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Conserved domains on  [gi|1033937293|gb|ANI23661|]
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carbamoylphosphate synthetase, partial [Rhaphiomidas parkeri]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK12564 super family cl36145
carbamoyl-phosphate synthase small subunit;
1-288 2.91e-125

carbamoyl-phosphate synthase small subunit;


The actual alignment was detected with superfamily member PRK12564:

Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 361.31  E-value: 2.91e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033937293   1 TDRSYRAQILVLTYPLVGNYGIPSLDdcdeyglpkhFEwTDGISVSGLVVGEVCDTPSHWQQTGTLSKWMEQQGVPGISG 80
Cdd:PRK12564   44 TDPSYAGQIVTFTYPLIGNYGVNRED----------FE-SDRPHAKGLIVRELSDIPSNWRSEMSLDEYLKENGIPGISG 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033937293  81 IDTRALTKRIRENGSILG-------------R*LQNLPSPNSdykfldpniRNLVAECSVTTSITY---NPSGSPRICAI 144
Cdd:PRK12564  113 IDTRALTRKLREKGAMKGviatedfdaeellEKARAFPGLLG---------LDLVKEVSTKEPYPWpgpGGELKYKVVAI 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033937293 145 DCGLKLNQIRCFTSRGARVDLVPWNY------ELKPtefDGLFISNGPGDPIMCAETVNEIRKCLDKfEKPIFGICLGHQ 218
Cdd:PRK12564  184 DFGVKRNILRELAERGCRVTVVPATTtaeeilALNP---DGVFLSNGPGDPAALDYAIEMIRELLEK-KIPIFGICLGHQ 259

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033937293 219 LLSTAIGCKTYKMKYGNRGHNIPCIHHGTGRCFMTSQNHGFAVDIETLPKDWEPLFTNVNDKTNEGIIHK 288
Cdd:PRK12564  260 LLALALGAKTYKMKFGHRGANHPVKDLETGKVEITSQNHGFAVDEDSLPANLEVTHVNLNDGTVEGLRHK 329
 
Name Accession Description Interval E-value
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
1-288 2.91e-125

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 361.31  E-value: 2.91e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033937293   1 TDRSYRAQILVLTYPLVGNYGIPSLDdcdeyglpkhFEwTDGISVSGLVVGEVCDTPSHWQQTGTLSKWMEQQGVPGISG 80
Cdd:PRK12564   44 TDPSYAGQIVTFTYPLIGNYGVNRED----------FE-SDRPHAKGLIVRELSDIPSNWRSEMSLDEYLKENGIPGISG 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033937293  81 IDTRALTKRIRENGSILG-------------R*LQNLPSPNSdykfldpniRNLVAECSVTTSITY---NPSGSPRICAI 144
Cdd:PRK12564  113 IDTRALTRKLREKGAMKGviatedfdaeellEKARAFPGLLG---------LDLVKEVSTKEPYPWpgpGGELKYKVVAI 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033937293 145 DCGLKLNQIRCFTSRGARVDLVPWNY------ELKPtefDGLFISNGPGDPIMCAETVNEIRKCLDKfEKPIFGICLGHQ 218
Cdd:PRK12564  184 DFGVKRNILRELAERGCRVTVVPATTtaeeilALNP---DGVFLSNGPGDPAALDYAIEMIRELLEK-KIPIFGICLGHQ 259

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033937293 219 LLSTAIGCKTYKMKYGNRGHNIPCIHHGTGRCFMTSQNHGFAVDIETLPKDWEPLFTNVNDKTNEGIIHK 288
Cdd:PRK12564  260 LLALALGAKTYKMKFGHRGANHPVKDLETGKVEITSQNHGFAVDEDSLPANLEVTHVNLNDGTVEGLRHK 329
CPSaseIIsmall TIGR01368
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ...
 1-288 1.61e-123

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: 356.55  E-value: 1.61e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033937293   1 TDRSYRAQILVLTYPLVGNYGIPslddcdeyglPKHFEwTDGISVSGLVVGEVCDTPSHWQQTGTLSKWMEQQGVPGISG 80
Cdd:TIGR01368  40 TDPSYKGQIVVFTYPLIGNYGVN----------DEDAE-SKGIHVSGLVVRELSDRYSNWRATESLDQFLKRHGIPGIYG 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033937293  81 IDTRALTKRIRENGSILGR*LQNLPSPNSDYK---FLDPNIR--NLVAECSVTTSITYNPSGSP--RICAIDCGLKLNQI 153
Cdd:TIGR01368 109 VDTRALVKKIREKGTMKGV-ISTEDSNDEELVekaRVSPDITgiNLVAEVSTKEPYTWGQRGGKgkRVVVIDFGVKRNIL 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033937293 154 RCFTSRGARVDLVPWNY---ELKPTEFDGLFISNGPGDPIMCAETVNEIRKCLDKfeKPIFGICLGHQLLSTAIGCKTYK 230
Cdd:TIGR01368 188 RRLVKRGCEVTVVPYDTdaeEIKKYNPDGIFLSNGPGDPAAVEPAIETIRKLLEK--IPIFGICLGHQLLALAFGAKTYK 265

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1033937293 231 MKYGNRGHNIPCIHHGTGRCFMTSQNHGFAVDIETLPK-DWEPLFTNVNDKTNEGIIHK 288
Cdd:TIGR01368 266 MKFGHRGGNHPVKDLITGRVEITSQNHGYAVDPDSLPAgDLEVTHVNLNDGTVEGIRHK 324
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 1-288 1.43e-122

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: 354.33  E-value: 1.43e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033937293   1 TDRSYRAQILVLTYPLVGNYGIPSLDdcdeyglpkhFEwTDGISVSGLVVGEVCDTPSHWQQTGTLSKWMEQQGVPGISG 80
Cdd:COG0505    44 TDPSYAGQIVTFTYPHIGNYGVNDED----------FE-SDRPWVAGLVVRELSRRPSNWRSEESLDEYLKEHGIPGISG 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033937293  81 IDTRALTKRIRENGSILG-------------R*LQNLPSPNSdykfldpniRNLVAECSVTTSITYNPSG--SPRICAID 145
Cdd:COG0505   113 IDTRALTRHLREKGAMKGvistgdldieellEKARAAPGMEG---------LDLVKEVSTKEPYEWTEAPgaGFHVVALD 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033937293 146 CGLKLNQIRCFTSRGARVDLVPWNY------ELKPtefDGLFISNGPGDPIMCAETVNEIRKCLDKfEKPIFGICLGHQL 219
Cdd:COG0505   184 FGVKRNILRELAERGCRVTVVPATTsaeeilALNP---DGVFLSNGPGDPAALDYAIETIRELLGK-GIPIFGICLGHQL 259

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033937293 220 LSTAIGCKTYKMKYGNRGHNIPCIHHGTGRCFMTSQNHGFAVDIETLPK-DWEPLFTNVNDKTNEGIIHK 288
Cdd:COG0505   260 LALALGAKTYKLKFGHRGANHPVKDLETGRVEITSQNHGFAVDEDSLPAtDLEVTHVNLNDGTVEGLRHK 329
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 141-288 4.07e-86

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: 255.11  E-value: 4.07e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033937293 141 ICAIDCGLKLNQIRCFTSRGARVDLVPWNYELKPT---EFDGLFISNGPGDPIMCAETVNEIRKCLDKfEKPIFGICLGH 217
Cdd:cd01744     1 VVVIDFGVKHNILRELLKRGCEVTVVPYNTDAEEIlklDPDGIFLSNGPGDPALLDEAIKTVRKLLGK-KIPIFGICLGH 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1033937293 218 QLLSTAIGCKTYKMKYGNRGHNIPCIHHGTGRCFMTSQNHGFAVDIETLPKDWEPLFTNVNDKTNEGIIHK 288
Cdd:cd01744    80 QLLALALGAKTYKMKFGHRGSNHPVKDLITGRVYITSQNHGYAVDPDSLPGGLEVTHVNLNDGTVEGIRHK 150
GATase pfam00117
Glutamine amidotransferase class-I;
144-288 6.54e-48

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 158.17  E-value: 6.54e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033937293 144 IDCGL--KLNQIRCFTSRGARVDLVPWNY---ELKPTEFDGLFISNGPGDPIMCAETVNEIRKCLDkFEKPIFGICLGHQ 218
Cdd:pfam00117   3 IDNGDsfTYNLARALRELGVEVTVVPNDTpaeEILEENPDGIILSGGPGSPGAAGGAIEAIREARE-LKIPILGICLGHQ 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1033937293 219 LLSTAIGCKTYKMK-YGNRGHNIPCIH------HGTGRCFMTSQNHGFAVDIETLPKDWEPLFTNVNDKTNEGIIHK 288
Cdd:pfam00117  82 LLALAFGGKVVKAKkFGHHGKNSPVGDdgcglfYGLPNVFIVRRYHSYAVDPDTLPDGLEVTATSENDGTIMGIRHK 158
CPSase_sm_chain smart01097
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 1-98 7.98e-43

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: 142.90  E-value: 7.98e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033937293    1 TDRSYRAQILVLTYPLVGNYGIPSLDdcdeyglpkhFEwTDGISVSGLVVGEVCDTPSHWQQTGTLSKWMEQQGVPGISG 80
Cdd:smart01097  42 TDPSYAGQIVVFTYPLIGNYGVNDED----------FE-SDKIQVKGLVVRELSDEPSNWRSEQSLDEFLKENGIPGISG 110

                           90
                   ....*....|....*...
gi 1033937293   81 IDTRALTKRIRENGSILG 98
Cdd:smart01097 111 IDTRALTRKLREKGAMKG 128
 
Name Accession Description Interval E-value
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
1-288 2.91e-125

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 361.31  E-value: 2.91e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033937293   1 TDRSYRAQILVLTYPLVGNYGIPSLDdcdeyglpkhFEwTDGISVSGLVVGEVCDTPSHWQQTGTLSKWMEQQGVPGISG 80
Cdd:PRK12564   44 TDPSYAGQIVTFTYPLIGNYGVNRED----------FE-SDRPHAKGLIVRELSDIPSNWRSEMSLDEYLKENGIPGISG 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033937293  81 IDTRALTKRIRENGSILG-------------R*LQNLPSPNSdykfldpniRNLVAECSVTTSITY---NPSGSPRICAI 144
Cdd:PRK12564  113 IDTRALTRKLREKGAMKGviatedfdaeellEKARAFPGLLG---------LDLVKEVSTKEPYPWpgpGGELKYKVVAI 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033937293 145 DCGLKLNQIRCFTSRGARVDLVPWNY------ELKPtefDGLFISNGPGDPIMCAETVNEIRKCLDKfEKPIFGICLGHQ 218
Cdd:PRK12564  184 DFGVKRNILRELAERGCRVTVVPATTtaeeilALNP---DGVFLSNGPGDPAALDYAIEMIRELLEK-KIPIFGICLGHQ 259

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033937293 219 LLSTAIGCKTYKMKYGNRGHNIPCIHHGTGRCFMTSQNHGFAVDIETLPKDWEPLFTNVNDKTNEGIIHK 288
Cdd:PRK12564  260 LLALALGAKTYKMKFGHRGANHPVKDLETGKVEITSQNHGFAVDEDSLPANLEVTHVNLNDGTVEGLRHK 329
CPSaseIIsmall TIGR01368
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ...
 1-288 1.61e-123

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: 356.55  E-value: 1.61e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033937293   1 TDRSYRAQILVLTYPLVGNYGIPslddcdeyglPKHFEwTDGISVSGLVVGEVCDTPSHWQQTGTLSKWMEQQGVPGISG 80
Cdd:TIGR01368  40 TDPSYKGQIVVFTYPLIGNYGVN----------DEDAE-SKGIHVSGLVVRELSDRYSNWRATESLDQFLKRHGIPGIYG 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033937293  81 IDTRALTKRIRENGSILGR*LQNLPSPNSDYK---FLDPNIR--NLVAECSVTTSITYNPSGSP--RICAIDCGLKLNQI 153
Cdd:TIGR01368 109 VDTRALVKKIREKGTMKGV-ISTEDSNDEELVekaRVSPDITgiNLVAEVSTKEPYTWGQRGGKgkRVVVIDFGVKRNIL 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033937293 154 RCFTSRGARVDLVPWNY---ELKPTEFDGLFISNGPGDPIMCAETVNEIRKCLDKfeKPIFGICLGHQLLSTAIGCKTYK 230
Cdd:TIGR01368 188 RRLVKRGCEVTVVPYDTdaeEIKKYNPDGIFLSNGPGDPAAVEPAIETIRKLLEK--IPIFGICLGHQLLALAFGAKTYK 265

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1033937293 231 MKYGNRGHNIPCIHHGTGRCFMTSQNHGFAVDIETLPK-DWEPLFTNVNDKTNEGIIHK 288
Cdd:TIGR01368 266 MKFGHRGGNHPVKDLITGRVEITSQNHGYAVDPDSLPAgDLEVTHVNLNDGTVEGIRHK 324
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 1-288 1.43e-122

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: 354.33  E-value: 1.43e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033937293   1 TDRSYRAQILVLTYPLVGNYGIPSLDdcdeyglpkhFEwTDGISVSGLVVGEVCDTPSHWQQTGTLSKWMEQQGVPGISG 80
Cdd:COG0505    44 TDPSYAGQIVTFTYPHIGNYGVNDED----------FE-SDRPWVAGLVVRELSRRPSNWRSEESLDEYLKEHGIPGISG 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033937293  81 IDTRALTKRIRENGSILG-------------R*LQNLPSPNSdykfldpniRNLVAECSVTTSITYNPSG--SPRICAID 145
Cdd:COG0505   113 IDTRALTRHLREKGAMKGvistgdldieellEKARAAPGMEG---------LDLVKEVSTKEPYEWTEAPgaGFHVVALD 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033937293 146 CGLKLNQIRCFTSRGARVDLVPWNY------ELKPtefDGLFISNGPGDPIMCAETVNEIRKCLDKfEKPIFGICLGHQL 219
Cdd:COG0505   184 FGVKRNILRELAERGCRVTVVPATTsaeeilALNP---DGVFLSNGPGDPAALDYAIETIRELLGK-GIPIFGICLGHQL 259

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033937293 220 LSTAIGCKTYKMKYGNRGHNIPCIHHGTGRCFMTSQNHGFAVDIETLPK-DWEPLFTNVNDKTNEGIIHK 288
Cdd:COG0505   260 LALALGAKTYKLKFGHRGANHPVKDLETGRVEITSQNHGFAVDEDSLPAtDLEVTHVNLNDGTVEGLRHK 329
PRK12838 PRK12838
carbamoyl phosphate synthase small subunit; Reviewed
 1-288 1.34e-96

carbamoyl phosphate synthase small subunit; Reviewed


Pssm-ID: 183784 [Multi-domain]  Cd Length: 354  Bit Score: 288.33  E-value: 1.34e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033937293   1 TDRSYRAQILVLTYPLVGNYGIPSLDdcdeyglpkhFEWTDgISVSGLVVGEVCDTPSHWQQTGTLSKWMEQQGVPGISG 80
Cdd:PRK12838   42 TDPSYKGQIVVFTYPLIGNYGINADD----------YESKQ-PQVKGVIVYELSREGSHYRAKQSLDDFLKEWNIPGISG 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033937293  81 IDTRALTKRIRENGSILGR*LQNLPSPNSDYKFLDPNIRNLVAECSVTTSITYnPSGSPRICAIDCGLKLNQIRCFTSRG 160
Cdd:PRK12838  111 VDTRALVKHIREKGTMKASITTTDDAHAFDQIKALVLPKNVVAQVSTKEPYTY-GNGGKHVALIDFGYKKSILRSLSKRG 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033937293 161 ARVDLVPWN------YELKPtefDGLFISNGPGDPIMCAETVNEIRKCLDKFekPIFGICLGHQLLSTAIGCKTYKMKYG 234
Cdd:PRK12838  190 CKVTVLPYDtsleeiKNLNP---DGIVLSNGPGDPKELQPYLPEIKKLISSY--PILGICLGHQLIALALGADTEKLPFG 264

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1033937293 235 NRGHNIPCIHHGTGRCFMTSQNHGFAVDIETL-PKDWEPLFTNVNDKTNEGIIHK 288
Cdd:PRK12838  265 HRGANHPVIDLTTGRVWMTSQNHGYVVDEDSLdGTPLSVRFFNVNDGSIEGLRHK 319
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 141-288 4.07e-86

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: 255.11  E-value: 4.07e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033937293 141 ICAIDCGLKLNQIRCFTSRGARVDLVPWNYELKPT---EFDGLFISNGPGDPIMCAETVNEIRKCLDKfEKPIFGICLGH 217
Cdd:cd01744     1 VVVIDFGVKHNILRELLKRGCEVTVVPYNTDAEEIlklDPDGIFLSNGPGDPALLDEAIKTVRKLLGK-KIPIFGICLGH 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1033937293 218 QLLSTAIGCKTYKMKYGNRGHNIPCIHHGTGRCFMTSQNHGFAVDIETLPKDWEPLFTNVNDKTNEGIIHK 288
Cdd:cd01744    80 QLLALALGAKTYKMKFGHRGSNHPVKDLITGRVYITSQNHGYAVDPDSLPGGLEVTHVNLNDGTVEGIRHK 150
carA CHL00197
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
 1-287 1.03e-56

carbamoyl-phosphate synthase arginine-specific small subunit; Provisional


Pssm-ID: 214392 [Multi-domain]  Cd Length: 382  Bit Score: 186.93  E-value: 1.03e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033937293   1 TDRSYRAQILVLTYPLVGNYGIpSLDDCDeyglpkhfewTDGISVSGLVVGEVCDTPSHWQQTGTLSKWMEQQGVPGISG 80
Cdd:CHL00197   46 TDPSYFEQIVTFTYPEIGNTGI-NLEDIE----------SVKIQVKGIIAKNICKSSSNWRQQESLVSYLQRHKIPFIFG 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033937293  81 IDTRALTKRIRENGSILG-------------R*LQNLPS-----------PNSDYKFLDPNIRNLVAECSVTTSITYnps 136
Cdd:CHL00197  115 IDTRALTQHLRRFGTMNGcisnqnlnlsylrAKIKESPHmpssdliprvtTSSYYEWDEKSHPSFYLADNKRPHSSY--- 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033937293 137 gSPRICAIDCGLKLNQIRCFTSRGARVDLVPWNYELKPTEF---DGLFISNGPGDPIMCAETVNEIRKCLDKfEKPIFGI 213
Cdd:CHL00197  192 -QLKIIVIDFGVKYNILRRLKSFGCSITVVPATSPYQDILSyqpDGILLSNGPGDPSAIHYGIKTVKKLLKY-NIPIFGI 269

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033937293 214 CLGHQLLSTAIGCKTYKMKYGNRGhnipcIHHGTG---RCFMTSQNHGFAVDIETLPKDwePLFT---NVNDKTNEGIIH 287
Cdd:CHL00197  270 CMGHQILSLALEAKTFKLKFGHRG-----LNHPSGlnqQVEITSQNHGFAVNLESLAKN--KFYIthfNLNDGTVAGISH 342
PLN02771 PLN02771
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
 1-285 4.92e-49

carbamoyl-phosphate synthase (glutamine-hydrolyzing)


Pssm-ID: 178370 [Multi-domain]  Cd Length: 415  Bit Score: 167.85  E-value: 4.92e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033937293   1 TDRSYRAQILVLTYPLVGNYGIpSLDDcdeyglpkhfEWTDGISVSGLVVGEVCDTPSHWQQTGTLSKWMEQQGVPGISG 80
Cdd:PLN02771   96 TDPSYAGQFVLMTNPHIGNTGV-NFDD----------EESRQCFLAGLVIRSLSISTSNWRCTKTLGDYLAERNIMGIYD 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033937293  81 IDTRALTKRIRENGS------------------------ILGR*LQNLPSPNSDYKFLDPNIRNLVAECSVTTSITYnps 136
Cdd:PLN02771  165 VDTRAITRRLREDGSligvlstedsktdeellkmsrswdIVGIDLISGVSCKSPYEWVDKTNPEWDFNTNSRDGESY--- 241

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033937293 137 gspRICAIDCGLKLNQIRCFTSRGARVDLVPWNY------ELKPtefDGLFISNGPGDPIMCAETVNEIRKCLDKFekPI 210
Cdd:PLN02771  242 ---HVIAYDFGIKHNILRRLASYGCKITVVPSTWpasealKMKP---DGVLFSNGPGDPSAVPYAVETVKELLGKV--PV 313

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1033937293 211 FGICLGHQLLSTAIGCKTYKMKYGNRGHNIPCIHHGTGRCFMTSQNHGFAVDIETLPKDWEPLFTNVNDKTNEGI 285
Cdd:PLN02771  314 FGICMGHQLLGQALGGKTFKMKFGHHGGNHPVRNNRTGRVEISAQNHNYAVDPASLPEGVEVTHVNLNDGSCAGL 388
GATase pfam00117
Glutamine amidotransferase class-I;
144-288 6.54e-48

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 158.17  E-value: 6.54e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033937293 144 IDCGL--KLNQIRCFTSRGARVDLVPWNY---ELKPTEFDGLFISNGPGDPIMCAETVNEIRKCLDkFEKPIFGICLGHQ 218
Cdd:pfam00117   3 IDNGDsfTYNLARALRELGVEVTVVPNDTpaeEILEENPDGIILSGGPGSPGAAGGAIEAIREARE-LKIPILGICLGHQ 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1033937293 219 LLSTAIGCKTYKMK-YGNRGHNIPCIH------HGTGRCFMTSQNHGFAVDIETLPKDWEPLFTNVNDKTNEGIIHK 288
Cdd:pfam00117  82 LLALAFGGKVVKAKkFGHHGKNSPVGDdgcglfYGLPNVFIVRRYHSYAVDPDTLPDGLEVTATSENDGTIMGIRHK 158
CPSase_sm_chain pfam00988
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 1-99 5.32e-46

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: 150.94  E-value: 5.32e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033937293   1 TDRSYRAQILVLTYPLVGNYGIPSLDdcdeyglpkhFEwTDGISVSGLVVGEVCDTPSHWQQTGTLSKWMEQQGVPGISG 80
Cdd:pfam00988  38 TDPSYAGQIVVFTYPLIGNYGVNPED----------FE-SDKIHVAGLVVREYSDEPSNWRAEESLDEWLKEQGIPGISG 106

                          90
                  ....*....|....*....
gi 1033937293  81 IDTRALTKRIRENGSILGR 99
Cdd:pfam00988 107 VDTRALTRKIREKGAMKGV 125
CPSase_sm_chain smart01097
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 1-98 7.98e-43

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: 142.90  E-value: 7.98e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033937293    1 TDRSYRAQILVLTYPLVGNYGIPSLDdcdeyglpkhFEwTDGISVSGLVVGEVCDTPSHWQQTGTLSKWMEQQGVPGISG 80
Cdd:smart01097  42 TDPSYAGQIVVFTYPLIGNYGVNDED----------FE-SDKIQVKGLVVRELSDEPSNWRSEQSLDEFLKENGIPGISG 110

                           90
                   ....*....|....*...
gi 1033937293   81 IDTRALTKRIRENGSILG 98
Cdd:smart01097 111 IDTRALTRKLREKGAMKG 128
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 156-287 1.33e-14

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: 70.26  E-value: 1.33e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033937293 156 FTSRGARVDLVPWN----YELKPTEFDGLFISNGPGDPiMCAETVNEIRKCLDKfEKPIFGICLGHQLLSTAIGCKTYKM 231
Cdd:cd01743    18 LRELGAEVVVVRNDeitlEELELLNPDAIVISPGPGHP-EDAGISLEIIRALAG-KVPILGVCLGHQAIAEAFGGKVVRA 95

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1033937293 232 KYGNRGHNIPCIHHGTGRCFMTSQN------HGFAVDIETLPKDWEplftnVNDKTNEGIIH 287
Cdd:cd01743    96 PEPMHGKTSEIHHDGSGLFKGLPQPftvgryHSLVVDPDPLPDLLE-----VTASTEDGVIM 152
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 174-276 1.01e-11

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: 62.26  E-value: 1.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033937293 174 PTEFDGLFISNGP------GDPIMcAETVNEIRKCLDKfEKPIFGICLGHQLLSTAIGCKTYKMKYG-----------NR 236
Cdd:cd01741    44 LDDYDGLVILGGPmsvdedDYPWL-KKLKELIRQALAA-GKPVLGICLGHQLLARALGGKVGRNPKGweigwfpvtltEA 121

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1033937293 237 GHNIPcIHHGTGRCFMTSQNHGFAVdiETLPKDWEPLFTN 276
Cdd:cd01741   122 GKADP-LFAGLPDEFPVFHWHGDTV--VELPPGAVLLASS 158
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 153-220 4.50e-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: 58.76  E-value: 4.50e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1033937293 153 IRCFTSRGARVDLVPWN-----YELKPTEFDGLFISNGPGDP---IMCAETVNEIRKCLDKfEKPIFGICLGHQLL 220
Cdd:cd01653    18 LDALREAGAEVDVVSPDggpveSDVDLDDYDGLILPGGPGTPddlARDEALLALLREAAAA-GKPILGICLGAQLL 92
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 153-220 1.07e-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: 57.21  E-value: 1.07e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1033937293 153 IRCFTSRGARVDLVPWN-----YELKPTEFDGLFISNGPGDPIMCAETVNEIRKCLDKFE--KPIFGICLGHQLL 220
Cdd:cd03128    18 LDALREAGAEVDVVSPDggpveSDVDLDDYDGLILPGGPGTPDDLAWDEALLALLREAAAagKPVLGICLGAQLL 92
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 164-288 2.70e-09

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: 56.11  E-value: 2.70e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033937293 164 DLVPWNYElkPTEFDGLFISNGPGDPIMCAETVNEIRKCLDKF---EKPIFGICLGHQLLSTAIGCKTYKMKYGNRG--- 237
Cdd:COG0518    38 EILPYDPD--LEDPDGLILSGGPMSVYDEDPWLEDEPALIREAfelGKPVLGICYGAQLLAHALGGKVEPGPGREIGwap 115

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1033937293 238 ----------HNIPcihhGTGRCFMTsqnHGFAVDieTLPKDWEPLFTNVNDKtNEGIIHK 288
Cdd:COG0518   116 velteadplfAGLP----DEFTVWMS---HGDTVT--ELPEGAEVLASSDNCP-NQAFRYG 166
PRK07765 PRK07765
aminodeoxychorismate/anthranilate synthase component II;
176-286 9.04e-09

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181107 [Multi-domain]  Cd Length: 214  Bit Score: 54.29  E-value: 9.04e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033937293 176 EFDGLFISNGPGDPIMCAETVNEIRKCLDKfEKPIFGICLGHQLLSTAIGC-----------KTYKMKYGNRGhnipcIH 244
Cdd:PRK07765   46 QFDGVLLSPGPGTPERAGASIDMVRACAAA-GTPLLGVCLGHQAIGVAFGAtvdrapellhgKTSSVHHTGVG-----VL 119

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1033937293 245 HGTGRCFMTSQNHGFAVDIETLPKDWEplftnVNDKTNEGII 286
Cdd:PRK07765  120 AGLPDPFTATRYHSLTILPETLPAELE-----VTARTDSGVI 156
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 162-246 1.75e-08

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: 53.12  E-value: 1.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033937293 162 RVDLVPWNyELKPTEFDGLFISNGPGDP----IMCAetVneIRKCLDKfeKPIFGICLGHQLLSTAIGCKTYKMKYgnrg 237
Cdd:COG0512    29 RNDEITLE-EIEALAPDGIVLSPGPGTPeeagISLE--V--IRAFAGK--IPILGVCLGHQAIGEAFGGKVVRAPE---- 97


                  ....*....
gi 1033937293 238 hnipcIHHG 246
Cdd:COG0512    98 -----PMHG 101
PRK06774 PRK06774
aminodeoxychorismate synthase component II;
151-271 1.21e-07

aminodeoxychorismate synthase component II;


Pssm-ID: 180689 [Multi-domain]  Cd Length: 191  Bit Score: 51.02  E-value: 1.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033937293 151 NQIRCFTSRGARVdLVPWNYELKPTEFDGL-----FISNGPGDPIMCAETVNEIRKCLDKFekPIFGICLGHQLLSTAIG 225
Cdd:PRK06774   14 NLYQYFCELGTEV-MVKRNDELQLTDIEQLapshlVISPGPCTPNEAGISLAVIRHFADKL--PILGVCLGHQALGQAFG 90

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1033937293 226 CKTYKMKYGNRG------HNIPCIHHGTGRCFMTSQNHGFAVDIETLPKDWE 271
Cdd:PRK06774   91 ARVVRARQVMHGktsaicHSGQGVFRGLNQPLTVTRYHSLVIAADSLPGCFE 142
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 171-288 1.56e-07

anthranilate synthase component II; Provisional


Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 50.51  E-value: 1.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033937293 171 ELKPtefDGLFISNGPGDPimcaetvNEIRKCLD-----KFEKPIFGICLGHQLLSTAIGCKTykmkygNRGHNI----- 240
Cdd:PRK05670   41 ALNP---DAIVLSPGPGTP-------AEAGISLElirefAGKVPILGVCLGHQAIGEAFGGKV------VRAKEImhgkt 104

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1033937293 241 -PCIHHGTG------RCFMTSQNHGFAVDIETLPKDWEplftnVNDKTNEGII----HK 288
Cdd:PRK05670  105 sPIEHDGSGifaglpNPFTVTRYHSLVVDRESLPDCLE-----VTAWTDDGEImgvrHK 158
PRK14607 PRK14607
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
171-272 5.32e-07

bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;


Pssm-ID: 237764 [Multi-domain]  Cd Length: 534  Bit Score: 50.49  E-value: 5.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033937293 171 ELKPTEfdgLFISNGPGDPIMCAETVNEIRKCLDKFekPIFGICLGHQLLSTAIGCKTYKMKYGNRGHNIPCIHHGTGrC 250
Cdd:PRK14607   42 ALNPSH---IVISPGPGRPEEAGISVEVIRHFSGKV--PILGVCLGHQAIGYAFGGKIVHAKRILHGKTSPIDHNGKG-L 115

                          90       100
                  ....*....|....*....|....*....
gi 1033937293 251 FMTSQN-------HGFAVDIETLPKDWEP 272
Cdd:PRK14607  116 FRGIPNptvatryHSLVVEEASLPECLEV 144
PLN02889 PLN02889
oxo-acid-lyase/anthranilate synthase
 177-273 5.72e-07

oxo-acid-lyase/anthranilate synthase


Pssm-ID: 215481 [Multi-domain]  Cd Length: 918  Bit Score: 50.62  E-value: 5.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033937293 177 FDGLFISNGPGDPiMCAETV----NEIRKCLDKfekPIFGICLGHQLL-----------STAIGCKTYKMKY-GNR-GHN 239
Cdd:PLN02889  132 FDNIVISPGPGSP-TCPADIgiclRLLLECRDI---PILGVCLGHQALgyvhgarivhaPEPVHGRLSEIEHnGCRlFDD 207

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1033937293 240 IPcihHGTGRCFMTSQNHGFAVDIETLPKDWEPL 273
Cdd:PLN02889  208 IP---SGRNSGFKVVRYHSLVIDAESLPKELVPI 238
PRK08007 PRK08007
aminodeoxychorismate synthase component 2;
151-271 1.03e-06

aminodeoxychorismate synthase component 2;


Pssm-ID: 181194 [Multi-domain]  Cd Length: 187  Bit Score: 47.99  E-value: 1.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033937293 151 NQIRCFTSRGARVdLVPWNYELKPTEFDGL-----FISNGPGDPIMCAETVNEIRKCLDKFekPIFGICLGHQLLSTAIG 225
Cdd:PRK08007   14 NLYQYFCELGADV-LVKRNDALTLADIDALkpqkiVISPGPCTPDEAGISLDVIRHYAGRL--PILGVCLGHQAMAQAFG 90

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1033937293 226 CKTYKMKYGNRGHNIPCIHHGTG------RCFMTSQNHGFAVDIETLPKDWE 271
Cdd:PRK08007   91 GKVVRAAKVMHGKTSPITHNGEGvfrglaNPLTVTRYHSLVVEPDSLPACFE 142
trpG_papA TIGR00566
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ...
 151-267 1.10e-06

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: 47.86  E-value: 1.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033937293 151 NQIRCFTSRGARVdLVPWNYELKPTEFDGLF-----ISNGPGDPIMCAETVNEIRKCLDKFekPIFGICLGHQLLSTAIG 225
Cdd:TIGR00566  14 NLVQYFCELGAEV-VVKRNDSLTLQEIEALLpllivISPGPCTPNEAGISLEAIRHFAGKL--PILGVCLGHQAMGQAFG 90

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1033937293 226 CKTYKMKYGNRGHNIPCIHHGTGRC------FMTSQNHGFAVDIETLP 267
Cdd:TIGR00566  91 GDVVRANTVMHGKTSEIEHNGAGIFrglfnpLTATRYHSLVVEPETLP 138
PRK07649 PRK07649
aminodeoxychorismate/anthranilate synthase component II;
171-288 5.83e-06

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181066 [Multi-domain]  Cd Length: 195  Bit Score: 45.95  E-value: 5.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033937293 171 ELKPtefDGLFISNGPGDPIMCAETVNEIRKCLDKFekPIFGICLGHQLLSTAIGCKTYKM------KYGNRGHNIPCIH 244
Cdd:PRK07649   41 NMKP---DFLMISPGPCSPNEAGISMEVIRYFAGKI--PIFGVCLGHQSIAQVFGGEVVRAerlmhgKTSLMHHDGKTIF 115

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1033937293 245 HGTGRCFMTSQNHGFAVDIETLPKDWEplftnVNDKTNEG----IIHK 288
Cdd:PRK07649  116 SDIPNPFTATRYHSLIVKKETLPDCLE-----VTSWTEEGeimaIRHK 158
PRK00758 PRK00758
GMP synthase subunit A; Validated
 178-234 4.44e-05

GMP synthase subunit A; Validated


Pssm-ID: 179112 [Multi-domain]  Cd Length: 184  Bit Score: 43.30  E-value: 4.44e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033937293 178 DGLFISNGPgdpimcaeTVNEIRKC---LDKFEKPIFGICLGHQLLSTAIGCKTYKMKYG 234
Cdd:PRK00758   43 DGLILSGGP--------DIERAGNCpeyLKELDVPILGICLGHQLIAKAFGGEVGRGEYG 94
guaA_Nterm TIGR00888
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ...
 141-225 4.65e-05

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: 43.07  E-value: 4.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033937293 141 ICAIDCGLKLNQIRCFTSRGARV--DLVPWNY---ELKPTEFDGLFISNGPGdpIMCAETVNEIRKCLDKFEKPIFGICL 215
Cdd:TIGR00888   1 ILVLDFGSQYTQLIARRLRELGVysELVPNTTpleEIREKNPKGIILSGGPS--SVYAENAPRADEKIFELGVPVLGICY 78

                          90
                  ....*....|
gi 1033937293 216 GHQLLSTAIG 225
Cdd:TIGR00888  79 GMQLMAKQLG 88
PLN02335 PLN02335
anthranilate synthase
 171-269 6.60e-05

anthranilate synthase


Pssm-ID: 177969 [Multi-domain]  Cd Length: 222  Bit Score: 43.25  E-value: 6.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033937293 171 ELKPTEFDGLFISNGPGDPI---MCAETVNEIRKcldkfEKPIFGICLGHQLLSTAIGCKTYKMKYG-NRGHNIPCIH-- 244
Cdd:PLN02335   57 ELKRKNPRGVLISPGPGTPQdsgISLQTVLELGP-----LVPLFGVCMGLQCIGEAFGGKIVRSPFGvMHGKSSPVHYde 131

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1033937293 245 -------HGTGRCFMTSQNHGFAVDIETLPKD 269
Cdd:PLN02335  132 kgeeglfSGLPNPFTAGRYHSLVIEKDTFPSD 163
PRK08857 PRK08857
aminodeoxychorismate/anthranilate synthase component II;
172-271 2.01e-04

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181566 [Multi-domain]  Cd Length: 193  Bit Score: 41.40  E-value: 2.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033937293 172 LKPTEfdgLFISNGPGDPIMCAETVNEIRKCLDKFekPIFGICLGHQLLSTAIGCKTYKMKYGNRGHNIPCIHhgTGRCF 251
Cdd:PRK08857   42 LNPTH---LVISPGPCTPNEAGISLQAIEHFAGKL--PILGVCLGHQAIAQVFGGQVVRARQVMHGKTSPIRH--TGRSV 114

                          90       100
                  ....*....|....*....|....*...
gi 1033937293 252 MTSQN--------HGFAVDIETLPKDWE 271
Cdd:PRK08857  115 FKGLNnpltvtryHSLVVKNDTLPECFE 142
PRK08250 PRK08250
glutamine amidotransferase; Provisional
 176-227 4.11e-04

glutamine amidotransferase; Provisional


Pssm-ID: 181323 [Multi-domain]  Cd Length: 235  Bit Score: 40.72  E-value: 4.11e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1033937293 176 EFDGLFISNGPGDPimcAETVNE------------IRKCLdKFEKPIFGICLGHQLLSTAIGCK 227
Cdd:PRK08250   45 GFDLLIVMGGPQSP---RTTREEcpyfdskaeqrlINQAI-KAGKAVIGVCLGAQLIGEALGAK 104
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 199-242 5.00e-04

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: 40.32  E-value: 5.00e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1033937293 199 IRKCLDKfEKPIFGICLGHQLLSTAIGCKTY---KMKYGNRGHNIPC 242
Cdd:pfam07722  98 IRAALAR-GKPILGICRGFQLLNVALGGTLYqdiQEQPGFTDHREHC 143
GATase1_Glutamyl_Hydrolase cd01747
Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase; Type 1 ...
 158-280 6.61e-04

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


Pssm-ID: 153218 [Multi-domain]  Cd Length: 273  Bit Score: 40.38  E-value: 6.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033937293 158 SRGARVdlVPWNYELKPTEFDGLFIS-NG---PG-----DPIMCAETVNEI-RKCLDKFEK----PIFGICLGHQLLS-- 221
Cdd:cd01747    31 SAGARV--VPIWINESEEYYDKLFKSiNGilfPGgavdiDTSGYARTAKIIyNLALERNDAgdyfPVWGTCLGFELLTyl 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033937293 222 ------TAIGCKT--YKMKYGNRGHNIPC----------IHHGTGRCFmTSQNHGFAVDIETLP-----KDWEPLFTNVN 278
Cdd:cd01747   109 tsgetlLLEATEAtnSALPLNFTEDALQSrlfkrfppdlLKSLATEPL-TMNNHRYGISPENFTengllSDFFNVLTTND 187


                  ..
gi 1033937293 279 DK 280
Cdd:cd01747   188 DW 189
GATase1_GMP_Synthase cd01742
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ...
 160-225 1.07e-03

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: 39.06  E-value: 1.07e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1033937293 160 GARVDLVPWNY---ELKPTEFDGLFISNGPG---DPimCAETVNEIrkcLDKFEKPIFGICLGHQLLSTAIG 225
Cdd:cd01742    22 GVYSEILPNTTpleEIKLKNPKGIILSGGPSsvyEE--DAPRVDPE---IFELGVPVLGICYGMQLIAKALG 88
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 177-225 2.62e-03

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: 37.94  E-value: 2.62e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1033937293 177 FDGLFISNGP--------GDPIMCAETVNEIRkclDKFE-----------KPIFGICLGHQLLSTAIG 225
Cdd:cd01745    54 LDGLLLTGGGdvdpplygEEPHPELGPIDPER---DAFElallraalergKPILGICRGMQLLNVALG 118
trpG CHL00101
anthranilate synthase component 2
 171-286 7.04e-03

anthranilate synthase component 2


Pssm-ID: 214365 [Multi-domain]  Cd Length: 190  Bit Score: 36.63  E-value: 7.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033937293 171 ELKPTEFDGLFISNGPGDPIMCAETVNEIRKCLDKFekPIFGICLGHQLLSTAIGCKTYKMKYGNRG------HNIPCIH 244
Cdd:CHL00101   38 KIKNLNIRHIIISPGPGHPRDSGISLDVISSYAPYI--PILGVCLGHQSIGYLFGGKIIKAPKPMHGktskiyHNHDDLF 115

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1033937293 245 HGTGRCFMTSQNHGFAVDIETLPKDWEplftnVNDKTNEGII 286
Cdd:CHL00101  116 QGLPNPFTATRYHSLIIDPLNLPSPLE-----ITAWTEDGLI 152
PuuD COG2071
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ...
 177-220 8.38e-03

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: 36.69  E-value: 8.38e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1033937293 177 FDGLFISNGP--------GDPIMCAETVNEIRkclDKFE-----------KPIFGICLGHQLL 220
Cdd:COG2071    50 LDGLVLTGGAdvdpalygEEPHPELGPIDPER---DAFElaliraalergKPVLGICRGMQLL 109
 
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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