 238
Cdd:PRK13143    1 MMIVIIDYGVGNlrSVSKALERAGAEVVIT--SDP-EEILDA--DGIVL---PG----VgafGAAMENLSPLRDVileaa 68

                          90
                  ....*....|....*
gi 1333889359 239 ---VPMFGICLGHQL 250
Cdd:PRK13143   69 rsgKPFLGICLGMQL 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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