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Conserved domains on  [gi|1085944882|emb|SDS73725|]
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carbamoyl-phosphate synthase small subunit [Winogradskyella sediminis]

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 ...
 5-365 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: 639.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085944882   5 QRKKALILLADGTIFHGKSIGKEGSAFGEVCFNTGTTGYQEIFTDPSYYGQLMVTTNAHIGNYGTKEEEVESDDVKIAGL 84
Cdd:COG0505     1 MMMKALLVLEDGTVFEGKSFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVTFTYPHIGNYGVNDEDFESDRPWVAGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085944882  85 ICKNFSFNYSRPAADASLEDFFEKHNTLAIADVDTRALVSYIRDNGAMNAVITTEIDNLEALKKQLAEFPSMKGLELASK 164
Cdd:COG0505    81 VVRELSRRPSNWRSEESLDEYLKEHGIPGISGIDTRALTRHLREKGAMKGVISTGDLDIEELLEKARAAPGMEGLDLVKE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085944882 165 VSTKEPYFVGD-ENATYKIAALDIGIKKNILRNLAKRDAYIKVFPYNAKFEDLEAFNPDGYFLSNGPGDPEPLSDAIDLA 243
Cdd:COG0505   161 VSTKEPYEWTEaPGAGFHVVALDFGVKRNILRELAERGCRVTVVPATTSAEEILALNPDGVFLSNGPGDPAALDYAIETI 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085944882 244 KDIIANNKPLFGICLGHQIIALANGISTYKMHNGHRGINHPVKNLVTGKGEITSQNHGFAINrEETEANANVEITHVHLN 323
Cdd:COG0505   241 RELLGKGIPIFGICLGHQLLALALGAKTYKLKFGHRGANHPVKDLETGRVEITSQNHGFAVD-EDSLPATDLEVTHVNLN 319

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1085944882 324 DHTVAGIKIKDKNCFSVQYHPEASPGPNDSLYLFDQFIENIK 365
Cdd:COG0505   320 DGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDRFIELME 361
 
Name Accession Description Interval E-value
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 5-365 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: 639.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085944882   5 QRKKALILLADGTIFHGKSIGKEGSAFGEVCFNTGTTGYQEIFTDPSYYGQLMVTTNAHIGNYGTKEEEVESDDVKIAGL 84
Cdd:COG0505     1 MMMKALLVLEDGTVFEGKSFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVTFTYPHIGNYGVNDEDFESDRPWVAGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085944882  85 ICKNFSFNYSRPAADASLEDFFEKHNTLAIADVDTRALVSYIRDNGAMNAVITTEIDNLEALKKQLAEFPSMKGLELASK 164
Cdd:COG0505    81 VVRELSRRPSNWRSEESLDEYLKEHGIPGISGIDTRALTRHLREKGAMKGVISTGDLDIEELLEKARAAPGMEGLDLVKE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085944882 165 VSTKEPYFVGD-ENATYKIAALDIGIKKNILRNLAKRDAYIKVFPYNAKFEDLEAFNPDGYFLSNGPGDPEPLSDAIDLA 243
Cdd:COG0505   161 VSTKEPYEWTEaPGAGFHVVALDFGVKRNILRELAERGCRVTVVPATTSAEEILALNPDGVFLSNGPGDPAALDYAIETI 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085944882 244 KDIIANNKPLFGICLGHQIIALANGISTYKMHNGHRGINHPVKNLVTGKGEITSQNHGFAINrEETEANANVEITHVHLN 323
Cdd:COG0505   241 RELLGKGIPIFGICLGHQLLALALGAKTYKLKFGHRGANHPVKDLETGRVEITSQNHGFAVD-EDSLPATDLEVTHVNLN 319

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1085944882 324 DHTVAGIKIKDKNCFSVQYHPEASPGPNDSLYLFDQFIENIK 365
Cdd:COG0505   320 DGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDRFIELME 361
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
5-364 0e+00

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 606.69  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085944882   5 QRKKALILLADGTIFHGKSIGKEGSAFGEVCFNTGTTGYQEIFTDPSYYGQLMVTTNAHIGNYGTKEEEVESDDVKIAGL 84
Cdd:PRK12564    1 MMMKAYLVLEDGTVFEGKAFGAEGETVGEVVFNTSMTGYQEILTDPSYAGQIVTFTYPLIGNYGVNREDFESDRPHAKGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085944882  85 ICKNFSFNYSRPAADASLEDFFEKHNTLAIADVDTRALVSYIRDNGAMNAVITTEIDNLEALKKQLAEFPSMKGLELASK 164
Cdd:PRK12564   81 IVRELSDIPSNWRSEMSLDEYLKENGIPGISGIDTRALTRKLREKGAMKGVIATEDFDAEELLEKARAFPGLLGLDLVKE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085944882 165 VSTKEPYFVGDE--NATYKIAALDIGIKKNILRNLAKRDAYIKVFPYNAKFEDLEAFNPDGYFLSNGPGDPEPLSDAIDL 242
Cdd:PRK12564  161 VSTKEPYPWPGPggELKYKVVAIDFGVKRNILRELAERGCRVTVVPATTTAEEILALNPDGVFLSNGPGDPAALDYAIEM 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085944882 243 AKDIIANNKPLFGICLGHQIIALANGISTYKMHNGHRGINHPVKNLVTGKGEITSQNHGFAINREETeaNANVEITHVHL 322
Cdd:PRK12564  241 IRELLEKKIPIFGICLGHQLLALALGAKTYKMKFGHRGANHPVKDLETGKVEITSQNHGFAVDEDSL--PANLEVTHVNL 318

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1085944882 323 NDHTVAGIKIKDKNCFSVQYHPEASPGPNDSLYLFDQFIENI 364
Cdd:PRK12564  319 NDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDEFVELM 360
CPSaseIIsmall TIGR01368
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ...
 9-365 2.89e-174

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: 488.67  E-value: 2.89e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085944882   9 ALILLADGTIFHGKSIGKEGSAFGEVCFNTGTTGYQEIFTDPSYYGQLMVTTNAHIGNYGTKEEEVESDDVKIAGLICKN 88
Cdd:TIGR01368   1 AYLVLEDGTVFRGYSFGAEGTVAGEVVFNTGMTGYQEILTDPSYKGQIVVFTYPLIGNYGVNDEDAESKGIHVSGLVVRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085944882  89 FSFNYSRPAADASLEDFFEKHNTLAIADVDTRALVSYIRDNGAMNAVITTEIDNLEALKKQLAEFPSMKGLELASKVSTK 168
Cdd:TIGR01368  81 LSDRYSNWRATESLDQFLKRHGIPGIYGVDTRALVKKIREKGTMKGVISTEDSNDEELVEKARVSPDITGINLVAEVSTK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085944882 169 EPYFVGDENA-TYKIAALDIGIKKNILRNLAKRDAYIKVFPYNAKFEDLEAFNPDGYFLSNGPGDPEPLSDAIDLAKDII 247
Cdd:TIGR01368 161 EPYTWGQRGGkGKRVVVIDFGVKRNILRRLVKRGCEVTVVPYDTDAEEIKKYNPDGIFLSNGPGDPAAVEPAIETIRKLL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085944882 248 aNNKPLFGICLGHQIIALANGISTYKMHNGHRGINHPVKNLVTGKGEITSQNHGFAINREETEANAnVEITHVHLNDHTV 327
Cdd:TIGR01368 241 -EKIPIFGICLGHQLLALAFGAKTYKMKFGHRGGNHPVKDLITGRVEITSQNHGYAVDPDSLPAGD-LEVTHVNLNDGTV 318

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1085944882 328 AGIKIKDKNCFSVQYHPEASPGPNDSLYLFDQFIENIK 365
Cdd:TIGR01368 319 EGIRHKDLPVFSVQYHPEASPGPHDTEYLFDEFIDLMK 356
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 182-361 3.50e-104

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: 304.03  E-value: 3.50e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085944882 182 IAALDIGIKKNILRNLAKRDAYIKVFPYNAKFEDLEAFNPDGYFLSNGPGDPEPLSDAIDLAKDIIANNKPLFGICLGHQ 261
Cdd:cd01744     1 VVVIDFGVKHNILRELLKRGCEVTVVPYNTDAEEILKLDPDGIFLSNGPGDPALLDEAIKTVRKLLGKKIPIFGICLGHQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085944882 262 IIALANGISTYKMHNGHRGINHPVKNLVTGKGEITSQNHGFAINREETeaNANVEITHVHLNDHTVAGIKIKDKNCFSVQ 341
Cdd:cd01744    81 LLALALGAKTYKMKFGHRGSNHPVKDLITGRVYITSQNHGYAVDPDSL--PGGLEVTHVNLNDGTVEGIRHKDLPVFSVQ 158

                         170       180
                  ....*....|....*....|
gi 1085944882 342 YHPEASPGPNDSLYLFDQFI 361
Cdd:cd01744   159 FHPEASPGPHDTEYLFDEFL 178
CPSase_sm_chain pfam00988
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 11-136 2.77e-70

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: 215.65  E-value: 2.77e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085944882  11 ILLADGTIFHGKSIGKEGSAFGEVCFNTGTTGYQEIFTDPSYYGQLMVTTNAHIGNYGTKEEEVESDDVKIAGLICKNFS 90
Cdd:pfam00988   1 LVLEDGTVFEGKSFGAAGSTVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNPEDFESDKIHVAGLVVREYS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1085944882  91 FNYSRPAADASLEDFFEKHNTLAIADVDTRALVSYIRDNGAMNAVI 136
Cdd:pfam00988  81 DEPSNWRAEESLDEWLKEQGIPGISGVDTRALTRKIREKGAMKGVI 126
CPSase_sm_chain smart01097
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 7-136 3.46e-67

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: 208.00  E-value: 3.46e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085944882    7 KKALILLADGTIFHGKSIGKEGSAFGEVCFNTGTTGYQEIFTDPSYYGQLMVTTNAHIGNYGTKEEEVESDDVKIAGLIC 86
Cdd:smart01097   1 MKAYLVLEDGTVFEGESFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNDEDFESDKIQVKGLVV 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1085944882   87 KNFSFNYSRPAADASLEDFFEKHNTLAIADVDTRALVSYIRDNGAMNAVI 136
Cdd:smart01097  81 RELSDEPSNWRSEQSLDEFLKENGIPGISGIDTRALTRKLREKGAMKGVI 130
 
Name Accession Description Interval E-value
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 5-365 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: 639.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085944882   5 QRKKALILLADGTIFHGKSIGKEGSAFGEVCFNTGTTGYQEIFTDPSYYGQLMVTTNAHIGNYGTKEEEVESDDVKIAGL 84
Cdd:COG0505     1 MMMKALLVLEDGTVFEGKSFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVTFTYPHIGNYGVNDEDFESDRPWVAGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085944882  85 ICKNFSFNYSRPAADASLEDFFEKHNTLAIADVDTRALVSYIRDNGAMNAVITTEIDNLEALKKQLAEFPSMKGLELASK 164
Cdd:COG0505    81 VVRELSRRPSNWRSEESLDEYLKEHGIPGISGIDTRALTRHLREKGAMKGVISTGDLDIEELLEKARAAPGMEGLDLVKE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085944882 165 VSTKEPYFVGD-ENATYKIAALDIGIKKNILRNLAKRDAYIKVFPYNAKFEDLEAFNPDGYFLSNGPGDPEPLSDAIDLA 243
Cdd:COG0505   161 VSTKEPYEWTEaPGAGFHVVALDFGVKRNILRELAERGCRVTVVPATTSAEEILALNPDGVFLSNGPGDPAALDYAIETI 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085944882 244 KDIIANNKPLFGICLGHQIIALANGISTYKMHNGHRGINHPVKNLVTGKGEITSQNHGFAINrEETEANANVEITHVHLN 323
Cdd:COG0505   241 RELLGKGIPIFGICLGHQLLALALGAKTYKLKFGHRGANHPVKDLETGRVEITSQNHGFAVD-EDSLPATDLEVTHVNLN 319

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1085944882 324 DHTVAGIKIKDKNCFSVQYHPEASPGPNDSLYLFDQFIENIK 365
Cdd:COG0505   320 DGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDRFIELME 361
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
5-364 0e+00

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 606.69  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085944882   5 QRKKALILLADGTIFHGKSIGKEGSAFGEVCFNTGTTGYQEIFTDPSYYGQLMVTTNAHIGNYGTKEEEVESDDVKIAGL 84
Cdd:PRK12564    1 MMMKAYLVLEDGTVFEGKAFGAEGETVGEVVFNTSMTGYQEILTDPSYAGQIVTFTYPLIGNYGVNREDFESDRPHAKGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085944882  85 ICKNFSFNYSRPAADASLEDFFEKHNTLAIADVDTRALVSYIRDNGAMNAVITTEIDNLEALKKQLAEFPSMKGLELASK 164
Cdd:PRK12564   81 IVRELSDIPSNWRSEMSLDEYLKENGIPGISGIDTRALTRKLREKGAMKGVIATEDFDAEELLEKARAFPGLLGLDLVKE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085944882 165 VSTKEPYFVGDE--NATYKIAALDIGIKKNILRNLAKRDAYIKVFPYNAKFEDLEAFNPDGYFLSNGPGDPEPLSDAIDL 242
Cdd:PRK12564  161 VSTKEPYPWPGPggELKYKVVAIDFGVKRNILRELAERGCRVTVVPATTTAEEILALNPDGVFLSNGPGDPAALDYAIEM 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085944882 243 AKDIIANNKPLFGICLGHQIIALANGISTYKMHNGHRGINHPVKNLVTGKGEITSQNHGFAINREETeaNANVEITHVHL 322
Cdd:PRK12564  241 IRELLEKKIPIFGICLGHQLLALALGAKTYKMKFGHRGANHPVKDLETGKVEITSQNHGFAVDEDSL--PANLEVTHVNL 318

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1085944882 323 NDHTVAGIKIKDKNCFSVQYHPEASPGPNDSLYLFDQFIENI 364
Cdd:PRK12564  319 NDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDEFVELM 360
CPSaseIIsmall TIGR01368
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ...
 9-365 2.89e-174

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: 488.67  E-value: 2.89e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085944882   9 ALILLADGTIFHGKSIGKEGSAFGEVCFNTGTTGYQEIFTDPSYYGQLMVTTNAHIGNYGTKEEEVESDDVKIAGLICKN 88
Cdd:TIGR01368   1 AYLVLEDGTVFRGYSFGAEGTVAGEVVFNTGMTGYQEILTDPSYKGQIVVFTYPLIGNYGVNDEDAESKGIHVSGLVVRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085944882  89 FSFNYSRPAADASLEDFFEKHNTLAIADVDTRALVSYIRDNGAMNAVITTEIDNLEALKKQLAEFPSMKGLELASKVSTK 168
Cdd:TIGR01368  81 LSDRYSNWRATESLDQFLKRHGIPGIYGVDTRALVKKIREKGTMKGVISTEDSNDEELVEKARVSPDITGINLVAEVSTK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085944882 169 EPYFVGDENA-TYKIAALDIGIKKNILRNLAKRDAYIKVFPYNAKFEDLEAFNPDGYFLSNGPGDPEPLSDAIDLAKDII 247
Cdd:TIGR01368 161 EPYTWGQRGGkGKRVVVIDFGVKRNILRRLVKRGCEVTVVPYDTDAEEIKKYNPDGIFLSNGPGDPAAVEPAIETIRKLL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085944882 248 aNNKPLFGICLGHQIIALANGISTYKMHNGHRGINHPVKNLVTGKGEITSQNHGFAINREETEANAnVEITHVHLNDHTV 327
Cdd:TIGR01368 241 -EKIPIFGICLGHQLLALAFGAKTYKMKFGHRGGNHPVKDLITGRVEITSQNHGYAVDPDSLPAGD-LEVTHVNLNDGTV 318

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1085944882 328 AGIKIKDKNCFSVQYHPEASPGPNDSLYLFDQFIENIK 365
Cdd:TIGR01368 319 EGIRHKDLPVFSVQYHPEASPGPHDTEYLFDEFIDLMK 356
PRK12838 PRK12838
carbamoyl phosphate synthase small subunit; Reviewed
 8-365 6.71e-141

carbamoyl phosphate synthase small subunit; Reviewed


Pssm-ID: 183784 [Multi-domain]  Cd Length: 354  Bit Score: 403.89  E-value: 6.71e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085944882   8 KALILLADGTIFHGKSIGKEGSAFGEVCFNTGTTGYQEIFTDPSYYGQLMVTTNAHIGNYGTKEEEVESDDVKIAGLICK 87
Cdd:PRK12838    2 KAYLILEDGTVFEGELIGAPIDVTGEIVFNTGMTGYQEVLTDPSYKGQIVVFTYPLIGNYGINADDYESKQPQVKGVIVY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085944882  88 NFSFNYSRPAADASLEDFFEKHNTLAIADVDTRALVSYIRDNGAMNAVITTeiDNLEALKKQLAEFPSMKGleLASKVST 167
Cdd:PRK12838   82 ELSREGSHYRAKQSLDDFLKEWNIPGISGVDTRALVKHIREKGTMKASITT--TDDAHAFDQIKALVLPKN--VVAQVST 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085944882 168 KEPYFVGdeNATYKIAALDIGIKKNILRNLAKRDAYIKVFPYNAKFEDLEAFNPDGYFLSNGPGDPEPLSDAIDLAKDII 247
Cdd:PRK12838  158 KEPYTYG--NGGKHVALIDFGYKKSILRSLSKRGCKVTVLPYDTSLEEIKNLNPDGIVLSNGPGDPKELQPYLPEIKKLI 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085944882 248 aNNKPLFGICLGHQIIALANGISTYKMHNGHRGINHPVKNLVTGKGEITSQNHGFAINrEETEANANVEITHVHLNDHTV 327
Cdd:PRK12838  236 -SSYPILGICLGHQLIALALGADTEKLPFGHRGANHPVIDLTTGRVWMTSQNHGYVVD-EDSLDGTPLSVRFFNVNDGSI 313

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1085944882 328 AGIKIKDKNCFSVQYHPEASPGPNDSLYLFDQFIENIK 365
Cdd:PRK12838  314 EGLRHKKKPVLSVQFHPEAHPGPHDAEYIFDEFLEMME 351
carA CHL00197
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
 6-365 8.08e-125

carbamoyl-phosphate synthase arginine-specific small subunit; Provisional


Pssm-ID: 214392 [Multi-domain]  Cd Length: 382  Bit Score: 364.12  E-value: 8.08e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085944882   6 RKKALILLADGTIFHGKSIGKEGSAFGEVCFNTGTTGYQEIFTDPSYYGQLMVTTNAHIGNYGTKEEEVESDDVKIAGLI 85
Cdd:CHL00197    4 MIPAILVLEDGTYYRGWSFSNPITTIGEVVFNTGMTGYQEIITDPSYFEQIVTFTYPEIGNTGINLEDIESVKIQVKGII 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085944882  86 CKNFSFNYSRPAADASLEDFFEKHNTLAIADVDTRALVSYIRDNGAMNAVITTEIDNLEALKKQLAEFPSMKGLELASKV 165
Cdd:CHL00197   84 AKNICKSSSNWRQQESLVSYLQRHKIPFIFGIDTRALTQHLRRFGTMNGCISNQNLNLSYLRAKIKESPHMPSSDLIPRV 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085944882 166 STKEPY-------------FVGDENATY--KIAALDIGIKKNILRNLAKRDAYIKVFPYNAKFEDLEAFNPDGYFLSNGP 230
Cdd:CHL00197  164 TTSSYYewdekshpsfylaDNKRPHSSYqlKIIVIDFGVKYNILRRLKSFGCSITVVPATSPYQDILSYQPDGILLSNGP 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085944882 231 GDPEPLSDAIDLAKDIIANNKPLFGICLGHQIIALANGISTYKMHNGHRGINHPVKnlVTGKGEITSQNHGFAINREETE 310
Cdd:CHL00197  244 GDPSAIHYGIKTVKKLLKYNIPIFGICMGHQILSLALEAKTFKLKFGHRGLNHPSG--LNQQVEITSQNHGFAVNLESLA 321

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1085944882 311 ANAnVEITHVHLNDHTVAGIKIKDKNCFSVQYHPEASPGPNDSLYLFDQFIENIK 365
Cdd:CHL00197  322 KNK-FYITHFNLNDGTVAGISHSPKPYFSVQYHPEASPGPHDADYLFEYFIEIIK 375
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 182-361 3.50e-104

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: 304.03  E-value: 3.50e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085944882 182 IAALDIGIKKNILRNLAKRDAYIKVFPYNAKFEDLEAFNPDGYFLSNGPGDPEPLSDAIDLAKDIIANNKPLFGICLGHQ 261
Cdd:cd01744     1 VVVIDFGVKHNILRELLKRGCEVTVVPYNTDAEEILKLDPDGIFLSNGPGDPALLDEAIKTVRKLLGKKIPIFGICLGHQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085944882 262 IIALANGISTYKMHNGHRGINHPVKNLVTGKGEITSQNHGFAINREETeaNANVEITHVHLNDHTVAGIKIKDKNCFSVQ 341
Cdd:cd01744    81 LLALALGAKTYKMKFGHRGSNHPVKDLITGRVYITSQNHGYAVDPDSL--PGGLEVTHVNLNDGTVEGIRHKDLPVFSVQ 158

                         170       180
                  ....*....|....*....|
gi 1085944882 342 YHPEASPGPNDSLYLFDQFI 361
Cdd:cd01744   159 FHPEASPGPHDTEYLFDEFL 178
PLN02771 PLN02771
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
 9-353 6.72e-99

carbamoyl-phosphate synthase (glutamine-hydrolyzing)


Pssm-ID: 178370 [Multi-domain]  Cd Length: 415  Bit Score: 299.20  E-value: 6.72e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085944882   9 ALILLADGTIFHGKSIGKEGSAFGEVCFNTGTTGYQEIFTDPSYYGQLMVTTNAHIGNYGTKEEEVESDDVKIAGLICKN 88
Cdd:PLN02771   57 ARLVLEDGSVWKAKSFGARGTQVGEVVFNTSLTGYQEILTDPSYAGQFVLMTNPHIGNTGVNFDDEESRQCFLAGLVIRS 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085944882  89 FSFNYSRPAADASLEDFFEKHNTLAIADVDTRALVSYIRDNGAMNAVITTEIDNLEALKKQLAEFPSMKGLELASKVSTK 168
Cdd:PLN02771  137 LSISTSNWRCTKTLGDYLAERNIMGIYDVDTRAITRRLREDGSLIGVLSTEDSKTDEELLKMSRSWDIVGIDLISGVSCK 216

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085944882 169 EPY-FV------------GDENATYKIAALDIGIKKNILRNLAKRDAYIKVFPYNAKFEDLEAFNPDGYFLSNGPGDPEP 235
Cdd:PLN02771  217 SPYeWVdktnpewdfntnSRDGESYHVIAYDFGIKHNILRRLASYGCKITVVPSTWPASEALKMKPDGVLFSNGPGDPSA 296

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085944882 236 LSDAIDLAKDIIAnNKPLFGICLGHQIIALANGISTYKMHNGHRGINHPVKNLVTGKGEITSQNHGFAInrEETEANANV 315
Cdd:PLN02771  297 VPYAVETVKELLG-KVPVFGICMGHQLLGQALGGKTFKMKFGHHGGNHPVRNNRTGRVEISAQNHNYAV--DPASLPEGV 373

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1085944882 316 EITHVHLNDHTVAGIKIKDKNCFSVQYHPEASPGPNDS 353
Cdd:PLN02771  374 EVTHVNLNDGSCAGLAFPALNVMSLQYHPEASPGPHDS 411
CPSase_sm_chain pfam00988
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 11-136 2.77e-70

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: 215.65  E-value: 2.77e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085944882  11 ILLADGTIFHGKSIGKEGSAFGEVCFNTGTTGYQEIFTDPSYYGQLMVTTNAHIGNYGTKEEEVESDDVKIAGLICKNFS 90
Cdd:pfam00988   1 LVLEDGTVFEGKSFGAAGSTVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNPEDFESDKIHVAGLVVREYS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1085944882  91 FNYSRPAADASLEDFFEKHNTLAIADVDTRALVSYIRDNGAMNAVI 136
Cdd:pfam00988  81 DEPSNWRAEESLDEWLKEQGIPGISGVDTRALTRKIREKGAMKGVI 126
CPSase_sm_chain smart01097
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 7-136 3.46e-67

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: 208.00  E-value: 3.46e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085944882    7 KKALILLADGTIFHGKSIGKEGSAFGEVCFNTGTTGYQEIFTDPSYYGQLMVTTNAHIGNYGTKEEEVESDDVKIAGLIC 86
Cdd:smart01097   1 MKAYLVLEDGTVFEGESFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNDEDFESDKIQVKGLVV 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1085944882   87 KNFSFNYSRPAADASLEDFFEKHNTLAIADVDTRALVSYIRDNGAMNAVI 136
Cdd:smart01097  81 RELSDEPSNWRSEQSLDEFLKENGIPGISGIDTRALTRKLREKGAMKGVI 130
GATase pfam00117
Glutamine amidotransferase class-I;
187-362 9.90e-57

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 183.21  E-value: 9.90e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085944882 187 IGIKKNILRNLAKRDAYIKVFPYNAKFEDLEAFNPDGYFLSNGPGDPEPLSDAIDLAKDIIANNKPLFGICLGHQIIALA 266
Cdd:pfam00117   7 DSFTYNLARALRELGVEVTVVPNDTPAEEILEENPDGIILSGGPGSPGAAGGAIEAIREARELKIPILGICLGHQLLALA 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085944882 267 NGISTYKMHN-GHRGINHPVKNLV------TGKGEITSQNHGFAINrEETEaNANVEITHVHLNDHTVAGIKIKDKNCFS 339
Cdd:pfam00117  87 FGGKVVKAKKfGHHGKNSPVGDDGcglfygLPNVFIVRRYHSYAVD-PDTL-PDGLEVTATSENDGTIMGIRHKKLPIFG 164

                         170       180
                  ....*....|....*....|...
gi 1085944882 340 VQYHPEASPGPNDSLYLFDQFIE 362
Cdd:pfam00117 165 VQFHPESILTPHGPEILFNFFIK 187
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 192-345 2.72e-19

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: 84.51  E-value: 2.72e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085944882 192 NILRNLAKRDAYIKVFPYNAKFED-LEAFNPDGYFLSNGPGDPEPLSDAIDLAKdIIANNKPLFGICLGHQIIALANGIS 270
Cdd:cd01743    13 NLVQYLRELGAEVVVVRNDEITLEeLELLNPDAIVISPGPGHPEDAGISLEIIR-ALAGKVPILGVCLGHQAIAEAFGGK 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085944882 271 TYKMHNGHRGINHPVKnlVTGKGEIT--SQN------HGFAINREETEANAnveITHVHLNDHTVAGIKIKDKNCFSVQY 342
Cdd:cd01743    92 VVRAPEPMHGKTSEIH--HDGSGLFKglPQPftvgryHSLVVDPDPLPDLL---EVTASTEDGVIMALRHRDLPIYGVQF 166


                  ...
gi 1085944882 343 HPE 345
Cdd:cd01743   167 HPE 169
GATase1_GMP_Synthase cd01742
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ...
 193-345 1.81e-14

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: 70.64  E-value: 1.81e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085944882 193 ILRNLAKRDAYIKVFPYNAKFEDLEAFNPDGYFLSNGPG---DPeplsDAIDLAKDIIANNKPLFGICLGHQIIALANGI 269
Cdd:cd01742    14 IARRVRELGVYSEILPNTTPLEEIKLKNPKGIILSGGPSsvyEE----DAPRVDPEIFELGVPVLGICYGMQLIAKALGG 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085944882 270 STYKMHN---GHRGINHPVKNLVTGKGEITSQ---NHGFAInreeTEANANVEITHVHLNDHtVAGIKIKDKNCFSVQYH 343
Cdd:cd01742    90 KVERGDKreyGKAEIEIDDSSPLFEGLPDEQTvwmSHGDEV----VKLPEGFKVIASSDNCP-VAAIANEEKKIYGVQFH 164


                  ..
gi 1085944882 344 PE 345
Cdd:cd01742   165 PE 166
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 214-362 2.92e-14

anthranilate synthase component II; Provisional


Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 70.54  E-value: 2.92e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085944882 214 EDLEAFNPDGYFLSNGPGDPEplsDA---IDLAKDIiANNKPLFGICLGHQIIALANGistykmhnGHrgINHpVKNLVT 290
Cdd:PRK05670   37 EEIEALNPDAIVLSPGPGTPA---EAgisLELIREF-AGKVPILGVCLGHQAIGEAFG--------GK--VVR-AKEIMH 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085944882 291 GK-GEITSQNHG--------FAINR------EETEANANVEIThVHLNDHTVAGIKIKDKNCFSVQYHPEaSPGPNDSLY 355
Cdd:PRK05670  102 GKtSPIEHDGSGifaglpnpFTVTRyhslvvDRESLPDCLEVT-AWTDDGEIMGVRHKELPIYGVQFHPE-SILTEHGHK 179


                  ....*..
gi 1085944882 356 LFDQFIE 362
Cdd:PRK05670  180 LLENFLE 186
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 201-345 4.65e-14

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: 69.68  E-value: 4.65e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085944882 201 DAYIKVFPYNA-KFEDLEAFNPDGYFLSNGPGDPEplsDAiDLAKDII---ANNKPLFGICLGHQIIALANGISTYK--- 273
Cdd:COG0512    22 GAEVVVVRNDEiTLEEIEALAPDGIVLSPGPGTPE---EA-GISLEVIrafAGKIPILGVCLGHQAIGEAFGGKVVRape 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085944882 274 -MHnghrGINHPVKnlVTGKG---EITSQnhgFAINR------EETEANANVEIThVHLNDHTVAGIKIKDKNCFSVQYH 343
Cdd:COG0512    98 pMH----GKTSPIT--HDGSGlfaGLPNP---FTATRyhslvvDRETLPDELEVT-AWTEDGEIMGIRHRELPIEGVQFH 167


                  ..
gi 1085944882 344 PE 345
Cdd:COG0512   168 PE 169
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 193-348 2.54e-13

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


Pssm-ID: 440284 [Multi-domain]  Cd Length: 225  Bit Score: 68.43  E-value: 2.54e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085944882 193 ILRNLAKRDAYIKVF-PYNAKF--EDLEAFNPDGYFLSNGPG----DPEPLSDAIDLAKDIIANNKPLFGICLGHQIIAL 265
Cdd:COG0518    18 IARRLREAGIELDVLrVYAGEIlpYDPDLEDPDGLILSGGPMsvydEDPWLEDEPALIREAFELGKPVLGICYGAQLLAH 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085944882 266 ANGISTYKmhNGHRGI-NHPVKnlVTGKGEITS---------QNHGFAInrEETEANAnveithVHL--NDHT-VAGIKI 332
Cdd:COG0518    98 ALGGKVEP--GPGREIgWAPVE--LTEADPLFAglpdeftvwMSHGDTV--TELPEGA------EVLasSDNCpNQAFRY 165

                         170
                  ....*....|....*.
gi 1085944882 333 kDKNCFSVQYHPEASP 348
Cdd:COG0518   166 -GRRVYGVQFHPEVTH 180
guaA_Nterm TIGR00888
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ...
 182-364 5.09e-12

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: 63.87  E-value: 5.09e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085944882 182 IAALDIGIKKN--ILRNLAKRDAYIKVFPYNAKFEDLEAFNPDGYFLSNGPgDPEPLSDAIDLAKDIIANNKPLFGICLG 259
Cdd:TIGR00888   1 ILVLDFGSQYTqlIARRLRELGVYSELVPNTTPLEEIREKNPKGIILSGGP-SSVYAENAPRADEKIFELGVPVLGICYG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085944882 260 HQIIALANGISTYKMHNGHRGinhPVKNLVTGKGEITS---------QNHGFAINR--EETEANANVEIThvhlndhTVA 328
Cdd:TIGR00888  80 MQLMAKQLGGEVGRAEKREYG---KAELEILDEDDLFRglpdestvwMSHGDKVKElpEGFKVLATSDNC-------PVA 149

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1085944882 329 GIKIKDKNCFSVQYHPEA--SPGPNDslyLFDQFIENI 364
Cdd:TIGR00888 150 AMAHEEKPIYGVQFHPEVthTEYGNE---LLENFVYDV 184
PRK14607 PRK14607
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
214-361 1.14e-10

bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;


Pssm-ID: 237764 [Multi-domain]  Cd Length: 534  Bit Score: 62.81  E-value: 1.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085944882 214 EDLEAFNPDGYFLSNGPGDPEPLSDAIDLAKDIiANNKPLFGICLGHQIIALANG--ISTYK--MHNGHRGINHPVKNL- 288
Cdd:PRK14607   38 EEIEALNPSHIVISPGPGRPEEAGISVEVIRHF-SGKVPILGVCLGHQAIGYAFGgkIVHAKriLHGKTSPIDHNGKGLf 116

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1085944882 289 --VTGKGEITsQNHGFAInrEETEANANVEIThVHLNDHTVAGIKIKDKNCFSVQYHPEaSPGPNDSLYLFDQFI 361
Cdd:PRK14607  117 rgIPNPTVAT-RYHSLVV--EEASLPECLEVT-AKSDDGEIMGIRHKEHPIFGVQFHPE-SILTEEGKRILKNFL 186
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 192-266 2.10e-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: 57.61  E-value: 2.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085944882 192 NILRNLAKRDAYIKVFPYNAKFE--DLEAFNPDGYFLSNGPGDPEPL---SDAIDLAKDIIANNKPLFGICLGHQIIALA 266
Cdd:cd01653    16 SPLDALREAGAEVDVVSPDGGPVesDVDLDDYDGLILPGGPGTPDDLardEALLALLREAAAAGKPILGICLGAQLLVLG 95
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 192-277 3.93e-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: 3.93e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085944882 192 NILRNLAKRDAYIKVFPYNAKFEDLEAFNPDGYFLSNGP----GDPEP-LSDAIDLAKDIIANNKPLFGICLGHQIIALA 266
Cdd:cd01741    18 DLLREAGAETIEIDVVDVYAGELLPDLDDYDGLVILGGPmsvdEDDYPwLKKLKELIRQALAAGKPVLGICLGHQLLARA 97

                          90
                  ....*....|.
gi 1085944882 267 NGISTYKMHNG 277
Cdd:cd01741    98 LGGKVGRNPKG 108
trpG_papA TIGR00566
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ...
 213-346 1.57e-09

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: 56.72  E-value: 1.57e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085944882 213 FEDLEAFNPDGYFLSNGPGDPEplSDAIDLAKDIIANNK-PLFGICLGHQIIALANGI-----------STYKMHNGHRG 280
Cdd:TIGR00566  36 LQEIEALLPLLIVISPGPCTPN--EAGISLEAIRHFAGKlPILGVCLGHQAMGQAFGGdvvrantvmhgKTSEIEHNGAG 113

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1085944882 281 INHPVKNLVTgkgeiTSQNHGFAINREETEANANVEITHVhlNDHTVAGIKIKDKNCFSVQYHPEA 346
Cdd:TIGR00566 114 IFRGLFNPLT-----ATRYHSLVVEPETLPTCFPVTAWEE--ENIEIMAIRHRDLPLEGVQFHPES 172
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 192-263 1.70e-09

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


Pssm-ID: 153222 [Multi-domain]  Cd Length: 92  Bit Score: 54.13  E-value: 1.70e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1085944882 192 NILRNLAKRDAYIKVFPYNAKFE--DLEAFNPDGYFLSNGPGDPEPL---SDAIDLAKDIIANNKPLFGICLGHQII 263
Cdd:cd03128    16 SPLDALREAGAEVDVVSPDGGPVesDVDLDDYDGLILPGGPGTPDDLawdEALLALLREAAAAGKPVLGICLGAQLL 92
trpG CHL00101
anthranilate synthase component 2
 216-346 6.36e-09

anthranilate synthase component 2


Pssm-ID: 214365 [Multi-domain]  Cd Length: 190  Bit Score: 55.12  E-value: 6.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085944882 216 LEAFNPDGYFLSNGPGDPEPLSDAIDLAKDIiANNKPLFGICLGHQIIALANGISTYK----MHNGHRGINHPVKNLVTG 291
Cdd:CHL00101   39 IKNLNIRHIIISPGPGHPRDSGISLDVISSY-APYIPILGVCLGHQSIGYLFGGKIIKapkpMHGKTSKIYHNHDDLFQG 117

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1085944882 292 KGE--ITSQNHGFAINREetEANANVEIThVHLNDHTVAGIKIKD-KNCFSVQYHPEA 346
Cdd:CHL00101  118 LPNpfTATRYHSLIIDPL--NLPSPLEIT-AWTEDGLIMACRHKKyKMLRGIQFHPES 172
guaA PRK00074
GMP synthase; Reviewed
 203-345 6.43e-09

GMP synthase; Reviewed


Pssm-ID: 234614 [Multi-domain]  Cd Length: 511  Bit Score: 57.36  E-value: 6.43e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085944882 203 YIKVFPYNAKFEDLEAFNPDGYFLSNGPG---DPeplsDAIDLAKDIIANNKPLFGICLGHQIIALANGISTYKMHNGHr 279
Cdd:PRK00074   29 YSEIVPYDISAEEIRAFNPKGIILSGGPAsvyEE----GAPRADPEIFELGVPVLGICYGMQLMAHQLGGKVERAGKRE- 103

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1085944882 280 ginhpvknlvTGKGEITSQNHG--FA-INREE----------TEANANVEIThVHLNDHTVAGIKIKDKNCFSVQYHPE 345
Cdd:PRK00074  104 ----------YGRAELEVDNDSplFKgLPEEQdvwmshgdkvTELPEGFKVI-ASTENCPIAAIANEERKFYGVQFHPE 171
PRK07765 PRK07765
aminodeoxychorismate/anthranilate synthase component II;
222-268 1.38e-08

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181107 [Multi-domain]  Cd Length: 214  Bit Score: 54.67  E-value: 1.38e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1085944882 222 DGYFLSNGPGDPEPLSDAIDLAKDIIANNKPLFGICLGHQIIALANG 268
Cdd:PRK07765   48 DGVLLSPGPGTPERAGASIDMVRACAAAGTPLLGVCLGHQAIGVAFG 94
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 206-361 2.32e-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: 53.35  E-value: 2.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085944882 206 VFPYNAKFEDLEA--FNPDGYFLSNGP--------GDPEPLSDAIDLAKD---------IIANNKPLFGICLGHQIIALA 266
Cdd:cd01745    37 LLPPVDDEEDLEQylELLDGLLLTGGGdvdpplygEEPHPELGPIDPERDafelallraALERGKPILGICRGMQLLNVA 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085944882 267 NGISTYKmhngHRGINhpvknlvtgkgeitSqNHGFAINR----EETEANAnveithvhlNDHTVAGIKIKDKN-CFSVQ 341
Cdd:cd01745   117 LGGTLYQ----DIRVN--------------S-LHHQAIKRladgLRVEARA---------PDGVIEAIESPDRPfVLGVQ 168

                         170       180
                  ....*....|....*....|.
gi 1085944882 342 YHPEASPGPN-DSLYLFDQFI 361
Cdd:cd01745   169 WHPEWLADTDpDSLKLFEAFV 189
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 222-345 1.18e-07

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: 51.87  E-value: 1.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085944882 222 DGYFLSNGP--------GDPEPLSDAIDLAKDI---------IANNKPLFGICLGHQIIALANGISTY------KMHNGH 278
Cdd:pfam07722  60 DGLLLTGGPnvdphfygEEPSESGGPYDPARDAyelaliraaLARGKPILGICRGFQLLNVALGGTLYqdiqeqPGFTDH 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085944882 279 R--------GINHPVkNLVTGK--GEITSQN-------HGFAINR--EETEANAnveithvHLNDHTVAGIKIKDKNCF- 338
Cdd:pfam07722 140 RehcqvapyAPSHAV-NVEPGSllASLLGSEefrvnslHHQAIDRlaPGLRVEA-------VAPDGTIEAIESPNAKGFa 211


                  ....*...
gi 1085944882 339 -SVQYHPE 345
Cdd:pfam07722 212 lGVQWHPE 219
PLN02335 PLN02335
anthranilate synthase
 214-346 3.78e-07

anthranilate synthase


Pssm-ID: 177969 [Multi-domain]  Cd Length: 222  Bit Score: 50.57  E-value: 3.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085944882 214 EDLEAFNPDGYFLSNGPGDPE----PLSDAIDLAKDIiannkPLFGICLGHQIIALANGISTYKMHNG--HrGINHPVKN 287
Cdd:PLN02335   56 EELKRKNPRGVLISPGPGTPQdsgiSLQTVLELGPLV-----PLFGVCMGLQCIGEAFGGKIVRSPFGvmH-GKSSPVHY 129

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1085944882 288 LVTGKGEITS---------QNHGFAINREETEANAnVEIThVHLNDHTVAGIKIKD-KNCFSVQYHPEA 346
Cdd:PLN02335  130 DEKGEEGLFSglpnpftagRYHSLVIEKDTFPSDE-LEVT-AWTEDGLIMAARHRKyKHIQGVQFHPES 196
PRK00758 PRK00758
GMP synthase subunit A; Validated
 193-268 1.62e-06

GMP synthase subunit A; Validated


Pssm-ID: 179112 [Multi-domain]  Cd Length: 184  Bit Score: 47.92  E-value: 1.62e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1085944882 193 ILRNLAKRDAYIKVFPYNAKFEDLEAfNPDGYFLSNGPgDPEPLSDAIDLAKDIianNKPLFGICLGHQIIALANG 268
Cdd:PRK00758   15 IHRTLRYLGVDAKIIPNTTPVEEIKA-FEDGLILSGGP-DIERAGNCPEYLKEL---DVPILGICLGHQLIAKAFG 85
PRK08007 PRK08007
aminodeoxychorismate synthase component 2;
213-346 2.41e-06

aminodeoxychorismate synthase component 2;


Pssm-ID: 181194 [Multi-domain]  Cd Length: 187  Bit Score: 47.60  E-value: 2.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085944882 213 FEDLEAFNPDGYFLSNGPGDPEPLSDAIDLAKDIiANNKPLFGICLGHQIIALANGISTYKMHNGHRGINHPVKNlvTGK 292
Cdd:PRK08007   36 LADIDALKPQKIVISPGPCTPDEAGISLDVIRHY-AGRLPILGVCLGHQAMAQAFGGKVVRAAKVMHGKTSPITH--NGE 112

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085944882 293 GEITSQNHGFAINR------EETEANANVEIThVHLNDHTVAGIKIKDKNCFSVQYHPEA 346
Cdd:PRK08007  113 GVFRGLANPLTVTRyhslvvEPDSLPACFEVT-AWSETREIMGIRHRQWDLEGVQFHPES 171
PRK07649 PRK07649
aminodeoxychorismate/anthranilate synthase component II;
214-367 4.54e-06

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181066 [Multi-domain]  Cd Length: 195  Bit Score: 46.72  E-value: 4.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085944882 214 EDLEAFNPDGYFLSNGPGDPEPLSDAIDlAKDIIANNKPLFGICLGHQIIALANGISTYK----MHNGHRGINHPVKNLV 289
Cdd:PRK07649   37 SDIENMKPDFLMISPGPCSPNEAGISME-VIRYFAGKIPIFGVCLGHQSIAQVFGGEVVRaerlMHGKTSLMHHDGKTIF 115

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1085944882 290 TG-KGEITSQNHGFAINREETEANAnVEITHVHLNDHTVAgIKIKDKNCFSVQYHPEaSPGPNDSLYLFDQFIENIKNK 367
Cdd:PRK07649  116 SDiPNPFTATRYHSLIVKKETLPDC-LEVTSWTEEGEIMA-IRHKTLPIEGVQFHPE-SIMTSHGKELLQNFIRKYSPS 191
PRK07053 PRK07053
glutamine amidotransferase; Provisional
 236-275 2.03e-05

glutamine amidotransferase; Provisional


Pssm-ID: 235919 [Multi-domain]  Cd Length: 234  Bit Score: 45.32  E-value: 2.03e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1085944882 236 LSDAIDLAKDIIANNKPLFGICLGHQIIALANGISTYKMH 275
Cdd:PRK07053   69 LAPEIALLRQRLAAGLPTLGICLGAQLIARALGARVYPGG 108
PRK06774 PRK06774
aminodeoxychorismate synthase component II;
212-346 9.40e-05

aminodeoxychorismate synthase component II;


Pssm-ID: 180689 [Multi-domain]  Cd Length: 191  Bit Score: 42.93  E-value: 9.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085944882 212 KFEDLEAFNPDGYFLSNGPGDPEPLSDAIDLAKDIiANNKPLFGICLGHQIIALANGISTYK----MHNGHRGINHpvkn 287
Cdd:PRK06774   35 QLTDIEQLAPSHLVISPGPCTPNEAGISLAVIRHF-ADKLPILGVCLGHQALGQAFGARVVRarqvMHGKTSAICH---- 109

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1085944882 288 lvTGKGEITSQNHGFAINR------EETEANANVEITHVHLNDHTV---AGIKIKDKNCFSVQYHPEA 346
Cdd:PRK06774  110 --SGQGVFRGLNQPLTVTRyhslviAADSLPGCFELTAWSERGGEMdeiMGIRHRTLPLEGVQFHPES 175
PRK13566 PRK13566
anthranilate synthase component I;
216-268 1.65e-04

anthranilate synthase component I;


Pssm-ID: 237429 [Multi-domain]  Cd Length: 720  Bit Score: 43.75  E-value: 1.65e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1085944882 216 LEAFNPDGYFLSNGPGDPEP--LSDAIDLAkdiIANNKPLFGICLGHQIIALANG 268
Cdd:PRK13566  565 LDRVNPDLVVLSPGPGRPSDfdCKATIDAA---LARNLPIFGVCLGLQAIVEAFG 616
PRK09522 PRK09522
bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate ...
 203-346 6.21e-04

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


Pssm-ID: 181927 [Multi-domain]  Cd Length: 531  Bit Score: 41.55  E-value: 6.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085944882 203 YIKVFPYNAKFEDLEAFNPDGYFLSNGPGDPEPLSDAIDLAKDIiANNKPLFGICLGHQIIalangISTYKMHNGHRG-I 281
Cdd:PRK09522   31 YRNHIPAQTLIERLATMSNPVLMLSPGPGVPSEAGCMPELLTRL-RGKLPIIGICLGHQAI-----VEAYGGYVGQAGeI 104

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085944882 282 NHPVKNLVTGKGE--ITSQNHGFAINREETEANANV--EIT-HVHLNDHTVAGIKIKDKNCfSVQYHPEA 346
Cdd:PRK09522  105 LHGKASSIEHDGQamFAGLTNPLPVARYHSLVGSNIpaGLTiNAHFNGMVMAVRHDADRVC-GFQFHPES 173
PRK08857 PRK08857
aminodeoxychorismate/anthranilate synthase component II;
216-346 7.56e-04

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181566 [Multi-domain]  Cd Length: 193  Bit Score: 40.25  E-value: 7.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085944882 216 LEAFNPDGYFLSNGPGDPEPLSDAIDlAKDIIANNKPLFGICLGHQIIALANGISTYKMHNGHRGINHPVKNlvTGKGEI 295
Cdd:PRK08857   39 IEALNPTHLVISPGPCTPNEAGISLQ-AIEHFAGKLPILGVCLGHQAIAQVFGGQVVRARQVMHGKTSPIRH--TGRSVF 115

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1085944882 296 TSQNHGFAINREET------------EANANVEITHVHLNDhtVAGIKIKDKNCFSVQYHPEA 346
Cdd:PRK08857  116 KGLNNPLTVTRYHSlvvkndtlpecfELTAWTELEDGSMDE--IMGFQHKTLPIEAVQFHPES 176
GATase1_PfpI_1 cd03169
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 207-274 1.05e-03

Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins similar to PfpI from Pyrococcus furiosus; Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins similar to PfpI from Pyrococcus furiosus. PfpI is an ATP-independent intracellular proteases which may hydrolyze small peptides to provide a nutritional source. Only Cys of the catalytic triad typical of GATase1 domains is conserved in this group. This Cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow.


Pssm-ID: 153243 [Multi-domain]  Cd Length: 180  Bit Score: 39.55  E-value: 1.05e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1085944882 207 FPYNAKFEDLEAFNPDGYFLSNGPGdPEPLS---DAIDLAKDIIANNKPLFGICLGHQIIALANGISTYKM 274
Cdd:cd03169    63 FAVTADFDEVDPDDYDALVIPGGRA-PEYLRldeKVLAIVRHFAEANKPVAAICHGPQILAAAGVLKGRRC 132
hisH PRK13170
imidazole glycerol phosphate synthase subunit HisH; Provisional
 240-347 3.24e-03

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 183877 [Multi-domain]  Cd Length: 196  Bit Score: 38.30  E-value: 3.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085944882 240 IDLakdIIANNKPLFGICLGHQIIALA----NGISTYKMhnghrgINHPVKNLVT--------GKGEITSQ--NHGFAin 305
Cdd:PRK13170   63 IDL---IKACTQPVLGICLGMQLLGERseesGGVDCLGI------IDGPVKKMTDfglplphmGWNQVTPQagHPLFQ-- 131

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1085944882 306 reETEANANVEITH---VHLNDHTVA----GIK----IKDKNCFSVQYHPEAS 347
Cdd:PRK13170  132 --GIEDGSYFYFVHsyaMPVNEYTIAqcnyGEPfsaaIQKDNFFGVQFHPERS 182
PfpI TIGR01382
intracellular protease, PfpI family; The member of this family from Pyrococcus horikoshii has ...
 210-284 5.45e-03

intracellular protease, PfpI family; The member of this family from Pyrococcus horikoshii has been solved to 2 Angstrom resolution. It is an ATP-independent intracellular protease that crystallizes as a hexameric ring. Cys-101 is proposed as the active site residue in a catalytic triad with the adjacent His-102 and a Glu residue from an adjacent monomer. A member of this family from Bacillus subtilis, GSP18, has been shown to be expressed in response to several forms of stress. A role in the degradation of small peptides has been suggested. A closely related family consists of the thiamine biosynthesis protein ThiJ and its homologs. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 273591 [Multi-domain]  Cd Length: 166  Bit Score: 37.40  E-value: 5.45e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1085944882 210 NAKFEDLEAFNPDGYFLSNGPGdPEPL---SDAIDLAKDIIANNKPLFGICLGHQIIALANGIStykmhnGHRGINHP 284
Cdd:TIGR01382  50 DATIDEVNPEEYDALVIPGGRA-PEYLrlnNKAVRLVREFVEKGKPVAAICHGPQLLISAGVLR------GKKLTSYP 120
hisH PRK13141
imidazole glycerol phosphate synthase subunit HisH; Provisional
 236-263 5.66e-03

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237288 [Multi-domain]  Cd Length: 205  Bit Score: 37.80  E-value: 5.66e-03
                          10        20
                  ....*....|....*....|....*...
gi 1085944882 236 LSDAIdlaKDIIANNKPLFGICLGHQII 263
Cdd:PRK13141   61 LDEVI---KEAVASGKPLLGICLGMQLL 85
hisH PRK13143
imidazole glycerol phosphate synthase subunit HisH; Provisional
 234-262 6.43e-03

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237289 [Multi-domain]  Cd Length: 200  Bit Score: 37.54  E-value: 6.43e-03
                          10        20
                  ....*....|....*....|....*....
gi 1085944882 234 EPLSDAIDlakDIIANNKPLFGICLGHQI 262
Cdd:PRK13143   58 SPLRDVIL---EAARSGKPFLGICLGMQL 83
GATase1_IGP_Synthase cd01748
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ...
 240-262 7.19e-03

Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate synthase (IGPS); Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate synthase (IGPS). IGPS incorporates ammonia derived from glutamine into N1-[(5'-phosphoribulosyl)-formimino]-5-aminoimidazole-4-carboxamide ribonucleotide (PRFAR) to form 5'-(5-aminoimidazole-4-carboxamide) ribonucleotide (AICAR) and imidazole glycerol phosphate (IGP). The glutamine amidotransferase domain generates the ammonia nucleophile which is channeled from the glutaminase active site to the PRFAR active site. IGPS belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.


Pssm-ID: 153219 [Multi-domain]  Cd Length: 198  Bit Score: 37.09  E-value: 7.19e-03
                          10        20
                  ....*....|....*....|...
gi 1085944882 240 IDLAKDIIANNKPLFGICLGHQI 262
Cdd:cd01748    61 IEALKEAIASGKPFLGICLGMQL 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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