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Conserved domains on  [gi|1706895447|emb|VUX46097|]
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carbamoyl phosphate synthetase small subunit, glutamine amidotransferase [Candidatus Defluviicoccus seviourii]

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 ...
 20-394 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: 674.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447  20 AGANAALVLEDGMVFWGRGAGAVGVAIGEVCFNTSYTGYQEILTDPSYAGQIITFTFPHIGNVGVNPEDVESITPAVRGC 99
Cdd:COG0505     1 MMMKALLVLEDGTVFEGKSFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVTFTYPHIGNYGVNDEDFESDRPWVAGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 100 VMRQPVSSPSNWRAGGDLDAWLKKHGLVALTGVDTRRLTRRIRDGGAPRGTLIHAPddmIDVDVLRFMAERWPGLEGMDL 179
Cdd:COG0505    81 VVRELSRRPSNWRSEESLDEYLKEHGIPGISGIDTRALTRHLREKGAMKGVISTGD---LDIEELLEKARAAPGMEGLDL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 180 AKEVMCRQTYSWDEtawhwpegygrQAEPRFHVVAIDYGAKRNILRCLAAAGCRVTVVPGTASADDVLRHRPDGVFLSNG 259
Cdd:COG0505   158 VKEVSTKEPYEWTE-----------APGAGFHVVALDFGVKRNILRELAERGCRVTVVPATTSAEEILALNPDGVFLSNG 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 260 PGDPAATgAYAVPVIRAVLAQGVPLFGICLGHQMLALALGARTYKLHLGHRGANHPVKDLETGRVEITSQNHGFAVERAS 339
Cdd:COG0505   227 PGDPAAL-DYAIETIRELLGKGIPIFGICLGHQLLALALGAKTYKLKFGHRGANHPVKDLETGRVEITSQNHGFAVDEDS 305

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1706895447 340 LPA-GVVETHVSLFDSTNEGLRVEGAPAFSVQFHPEASPGPHDSHYLFGRFVEAMQ 394
Cdd:COG0505   306 LPAtDLEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDRFIELME 361
 
Name Accession Description Interval E-value
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 20-394 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: 674.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447  20 AGANAALVLEDGMVFWGRGAGAVGVAIGEVCFNTSYTGYQEILTDPSYAGQIITFTFPHIGNVGVNPEDVESITPAVRGC 99
Cdd:COG0505     1 MMMKALLVLEDGTVFEGKSFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVTFTYPHIGNYGVNDEDFESDRPWVAGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 100 VMRQPVSSPSNWRAGGDLDAWLKKHGLVALTGVDTRRLTRRIRDGGAPRGTLIHAPddmIDVDVLRFMAERWPGLEGMDL 179
Cdd:COG0505    81 VVRELSRRPSNWRSEESLDEYLKEHGIPGISGIDTRALTRHLREKGAMKGVISTGD---LDIEELLEKARAAPGMEGLDL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 180 AKEVMCRQTYSWDEtawhwpegygrQAEPRFHVVAIDYGAKRNILRCLAAAGCRVTVVPGTASADDVLRHRPDGVFLSNG 259
Cdd:COG0505   158 VKEVSTKEPYEWTE-----------APGAGFHVVALDFGVKRNILRELAERGCRVTVVPATTSAEEILALNPDGVFLSNG 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 260 PGDPAATgAYAVPVIRAVLAQGVPLFGICLGHQMLALALGARTYKLHLGHRGANHPVKDLETGRVEITSQNHGFAVERAS 339
Cdd:COG0505   227 PGDPAAL-DYAIETIRELLGKGIPIFGICLGHQLLALALGAKTYKLKFGHRGANHPVKDLETGRVEITSQNHGFAVDEDS 305

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1706895447 340 LPA-GVVETHVSLFDSTNEGLRVEGAPAFSVQFHPEASPGPHDSHYLFGRFVEAMQ 394
Cdd:COG0505   306 LPAtDLEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDRFIELME 361
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
23-393 0e+00

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 656.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447  23 NAALVLEDGMVFWGRGAGAVGVAIGEVCFNTSYTGYQEILTDPSYAGQIITFTFPHIGNVGVNPEDVESITPAVRGCVMR 102
Cdd:PRK12564    4 KAYLVLEDGTVFEGKAFGAEGETVGEVVFNTSMTGYQEILTDPSYAGQIVTFTYPLIGNYGVNREDFESDRPHAKGLIVR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 103 QPVSSPSNWRAGGDLDAWLKKHGLVALTGVDTRRLTRRIRDGGAPRGTLIHAPDDmidVDVLRFMAERWPGLEGMDLAKE 182
Cdd:PRK12564   84 ELSDIPSNWRSEMSLDEYLKENGIPGISGIDTRALTRKLREKGAMKGVIATEDFD---AEELLEKARAFPGLLGLDLVKE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 183 VMCRQTYSWDetawhwpegyGRQAEPRFHVVAIDYGAKRNILRCLAAAGCRVTVVPGTASADDVLRHRPDGVFLSNGPGD 262
Cdd:PRK12564  161 VSTKEPYPWP----------GPGGELKYKVVAIDFGVKRNILRELAERGCRVTVVPATTTAEEILALNPDGVFLSNGPGD 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 263 PAATGaYAVPVIRAVLAQGVPLFGICLGHQMLALALGARTYKLHLGHRGANHPVKDLETGRVEITSQNHGFAVERASLPA 342
Cdd:PRK12564  231 PAALD-YAIEMIRELLEKKIPIFGICLGHQLLALALGAKTYKMKFGHRGANHPVKDLETGKVEITSQNHGFAVDEDSLPA 309

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1706895447 343 GVVETHVSLFDSTNEGLRVEGAPAFSVQFHPEASPGPHDSHYLFGRFVEAM 393
Cdd:PRK12564  310 NLEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDEFVELM 360
CPSaseIIsmall TIGR01368
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ...
 24-395 0e+00

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


Pssm-ID: 273580 [Multi-domain]  Cd Length: 357  Bit Score: 514.48  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447  24 AALVLEDGMVFWGRGAGAVGVAIGEVCFNTSYTGYQEILTDPSYAGQIITFTFPHIGNVGVNPEDVESITPAVRGCVMRQ 103
Cdd:TIGR01368   1 AYLVLEDGTVFRGYSFGAEGTVAGEVVFNTGMTGYQEILTDPSYKGQIVVFTYPLIGNYGVNDEDAESKGIHVSGLVVRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 104 PVSSPSNWRAGGDLDAWLKKHGLVALTGVDTRRLTRRIRDGGAPRGTLIHAPddmIDVDVLRFMAERWPGLEGMDLAKEV 183
Cdd:TIGR01368  81 LSDRYSNWRATESLDQFLKRHGIPGIYGVDTRALVKKIREKGTMKGVISTED---SNDEELVEKARVSPDITGINLVAEV 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 184 MCRQTYSWdetawhwpegyGRQAEPRFHVVAIDYGAKRNILRCLAAAGCRVTVVPGTASADDVLRHRPDGVFLSNGPGDP 263
Cdd:TIGR01368 158 STKEPYTW-----------GQRGGKGKRVVVIDFGVKRNILRRLVKRGCEVTVVPYDTDAEEIKKYNPDGIFLSNGPGDP 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 264 AATgAYAVPVIRAVLAQgVPLFGICLGHQMLALALGARTYKLHLGHRGANHPVKDLETGRVEITSQNHGFAVERASLPAG 343
Cdd:TIGR01368 227 AAV-EPAIETIRKLLEK-IPIFGICLGHQLLALAFGAKTYKMKFGHRGGNHPVKDLITGRVEITSQNHGYAVDPDSLPAG 304

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1706895447 344 VVE-THVSLFDSTNEGLRVEGAPAFSVQFHPEASPGPHDSHYLFGRFVEAMQR 395
Cdd:TIGR01368 305 DLEvTHVNLNDGTVEGIRHKDLPVFSVQYHPEASPGPHDTEYLFDEFIDLMKK 357
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 212-390 2.51e-113

Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This group of sequences represents the small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II. CPSase II catalyzes the production of carbomyl phosphate (CP) from bicarbonate, glutamine and two molecules of MgATP. The reaction is believed to proceed by a series of four biochemical reactions involving a minimum of three discrete highly reactive intermediates. The synthesis of CP is critical for the initiation of two separate biosynthetic pathways. In one CP is coupled to aspartate, its carbon and nitrogen nuclei ultimately incorporated into the aromatic moieties of pyrimidine nucleotides. In the second pathway CP is condensed with ornithine at the start of the urea cycle and is utilized for the detoxification of ammonia and biosynthesis of arginine. CPSases may be encoded by one or by several genes, depending on the species. The E.coli enzyme is a heterodimer consisting of two polypeptide chains referred to as the small and large subunit. Ammonia an intermediate during the biosynthesis of carbomyl phosphate produced by the hydrolysis of glutamine in the small subunit of the enzyme is delivered via a molecular tunnel between the remotely located carboxyphosphate active site in the large subunit. CPSase IIs belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site. This group also contains the sequence from the mammalian urea cycle form which has lost the active site Cys, resulting in an ammonia-dependent form, CPSase I.


Pssm-ID: 153215 [Multi-domain]  Cd Length: 178  Bit Score: 328.69  E-value: 2.51e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 212 VVAIDYGAKRNILRCLAAAGCRVTVVPGTASADDVLRHRPDGVFLSNGPGDPAATgAYAVPVIRAVLAQGVPLFGICLGH 291
Cdd:cd01744     1 VVVIDFGVKHNILRELLKRGCEVTVVPYNTDAEEILKLDPDGIFLSNGPGDPALL-DEAIKTVRKLLGKKIPIFGICLGH 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 292 QMLALALGARTYKLHLGHRGANHPVKDLETGRVEITSQNHGFAVERASLPAGVVETHVSLFDSTNEGLRVEGAPAFSVQF 371
Cdd:cd01744    80 QLLALALGAKTYKMKFGHRGSNHPVKDLITGRVYITSQNHGYAVDPDSLPGGLEVTHVNLNDGTVEGIRHKDLPVFSVQF 159

                         170
                  ....*....|....*....
gi 1706895447 372 HPEASPGPHDSHYLFGRFV 390
Cdd:cd01744   160 HPEASPGPHDTEYLFDEFL 178
CPSase_sm_chain smart01097
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 22-151 6.36e-80

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: 241.51  E-value: 6.36e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447   22 ANAALVLEDGMVFWGRGAGAVGVAIGEVCFNTSYTGYQEILTDPSYAGQIITFTFPHIGNVGVNPEDVESITPAVRGCVM 101
Cdd:smart01097   1 MKAYLVLEDGTVFEGESFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNDEDFESDKIQVKGLVV 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1706895447  102 RQPVSSPSNWRAGGDLDAWLKKHGLVALTGVDTRRLTRRIRDGGAPRGTL 151
Cdd:smart01097  81 RELSDEPSNWRSEQSLDEFLKENGIPGISGIDTRALTRKLREKGAMKGVI 130
CPSase_sm_chain pfam00988
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 26-151 1.25e-79

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: 240.69  E-value: 1.25e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447  26 LVLEDGMVFWGRGAGAVGVAIGEVCFNTSYTGYQEILTDPSYAGQIITFTFPHIGNVGVNPEDVESITPAVRGCVMRQPV 105
Cdd:pfam00988   1 LVLEDGTVFEGKSFGAAGSTVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNPEDFESDKIHVAGLVVREYS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1706895447 106 SSPSNWRAGGDLDAWLKKHGLVALTGVDTRRLTRRIRDGGAPRGTL 151
Cdd:pfam00988  81 DEPSNWRAEESLDEWLKEQGIPGISGVDTRALTRKIREKGAMKGVI 126
 
Name Accession Description Interval E-value
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 20-394 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: 674.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447  20 AGANAALVLEDGMVFWGRGAGAVGVAIGEVCFNTSYTGYQEILTDPSYAGQIITFTFPHIGNVGVNPEDVESITPAVRGC 99
Cdd:COG0505     1 MMMKALLVLEDGTVFEGKSFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVTFTYPHIGNYGVNDEDFESDRPWVAGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 100 VMRQPVSSPSNWRAGGDLDAWLKKHGLVALTGVDTRRLTRRIRDGGAPRGTLIHAPddmIDVDVLRFMAERWPGLEGMDL 179
Cdd:COG0505    81 VVRELSRRPSNWRSEESLDEYLKEHGIPGISGIDTRALTRHLREKGAMKGVISTGD---LDIEELLEKARAAPGMEGLDL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 180 AKEVMCRQTYSWDEtawhwpegygrQAEPRFHVVAIDYGAKRNILRCLAAAGCRVTVVPGTASADDVLRHRPDGVFLSNG 259
Cdd:COG0505   158 VKEVSTKEPYEWTE-----------APGAGFHVVALDFGVKRNILRELAERGCRVTVVPATTSAEEILALNPDGVFLSNG 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 260 PGDPAATgAYAVPVIRAVLAQGVPLFGICLGHQMLALALGARTYKLHLGHRGANHPVKDLETGRVEITSQNHGFAVERAS 339
Cdd:COG0505   227 PGDPAAL-DYAIETIRELLGKGIPIFGICLGHQLLALALGAKTYKLKFGHRGANHPVKDLETGRVEITSQNHGFAVDEDS 305

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1706895447 340 LPA-GVVETHVSLFDSTNEGLRVEGAPAFSVQFHPEASPGPHDSHYLFGRFVEAMQ 394
Cdd:COG0505   306 LPAtDLEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDRFIELME 361
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
23-393 0e+00

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 656.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447  23 NAALVLEDGMVFWGRGAGAVGVAIGEVCFNTSYTGYQEILTDPSYAGQIITFTFPHIGNVGVNPEDVESITPAVRGCVMR 102
Cdd:PRK12564    4 KAYLVLEDGTVFEGKAFGAEGETVGEVVFNTSMTGYQEILTDPSYAGQIVTFTYPLIGNYGVNREDFESDRPHAKGLIVR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 103 QPVSSPSNWRAGGDLDAWLKKHGLVALTGVDTRRLTRRIRDGGAPRGTLIHAPDDmidVDVLRFMAERWPGLEGMDLAKE 182
Cdd:PRK12564   84 ELSDIPSNWRSEMSLDEYLKENGIPGISGIDTRALTRKLREKGAMKGVIATEDFD---AEELLEKARAFPGLLGLDLVKE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 183 VMCRQTYSWDetawhwpegyGRQAEPRFHVVAIDYGAKRNILRCLAAAGCRVTVVPGTASADDVLRHRPDGVFLSNGPGD 262
Cdd:PRK12564  161 VSTKEPYPWP----------GPGGELKYKVVAIDFGVKRNILRELAERGCRVTVVPATTTAEEILALNPDGVFLSNGPGD 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 263 PAATGaYAVPVIRAVLAQGVPLFGICLGHQMLALALGARTYKLHLGHRGANHPVKDLETGRVEITSQNHGFAVERASLPA 342
Cdd:PRK12564  231 PAALD-YAIEMIRELLEKKIPIFGICLGHQLLALALGAKTYKMKFGHRGANHPVKDLETGKVEITSQNHGFAVDEDSLPA 309

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1706895447 343 GVVETHVSLFDSTNEGLRVEGAPAFSVQFHPEASPGPHDSHYLFGRFVEAM 393
Cdd:PRK12564  310 NLEVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDEFVELM 360
CPSaseIIsmall TIGR01368
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ...
 24-395 0e+00

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


Pssm-ID: 273580 [Multi-domain]  Cd Length: 357  Bit Score: 514.48  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447  24 AALVLEDGMVFWGRGAGAVGVAIGEVCFNTSYTGYQEILTDPSYAGQIITFTFPHIGNVGVNPEDVESITPAVRGCVMRQ 103
Cdd:TIGR01368   1 AYLVLEDGTVFRGYSFGAEGTVAGEVVFNTGMTGYQEILTDPSYKGQIVVFTYPLIGNYGVNDEDAESKGIHVSGLVVRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 104 PVSSPSNWRAGGDLDAWLKKHGLVALTGVDTRRLTRRIRDGGAPRGTLIHAPddmIDVDVLRFMAERWPGLEGMDLAKEV 183
Cdd:TIGR01368  81 LSDRYSNWRATESLDQFLKRHGIPGIYGVDTRALVKKIREKGTMKGVISTED---SNDEELVEKARVSPDITGINLVAEV 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 184 MCRQTYSWdetawhwpegyGRQAEPRFHVVAIDYGAKRNILRCLAAAGCRVTVVPGTASADDVLRHRPDGVFLSNGPGDP 263
Cdd:TIGR01368 158 STKEPYTW-----------GQRGGKGKRVVVIDFGVKRNILRRLVKRGCEVTVVPYDTDAEEIKKYNPDGIFLSNGPGDP 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 264 AATgAYAVPVIRAVLAQgVPLFGICLGHQMLALALGARTYKLHLGHRGANHPVKDLETGRVEITSQNHGFAVERASLPAG 343
Cdd:TIGR01368 227 AAV-EPAIETIRKLLEK-IPIFGICLGHQLLALAFGAKTYKMKFGHRGGNHPVKDLITGRVEITSQNHGYAVDPDSLPAG 304

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1706895447 344 VVE-THVSLFDSTNEGLRVEGAPAFSVQFHPEASPGPHDSHYLFGRFVEAMQR 395
Cdd:TIGR01368 305 DLEvTHVNLNDGTVEGIRHKDLPVFSVQYHPEASPGPHDTEYLFDEFIDLMKK 357
PRK12838 PRK12838
carbamoyl phosphate synthase small subunit; Reviewed
 22-396 2.69e-161

carbamoyl phosphate synthase small subunit; Reviewed


Pssm-ID: 183784 [Multi-domain]  Cd Length: 354  Bit Score: 457.05  E-value: 2.69e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447  22 ANAALVLEDGMVFWGRGAGAVGVAIGEVCFNTSYTGYQEILTDPSYAGQIITFTFPHIGNVGVNPEDVESITPAVRGCVM 101
Cdd:PRK12838    1 MKAYLILEDGTVFEGELIGAPIDVTGEIVFNTGMTGYQEVLTDPSYKGQIVVFTYPLIGNYGINADDYESKQPQVKGVIV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 102 RQPVSSPSNWRAGGDLDAWLKKHGLVALTGVDTRRLTRRIRDGGAPRGTLIHAPDDMIDVDVLRFMAERwpglegmDLAK 181
Cdd:PRK12838   81 YELSREGSHYRAKQSLDDFLKEWNIPGISGVDTRALVKHIREKGTMKASITTTDDAHAFDQIKALVLPK-------NVVA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 182 EVMCRQTYswdetawHWPEGygrqaepRFHVVAIDYGAKRNILRCLAAAGCRVTVVPGTASADDVLRHRPDGVFLSNGPG 261
Cdd:PRK12838  154 QVSTKEPY-------TYGNG-------GKHVALIDFGYKKSILRSLSKRGCKVTVLPYDTSLEEIKNLNPDGIVLSNGPG 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 262 DPAATGAYaVPVIRAvLAQGVPLFGICLGHQMLALALGARTYKLHLGHRGANHPVKDLETGRVEITSQNHGFAVERASL- 340
Cdd:PRK12838  220 DPKELQPY-LPEIKK-LISSYPILGICLGHQLIALALGADTEKLPFGHRGANHPVIDLTTGRVWMTSQNHGYVVDEDSLd 297

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1706895447 341 PAGVVETHVSLFDSTNEGLRVEGAPAFSVQFHPEASPGPHDSHYLFGRFVEAMQRA 396
Cdd:PRK12838  298 GTPLSVRFFNVNDGSIEGLRHKKKPVLSVQFHPEAHPGPHDAEYIFDEFLEMMEKA 353
PLN02771 PLN02771
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
 6-386 1.76e-126

carbamoyl-phosphate synthase (glutamine-hydrolyzing)


Pssm-ID: 178370 [Multi-domain]  Cd Length: 415  Bit Score: 371.23  E-value: 1.76e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447   6 TPPSSAAASVAGRP-AGANAALVLEDGMVFWGRGAGAVGVAIGEVCFNTSYTGYQEILTDPSYAGQIITFTFPHIGNVGV 84
Cdd:PLN02771   38 SPLTSDGAGVVERPwKTSDARLVLEDGSVWKAKSFGARGTQVGEVVFNTSLTGYQEILTDPSYAGQFVLMTNPHIGNTGV 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447  85 NPEDVESITPAVRGCVMRQPVSSPSNWRAGGDLDAWLKKHGLVALTGVDTRRLTRRIRDGGAPRGTLiHAPDDMIDVDVL 164
Cdd:PLN02771  118 NFDDEESRQCFLAGLVIRSLSISTSNWRCTKTLGDYLAERNIMGIYDVDTRAITRRLREDGSLIGVL-STEDSKTDEELL 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 165 RfMAERWpGLEGMDLAKEVMCRQTYSW-DETAWHWPEGYGRQAEPRFHVVAIDYGAKRNILRCLAAAGCRVTVVPGTASA 243
Cdd:PLN02771  197 K-MSRSW-DIVGIDLISGVSCKSPYEWvDKTNPEWDFNTNSRDGESYHVIAYDFGIKHNILRRLASYGCKITVVPSTWPA 274

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 244 DDVLRHRPDGVFLSNGPGDPAATgAYAVPVIRAVLAQgVPLFGICLGHQMLALALGARTYKLHLGHRGANHPVKDLETGR 323
Cdd:PLN02771  275 SEALKMKPDGVLFSNGPGDPSAV-PYAVETVKELLGK-VPVFGICMGHQLLGQALGGKTFKMKFGHHGGNHPVRNNRTGR 352

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1706895447 324 VEITSQNHGFAVERASLPAGVVETHVSLFDSTNEGLRVEGAPAFSVQFHPEASPGPHDSHYLF 386
Cdd:PLN02771  353 VEISAQNHNYAVDPASLPEGVEVTHVNLNDGSCAGLAFPALNVMSLQYHPEASPGPHDSDNAF 415
carA CHL00197
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
 24-393 1.32e-125

carbamoyl-phosphate synthase arginine-specific small subunit; Provisional


Pssm-ID: 214392 [Multi-domain]  Cd Length: 382  Bit Score: 367.58  E-value: 1.32e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447  24 AALVLEDGMVFWGRGAGAVGVAIGEVCFNTSYTGYQEILTDPSYAGQIITFTFPHIGNVGVNPEDVESITPAVRGCVMRQ 103
Cdd:CHL00197    7 AILVLEDGTYYRGWSFSNPITTIGEVVFNTGMTGYQEIITDPSYFEQIVTFTYPEIGNTGINLEDIESVKIQVKGIIAKN 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 104 PVSSPSNWRAGGDLDAWLKKHGLVALTGVDTRRLTRRIRDGGAPRGTlihAPDDMIDVDVLRFMAERWPGLEGMDLAKEV 183
Cdd:CHL00197   87 ICKSSSNWRQQESLVSYLQRHKIPFIFGIDTRALTQHLRRFGTMNGC---ISNQNLNLSYLRAKIKESPHMPSSDLIPRV 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 184 MCRQTYSWDETA-WHWPEGYGRQAEP--RFHVVAIDYGAKRNILRCLAAAGCRVTVVPGTASADDVLRHRPDGVFLSNGP 260
Cdd:CHL00197  164 TTSSYYEWDEKShPSFYLADNKRPHSsyQLKIIVIDFGVKYNILRRLKSFGCSITVVPATSPYQDILSYQPDGILLSNGP 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 261 GDPAATgAYAVPVIRAVLAQGVPLFGICLGHQMLALALGARTYKLHLGHRGANHPvkdleTG---RVEITSQNHGFAVER 337
Cdd:CHL00197  244 GDPSAI-HYGIKTVKKLLKYNIPIFGICMGHQILSLALEAKTFKLKFGHRGLNHP-----SGlnqQVEITSQNHGFAVNL 317

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1706895447 338 ASLPAGVVE-THVSLFDSTNEGLRVEGAPAFSVQFHPEASPGPHDSHYLFGRFVEAM 393
Cdd:CHL00197  318 ESLAKNKFYiTHFNLNDGTVAGISHSPKPYFSVQYHPEASPGPHDADYLFEYFIEII 374
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 212-390 2.51e-113

Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This group of sequences represents the small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II. CPSase II catalyzes the production of carbomyl phosphate (CP) from bicarbonate, glutamine and two molecules of MgATP. The reaction is believed to proceed by a series of four biochemical reactions involving a minimum of three discrete highly reactive intermediates. The synthesis of CP is critical for the initiation of two separate biosynthetic pathways. In one CP is coupled to aspartate, its carbon and nitrogen nuclei ultimately incorporated into the aromatic moieties of pyrimidine nucleotides. In the second pathway CP is condensed with ornithine at the start of the urea cycle and is utilized for the detoxification of ammonia and biosynthesis of arginine. CPSases may be encoded by one or by several genes, depending on the species. The E.coli enzyme is a heterodimer consisting of two polypeptide chains referred to as the small and large subunit. Ammonia an intermediate during the biosynthesis of carbomyl phosphate produced by the hydrolysis of glutamine in the small subunit of the enzyme is delivered via a molecular tunnel between the remotely located carboxyphosphate active site in the large subunit. CPSase IIs belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site. This group also contains the sequence from the mammalian urea cycle form which has lost the active site Cys, resulting in an ammonia-dependent form, CPSase I.


Pssm-ID: 153215 [Multi-domain]  Cd Length: 178  Bit Score: 328.69  E-value: 2.51e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 212 VVAIDYGAKRNILRCLAAAGCRVTVVPGTASADDVLRHRPDGVFLSNGPGDPAATgAYAVPVIRAVLAQGVPLFGICLGH 291
Cdd:cd01744     1 VVVIDFGVKHNILRELLKRGCEVTVVPYNTDAEEILKLDPDGIFLSNGPGDPALL-DEAIKTVRKLLGKKIPIFGICLGH 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 292 QMLALALGARTYKLHLGHRGANHPVKDLETGRVEITSQNHGFAVERASLPAGVVETHVSLFDSTNEGLRVEGAPAFSVQF 371
Cdd:cd01744    80 QLLALALGAKTYKMKFGHRGSNHPVKDLITGRVYITSQNHGYAVDPDSLPGGLEVTHVNLNDGTVEGIRHKDLPVFSVQF 159

                         170
                  ....*....|....*....
gi 1706895447 372 HPEASPGPHDSHYLFGRFV 390
Cdd:cd01744   160 HPEASPGPHDTEYLFDEFL 178
CPSase_sm_chain smart01097
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 22-151 6.36e-80

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: 241.51  E-value: 6.36e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447   22 ANAALVLEDGMVFWGRGAGAVGVAIGEVCFNTSYTGYQEILTDPSYAGQIITFTFPHIGNVGVNPEDVESITPAVRGCVM 101
Cdd:smart01097   1 MKAYLVLEDGTVFEGESFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNDEDFESDKIQVKGLVV 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1706895447  102 RQPVSSPSNWRAGGDLDAWLKKHGLVALTGVDTRRLTRRIRDGGAPRGTL 151
Cdd:smart01097  81 RELSDEPSNWRSEQSLDEFLKENGIPGISGIDTRALTRKLREKGAMKGVI 130
CPSase_sm_chain pfam00988
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 26-151 1.25e-79

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: 240.69  E-value: 1.25e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447  26 LVLEDGMVFWGRGAGAVGVAIGEVCFNTSYTGYQEILTDPSYAGQIITFTFPHIGNVGVNPEDVESITPAVRGCVMRQPV 105
Cdd:pfam00988   1 LVLEDGTVFEGKSFGAAGSTVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNPEDFESDKIHVAGLVVREYS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1706895447 106 SSPSNWRAGGDLDAWLKKHGLVALTGVDTRRLTRRIRDGGAPRGTL 151
Cdd:pfam00988  81 DEPSNWRAEESLDEWLKEQGIPGISGVDTRALTRKIREKGAMKGVI 126
GATase pfam00117
Glutamine amidotransferase class-I;
213-392 7.14e-64

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 202.85  E-value: 7.14e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 213 VAIDYGA--KRNILRCLAAAGCRVTVVPGTASADDVLRHRPDGVFLSNGPGDPAATGaYAVPVIRAVLAQGVPLFGICLG 290
Cdd:pfam00117   1 LLIDNGDsfTYNLARALRELGVEVTVVPNDTPAEEILEENPDGIILSGGPGSPGAAG-GAIEAIREARELKIPILGICLG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 291 HQMLALALGARTYKLH-LGHRGANHPVKDLE------TGRVEITSQNHGFAVERASLPAGVVETHVSLFDSTNEGLRVEG 363
Cdd:pfam00117  80 HQLLALAFGGKVVKAKkFGHHGKNSPVGDDGcglfygLPNVFIVRRYHSYAVDPDTLPDGLEVTATSENDGTIMGIRHKK 159

                         170       180
                  ....*....|....*....|....*....
gi 1706895447 364 APAFSVQFHPEASPGPHDSHYLFGRFVEA 392
Cdd:pfam00117 160 LPIFGVQFHPESILTPHGPEILFNFFIKA 188
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 222-374 2.19e-26

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: 104.15  E-value: 2.19e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 222 NILRCLAAAGCRVTVVPGTASADDVLRH-RPDGVFLSNGPGDPAATGAYaVPVIRAvLAQGVPLFGICLGHQMLALALGA 300
Cdd:cd01743    13 NLVQYLRELGAEVVVVRNDEITLEELELlNPDAIVISPGPGHPEDAGIS-LEIIRA-LAGKVPILGVCLGHQAIAEAFGG 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 301 RTYKLHLGHRGANHPVKDLETGRVEITSQN------HGFAVERASLPAGvVETHVSLFDSTNEGLRVEGAPAFSVQFHPE 374
Cdd:cd01743    91 KVVRAPEPMHGKTSEIHHDGSGLFKGLPQPftvgryHSLVVDPDPLPDL-LEVTASTEDGVIMALRHRDLPIYGVQFHPE 169
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 222-374 3.19e-22

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: 93.18  E-value: 3.19e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 222 NILRCLAAAGCRVTVVPGTA-SADDVLRHRPDGVFLSNGPGDPAATGAyAVPVIRAvLAQGVPLFGICLGHQMLALALGA 300
Cdd:COG0512    13 NLVQYLGELGAEVVVVRNDEiTLEEIEALAPDGIVLSPGPGTPEEAGI-SLEVIRA-FAGKIPILGVCLGHQAIGEAFGG 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 301 RTYKlhlghrgANHPV--KdleTGRVEITSQN--------------HGFAVERASLPAGVVETHVSLfDSTNEGLRVEGA 364
Cdd:COG0512    91 KVVR-------APEPMhgK---TSPITHDGSGlfaglpnpftatryHSLVVDRETLPDELEVTAWTE-DGEIMGIRHREL 159

                         170
                  ....*....|
gi 1706895447 365 PAFSVQFHPE 374
Cdd:COG0512   160 PIEGVQFHPE 169
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 223-377 1.15e-19

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: 86.92  E-value: 1.15e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 223 ILRCLAAAGCRVTVV--------PGTASADDvlrhrPDGVFLSNGPGDPAATGAYAVP---VIRAVLAQGVPLFGICLGH 291
Cdd:COG0518    18 IARRLREAGIELDVLrvyageilPYDPDLED-----PDGLILSGGPMSVYDEDPWLEDepaLIREAFELGKPVLGICYGA 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 292 QMLALALGARTYKlhlghrganHPVKdlETGRVEITS-----------------QNHGFAVERasLPAGVVETHVSLFDs 354
Cdd:COG0518    93 QLLAHALGGKVEP---------GPGR--EIGWAPVELteadplfaglpdeftvwMSHGDTVTE--LPEGAEVLASSDNC- 158

                         170       180
                  ....*....|....*....|...
gi 1706895447 355 TNEGLRVeGAPAFSVQFHPEASP 377
Cdd:COG0518   159 PNQAFRY-GRRVYGVQFHPEVTH 180
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 222-391 2.74e-18

anthranilate synthase component II; Provisional


Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 82.10  E-value: 2.74e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 222 NILRCLAAAGCRVTVVPG-TASADDVLRHRPDGVFLSNGPGDPAATGAyAVPVIRAvLAQGVPLFGICLGHQMLALALGA 300
Cdd:PRK05670   14 NLVQYLGELGAEVVVYRNdEITLEEIEALNPDAIVLSPGPGTPAEAGI-SLELIRE-FAGKVPILGVCLGHQAIGEAFGG 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 301 RTyklhlghRGANHPVKdletGRV-EITSQNHG-FA---------------VERASLPAGVVETHVSlFDSTNEGLRVEG 363
Cdd:PRK05670   92 KV-------VRAKEIMH----GKTsPIEHDGSGiFAglpnpftvtryhslvVDRESLPDCLEVTAWT-DDGEIMGVRHKE 159

                         170       180
                  ....*....|....*....|....*...
gi 1706895447 364 APAFSVQFHPEaSPGPHDSHYLFGRFVE 391
Cdd:PRK05670  160 LPIYGVQFHPE-SILTEHGHKLLENFLE 186
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 211-375 6.38e-17

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: 78.06  E-value: 6.38e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 211 HVVAIDYGAKRNILRCLAAAGCRVTVVPGTASADDVLRHRPDGVFLSNGPGDPAATGAYAVP----VIRAVLAQGVPLFG 286
Cdd:cd01741     7 HDTPEGPGLFEDLLREAGAETIEIDVVDVYAGELLPDLDDYDGLVILGGPMSVDEDDYPWLKklkeLIRQALAAGKPVLG 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 287 ICLGHQMLALALGARTYKLHLGHRGANHPVKDLETGRVEITSQN----------HGFAVERasLPAGVVeTHVSLFDSTN 356
Cdd:cd01741    87 ICLGHQLLARALGGKVGRNPKGWEIGWFPVTLTEAGKADPLFAGlpdefpvfhwHGDTVVE--LPPGAV-LLASSEACPN 163

                         170
                  ....*....|....*....
gi 1706895447 357 EGLRVeGAPAFSVQFHPEA 375
Cdd:cd01741   164 QAFRY-GDRALGLQFHPEE 181
PuuD COG2071
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ...
 221-396 1.40e-15

Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains GATase1-like domain [Amino acid transport and metabolism];


Pssm-ID: 441674 [Multi-domain]  Cd Length: 231  Bit Score: 75.59  E-value: 1.40e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 221 RNILRCLAAAGCRVTVVPGTASADDV--LRHRPDGVFLS-----------------NGPGDPAATgAYAVPVIRAVLAQG 281
Cdd:COG2071    18 EDYVRAVRAAGGLPVLLPPVGDEEDLdeLLDRLDGLVLTggadvdpalygeephpeLGPIDPERD-AFELALIRAALERG 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 282 VPLFGICLGHQMLALALG-------ARTYKLHLGHRGAN------HPV---KD------LETGRVEITSQnHGFAVERas 339
Cdd:COG2071    97 KPVLGICRGMQLLNVALGgtlyqdlPDQVPGALDHRQPApryaprHTVeiePGsrlariLGEEEIRVNSL-HHQAVKR-- 173

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1706895447 340 LPAGVVETHVSLfDSTNEGLRVEGAP-AFSVQFHPEASPGPHDSHY-LFGRFVEAMQRA 396
Cdd:COG2071   174 LGPGLRVSARAP-DGVIEAIESPGAPfVLGVQWHPEWLAASDPLSRrLFEAFVEAARAR 231
GATase1_GMP_Synthase cd01742
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ...
 212-374 2.92e-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: 73.34  E-value: 2.92e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 212 VVAIDYGAKRN--ILRCLAAAGCRVTVVPGTASADDVLRHRPDGVFLSNGPGDPAATGAYAVPviRAVLAQGVPLFGICL 289
Cdd:cd01742     1 ILILDFGSQYThlIARRVRELGVYSEILPNTTPLEEIKLKNPKGIILSGGPSSVYEEDAPRVD--PEIFELGVPVLGICY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 290 GHQMLALALGArtyKLHLGHRGanhpvkdlETGRVEITSQ-----------------NHGFAVERasLPAG--VVETHVs 350
Cdd:cd01742    79 GMQLIAKALGG---KVERGDKR--------EYGKAEIEIDdssplfeglpdeqtvwmSHGDEVVK--LPEGfkVIASSD- 144

                         170       180
                  ....*....|....*....|....
gi 1706895447 351 lfDSTNEGLRVEGAPAFSVQFHPE 374
Cdd:cd01742   145 --NCPVAAIANEEKKIYGVQFHPE 166
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 210-374 5.28e-14

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: 70.75  E-value: 5.28e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 210 FHVVAIDYGAKRNIlRCLAAAGCRVTVVPGTASADDVlRH---RPDGVFLSNGP--------------GDPAATG--AYA 270
Cdd:pfam07722  17 FHGAGESYLAAGYV-EAVEGAGGLPVLLPILGDPEDA-AAildRLDGLLLTGGPnvdphfygeepsesGGPYDPArdAYE 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 271 VPVIRAVLAQGVPLFGICLGHQMLALALGARTY------KLHLGHR--------GANHPVkDLETGRV--EITSQN---- 330
Cdd:pfam07722  95 LALIRAALARGKPILGICRGFQLLNVALGGTLYqdiqeqPGFTDHRehcqvapyAPSHAV-NVEPGSLlaSLLGSEefrv 173

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1706895447 331 ---HGFAVERasLPAG-VVETHVSlfDSTNEGLRVEGAPAF--SVQFHPE 374
Cdd:pfam07722 174 nslHHQAIDR--LAPGlRVEAVAP--DGTIEAIESPNAKGFalGVQWHPE 219
guaA_Nterm TIGR00888
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ...
 212-374 1.05e-13

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: 69.27  E-value: 1.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 212 VVAIDYGAKRN--ILRCLAAAGCRVTVVPGTASADDVLRHRPDGVFLSNGPGDPAATGAYAVPviRAVLAQGVPLFGICL 289
Cdd:TIGR00888   1 ILVLDFGSQYTqlIARRLRELGVYSELVPNTTPLEEIREKNPKGIILSGGPSSVYAENAPRAD--EKIFELGVPVLGICY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 290 GHQMLALALGARTYKlhlghrgANHPvkdlETGRVEITSQN-----------------HGFAVERasLPAGVVETHVSLf 352
Cdd:TIGR00888  79 GMQLMAKQLGGEVGR-------AEKR----EYGKAELEILDeddlfrglpdestvwmsHGDKVKE--LPEGFKVLATSD- 144

                         170       180
                  ....*....|....*....|..
gi 1706895447 353 DSTNEGLRVEGAPAFSVQFHPE 374
Cdd:TIGR00888 145 NCPVAAMAHEEKPIYGVQFHPE 166
PRK14607 PRK14607
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
230-389 1.92e-13

bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;


Pssm-ID: 237764 [Multi-domain]  Cd Length: 534  Bit Score: 71.67  E-value: 1.92e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 230 AGCRVTVVPGTASADDVLRHRPDGVFLSNGPGDPAATGAyAVPVIRAvLAQGVPLFGICLGHQMLALALGAR-------- 301
Cdd:PRK14607   24 PEEIEVVRNDEITIEEIEALNPSHIVISPGPGRPEEAGI-SVEVIRH-FSGKVPILGVCLGHQAIGYAFGGKivhakril 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 302 ---TYKLHLGHRGANHPVKDLetgrVEITsQNHGFAVERASLPaGVVETHVSLFDSTNEGLRVEGAPAFSVQFHPEaSPG 378
Cdd:PRK14607  102 hgkTSPIDHNGKGLFRGIPNP----TVAT-RYHSLVVEEASLP-ECLEVTAKSDDGEIMGIRHKEHPIFGVQFHPE-SIL 174

                         170
                  ....*....|.
gi 1706895447 379 PHDSHYLFGRF 389
Cdd:PRK14607  175 TEEGKRILKNF 185
PRK07765 PRK07765
aminodeoxychorismate/anthranilate synthase component II;
238-374 6.85e-13

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181107 [Multi-domain]  Cd Length: 214  Bit Score: 67.38  E-value: 6.85e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 238 PGTASADDVLRhRPDGVFLSNGPGDPAATGAyAVPVIRAVLAQGVPLFGICLGHQMLALALGARTYK----LHlghrGAN 313
Cdd:PRK07765   35 PRLADEAAVAA-QFDGVLLSPGPGTPERAGA-SIDMVRACAAAGTPLLGVCLGHQAIGVAFGATVDRapelLH----GKT 108

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1706895447 314 HPVKDLETGRVE------ITSQNHGFAVERASLPAgVVETHVSLFDSTNEGLRVEGAPAFSVQFHPE 374
Cdd:PRK07765  109 SSVHHTGVGVLAglpdpfTATRYHSLTILPETLPA-ELEVTARTDSGVIMAVRHRELPIHGVQFHPE 174
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 207-390 1.60e-12

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: 65.67  E-value: 1.60e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 207 EPRFHVVAIDYGAkRNILRCLAAAGCRVTVVP---GTASADDVLRhRPDGVFLSNGPG-DPAATG--------------- 267
Cdd:cd01745     9 EEEGGYERRDYLN-QYYVDAVRKAGGLPVLLPpvdDEEDLEQYLE-LLDGLLLTGGGDvDPPLYGeephpelgpidperd 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 268 AYAVPVIRAVLAQGVPLFGICLGHQMLALALGARTYkLHLG----HRGAnhpVKDLETG-RVEITSqnhgfaveraslPA 342
Cdd:cd01745    87 AFELALLRAALERGKPILGICRGMQLLNVALGGTLY-QDIRvnslHHQA---IKRLADGlRVEARA------------PD 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1706895447 343 GVVethvslfdstnEGLRVEGAP-AFSVQFHPE-ASPGPHDSHYLFGRFV 390
Cdd:cd01745   151 GVI-----------EAIESPDRPfVLGVQWHPEwLADTDPDSLKLFEAFV 189
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 212-312 1.84e-11

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: 60.69  E-value: 1.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 212 VVAIDYGAK-----RNILRCLAAAGCRVTVVP--GTASADDVLRHRPDGVFLSNGPGDPAATGAYA--VPVIRAVLAQGV 282
Cdd:cd01653     1 VAVLLFPGFeelelASPLDALREAGAEVDVVSpdGGPVESDVDLDDYDGLILPGGPGTPDDLARDEalLALLREAAAAGK 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 1706895447 283 PLFGICLGHQMLALALGARTYKLHLGHRGA 312
Cdd:cd01653    81 PILGICLGAQLLVLGVQFHPEAIDGAEAGA 110
guaA PRK00074
GMP synthase; Reviewed
 236-374 1.84e-11

GMP synthase; Reviewed


Pssm-ID: 234614 [Multi-domain]  Cd Length: 511  Bit Score: 65.45  E-value: 1.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 236 VVPGTASADDVLRHRPDGVFLSNGPGDPAATGAYAVPviRAVLAQGVPLFGICLGHQMLALALGARTyklhlghRGANHP 315
Cdd:PRK00074   32 IVPYDISAEEIRAFNPKGIILSGGPASVYEEGAPRAD--PEIFELGVPVLGICYGMQLMAHQLGGKV-------ERAGKR 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 316 vkdlETGRVEITSQN-----------------HGFAVERasLPAGVVETHVSlfDST------NEGLRVEGapafsVQFH 372
Cdd:PRK00074  103 ----EYGRAELEVDNdsplfkglpeeqdvwmsHGDKVTE--LPEGFKVIAST--ENCpiaaiaNEERKFYG-----VQFH 169


                  ..
gi 1706895447 373 PE 374
Cdd:PRK00074  170 PE 171
HisH COG0118
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ...
 212-376 4.85e-11

Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid transport and metabolism]; Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH is part of the Pathway/BioSystem: Histidine biosynthesis


Pssm-ID: 439888 [Multi-domain]  Cd Length: 196  Bit Score: 61.59  E-value: 4.85e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 212 VVAIDYGAK--RNILRCLAAAGCRVTVvpgTASADDVLRhrPDGVFLsngPGDpaatGAYA-----------VPVIRAVL 278
Cdd:COG0118     3 IAIIDYGMGnlRSVAKALERLGAEVVV---TSDPDEIRA--ADRLVL---PGV----GAFGdamenlrerglDEAIREAV 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 279 AQGVPLFGICLGHQMLA-------------------LALGARTYKL-HLG----HRGANHPV-KDLETGR----Veitsq 329
Cdd:COG0118    71 AGGKPVLGICLGMQLLFerseengdteglglipgevVRFPASDLKVpHMGwntvEIAKDHPLfAGIPDGEyfyfV----- 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1706895447 330 nHGFAVErASLPAGVVEThvslfdsTNEGLR----VEGAPAFSVQFHPEAS 376
Cdd:COG0118   146 -HSYYVP-PDDPEDVVAT-------TDYGVPftaaVERGNVFGTQFHPEKS 187
trpG_papA TIGR00566
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ...
 244-375 8.03e-11

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: 60.96  E-value: 8.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 244 DDVLRHRPDGVFLSNGPGDPAaTGAYAVPVIRAvLAQGVPLFGICLGHQMLALALGARTYKLHLGHRGANHPVKDLETGR 323
Cdd:TIGR00566  37 QEIEALLPLLIVISPGPCTPN-EAGISLEAIRH-FAGKLPILGVCLGHQAMGQAFGGDVVRANTVMHGKTSEIEHNGAGI 114

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1706895447 324 VE------ITSQNHGFAVERASLPAGVVETHVSLFDSTNEGLRVEGAPAFSVQFHPEA 375
Cdd:TIGR00566 115 FRglfnplTATRYHSLVVEPETLPTCFPVTAWEEENIEIMAIRHRDLPLEGVQFHPES 172
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 212-294 1.14e-10

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


Pssm-ID: 153222 [Multi-domain]  Cd Length: 92  Bit Score: 57.60  E-value: 1.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 212 VVAIDYGAK-----RNILRCLAAAGCRVTVVP--GTASADDVLRHRPDGVFLSNGPGDPAATGAYA--VPVIRAVLAQGV 282
Cdd:cd03128     1 VAVLLFGGSeelelASPLDALREAGAEVDVVSpdGGPVESDVDLDDYDGLILPGGPGTPDDLAWDEalLALLREAAAAGK 80

                          90
                  ....*....|..
gi 1706895447 283 PLFGICLGHQML 294
Cdd:cd03128    81 PVLGICLGAQLL 92
PRK13566 PRK13566
anthranilate synthase component I;
231-374 1.24e-10

anthranilate synthase component I;


Pssm-ID: 237429 [Multi-domain]  Cd Length: 720  Bit Score: 63.01  E-value: 1.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 231 GCRVTVVPGTASADDVLRHRPDGVFLSNGPGDPAATGAYAVpvIRAVLAQGVPLFGICLGHQMLALALGARTYKLHLGHR 310
Cdd:PRK13566  550 GAEVTTVRYGFAEEMLDRVNPDLVVLSPGPGRPSDFDCKAT--IDAALARNLPIFGVCLGLQAIVEAFGGELGQLAYPMH 627

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1706895447 311 GANHPVKDLETGRV------EIT-SQNHGFAVERASLPAGVVETHVSLfDSTNEGLRVEGAPAFSVQFHPE 374
Cdd:PRK13566  628 GKPSRIRVRGPGRLfsglpeEFTvGRYHSLFADPETLPDELLVTAETE-DGVIMAIEHKTLPVAAVQFHPE 697
hisH PRK13146
imidazole glycerol phosphate synthase subunit HisH; Provisional
 212-376 1.30e-10

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237290 [Multi-domain]  Cd Length: 209  Bit Score: 60.57  E-value: 1.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 212 VVAIDYG------AKRNILRclAAAGCRVTVvpgTASADDVLRhrPDGVFLsngPGDpaatGAYA------------VPV 273
Cdd:PRK13146    4 VAIIDYGsgnlrsAAKALER--AGAGADVVV---TADPDAVAA--ADRVVL---PGV----GAFAdcmrglravglgEAV 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 274 IRAVLAQGVPLFGICLGHQMLA---------------------LALGARTYKL-HLG----HRGANHPV-KDLETGR--- 323
Cdd:PRK13146   70 IEAVLAAGRPFLGICVGMQLLFerglehgdtpglglipgevvrFQPDGPALKVpHMGwntvDQTRDHPLfAGIPDGArfy 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1706895447 324 -VeitsqnHGFAVeRASLPAGVVEThvslfdsTNEGLR----VEGAPAFSVQFHPEAS 376
Cdd:PRK13146  150 fV------HSYYA-QPANPADVVAW-------TDYGGPftaaVARDNLFATQFHPEKS 193
PRK05637 PRK05637
anthranilate synthase component II; Provisional
 211-379 6.02e-10

anthranilate synthase component II; Provisional


Pssm-ID: 180178 [Multi-domain]  Cd Length: 208  Bit Score: 58.70  E-value: 6.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 211 HVVAIDYGAK--RNILRCLAAAGCRVTVVPGTASADDVLRHRPDGVFLSNGPGDPAATGAyAVPVIRAVLAQgVPLFGIC 288
Cdd:PRK05637    3 HVVLIDNHDSfvYNLVDAFAVAGYKCTVFRNTVPVEEILAANPDLICLSPGPGHPRDAGN-MMALIDRTLGQ-IPLLGIC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 289 LGHQMLALALGAR----------TYKLHLGHRGANHPVKDLETGRVEITSQN-HGFAVERA---SL-----PAGVVE--T 347
Cdd:PRK05637   81 LGFQALLEHHGGKvepcgpvhgtTDNMILTDAGVQSPVFAGLATDVEPDHPEiPGRKVPIAryhSLgcvvaPDGMESlgT 160

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1706895447 348 HVSLFDSTNEGLRVEGAPAFSVQFHPEA--SP-GP 379
Cdd:PRK05637  161 CSSEIGPVIMAAETTDGKAIGLQFHPESvlSPtGP 195
PRK07649 PRK07649
aminodeoxychorismate/anthranilate synthase component II;
245-399 1.70e-09

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181066 [Multi-domain]  Cd Length: 195  Bit Score: 57.12  E-value: 1.70e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 245 DVLRHRPDGVFLSNGPGDPAATGAyAVPVIRAvLAQGVPLFGICLGHQMLALALGARTYKLHLGHRGANHPVK-DLETGR 323
Cdd:PRK07649   38 DIENMKPDFLMISPGPCSPNEAGI-SMEVIRY-FAGKIPIFGVCLGHQSIAQVFGGEVVRAERLMHGKTSLMHhDGKTIF 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 324 VEITS-----QNHGFAVERASLPAGVVEThvslfDSTNEG----LRVEGAPAFSVQFHPEASPGPHDSHyLFGRFVEAMQ 394
Cdd:PRK07649  116 SDIPNpftatRYHSLIVKKETLPDCLEVT-----SWTEEGeimaIRHKTLPIEGVQFHPESIMTSHGKE-LLQNFIRKYS 189


                  ....*
gi 1706895447 395 RATVS 399
Cdd:PRK07649  190 PSVTS 194
PLN02347 PLN02347
GMP synthetase
 212-387 3.29e-09

GMP synthetase


Pssm-ID: 215197 [Multi-domain]  Cd Length: 536  Bit Score: 58.54  E-value: 3.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 212 VVAIDYGAKRN--ILRCLAAAGCRVTVVPGTASADDVLRHRPDGVFLSNGPGDPAATGAYAVP--VIRAVLAQGVPLFGI 287
Cdd:PLN02347   13 VLILDYGSQYThlITRRVRELGVYSLLLSGTASLDRIASLNPRVVILSGGPHSVHVEGAPTVPegFFDYCRERGVPVLGI 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 288 CLGHQMLALALGARTYKLHLGHRG-ANHPVK-------DLETGRVEITSQNHGfaVERASLPAG---VVETHVSLFDST- 355
Cdd:PLN02347   93 CYGMQLIVQKLGGEVKPGEKQEYGrMEIRVVcgsqlfgDLPSGETQTVWMSHG--DEAVKLPEGfevVAKSVQGAVVAIe 170

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1706895447 356 NEGLRVegapaFSVQFHPEASPGPHD----SHYLFG 387
Cdd:PLN02347  171 NRERRI-----YGLQYHPEVTHSPKGmetlRHFLFD 201
PRK00758 PRK00758
GMP synthase subunit A; Validated
 211-376 4.08e-09

GMP synthase subunit A; Validated


Pssm-ID: 179112 [Multi-domain]  Cd Length: 184  Bit Score: 55.63  E-value: 4.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 211 HVVAIDYGAKRN--ILRCLAAAGCRVTVVPGTASADDVLRhRPDGVFLSNGPgDPAATG---AYavpviraVLAQGVPLF 285
Cdd:PRK00758    1 KIVVVDNGGQYNhlIHRTLRYLGVDAKIIPNTTPVEEIKA-FEDGLILSGGP-DIERAGncpEY-------LKELDVPIL 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 286 GICLGHQMLALALGARTyklhlghRGANHPvkdlETGRVEITSQNH-----GF----------AVERASLPAGVVETHVS 350
Cdd:PRK00758   72 GICLGHQLIAKAFGGEV-------GRGEYG----EYALVEVEILDEddilkGLppeirvwashADEVKELPDGFEILARS 140

                         170       180
                  ....*....|....*....|....*..
gi 1706895447 351 lfDSTN-EGLRVEGAPAFSVQFHPEAS 376
Cdd:PRK00758  141 --DICEvEAMKHKEKPIYGVQFHPEVA 165
PLN02335 PLN02335
anthranilate synthase
 242-375 6.57e-09

anthranilate synthase


Pssm-ID: 177969 [Multi-domain]  Cd Length: 222  Bit Score: 55.96  E-value: 6.57e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 242 SADDVLRHRPDGVFLSNGPGDPAATGAyavpVIRAVLAQG--VPLFGICLGHQMLALALGARTYKLHLG--HrGANHPVK 317
Cdd:PLN02335   54 TVEELKRKNPRGVLISPGPGTPQDSGI----SLQTVLELGplVPLFGVCMGLQCIGEAFGGKIVRSPFGvmH-GKSSPVH 128

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1706895447 318 DLETGRVEITS---------QNHGFAVERASLPAGVVETHVSLFDSTNEGLRVEGAPAFS-VQFHPEA 375
Cdd:PLN02335  129 YDEKGEEGLFSglpnpftagRYHSLVIEKDTFPSDELEVTAWTEDGLIMAARHRKYKHIQgVQFHPES 196
PRK06774 PRK06774
aminodeoxychorismate synthase component II;
245-375 1.18e-08

aminodeoxychorismate synthase component II;


Pssm-ID: 180689 [Multi-domain]  Cd Length: 191  Bit Score: 54.48  E-value: 1.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 245 DVLRHRPDGVFLSNGPGDPAATGAyAVPVIRAvLAQGVPLFGICLGHQMLALALGARTYKLHLGHRGANHPVKDLETG-- 322
Cdd:PRK06774   38 DIEQLAPSHLVISPGPCTPNEAGI-SLAVIRH-FADKLPILGVCLGHQALGQAFGARVVRARQVMHGKTSAICHSGQGvf 115

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 323 ----RVEITSQNHGFAVERASLPAGVVETHVSLFDSTNE---GLRVEGAPAFSVQFHPEA 375
Cdd:PRK06774  116 rglnQPLTVTRYHSLVIAADSLPGCFELTAWSERGGEMDeimGIRHRTLPLEGVQFHPES 175
hisH PRK13141
imidazole glycerol phosphate synthase subunit HisH; Provisional
 215-294 5.14e-08

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237288 [Multi-domain]  Cd Length: 205  Bit Score: 52.83  E-value: 5.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 215 IDYGAK--RNILRCLAAAGCRVTVvpgTASADDVLRhrPDGVFLsngPGDpaatGAYA-----------VPVIRAVLAQG 281
Cdd:PRK13141    5 IDYGMGnlRSVEKALERLGAEAVI---TSDPEEILA--ADGVIL---PGV----GAFPdamanlrerglDEVIKEAVASG 72

                          90
                  ....*....|...
gi 1706895447 282 VPLFGICLGHQML 294
Cdd:PRK13141   73 KPLLGICLGMQLL 85
PRK08007 PRK08007
aminodeoxychorismate synthase component 2;
251-375 1.48e-07

aminodeoxychorismate synthase component 2;


Pssm-ID: 181194 [Multi-domain]  Cd Length: 187  Bit Score: 51.07  E-value: 1.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 251 PDGVFLSNGPGDPAATGAyAVPVIRAvLAQGVPLFGICLGHQMLALALGARTYKLHLGHRGANHPVKDLETGRVE----- 325
Cdd:PRK08007   44 PQKIVISPGPCTPDEAGI-SLDVIRH-YAGRLPILGVCLGHQAMAQAFGGKVVRAAKVMHGKTSPITHNGEGVFRglanp 121

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1706895447 326 -ITSQNHGFAVERASLPAgvvETHVSLFDSTNE--GLRVEGAPAFSVQFHPEA 375
Cdd:PRK08007  122 lTVTRYHSLVVEPDSLPA---CFEVTAWSETREimGIRHRQWDLEGVQFHPES 171
hisH PRK13143
imidazole glycerol phosphate synthase subunit HisH; Provisional
 212-294 1.53e-07

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237289 [Multi-domain]  Cd Length: 200  Bit Score: 51.41  E-value: 1.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 212 VVAIDYGAK--RNILRCLAAAGCRVTVVPGTASADDVlrhrpDGVFLSnGPGDPAATGAYAVPVIRAVLAQ---GVPLFG 286
Cdd:PRK13143    3 IVIIDYGVGnlRSVSKALERAGAEVVITSDPEEILDA-----DGIVLP-GVGAFGAAMENLSPLRDVILEAarsGKPFLG 76


                  ....*...
gi 1706895447 287 ICLGHQML 294
Cdd:PRK13143   77 ICLGMQLL 84
GATase1_IGP_Synthase cd01748
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ...
 212-295 1.60e-07

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: 51.34  E-value: 1.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 212 VVAIDYGAK--RNILRCLAAAGCRVTVvpgTASADDVLRHrpDGVFLsngPGDpaatGAYA-----------VPVIRAVL 278
Cdd:cd01748     1 IAIIDYGMGnlRSVANALERLGAEVII---TSDPEEILSA--DKLIL---PGV----GAFGdamanlrerglIEALKEAI 68

                          90
                  ....*....|....*..
gi 1706895447 279 AQGVPLFGICLGHQMLA 295
Cdd:cd01748    69 ASGKPFLGICLGMQLLF 85
PRK09065 PRK09065
glutamine amidotransferase; Provisional
 223-377 6.68e-07

glutamine amidotransferase; Provisional


Pssm-ID: 181635 [Multi-domain]  Cd Length: 237  Bit Score: 49.96  E-value: 6.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 223 ILRCLAAAGCRVTVVPgtASADDVLRHRPD--GVFLSNGPG---DPAATGAYAVPVIRAVLAQGVPLFGICLGHQMLALA 297
Cdd:PRK09065   27 IRVALGLAEQPVVVVR--VFAGEPLPAPDDfaGVIITGSWAmvtDRLDWSERTADWLRQAAAAGMPLLGICYGHQLLAHA 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 298 LGARTyklhlghrgANHPvKDLETGRVEITSQNHG-----FAVERASLPAGVveTH-----------VSLFDSTNEG--- 358
Cdd:PRK09065  105 LGGEV---------GYNP-AGRESGTVTVELHPAAaddplFAGLPAQFPAHL--THlqsvlrlppgaVVLARSAQDPhqa 172

                         170
                  ....*....|....*....
gi 1706895447 359 LRVeGAPAFSVQFHPEASP 377
Cdd:PRK09065  173 FRY-GPHAWGVQFHPEFTA 190
PRK07053 PRK07053
glutamine amidotransferase; Provisional
 274-377 6.76e-07

glutamine amidotransferase; Provisional


Pssm-ID: 235919 [Multi-domain]  Cd Length: 234  Bit Score: 49.94  E-value: 6.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 274 IRAVLAQGVPLFGICLGHQMLALALGARTYKLHlghrganhpVKdlETGRVEITSQNHGFAVERASLPAG--VVETHVSL 351
Cdd:PRK07053   76 LRQRLAAGLPTLGICLGAQLIARALGARVYPGG---------QK--EIGWAPLTLTDAGRASPLRHLGAGtpVLHWHGDT 144

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1706895447 352 FDSTNEGLRVEGAP-----AFSV-------QFHPEASP 377
Cdd:PRK07053  145 FDLPEGATLLASTPacrhqAFAWgnhvlalQFHPEARE 182
trpG CHL00101
anthranilate synthase component 2
 249-375 1.39e-06

anthranilate synthase component 2


Pssm-ID: 214365 [Multi-domain]  Cd Length: 190  Bit Score: 48.57  E-value: 1.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 249 HRPDGVFLSNGPGDPAATGaYAVPVIRAvLAQGVPLFGICLGHQMLALALGARTYKL-HLGHRGAN---HPVKDLETGRV 324
Cdd:CHL00101   42 LNIRHIIISPGPGHPRDSG-ISLDVISS-YAPYIPILGVCLGHQSIGYLFGGKIIKApKPMHGKTSkiyHNHDDLFQGLP 119

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1706895447 325 E--ITSQNHGFAVERASLPAGVVETHVSlFDSTNEGLRVEGAPA-FSVQFHPEA 375
Cdd:CHL00101  120 NpfTATRYHSLIIDPLNLPSPLEITAWT-EDGLIMACRHKKYKMlRGIQFHPES 172
PRK06490 PRK06490
glutamine amidotransferase; Provisional
 274-374 1.65e-06

glutamine amidotransferase; Provisional


Pssm-ID: 180590 [Multi-domain]  Cd Length: 239  Bit Score: 48.80  E-value: 1.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 274 IRAVLAQGVPLFGICLGHQMLAlalgartykLHLGHRGANHPvkdleTGRVEI-------TSQNHG----------FAVE 336
Cdd:PRK06490   79 ISVPLKENKPFLGICLGAQMLA---------RHLGARVAPHP-----DGRVEIgyyplrpTEAGRAlmhwpemvyhWHRE 144

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1706895447 337 RASLPAGvVETHVSLFDSTNEGLRVeGAPAFSVQFHPE 374
Cdd:PRK06490  145 GFDLPAG-AELLATGDDFPNQAFRY-GDNAWGLQFHPE 180
PRK08857 PRK08857
aminodeoxychorismate/anthranilate synthase component II;
251-390 1.66e-05

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181566 [Multi-domain]  Cd Length: 193  Bit Score: 45.25  E-value: 1.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 251 PDGVFLSNGPGDPAATGAyAVPVIRAVLAQgVPLFGICLGHQMLALALGARTYKLHLGHRGANHPVKdlETGRVEITSQN 330
Cdd:PRK08857   44 PTHLVISPGPCTPNEAGI-SLQAIEHFAGK-LPILGVCLGHQAIAQVFGGQVVRARQVMHGKTSPIR--HTGRSVFKGLN 119

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1706895447 331 --------HGFAVERASLPAGVVETHVSLFD--STNE--GLRVEGAPAFSVQFHPEaSPGPHDSHYLFGRFV 390
Cdd:PRK08857  120 npltvtryHSLVVKNDTLPECFELTAWTELEdgSMDEimGFQHKTLPIEAVQFHPE-SIKTEQGHQLLANFL 190
hisH PRK13181
imidazole glycerol phosphate synthase subunit HisH; Provisional
 212-295 5.01e-05

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 183878 [Multi-domain]  Cd Length: 199  Bit Score: 44.09  E-value: 5.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 212 VVAIDYGAK--RNILRCLAAAGCRVTVvpgTASADDVLRHrpDGVFLsngPGDPAATGAYA-------VPVIRAVLAQGV 282
Cdd:PRK13181    2 IAIIDYGAGnlRSVANALKRLGVEAVV---SSDPEEIAGA--DKVIL---PGVGAFGQAMRslresglDEALKEHVEKKQ 73

                          90
                  ....*....|...
gi 1706895447 283 PLFGICLGHQMLA 295
Cdd:PRK13181   74 PVLGICLGMQLLF 86
IMP_synth_hisH TIGR01855
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model ...
 212-294 1.26e-04

imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model represents the glutamine amidotransferase subunit (or domain, in eukaryotic systems) of imidazole glycerol phosphate synthase. This subunit catalyzes step 5 of histidine biosynthesis from PRPP. The other subunit, the cyclase, catalyzes step 6. [Amino acid biosynthesis, Histidine family]


Pssm-ID: 273836 [Multi-domain]  Cd Length: 196  Bit Score: 42.70  E-value: 1.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 212 VVAIDYGAK--RNILRCLAAAGCRVTVVPGTASADDVlrhrpDGVFLsngPGDPAATGAYA------VPVIRA-VLAQGV 282
Cdd:TIGR01855   1 IVIIDYGVGnlGSVKRALKRVGAEPVVVKDSKEAELA-----DKLIL---PGVGAFGAAMArlrengLDLFVElVVRLGK 72

                          90
                  ....*....|..
gi 1706895447 283 PLFGICLGHQML 294
Cdd:TIGR01855  73 PVLGICLGMQLL 84
PRK06895 PRK06895
anthranilate synthase component II;
254-375 3.44e-04

anthranilate synthase component II;


Pssm-ID: 235882 [Multi-domain]  Cd Length: 190  Bit Score: 41.26  E-value: 3.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 254 VFLSNGPGDPAAtgayaVPVIRAVLA---QGVPLFGICLGHQMLALALGARTYKLH---------LGHRGANHPVKDLET 321
Cdd:PRK06895   47 ILISPGPDVPRA-----YPQLFAMLEryhQHKSILGVCLGHQTLCEFFGGELYNLNnvrhgqqrpLKVRSNSPLFDGLPE 121

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1706895447 322 gRVEItSQNHGFAVERASLPAGVVETHVSlFDSTNEGLRVEGAPAFSVQFHPEA 375
Cdd:PRK06895  122 -EFNI-GLYHSWAVSEENFPTPLEITAVC-DENVVMAMQHKTLPIYGVQFHPES 172
PRK09522 PRK09522
bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate ...
 254-375 1.73e-03

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


Pssm-ID: 181927 [Multi-domain]  Cd Length: 531  Bit Score: 40.39  E-value: 1.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 254 VFLSNGPGDPAATGAyaVPVIRAVLAQGVPLFGICLGHQMLALALGARTYK----LHLGHRGANHPVKDLETGRVEITSQ 329
Cdd:PRK09522   52 LMLSPGPGVPSEAGC--MPELLTRLRGKLPIIGICLGHQAIVEAYGGYVGQageiLHGKASSIEHDGQAMFAGLTNPLPV 129

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1706895447 330 NHGFAVERASLPAGV-VETHvslFDSTNEGLRVEGAPAFSVQFHPEA 375
Cdd:PRK09522  130 ARYHSLVGSNIPAGLtINAH---FNGMVMAVRHDADRVCGFQFHPES 173
GATase1_Glutamyl_Hydrolase cd01747
Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase; Type 1 ...
 283-395 3.16e-03

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


Pssm-ID: 153218 [Multi-domain]  Cd Length: 273  Bit Score: 39.23  E-value: 3.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706895447 283 PLFGICLGHQMLA-LALGARTYKLHLGHRGANHPVK---DLETGRVE---------------ITSQNHGFAVERASLPAG 343
Cdd:cd01747    94 PVWGTCLGFELLTyLTSGETLLLEATEATNSALPLNfteDALQSRLFkrfppdllkslatepLTMNNHRYGISPENFTEN 173

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1706895447 344 --------VVETHVSL----FDSTNEGLRVegaPAFSVQFHPEASP--------GPHD------SHYLFGRFVEAMQR 395
Cdd:cd01747   174 gllsdffnVLTTNDDWngveFISTVEAYKY---PIYGVQWHPEKNAfewkksssIPHSeeairlTQYFANFFVNEARK 248
 
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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