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Conserved domains on  [gi|1384927372|gb|AWG25340|]
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carbamoyl phosphate synthase small subunit [Flavobacterium kingsejongi]

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 ...
 6-365 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: 632.06  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372   6 RKQAILLLNDGTIFYGKSIGIEGTVFGEVCFNTGMTGYQEIFTDPSYFGQIMVATNAHIGNYGVNDEDVESDKIMISGLV 85
Cdd:COG0505     2 MMKALLVLEDGTVFEGKSFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVTFTYPHIGNYGVNDEDFESDRPWVAGLV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372  86 CKNFSFTHSRVNSTESLQDYFAKQNLVVISDVDTRALVSYIRDNGAMNAVISTDTENIEGLKEQLSKVPDMKGLELASKV 165
Cdd:COG0505    82 VRELSRRPSNWRSEESLDEYLKEHGIPGISGIDTRALTRHLREKGAMKGVISTGDLDIEELLEKARAAPGMEGLDLVKEV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372 166 SAKEAYYVGE-PTAKYKIAALDLGIKKNILRNLVKRDCYVKVFPFDTTFEIMSEFNPDGYFLSNGPGDPDPLYGAIEVAQ 244
Cdd:COG0505   162 STKEPYEWTEaPGAGFHVVALDFGVKRNILRELAERGCRVTVVPATTSAEEILALNPDGVFLSNGPGDPAALDYAIETIR 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372 245 KILSADKPLFGICLGHQVIALANGISTYKMFNGHRGINHPVKNVITGKGEITSQNHGFAVNKEEAENHpDFEITHFHIND 324
Cdd:COG0505   242 ELLGKGIPIFGICLGHQLLALALGAKTYKLKFGHRGANHPVKDLETGRVEITSQNHGFAVDEDSLPAT-DLEVTHVNLND 320

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1384927372 325 GTVAGMRMKSKNCFSVQYHPEASPGPQDATYLFDQFIENIN 365
Cdd:COG0505   321 GTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDRFIELME 361
 
Name Accession Description Interval E-value
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 6-365 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: 632.06  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372   6 RKQAILLLNDGTIFYGKSIGIEGTVFGEVCFNTGMTGYQEIFTDPSYFGQIMVATNAHIGNYGVNDEDVESDKIMISGLV 85
Cdd:COG0505     2 MMKALLVLEDGTVFEGKSFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVTFTYPHIGNYGVNDEDFESDRPWVAGLV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372  86 CKNFSFTHSRVNSTESLQDYFAKQNLVVISDVDTRALVSYIRDNGAMNAVISTDTENIEGLKEQLSKVPDMKGLELASKV 165
Cdd:COG0505    82 VRELSRRPSNWRSEESLDEYLKEHGIPGISGIDTRALTRHLREKGAMKGVISTGDLDIEELLEKARAAPGMEGLDLVKEV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372 166 SAKEAYYVGE-PTAKYKIAALDLGIKKNILRNLVKRDCYVKVFPFDTTFEIMSEFNPDGYFLSNGPGDPDPLYGAIEVAQ 244
Cdd:COG0505   162 STKEPYEWTEaPGAGFHVVALDFGVKRNILRELAERGCRVTVVPATTSAEEILALNPDGVFLSNGPGDPAALDYAIETIR 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372 245 KILSADKPLFGICLGHQVIALANGISTYKMFNGHRGINHPVKNVITGKGEITSQNHGFAVNKEEAENHpDFEITHFHIND 324
Cdd:COG0505   242 ELLGKGIPIFGICLGHQLLALALGAKTYKLKFGHRGANHPVKDLETGRVEITSQNHGFAVDEDSLPAT-DLEVTHVNLND 320

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1384927372 325 GTVAGMRMKSKNCFSVQYHPEASPGPQDATYLFDQFIENIN 365
Cdd:COG0505   321 GTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDRFIELME 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: 598.98  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372   5 NRKQAILLLNDGTIFYGKSIGIEGTVFGEVCFNTGMTGYQEIFTDPSYFGQIMVATNAHIGNYGVNDEDVESDKIMISGL 84
Cdd:PRK12564    1 MMMKAYLVLEDGTVFEGKAFGAEGETVGEVVFNTSMTGYQEILTDPSYAGQIVTFTYPLIGNYGVNREDFESDRPHAKGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372  85 VCKNFSFTHSRVNSTESLQDYFAKQNLVVISDVDTRALVSYIRDNGAMNAVISTDTENIEGLKEQLSKVPDMKGLELASK 164
Cdd:PRK12564   81 IVRELSDIPSNWRSEMSLDEYLKENGIPGISGIDTRALTRKLREKGAMKGVIATEDFDAEELLEKARAFPGLLGLDLVKE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372 165 VSAKEAYYVGEP--TAKYKIAALDLGIKKNILRNLVKRDCYVKVFPFDTTFEIMSEFNPDGYFLSNGPGDPDPLYGAIEV 242
Cdd:PRK12564  161 VSTKEPYPWPGPggELKYKVVAIDFGVKRNILRELAERGCRVTVVPATTTAEEILALNPDGVFLSNGPGDPAALDYAIEM 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372 243 AQKILSADKPLFGICLGHQVIALANGISTYKMFNGHRGINHPVKNVITGKGEITSQNHGFAVNKEEAENhpDFEITHFHI 322
Cdd:PRK12564  241 IRELLEKKIPIFGICLGHQLLALALGAKTYKMKFGHRGANHPVKDLETGKVEITSQNHGFAVDEDSLPA--NLEVTHVNL 318

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1384927372 323 NDGTVAGMRMKSKNCFSVQYHPEASPGPQDATYLFDQFIENI 364
Cdd:PRK12564  319 NDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDEFVELM 360
CPSaseIIsmall TIGR01368
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ...
 9-365 2.68e-180

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: 504.08  E-value: 2.68e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372   9 AILLLNDGTIFYGKSIGIEGTVFGEVCFNTGMTGYQEIFTDPSYFGQIMVATNAHIGNYGVNDEDVESDKIMISGLVCKN 88
Cdd:TIGR01368   1 AYLVLEDGTVFRGYSFGAEGTVAGEVVFNTGMTGYQEILTDPSYKGQIVVFTYPLIGNYGVNDEDAESKGIHVSGLVVRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372  89 FSFTHSRVNSTESLQDYFAKQNLVVISDVDTRALVSYIRDNGAMNAVISTDTENIEGLKEQLSKVPDMKGLELASKVSAK 168
Cdd:TIGR01368  81 LSDRYSNWRATESLDQFLKRHGIPGIYGVDTRALVKKIREKGTMKGVISTEDSNDEELVEKARVSPDITGINLVAEVSTK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372 169 EAYYVG-EPTAKYKIAALDLGIKKNILRNLVKRDCYVKVFPFDTTFEIMSEFNPDGYFLSNGPGDPDPLYGAIEVAQKIL 247
Cdd:TIGR01368 161 EPYTWGqRGGKGKRVVVIDFGVKRNILRRLVKRGCEVTVVPYDTDAEEIKKYNPDGIFLSNGPGDPAAVEPAIETIRKLL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372 248 SaDKPLFGICLGHQVIALANGISTYKMFNGHRGINHPVKNVITGKGEITSQNHGFAVnKEEAENHPDFEITHFHINDGTV 327
Cdd:TIGR01368 241 E-KIPIFGICLGHQLLALAFGAKTYKMKFGHRGGNHPVKDLITGRVEITSQNHGYAV-DPDSLPAGDLEVTHVNLNDGTV 318

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1384927372 328 AGMRMKSKNCFSVQYHPEASPGPQDATYLFDQFIENIN 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 5.25e-100

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: 293.63  E-value: 5.25e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372 182 IAALDLGIKKNILRNLVKRDCYVKVFPFDTTFEIMSEFNPDGYFLSNGPGDPDPLYGAIEVAQKILSADKPLFGICLGHQ 261
Cdd:cd01744     1 VVVIDFGVKHNILRELLKRGCEVTVVPYNTDAEEILKLDPDGIFLSNGPGDPALLDEAIKTVRKLLGKKIPIFGICLGHQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372 262 VIALANGISTYKMFNGHRGINHPVKNVITGKGEITSQNHGFAVNkeeAENHP-DFEITHFHINDGTVAGMRMKSKNCFSV 340
Cdd:cd01744    81 LLALALGAKTYKMKFGHRGSNHPVKDLITGRVYITSQNHGYAVD---PDSLPgGLEVTHVNLNDGTVEGIRHKDLPVFSV 157

                         170       180
                  ....*....|....*....|.
gi 1384927372 341 QYHPEASPGPQDATYLFDQFI 361
Cdd:cd01744   158 QFHPEASPGPHDTEYLFDEFL 178
CPSase_sm_chain pfam00988
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 11-136 1.14e-75

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: 229.52  E-value: 1.14e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372  11 LLLNDGTIFYGKSIGIEGTVFGEVCFNTGMTGYQEIFTDPSYFGQIMVATNAHIGNYGVNDEDVESDKIMISGLVCKNFS 90
Cdd:pfam00988   1 LVLEDGTVFEGKSFGAAGSTVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNPEDFESDKIHVAGLVVREYS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1384927372  91 FTHSRVNSTESLQDYFAKQNLVVISDVDTRALVSYIRDNGAMNAVI 136
Cdd:pfam00988  81 DEPSNWRAEESLDEWLKEQGIPGISGVDTRALTRKIREKGAMKGVI 126
CPSase_sm_chain smart01097
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 9-136 3.22e-73

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: 223.41  E-value: 3.22e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372    9 AILLLNDGTIFYGKSIGIEGTVFGEVCFNTGMTGYQEIFTDPSYFGQIMVATNAHIGNYGVNDEDVESDKIMISGLVCKN 88
Cdd:smart01097   3 AYLVLEDGTVFEGESFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNDEDFESDKIQVKGLVVRE 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1384927372   89 FSFTHSRVNSTESLQDYFAKQNLVVISDVDTRALVSYIRDNGAMNAVI 136
Cdd:smart01097  83 LSDEPSNWRSEQSLDEFLKENGIPGISGIDTRALTRKLREKGAMKGVI 130
 
Name Accession Description Interval E-value
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 6-365 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: 632.06  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372   6 RKQAILLLNDGTIFYGKSIGIEGTVFGEVCFNTGMTGYQEIFTDPSYFGQIMVATNAHIGNYGVNDEDVESDKIMISGLV 85
Cdd:COG0505     2 MMKALLVLEDGTVFEGKSFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVTFTYPHIGNYGVNDEDFESDRPWVAGLV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372  86 CKNFSFTHSRVNSTESLQDYFAKQNLVVISDVDTRALVSYIRDNGAMNAVISTDTENIEGLKEQLSKVPDMKGLELASKV 165
Cdd:COG0505    82 VRELSRRPSNWRSEESLDEYLKEHGIPGISGIDTRALTRHLREKGAMKGVISTGDLDIEELLEKARAAPGMEGLDLVKEV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372 166 SAKEAYYVGE-PTAKYKIAALDLGIKKNILRNLVKRDCYVKVFPFDTTFEIMSEFNPDGYFLSNGPGDPDPLYGAIEVAQ 244
Cdd:COG0505   162 STKEPYEWTEaPGAGFHVVALDFGVKRNILRELAERGCRVTVVPATTSAEEILALNPDGVFLSNGPGDPAALDYAIETIR 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372 245 KILSADKPLFGICLGHQVIALANGISTYKMFNGHRGINHPVKNVITGKGEITSQNHGFAVNKEEAENHpDFEITHFHIND 324
Cdd:COG0505   242 ELLGKGIPIFGICLGHQLLALALGAKTYKLKFGHRGANHPVKDLETGRVEITSQNHGFAVDEDSLPAT-DLEVTHVNLND 320

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1384927372 325 GTVAGMRMKSKNCFSVQYHPEASPGPQDATYLFDQFIENIN 365
Cdd:COG0505   321 GTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDRFIELME 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: 598.98  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372   5 NRKQAILLLNDGTIFYGKSIGIEGTVFGEVCFNTGMTGYQEIFTDPSYFGQIMVATNAHIGNYGVNDEDVESDKIMISGL 84
Cdd:PRK12564    1 MMMKAYLVLEDGTVFEGKAFGAEGETVGEVVFNTSMTGYQEILTDPSYAGQIVTFTYPLIGNYGVNREDFESDRPHAKGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372  85 VCKNFSFTHSRVNSTESLQDYFAKQNLVVISDVDTRALVSYIRDNGAMNAVISTDTENIEGLKEQLSKVPDMKGLELASK 164
Cdd:PRK12564   81 IVRELSDIPSNWRSEMSLDEYLKENGIPGISGIDTRALTRKLREKGAMKGVIATEDFDAEELLEKARAFPGLLGLDLVKE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372 165 VSAKEAYYVGEP--TAKYKIAALDLGIKKNILRNLVKRDCYVKVFPFDTTFEIMSEFNPDGYFLSNGPGDPDPLYGAIEV 242
Cdd:PRK12564  161 VSTKEPYPWPGPggELKYKVVAIDFGVKRNILRELAERGCRVTVVPATTTAEEILALNPDGVFLSNGPGDPAALDYAIEM 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372 243 AQKILSADKPLFGICLGHQVIALANGISTYKMFNGHRGINHPVKNVITGKGEITSQNHGFAVNKEEAENhpDFEITHFHI 322
Cdd:PRK12564  241 IRELLEKKIPIFGICLGHQLLALALGAKTYKMKFGHRGANHPVKDLETGKVEITSQNHGFAVDEDSLPA--NLEVTHVNL 318

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1384927372 323 NDGTVAGMRMKSKNCFSVQYHPEASPGPQDATYLFDQFIENI 364
Cdd:PRK12564  319 NDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDEFVELM 360
CPSaseIIsmall TIGR01368
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ...
 9-365 2.68e-180

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: 504.08  E-value: 2.68e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372   9 AILLLNDGTIFYGKSIGIEGTVFGEVCFNTGMTGYQEIFTDPSYFGQIMVATNAHIGNYGVNDEDVESDKIMISGLVCKN 88
Cdd:TIGR01368   1 AYLVLEDGTVFRGYSFGAEGTVAGEVVFNTGMTGYQEILTDPSYKGQIVVFTYPLIGNYGVNDEDAESKGIHVSGLVVRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372  89 FSFTHSRVNSTESLQDYFAKQNLVVISDVDTRALVSYIRDNGAMNAVISTDTENIEGLKEQLSKVPDMKGLELASKVSAK 168
Cdd:TIGR01368  81 LSDRYSNWRATESLDQFLKRHGIPGIYGVDTRALVKKIREKGTMKGVISTEDSNDEELVEKARVSPDITGINLVAEVSTK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372 169 EAYYVG-EPTAKYKIAALDLGIKKNILRNLVKRDCYVKVFPFDTTFEIMSEFNPDGYFLSNGPGDPDPLYGAIEVAQKIL 247
Cdd:TIGR01368 161 EPYTWGqRGGKGKRVVVIDFGVKRNILRRLVKRGCEVTVVPYDTDAEEIKKYNPDGIFLSNGPGDPAAVEPAIETIRKLL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372 248 SaDKPLFGICLGHQVIALANGISTYKMFNGHRGINHPVKNVITGKGEITSQNHGFAVnKEEAENHPDFEITHFHINDGTV 327
Cdd:TIGR01368 241 E-KIPIFGICLGHQLLALAFGAKTYKMKFGHRGGNHPVKDLITGRVEITSQNHGYAV-DPDSLPAGDLEVTHVNLNDGTV 318

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1384927372 328 AGMRMKSKNCFSVQYHPEASPGPQDATYLFDQFIENIN 365
Cdd:TIGR01368 319 EGIRHKDLPVFSVQYHPEASPGPHDTEYLFDEFIDLMK 356
PRK12838 PRK12838
carbamoyl phosphate synthase small subunit; Reviewed
 9-368 7.96e-145

carbamoyl phosphate synthase small subunit; Reviewed


Pssm-ID: 183784 [Multi-domain]  Cd Length: 354  Bit Score: 413.90  E-value: 7.96e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372   9 AILLLNDGTIFYGKSIGIEGTVFGEVCFNTGMTGYQEIFTDPSYFGQIMVATNAHIGNYGVNDEDVESDKIMISGLVCKN 88
Cdd:PRK12838    3 AYLILEDGTVFEGELIGAPIDVTGEIVFNTGMTGYQEVLTDPSYKGQIVVFTYPLIGNYGINADDYESKQPQVKGVIVYE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372  89 FSFTHSRVNSTESLQDYFAKQNLVVISDVDTRALVSYIRDNGAMNAVISTDTENIEGLKEQLSKVPDmkglELASKVSAK 168
Cdd:PRK12838   83 LSREGSHYRAKQSLDDFLKEWNIPGISGVDTRALVKHIREKGTMKASITTTDDAHAFDQIKALVLPK----NVVAQVSTK 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372 169 EAYYVgePTAKYKIAALDLGIKKNILRNLVKRDCYVKVFPFDTTFEIMSEFNPDGYFLSNGPGDPDPLYGAIEVAQKILS 248
Cdd:PRK12838  159 EPYTY--GNGGKHVALIDFGYKKSILRSLSKRGCKVTVLPYDTSLEEIKNLNPDGIVLSNGPGDPKELQPYLPEIKKLIS 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372 249 aDKPLFGICLGHQVIALANGISTYKMFNGHRGINHPVKNVITGKGEITSQNHGFAVnKEEAENHPDFEITHFHINDGTVA 328
Cdd:PRK12838  237 -SYPILGICLGHQLIALALGADTEKLPFGHRGANHPVIDLTTGRVWMTSQNHGYVV-DEDSLDGTPLSVRFFNVNDGSIE 314

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1384927372 329 GMRMKSKNCFSVQYHPEASPGPQDATYLFDQFIENINNGR 368
Cdd:PRK12838  315 GLRHKKKPVLSVQFHPEAHPGPHDAEYIFDEFLEMMEKAR 354
carA CHL00197
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
 5-369 1.32e-130

carbamoyl-phosphate synthase arginine-specific small subunit; Provisional


Pssm-ID: 214392 [Multi-domain]  Cd Length: 382  Bit Score: 379.14  E-value: 1.32e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372   5 NRKQAILLLNDGTIFYGKSIGIEGTVFGEVCFNTGMTGYQEIFTDPSYFGQIMVATNAHIGNYGVNDEDVESDKIMISGL 84
Cdd:CHL00197    3 KMIPAILVLEDGTYYRGWSFSNPITTIGEVVFNTGMTGYQEIITDPSYFEQIVTFTYPEIGNTGINLEDIESVKIQVKGI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372  85 VCKNFSFTHSRVNSTESLQDYFAKQNLVVISDVDTRALVSYIRDNGAMNAVISTDTENIEGLKEQLSKVPDMKGLELASK 164
Cdd:CHL00197   83 IAKNICKSSSNWRQQESLVSYLQRHKIPFIFGIDTRALTQHLRRFGTMNGCISNQNLNLSYLRAKIKESPHMPSSDLIPR 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372 165 VSAKEAYYVGEPTAKY---------------KIAALDLGIKKNILRNLVKRDCYVKVFPFDTTFEIMSEFNPDGYFLSNG 229
Cdd:CHL00197  163 VTTSSYYEWDEKSHPSfyladnkrphssyqlKIIVIDFGVKYNILRRLKSFGCSITVVPATSPYQDILSYQPDGILLSNG 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372 230 PGDPDPLYGAIEVAQKILSADKPLFGICLGHQVIALANGISTYKMFNGHRGINHPVKnvITGKGEITSQNHGFAVNKEEA 309
Cdd:CHL00197  243 PGDPSAIHYGIKTVKKLLKYNIPIFGICMGHQILSLALEAKTFKLKFGHRGLNHPSG--LNQQVEITSQNHGFAVNLESL 320

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372 310 ENHPdFEITHFHINDGTVAGMRMKSKNCFSVQYHPEASPGPQDATYLFDQFIENINNGRS 369
Cdd:CHL00197  321 AKNK-FYITHFNLNDGTVAGISHSPKPYFSVQYHPEASPGPHDADYLFEYFIEIIKHSKS 379
PLN02771 PLN02771
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
 9-357 1.21e-105

carbamoyl-phosphate synthase (glutamine-hydrolyzing)


Pssm-ID: 178370 [Multi-domain]  Cd Length: 415  Bit Score: 316.54  E-value: 1.21e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372   9 AILLLNDGTIFYGKSIGIEGTVFGEVCFNTGMTGYQEIFTDPSYFGQIMVATNAHIGNYGVNDEDVESDKIMISGLVCKN 88
Cdd:PLN02771   57 ARLVLEDGSVWKAKSFGARGTQVGEVVFNTSLTGYQEILTDPSYAGQFVLMTNPHIGNTGVNFDDEESRQCFLAGLVIRS 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372  89 FSFTHSRVNSTESLQDYFAKQNLVVISDVDTRALVSYIRDNGAMNAVISTDTENIEGLKEQLSKVPDMKGLELASKVSAK 168
Cdd:PLN02771  137 LSISTSNWRCTKTLGDYLAERNIMGIYDVDTRAITRRLREDGSLIGVLSTEDSKTDEELLKMSRSWDIVGIDLISGVSCK 216

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372 169 EAYYVGEPT-------------AKYKIAALDLGIKKNILRNLVKRDCYVKVFPFDTTFEIMSEFNPDGYFLSNGPGDPDP 235
Cdd:PLN02771  217 SPYEWVDKTnpewdfntnsrdgESYHVIAYDFGIKHNILRRLASYGCKITVVPSTWPASEALKMKPDGVLFSNGPGDPSA 296

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372 236 LYGAIEVAQKILsADKPLFGICLGHQVIALANGISTYKMFNGHRGINHPVKNVITGKGEITSQNHGFAVnkEEAENHPDF 315
Cdd:PLN02771  297 VPYAVETVKELL-GKVPVFGICMGHQLLGQALGGKTFKMKFGHHGGNHPVRNNRTGRVEISAQNHNYAV--DPASLPEGV 373

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1384927372 316 EITHFHINDGTVAGMRMKSKNCFSVQYHPEASPGPQDATYLF 357
Cdd:PLN02771  374 EVTHVNLNDGSCAGLAFPALNVMSLQYHPEASPGPHDSDNAF 415
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 182-361 5.25e-100

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: 293.63  E-value: 5.25e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372 182 IAALDLGIKKNILRNLVKRDCYVKVFPFDTTFEIMSEFNPDGYFLSNGPGDPDPLYGAIEVAQKILSADKPLFGICLGHQ 261
Cdd:cd01744     1 VVVIDFGVKHNILRELLKRGCEVTVVPYNTDAEEILKLDPDGIFLSNGPGDPALLDEAIKTVRKLLGKKIPIFGICLGHQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372 262 VIALANGISTYKMFNGHRGINHPVKNVITGKGEITSQNHGFAVNkeeAENHP-DFEITHFHINDGTVAGMRMKSKNCFSV 340
Cdd:cd01744    81 LLALALGAKTYKMKFGHRGSNHPVKDLITGRVYITSQNHGYAVD---PDSLPgGLEVTHVNLNDGTVEGIRHKDLPVFSV 157

                         170       180
                  ....*....|....*....|.
gi 1384927372 341 QYHPEASPGPQDATYLFDQFI 361
Cdd:cd01744   158 QFHPEASPGPHDTEYLFDEFL 178
CPSase_sm_chain pfam00988
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 11-136 1.14e-75

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: 229.52  E-value: 1.14e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372  11 LLLNDGTIFYGKSIGIEGTVFGEVCFNTGMTGYQEIFTDPSYFGQIMVATNAHIGNYGVNDEDVESDKIMISGLVCKNFS 90
Cdd:pfam00988   1 LVLEDGTVFEGKSFGAAGSTVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNPEDFESDKIHVAGLVVREYS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1384927372  91 FTHSRVNSTESLQDYFAKQNLVVISDVDTRALVSYIRDNGAMNAVI 136
Cdd:pfam00988  81 DEPSNWRAEESLDEWLKEQGIPGISGVDTRALTRKIREKGAMKGVI 126
CPSase_sm_chain smart01097
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 9-136 3.22e-73

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: 223.41  E-value: 3.22e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372    9 AILLLNDGTIFYGKSIGIEGTVFGEVCFNTGMTGYQEIFTDPSYFGQIMVATNAHIGNYGVNDEDVESDKIMISGLVCKN 88
Cdd:smart01097   3 AYLVLEDGTVFEGESFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNDEDFESDKIQVKGLVVRE 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1384927372   89 FSFTHSRVNSTESLQDYFAKQNLVVISDVDTRALVSYIRDNGAMNAVI 136
Cdd:smart01097  83 LSDEPSNWRSEQSLDEFLKENGIPGISGIDTRALTRKLREKGAMKGVI 130
GATase pfam00117
Glutamine amidotransferase class-I;
188-362 2.02e-59

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 190.14  E-value: 2.02e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372 188 GIKKNILRNLVKRDCYVKVFPFDTTFEIMSEFNPDGYFLSNGPGDPDPLYGAIEVAQKILSADKPLFGICLGHQVIALAN 267
Cdd:pfam00117   8 SFTYNLARALRELGVEVTVVPNDTPAEEILEENPDGIILSGGPGSPGAAGGAIEAIREARELKIPILGICLGHQLLALAF 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372 268 GISTYKM-FNGHRGINHPVKN------VITGKGEITSQNHGFAVNKEEAEnhPDFEITHFHINDGTVAGMRMKSKNCFSV 340
Cdd:pfam00117  88 GGKVVKAkKFGHHGKNSPVGDdgcglfYGLPNVFIVRRYHSYAVDPDTLP--DGLEVTATSENDGTIMGIRHKKLPIFGV 165

                         170       180
                  ....*....|....*....|..
gi 1384927372 341 QYHPEASPGPQDATYLFDQFIE 362
Cdd:pfam00117 166 QFHPESILTPHGPEILFNFFIK 187
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 192-345 5.26e-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: 83.74  E-value: 5.26e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372 192 NILRNLVKRDCYVKVFPFD-TTFEIMSEFNPDGYFLSNGPGDPDPLYGAIEVAQKiLSADKPLFGICLGHQVIALANGIS 270
Cdd:cd01743    13 NLVQYLRELGAEVVVVRNDeITLEELELLNPDAIVISPGPGHPEDAGISLEIIRA-LAGKVPILGVCLGHQAIAEAFGGK 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372 271 TYKMFNGHRGINHPVKnvITGKGEIT--SQN------HGFAVNKEEaenHPDFEITHFHINDGTVAGMRMKSKNCFSVQY 342
Cdd:cd01743    92 VVRAPEPMHGKTSEIH--HDGSGLFKglPQPftvgryHSLVVDPDP---LPDLLEVTASTEDGVIMALRHRDLPIYGVQF 166


                  ...
gi 1384927372 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 5.17e-15

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: 72.57  E-value: 5.17e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372 193 ILRNLvkRDC--YVKVFPFDTTFEIMSEFNPDGYFLSNGPG---DPDplygAIEVAQKILSADKPLFGICLGHQVIALAN 267
Cdd:cd01742    14 IARRV--RELgvYSEILPNTTPLEEIKLKNPKGIILSGGPSsvyEED----APRVDPEIFELGVPVLGICYGMQLIAKAL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372 268 G---ISTYKMFNGHRGINHPVKNVITGKGEITSQ---NHGfavnkEEAENHPD-FEITHFHINDGtVAGMRMKSKNCFSV 340
Cdd:cd01742    88 GgkvERGDKREYGKAEIEIDDSSPLFEGLPDEQTvwmSHG-----DEVVKLPEgFKVIASSDNCP-VAAIANEEKKIYGV 161


                  ....*
gi 1384927372 341 QYHPE 345
Cdd:cd01742   162 QFHPE 166
guaA_Nterm TIGR00888
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ...
 182-364 8.58e-15

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


Pssm-ID: 129966 [Multi-domain]  Cd Length: 188  Bit Score: 71.96  E-value: 8.58e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372 182 IAALDLGIKKN--ILRNLVKRDCYVKVFPFDTTFEIMSEFNPDGYFLSNGPgdpDPLY--GAIEVAQKILSADKPLFGIC 257
Cdd:TIGR00888   1 ILVLDFGSQYTqlIARRLRELGVYSELVPNTTPLEEIREKNPKGIILSGGP---SSVYaeNAPRADEKIFELGVPVLGIC 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372 258 LGHQVIALANGISTYKMFNGHRGinhPVKNVITGKGEITS---------QNHGFAVNKEEaenhPDFEITHfHINDGTVA 328
Cdd:TIGR00888  78 YGMQLMAKQLGGEVGRAEKREYG---KAELEILDEDDLFRglpdestvwMSHGDKVKELP----EGFKVLA-TSDNCPVA 149

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1384927372 329 GMRMKSKNCFSVQYHPEASPGPQDATyLFDQFIENI 364
Cdd:TIGR00888 150 AMAHEEKPIYGVQFHPEVTHTEYGNE-LLENFVYDV 184
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 201-362 1.13e-13

anthranilate synthase component II; Provisional


Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 68.62  E-value: 1.13e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372 201 DCYVKVFPFDT-TFEIMSEFNPDGYFLSNGPGDPDPLYGAIEVAQKiLSADKPLFGICLGHQVIALAngistykmFNGHr 279
Cdd:PRK05670   23 GAEVVVYRNDEiTLEEIEALNPDAIVLSPGPGTPAEAGISLELIRE-FAGKVPILGVCLGHQAIGEA--------FGGK- 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372 280 gINHpVKNVITGK-GEITSQNHG--------FAVNK------EEAENHPDFEITHfHINDGTVAGMRMKSKNCFSVQYHP 344
Cdd:PRK05670   93 -VVR-AKEIMHGKtSPIEHDGSGifaglpnpFTVTRyhslvvDRESLPDCLEVTA-WTDDGEIMGVRHKELPIYGVQFHP 169

                         170
                  ....*....|....*...
gi 1384927372 345 EaSPGPQDATYLFDQFIE 362
Cdd:PRK05670  170 E-SILTEHGHKLLENFLE 186
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 194-348 7.08e-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: 67.28  E-value: 7.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372 194 LRNLVKRDCYVKVF-----PFDTTFEimsefNPDGYFLSNGPG---DPDP-LYGAIEVAQKILSADKPLFGICLGHQVIA 264
Cdd:COG0518    22 LREAGIELDVLRVYageilPYDPDLE-----DPDGLILSGGPMsvyDEDPwLEDEPALIREAFELGKPVLGICYGAQLLA 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372 265 LANGISTYKmfNGHRGI-NHPVKnvITGKGEITS---------QNHGFAVNKEeaenhPD-FEIThFHINDGTVAGMRMk 333
Cdd:COG0518    97 HALGGKVEP--GPGREIgWAPVE--LTEADPLFAglpdeftvwMSHGDTVTEL-----PEgAEVL-ASSDNCPNQAFRY- 165

                         170
                  ....*....|....*
gi 1384927372 334 SKNCFSVQYHPEASP 348
Cdd:COG0518   166 GRRVYGVQFHPEVTH 180
PRK14607 PRK14607
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
204-361 2.07e-12

bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;


Pssm-ID: 237764 [Multi-domain]  Cd Length: 534  Bit Score: 68.20  E-value: 2.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372 204 VKVFPFD-TTFEIMSEFNPDGYFLSNGPGDPDPLYGAIEVAQKiLSADKPLFGICLGHQVIALANGISTYKMFNGHRG-- 280
Cdd:PRK14607   27 IEVVRNDeITIEEIEALNPSHIVISPGPGRPEEAGISVEVIRH-FSGKVPILGVCLGHQAIGYAFGGKIVHAKRILHGkt 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372 281 --INHPVKNV---ITGKGEITsQNHGFAVnkEEAENHPDFEITHFHiNDGTVAGMRMKSKNCFSVQYHPEaSPGPQDATY 355
Cdd:PRK14607  106 spIDHNGKGLfrgIPNPTVAT-RYHSLVV--EEASLPECLEVTAKS-DDGEIMGIRHKEHPIFGVQFHPE-SILTEEGKR 180


                  ....*.
gi 1384927372 356 LFDQFI 361
Cdd:PRK14607  181 ILKNFL 186
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 204-345 6.67e-12

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: 63.52  E-value: 6.67e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372 204 VKVFPFD-TTFEIMSEFNPDGYFLSNGPGDPDPlYG-AIEVAQKiLSADKPLFGICLGHQVIALANGISTYKMfnghrgi 281
Cdd:COG0512    25 VVVVRNDeITLEEIEALAPDGIVLSPGPGTPEE-AGiSLEVIRA-FAGKIPILGVCLGHQAIGEAFGGKVVRA------- 95

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1384927372 282 nhpvKNVITGK-GEITSQNHG-FA-VNKE-----------EAENHPD-FEITHfHINDGTVAGMRMKSKNCFSVQYHPE 345
Cdd:COG0512    96 ----PEPMHGKtSPITHDGSGlFAgLPNPftatryhslvvDRETLPDeLEVTA-WTEDGEIMGIRHRELPIEGVQFHPE 169
guaA PRK00074
GMP synthase; Reviewed
 203-345 3.42e-11

GMP synthase; Reviewed


Pssm-ID: 234614 [Multi-domain]  Cd Length: 511  Bit Score: 64.30  E-value: 3.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372 203 YVKVFPFDTTFEIMSEFNPDGYFLSNGPG---DPDplygAIEVAQKILSADKPLFGICLGHQVIAlangistyKMFNGHr 279
Cdd:PRK00074   29 YSEIVPYDISAEEIRAFNPKGIILSGGPAsvyEEG----APRADPEIFELGVPVLGICYGMQLMA--------HQLGGK- 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372 280 ginhpVKNVIT---GKGEITSQNHG--FAVNKEEAE---NH--------PDFEITHfHINDGTVAGMRMKSKNCFSVQYH 343
Cdd:PRK00074   96 -----VERAGKreyGRAELEVDNDSplFKGLPEEQDvwmSHgdkvtelpEGFKVIA-STENCPIAAIANEERKFYGVQFH 169


                  ..
gi 1384927372 344 PE 345
Cdd:PRK00074  170 PE 171
trpG_papA TIGR00566
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ...
 212-346 5.67e-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: 55.18  E-value: 5.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372 212 TFEIMSEFNPDGYFLSNGPGDPDPlyGAIEV-AQKILSADKPLFGICLGHQVIALANGI-----------STYKMFNGHR 279
Cdd:TIGR00566  35 TLQEIEALLPLLIVISPGPCTPNE--AGISLeAIRHFAGKLPILGVCLGHQAMGQAFGGdvvrantvmhgKTSEIEHNGA 112

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1384927372 280 GINHPVKNVITgkgeiTSQNHGFAVnkeEAENHPD-FEITHFHINDGTVAGMRMKSKNCFSVQYHPEA 346
Cdd:TIGR00566 113 GIFRGLFNPLT-----ATRYHSLVV---EPETLPTcFPVTAWEEENIEIMAIRHRDLPLEGVQFHPES 172
PRK07765 PRK07765
aminodeoxychorismate/anthranilate synthase component II;
222-345 9.28e-09

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181107 [Multi-domain]  Cd Length: 214  Bit Score: 55.06  E-value: 9.28e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372 222 DGYFLSNGPGDPDPLYGAIEVAQKILSADKPLFGICLGHQVIALANGISTYK---MFNGHRG-INHPVKNVITGKGE--I 295
Cdd:PRK07765   48 DGVLLSPGPGTPERAGASIDMVRACAAAGTPLLGVCLGHQAIGVAFGATVDRapeLLHGKTSsVHHTGVGVLAGLPDpfT 127

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1384927372 296 TSQNHGFAVnkeEAENHPD-FEITHfHINDGTVAGMRMKSKNCFSVQYHPE 345
Cdd:PRK07765  128 ATRYHSLTI---LPETLPAeLEVTA-RTDSGVIMAVRHRELPIHGVQFHPE 174
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 192-266 1.98e-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: 51.83  E-value: 1.98e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372 192 NILRNLVKRDCYVKVFPFDTTFEIMSEF--NPDGYFLSNGPGDPDPLY---GAIEVAQKILSADKPLFGICLGHQVIALA 266
Cdd:cd01653    16 SPLDALREAGAEVDVVSPDGGPVESDVDldDYDGLILPGGPGTPDDLArdeALLALLREAAAAGKPILGICLGAQLLVLG 95
trpG CHL00101
anthranilate synthase component 2
 216-346 2.21e-08

anthranilate synthase component 2


Pssm-ID: 214365 [Multi-domain]  Cd Length: 190  Bit Score: 53.58  E-value: 2.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372 216 MSEFNPDGYFLSNGPGDPDPLYGAIEVAqKILSADKPLFGICLGHQVIALANGIS-----------TYKMFNGHRGINHP 284
Cdd:CHL00101   39 IKNLNIRHIIISPGPGHPRDSGISLDVI-SSYAPYIPILGVCLGHQSIGYLFGGKiikapkpmhgkTSKIYHNHDDLFQG 117

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1384927372 285 VKNVITGkgeitSQNHGFAVNKEEAenHPDFEITHfHINDGTVAGMRMKS-KNCFSVQYHPEA 346
Cdd:CHL00101  118 LPNPFTA-----TRYHSLIIDPLNL--PSPLEITA-WTEDGLIMACRHKKyKMLRGIQFHPES 172
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 231-345 4.60e-08

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


Pssm-ID: 429620 [Multi-domain]  Cd Length: 219  Bit Score: 53.03  E-value: 4.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372 231 GDPDPLYGAIEVA--QKILSADKPLFGICLGHQVIALANGISTY------KMFNGHR--------GINHPVKNV------ 288
Cdd:pfam07722  84 GPYDPARDAYELAliRAALARGKPILGICRGFQLLNVALGGTLYqdiqeqPGFTDHRehcqvapyAPSHAVNVEpgslla 163

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1384927372 289 -ITGKGEITSQN-HGFAVnKEEAenhPDFEITHfHINDGTVAGMRMKSKNCF--SVQYHPE 345
Cdd:pfam07722 164 sLLGSEEFRVNSlHHQAI-DRLA---PGLRVEA-VAPDGTIEAIESPNAKGFalGVQWHPE 219
PRK07649 PRK07649
aminodeoxychorismate/anthranilate synthase component II;
210-362 6.25e-08

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181066 [Multi-domain]  Cd Length: 195  Bit Score: 52.50  E-value: 6.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372 210 DTTFEIMSEFNPDGYFLSNGPGDPDPLYGAIEvAQKILSADKPLFGICLGHQVIALANG---ISTYKMFNGHRG-INHPV 285
Cdd:PRK07649   33 EVTISDIENMKPDFLMISPGPCSPNEAGISME-VIRYFAGKIPIFGVCLGHQSIAQVFGgevVRAERLMHGKTSlMHHDG 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372 286 KNVITGKGE--ITSQNHGFAVNKEEAenhPD-FEITHFhINDGTVAGMRMKSKNCFSVQYHPEA---SPGPQdatyLFDQ 359
Cdd:PRK07649  112 KTIFSDIPNpfTATRYHSLIVKKETL---PDcLEVTSW-TEEGEIMAIRHKTLPIEGVQFHPESimtSHGKE----LLQN 183


                  ...
gi 1384927372 360 FIE 362
Cdd:PRK07649  184 FIR 186
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 192-263 8.15e-08

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: 49.51  E-value: 8.15e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1384927372 192 NILRNLVKRDCYVKVFPFDTTFEIMSEF--NPDGYFLSNGPGDPDPLY---GAIEVAQKILSADKPLFGICLGHQVI 263
Cdd:cd03128    16 SPLDALREAGAEVDVVSPDGGPVESDVDldDYDGLILPGGPGTPDDLAwdeALLALLREAAAAGKPVLGICLGAQLL 92
PLN02335 PLN02335
anthranilate synthase
 202-346 2.59e-07

anthranilate synthase


Pssm-ID: 177969 [Multi-domain]  Cd Length: 222  Bit Score: 50.95  E-value: 2.59e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372 202 CYVKVFPFD-TTFEIMSEFNPDGYFLSNGPGDPDPLYGAIEVAQKiLSADKPLFGICLGHQVIALANGISTYKMFNG--H 278
Cdd:PLN02335   43 CHFEVYRNDeLTVEELKRKNPRGVLISPGPGTPQDSGISLQTVLE-LGPLVPLFGVCMGLQCIGEAFGGKIVRSPFGvmH 121

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1384927372 279 rGINHPVKNVITGKGEITS---------QNHGFAVNKEEAEnHPDFEITHFhINDGTVAGMRMKS-KNCFSVQYHPEA 346
Cdd:PLN02335  122 -GKSSPVHYDEKGEEGLFSglpnpftagRYHSLVIEKDTFP-SDELEVTAW-TEDGLIMAARHRKyKHIQGVQFHPES 196
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 206-361 3.05e-07

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: 50.27  E-value: 3.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372 206 VFPFDTTFEIMSE--FNPDGYFLSNGPGDPDPLYGA-----------------IEVAQKILSADKPLFGICLGHQVIALA 266
Cdd:cd01745    37 LLPPVDDEEDLEQylELLDGLLLTGGGDVDPPLYGEephpelgpidperdafeLALLRAALERGKPILGICRGMQLLNVA 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372 267 ngistykmFNG--HRGInhpvknvitgkgEITSqNHGFAVnKEEAenhPDFEITHfHINDGTVAGMRMKSKN-CFSVQYH 343
Cdd:cd01745   117 --------LGGtlYQDI------------RVNS-LHHQAI-KRLA---DGLRVEA-RAPDGVIEAIESPDRPfVLGVQWH 170

                         170       180
                  ....*....|....*....|
gi 1384927372 344 PE--ASPGPQDATyLFDQFI 361
Cdd:cd01745   171 PEwlADTDPDSLK-LFEAFV 189
PRK06774 PRK06774
aminodeoxychorismate synthase component II;
212-363 3.58e-07

aminodeoxychorismate synthase component II;


Pssm-ID: 180689 [Multi-domain]  Cd Length: 191  Bit Score: 49.86  E-value: 3.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372 212 TFEIMSEFNPDGYFLSNGPGDPDPLYGAIEVAQKIlsADK-PLFGICLGHQVIALANGISTYK----MFNGHRGINHPVK 286
Cdd:PRK06774   35 QLTDIEQLAPSHLVISPGPCTPNEAGISLAVIRHF--ADKlPILGVCLGHQALGQAFGARVVRarqvMHGKTSAICHSGQ 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372 287 NVITGKGE--ITSQNHGFAVnkeEAENHPD-FEITHFHINDGTV---AGMRMKSKNCFSVQYHPEASPGPQdATYLFDQF 360
Cdd:PRK06774  113 GVFRGLNQplTVTRYHSLVI---AADSLPGcFELTAWSERGGEMdeiMGIRHRTLPLEGVQFHPESILSEQ-GHQLLDNF 188


                  ...
gi 1384927372 361 IEN 363
Cdd:PRK06774  189 LKN 191
PRK00758 PRK00758
GMP synthase subunit A; Validated
 193-362 1.09e-06

GMP synthase subunit A; Validated


Pssm-ID: 179112 [Multi-domain]  Cd Length: 184  Bit Score: 48.31  E-value: 1.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372 193 ILRNLVKRDCYVKVFPFDTTFEIMSEfNPDGYFLSNGPgDPDPLYGAIEVAQKIlsaDKPLFGICLGHQVIALANGisty 272
Cdd:PRK00758   15 IHRTLRYLGVDAKIIPNTTPVEEIKA-FEDGLILSGGP-DIERAGNCPEYLKEL---DVPILGICLGHQLIAKAFG---- 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372 273 kmfnghrginhpvknvitgkGEITSQNHG-FA-----VNKEEA------------ENH--------PDFEIT-HFHINDg 325
Cdd:PRK00758   86 --------------------GEVGRGEYGeYAlveveILDEDDilkglppeirvwASHadevkelpDGFEILaRSDICE- 144

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1384927372 326 tVAGMRMKSKNCFSVQYHPEASpGPQDATYLFDQFIE 362
Cdd:PRK00758  145 -VEAMKHKEKPIYGVQFHPEVA-HTEYGEEIFKNFLE 179
PRK08007 PRK08007
aminodeoxychorismate synthase component 2;
210-346 1.82e-06

aminodeoxychorismate synthase component 2;


Pssm-ID: 181194 [Multi-domain]  Cd Length: 187  Bit Score: 47.99  E-value: 1.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372 210 DTTFEIMSEFNPDGYFLSNGPGDPDPLYGAIEVAQKiLSADKPLFGICLGHQVIALANGISTYKMFNGHRGINHPVKNvi 289
Cdd:PRK08007   33 ALTLADIDALKPQKIVISPGPCTPDEAGISLDVIRH-YAGRLPILGVCLGHQAMAQAFGGKVVRAAKVMHGKTSPITH-- 109

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1384927372 290 TGKGEITSQNHGFAVNKE-----EAENHPD-FEITHFHiNDGTVAGMRMKSKNCFSVQYHPEA 346
Cdd:PRK08007  110 NGEGVFRGLANPLTVTRYhslvvEPDSLPAcFEVTAWS-ETREIMGIRHRQWDLEGVQFHPES 171
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 222-266 3.73e-06

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


Pssm-ID: 153212 [Multi-domain]  Cd Length: 188  Bit Score: 46.85  E-value: 3.73e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1384927372 222 DGYFLSNGP----GDPDP-LYGAIEVAQKILSADKPLFGICLGHQVIALA 266
Cdd:cd01741    48 DGLVILGGPmsvdEDDYPwLKKLKELIRQALAAGKPVLGICLGHQLLARA 97
PRK08857 PRK08857
aminodeoxychorismate/anthranilate synthase component II;
219-346 8.23e-06

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181566 [Multi-domain]  Cd Length: 193  Bit Score: 46.02  E-value: 8.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372 219 FNPDGYFLSNGPGDPDPLYGAIEvAQKILSADKPLFGICLGHQVIALANGISTYKMFNGHRGINHPVKNviTGKGEITSQ 298
Cdd:PRK08857   42 LNPTHLVISPGPCTPNEAGISLQ-AIEHFAGKLPILGVCLGHQAIAQVFGGQVVRARQVMHGKTSPIRH--TGRSVFKGL 118

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1384927372 299 NHGFAVNKE-----EAENHPD-FEITHF-HINDGT---VAGMRMKSKNCFSVQYHPEA 346
Cdd:PRK08857  119 NNPLTVTRYhslvvKNDTLPEcFELTAWtELEDGSmdeIMGFQHKTLPIEAVQFHPES 176
PRK07053 PRK07053
glutamine amidotransferase; Provisional
 240-274 1.90e-04

glutamine amidotransferase; Provisional


Pssm-ID: 235919 [Multi-domain]  Cd Length: 234  Bit Score: 42.24  E-value: 1.90e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1384927372 240 IEVAQKILSADKPLFGICLGHQVIALANGISTYKM 274
Cdd:PRK07053   73 IALLRQRLAAGLPTLGICLGAQLIARALGARVYPG 107
PRK09522 PRK09522
bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate ...
 203-356 3.21e-04

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


Pssm-ID: 181927 [Multi-domain]  Cd Length: 531  Bit Score: 42.71  E-value: 3.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372 203 YVKVFPFDTTFEIMSEFNPDGYFLSNGPGDPDPLyGAIEVAQKILSADKPLFGICLGHQVIalangISTYKMFNGHRG-I 281
Cdd:PRK09522   31 YRNHIPAQTLIERLATMSNPVLMLSPGPGVPSEA-GCMPELLTRLRGKLPIIGICLGHQAI-----VEAYGGYVGQAGeI 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372 282 NHPVKNVITGKGEI----------TSQNHGFAvnkeeAENHPDFEITHFHINdGTVAGMRMKSKNCFSVQYHPEASPGPQ 351
Cdd:PRK09522  105 LHGKASSIEHDGQAmfagltnplpVARYHSLV-----GSNIPAGLTINAHFN-GMVMAVRHDADRVCGFQFHPESILTTQ 178


                  ....*
gi 1384927372 352 DATYL 356
Cdd:PRK09522  179 GARLL 183
PRK13566 PRK13566
anthranilate synthase component I;
204-345 1.33e-03

anthranilate synthase component I;


Pssm-ID: 237429 [Multi-domain]  Cd Length: 720  Bit Score: 40.67  E-value: 1.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384927372 204 VKVFPFDTTFEIMSEFNPDGYFLSNGPGDPDPlYGAIEVAQKILSADKPLFGICLGHQVIALAngistykmFNGHRG-IN 282
Cdd:PRK13566  553 VTTVRYGFAEEMLDRVNPDLVVLSPGPGRPSD-FDCKATIDAALARNLPIFGVCLGLQAIVEA--------FGGELGqLA 623

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1384927372 283 HPVKnvitGKGEITSQNHGFAV----NKE-----------EAENHPD-FEITHfHINDGTVAGMRMKSKNCFSVQYHPE 345
Cdd:PRK13566  624 YPMH----GKPSRIRVRGPGRLfsglPEEftvgryhslfaDPETLPDeLLVTA-ETEDGVIMAIEHKTLPVAAVQFHPE 697
 
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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