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Conserved domains on  [gi|808366157|ref|XP_012188561|]
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carbamoyl-phosphate synthase [Pseudozyma hubeiensis SY62]

Protein Classification

carbamoyl-phosphate synthase domain-containing protein( domain architecture ID 1003834)

carbamoyl-phosphate synthase domain-containing protein similar to 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
CPSaseIIsmall super family cl36883
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ...
 40-426 4.29e-153

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]


The actual alignment was detected with superfamily member TIGR01368:

Pssm-ID: 273580 [Multi-domain]  Cd Length: 357  Bit Score: 439.37  E-value: 4.29e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157   40 ATLHLKSGESFTGRSFGAPRSVFGETVFTTSITSYTESLTDPSYQGQILTFTQPLMGNYGVPDNGstqspvehpadvdvg 119
Cdd:TIGR01368   1 AYLVLEDGTVFRGYSFGAEGTVAGEVVFNTGMTGYQEILTDPSYKGQIVVFTYPLIGNYGVNDED--------------- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157  120 afLESNKVQAAGVIVSNLAERFSHYLAKESLATWCARHNVPGLFGVDTRAITSLLRDQGSTLGALLVGDGHDKAPA--VG 197
Cdd:TIGR01368  66 --AESKGIHVSGLVVRELSDRYSNWRATESLDQFLKRHGIPGIYGVDTRALVKKIREKGTMKGVISTEDSNDEELVekAR 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157  198 DYIDPMAENLIAKVSTKEPYVLHPVGGakaARAHVALMDFGCKANILRSLLRRGASVTVLPWDYDFNKVRDGF-DGLFLS 276
Cdd:TIGR01368 144 VSPDITGINLVAEVSTKEPYTWGQRGG---KGKRVVVIDFGVKRNILRRLVKRGCEVTVVPYDTDAEEIKKYNpDGIFLS 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157  277 NGPGSPYSIEPALNMARKaVAEwDRPIFGICMGHQVIGIAAGVEAYRMKFGNRGHNQPVVALKSagnfvkrGRVYITSQN 356
Cdd:TIGR01368 221 NGPGDPAAVEPAIETIRK-LLE-KIPIFGICLGHQLLALAFGAKTYKMKFGHRGGNHPVKDLIT-------GRVEITSQN 291

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157  357 HGYALTPDeSKWPQGWQPWFVNANDSSVEGIIRTELneqraMVWGVQFHPEHAGGPEDTNGIFEDFVEEV 426
Cdd:TIGR01368 292 HGYAVDPD-SLPAGDLEVTHVNLNDGTVEGIRHKDL-----PVFSVQYHPEASPGPHDTEYLFDEFIDLM 355
 
Name Accession Description Interval E-value
CPSaseIIsmall TIGR01368
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ...
 40-426 4.29e-153

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: 439.37  E-value: 4.29e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157   40 ATLHLKSGESFTGRSFGAPRSVFGETVFTTSITSYTESLTDPSYQGQILTFTQPLMGNYGVPDNGstqspvehpadvdvg 119
Cdd:TIGR01368   1 AYLVLEDGTVFRGYSFGAEGTVAGEVVFNTGMTGYQEILTDPSYKGQIVVFTYPLIGNYGVNDED--------------- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157  120 afLESNKVQAAGVIVSNLAERFSHYLAKESLATWCARHNVPGLFGVDTRAITSLLRDQGSTLGALLVGDGHDKAPA--VG 197
Cdd:TIGR01368  66 --AESKGIHVSGLVVRELSDRYSNWRATESLDQFLKRHGIPGIYGVDTRALVKKIREKGTMKGVISTEDSNDEELVekAR 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157  198 DYIDPMAENLIAKVSTKEPYVLHPVGGakaARAHVALMDFGCKANILRSLLRRGASVTVLPWDYDFNKVRDGF-DGLFLS 276
Cdd:TIGR01368 144 VSPDITGINLVAEVSTKEPYTWGQRGG---KGKRVVVIDFGVKRNILRRLVKRGCEVTVVPYDTDAEEIKKYNpDGIFLS 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157  277 NGPGSPYSIEPALNMARKaVAEwDRPIFGICMGHQVIGIAAGVEAYRMKFGNRGHNQPVVALKSagnfvkrGRVYITSQN 356
Cdd:TIGR01368 221 NGPGDPAAVEPAIETIRK-LLE-KIPIFGICLGHQLLALAFGAKTYKMKFGHRGGNHPVKDLIT-------GRVEITSQN 291

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157  357 HGYALTPDeSKWPQGWQPWFVNANDSSVEGIIRTELneqraMVWGVQFHPEHAGGPEDTNGIFEDFVEEV 426
Cdd:TIGR01368 292 HGYAVDPD-SLPAGDLEVTHVNLNDGTVEGIRHKDL-----PVFSVQYHPEASPGPHDTEYLFDEFIDLM 355
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
38-424 4.51e-149

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 429.11  E-value: 4.51e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157  38 KPATLHLKSGESFTGRSFGAPRSVFGETVFTTSITSYTESLTDPSYQGQILTFTQPLMGNYGVPDNgstqspvehpaDVd 117
Cdd:PRK12564   3 MKAYLVLEDGTVFEGKAFGAEGETVGEVVFNTSMTGYQEILTDPSYAGQIVTFTYPLIGNYGVNRE-----------DF- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157 118 vgaflESNKVQAAGVIVSNLAERFSHYLAKESLATWCARHNVPGLFGVDTRAITSLLRDQGSTLGALLVGDGH-----DK 192
Cdd:PRK12564  71 -----ESDRPHAKGLIVRELSDIPSNWRSEMSLDEYLKENGIPGISGIDTRALTRKLREKGAMKGVIATEDFDaeellEK 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157 193 APAVGDYIDpmaENLIAKVSTKEPYVLHpvGGAKAARAHVALMDFGCKANILRSLLRRGASVTVLPWDYDFNKVRD-GFD 271
Cdd:PRK12564 146 ARAFPGLLG---LDLVKEVSTKEPYPWP--GPGGELKYKVVAIDFGVKRNILRELAERGCRVTVVPATTTAEEILAlNPD 220

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157 272 GLFLSNGPGSPYSIEPALNMARKaVAEWDRPIFGICMGHQVIGIAAGVEAYRMKFGNRGHNQPVVALKSagnfvkrGRVY 351
Cdd:PRK12564 221 GVFLSNGPGDPAALDYAIEMIRE-LLEKKIPIFGICLGHQLLALALGAKTYKMKFGHRGANHPVKDLET-------GKVE 292

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 808366157 352 ITSQNHGYALtpDESKWPQGWQPWFVNANDSSVEGIIRTELNeqramVWGVQFHPEHAGGPEDTNGIFEDFVE 424
Cdd:PRK12564 293 ITSQNHGFAV--DEDSLPANLEVTHVNLNDGTVEGLRHKDLP-----AFSVQYHPEASPGPHDSAYLFDEFVE 358
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 36-426 1.29e-148

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: 427.90  E-value: 1.29e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157  36 ASKPATLHLKSGESFTGRSFGAPRSVFGETVFTTSITSYTESLTDPSYQGQILTFTQPLMGNYGVpdngstqspveHPAD 115
Cdd:COG0505    1 MMMKALLVLEDGTVFEGKSFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVTFTYPHIGNYGV-----------NDED 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157 116 VdvgaflESNKVQAAGVIVSNLAERFSHYLAKESLATWCARHNVPGLFGVDTRAITSLLRDQGSTLGALLVGDGH----- 190
Cdd:COG0505   70 F------ESDRPWVAGLVVRELSRRPSNWRSEESLDEYLKEHGIPGISGIDTRALTRHLREKGAMKGVISTGDLDieell 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157 191 DKAPAVGDYiDPMaeNLIAKVSTKEPYVLHPVGGAKaarAHVALMDFGCKANILRSLLRRGASVTVLPWDYDFNKVRD-G 269
Cdd:COG0505  144 EKARAAPGM-EGL--DLVKEVSTKEPYEWTEAPGAG---FHVVALDFGVKRNILRELAERGCRVTVVPATTSAEEILAlN 217

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157 270 FDGLFLSNGPGSPYSIEPALNMARKaVAEWDRPIFGICMGHQVIGIAAGVEAYRMKFGNRGHNQPVVALKSagnfvkrGR 349
Cdd:COG0505  218 PDGVFLSNGPGDPAALDYAIETIRE-LLGKGIPIFGICLGHQLLALALGAKTYKLKFGHRGANHPVKDLET-------GR 289

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 808366157 350 VYITSQNHGYALTPDESKwPQGWQPWFVNANDSSVEGIIRTELNeqramVWGVQFHPEHAGGPEDTNGIFEDFVEEV 426
Cdd:COG0505  290 VEITSQNHGFAVDEDSLP-ATDLEVTHVNLNDGTVEGLRHKDLP-----AFSVQYHPEASPGPHDSAYLFDRFIELM 360
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 232-423 4.71e-92

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: 276.68  E-value: 4.71e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157 232 VALMDFGCKANILRSLLRRGASVTVLPWDYDFNKV-RDGFDGLFLSNGPGSPYSIEPALNMARKAVAEWdRPIFGICMGH 310
Cdd:cd01744    1 VVVIDFGVKHNILRELLKRGCEVTVVPYNTDAEEIlKLDPDGIFLSNGPGDPALLDEAIKTVRKLLGKK-IPIFGICLGH 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157 311 QVIGIAAGVEAYRMKFGNRGHNQPVVALKSagnfvkrGRVYITSQNHGYALTPDESkwPQGWQPWFVNANDSSVEGIIRT 390
Cdd:cd01744   80 QLLALALGAKTYKMKFGHRGSNHPVKDLIT-------GRVYITSQNHGYAVDPDSL--PGGLEVTHVNLNDGTVEGIRHK 150

                        170       180       190
                 ....*....|....*....|....*....|...
gi 808366157 391 ELneqraMVWGVQFHPEHAGGPEDTNGIFEDFV 423
Cdd:cd01744  151 DL-----PVFSVQFHPEASPGPHDTEYLFDEFL 178
CPSase_sm_chain pfam00988
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 42-184 5.14e-64

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: 202.94  E-value: 5.14e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157   42 LHLKSGESFTGRSFGAPRSVFGETVFTTSITSYTESLTDPSYQGQILTFTQPLMGNYGVPDNgstqspvehpadvdvgaF 121
Cdd:pfam00988   1 LVLEDGTVFEGKSFGAAGSTVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNPE-----------------D 63

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 808366157  122 LESNKVQAAGVIVSNLAERFSHYLAKESLATWCARHNVPGLFGVDTRAITSLLRDQGSTLGAL 184
Cdd:pfam00988  64 FESDKIHVAGLVVREYSDEPSNWRAEESLDEWLKEQGIPGISGVDTRALTRKIREKGAMKGVI 126
CPSase_sm_chain smart01097
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 38-184 1.05e-62

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: 199.52  E-value: 1.05e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157    38 KPATLHLKSGESFTGRSFGAPRSVFGETVFTTSITSYTESLTDPSYQGQILTFTQPLMGNYGVPDNgstqspvehpaDVd 117
Cdd:smart01097   1 MKAYLVLEDGTVFEGESFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNDE-----------DF- 68

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 808366157   118 vgaflESNKVQAAGVIVSNLAERFSHYLAKESLATWCARHNVPGLFGVDTRAITSLLRDQGSTLGAL 184
Cdd:smart01097  69 -----ESDKIQVKGLVVRELSDEPSNWRSEQSLDEFLKENGIPGISGIDTRALTRKLREKGAMKGVI 130
 
Name Accession Description Interval E-value
CPSaseIIsmall TIGR01368
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ...
 40-426 4.29e-153

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: 439.37  E-value: 4.29e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157   40 ATLHLKSGESFTGRSFGAPRSVFGETVFTTSITSYTESLTDPSYQGQILTFTQPLMGNYGVPDNGstqspvehpadvdvg 119
Cdd:TIGR01368   1 AYLVLEDGTVFRGYSFGAEGTVAGEVVFNTGMTGYQEILTDPSYKGQIVVFTYPLIGNYGVNDED--------------- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157  120 afLESNKVQAAGVIVSNLAERFSHYLAKESLATWCARHNVPGLFGVDTRAITSLLRDQGSTLGALLVGDGHDKAPA--VG 197
Cdd:TIGR01368  66 --AESKGIHVSGLVVRELSDRYSNWRATESLDQFLKRHGIPGIYGVDTRALVKKIREKGTMKGVISTEDSNDEELVekAR 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157  198 DYIDPMAENLIAKVSTKEPYVLHPVGGakaARAHVALMDFGCKANILRSLLRRGASVTVLPWDYDFNKVRDGF-DGLFLS 276
Cdd:TIGR01368 144 VSPDITGINLVAEVSTKEPYTWGQRGG---KGKRVVVIDFGVKRNILRRLVKRGCEVTVVPYDTDAEEIKKYNpDGIFLS 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157  277 NGPGSPYSIEPALNMARKaVAEwDRPIFGICMGHQVIGIAAGVEAYRMKFGNRGHNQPVVALKSagnfvkrGRVYITSQN 356
Cdd:TIGR01368 221 NGPGDPAAVEPAIETIRK-LLE-KIPIFGICLGHQLLALAFGAKTYKMKFGHRGGNHPVKDLIT-------GRVEITSQN 291

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157  357 HGYALTPDeSKWPQGWQPWFVNANDSSVEGIIRTELneqraMVWGVQFHPEHAGGPEDTNGIFEDFVEEV 426
Cdd:TIGR01368 292 HGYAVDPD-SLPAGDLEVTHVNLNDGTVEGIRHKDL-----PVFSVQYHPEASPGPHDTEYLFDEFIDLM 355
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
38-424 4.51e-149

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 429.11  E-value: 4.51e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157  38 KPATLHLKSGESFTGRSFGAPRSVFGETVFTTSITSYTESLTDPSYQGQILTFTQPLMGNYGVPDNgstqspvehpaDVd 117
Cdd:PRK12564   3 MKAYLVLEDGTVFEGKAFGAEGETVGEVVFNTSMTGYQEILTDPSYAGQIVTFTYPLIGNYGVNRE-----------DF- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157 118 vgaflESNKVQAAGVIVSNLAERFSHYLAKESLATWCARHNVPGLFGVDTRAITSLLRDQGSTLGALLVGDGH-----DK 192
Cdd:PRK12564  71 -----ESDRPHAKGLIVRELSDIPSNWRSEMSLDEYLKENGIPGISGIDTRALTRKLREKGAMKGVIATEDFDaeellEK 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157 193 APAVGDYIDpmaENLIAKVSTKEPYVLHpvGGAKAARAHVALMDFGCKANILRSLLRRGASVTVLPWDYDFNKVRD-GFD 271
Cdd:PRK12564 146 ARAFPGLLG---LDLVKEVSTKEPYPWP--GPGGELKYKVVAIDFGVKRNILRELAERGCRVTVVPATTTAEEILAlNPD 220

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157 272 GLFLSNGPGSPYSIEPALNMARKaVAEWDRPIFGICMGHQVIGIAAGVEAYRMKFGNRGHNQPVVALKSagnfvkrGRVY 351
Cdd:PRK12564 221 GVFLSNGPGDPAALDYAIEMIRE-LLEKKIPIFGICLGHQLLALALGAKTYKMKFGHRGANHPVKDLET-------GKVE 292

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 808366157 352 ITSQNHGYALtpDESKWPQGWQPWFVNANDSSVEGIIRTELNeqramVWGVQFHPEHAGGPEDTNGIFEDFVE 424
Cdd:PRK12564 293 ITSQNHGFAV--DEDSLPANLEVTHVNLNDGTVEGLRHKDLP-----AFSVQYHPEASPGPHDSAYLFDEFVE 358
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 36-426 1.29e-148

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: 427.90  E-value: 1.29e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157  36 ASKPATLHLKSGESFTGRSFGAPRSVFGETVFTTSITSYTESLTDPSYQGQILTFTQPLMGNYGVpdngstqspveHPAD 115
Cdd:COG0505    1 MMMKALLVLEDGTVFEGKSFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVTFTYPHIGNYGV-----------NDED 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157 116 VdvgaflESNKVQAAGVIVSNLAERFSHYLAKESLATWCARHNVPGLFGVDTRAITSLLRDQGSTLGALLVGDGH----- 190
Cdd:COG0505   70 F------ESDRPWVAGLVVRELSRRPSNWRSEESLDEYLKEHGIPGISGIDTRALTRHLREKGAMKGVISTGDLDieell 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157 191 DKAPAVGDYiDPMaeNLIAKVSTKEPYVLHPVGGAKaarAHVALMDFGCKANILRSLLRRGASVTVLPWDYDFNKVRD-G 269
Cdd:COG0505  144 EKARAAPGM-EGL--DLVKEVSTKEPYEWTEAPGAG---FHVVALDFGVKRNILRELAERGCRVTVVPATTSAEEILAlN 217

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157 270 FDGLFLSNGPGSPYSIEPALNMARKaVAEWDRPIFGICMGHQVIGIAAGVEAYRMKFGNRGHNQPVVALKSagnfvkrGR 349
Cdd:COG0505  218 PDGVFLSNGPGDPAALDYAIETIRE-LLGKGIPIFGICLGHQLLALALGAKTYKLKFGHRGANHPVKDLET-------GR 289

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 808366157 350 VYITSQNHGYALTPDESKwPQGWQPWFVNANDSSVEGIIRTELNeqramVWGVQFHPEHAGGPEDTNGIFEDFVEEV 426
Cdd:COG0505  290 VEITSQNHGFAVDEDSLP-ATDLEVTHVNLNDGTVEGLRHKDLP-----AFSVQYHPEASPGPHDSAYLFDRFIELM 360
PRK12838 PRK12838
carbamoyl phosphate synthase small subunit; Reviewed
 39-426 1.27e-127

carbamoyl phosphate synthase small subunit; Reviewed


Pssm-ID: 183784 [Multi-domain]  Cd Length: 354  Bit Score: 374.23  E-value: 1.27e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157  39 PATLHLKSGESFTGRSFGAPRSVFGETVFTTSITSYTESLTDPSYQGQILTFTQPLMGNYGVPDNGStqspvehpadvdv 118
Cdd:PRK12838   2 KAYLILEDGTVFEGELIGAPIDVTGEIVFNTGMTGYQEVLTDPSYKGQIVVFTYPLIGNYGINADDY------------- 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157 119 gaflESNKVQAAGVIVSNLAERFSHYLAKESLATWCARHNVPGLFGVDTRAITSLLRDQGsTLGALLVGDGHDKAPAVGD 198
Cdd:PRK12838  69 ----ESKQPQVKGVIVYELSREGSHYRAKQSLDDFLKEWNIPGISGVDTRALVKHIREKG-TMKASITTTDDAHAFDQIK 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157 199 YIDPmAENLIAKVSTKEPYVLhPVGGakaarAHVALMDFGCKANILRSLLRRGASVTVLPWDYDFNKV-RDGFDGLFLSN 277
Cdd:PRK12838 144 ALVL-PKNVVAQVSTKEPYTY-GNGG-----KHVALIDFGYKKSILRSLSKRGCKVTVLPYDTSLEEIkNLNPDGIVLSN 216

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157 278 GPGSPYSIEPALNMARKaVAEwDRPIFGICMGHQVIGIAAGVEAYRMKFGNRGHNQPVVALKSagnfvkrGRVYITSQNH 357
Cdd:PRK12838 217 GPGDPKELQPYLPEIKK-LIS-SYPILGICLGHQLIALALGADTEKLPFGHRGANHPVIDLTT-------GRVWMTSQNH 287

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 808366157 358 GYALTPDESKwPQGWQPWFVNANDSSVEGIIRTELNeqramVWGVQFHPEHAGGPEDTNGIFEDFVEEV 426
Cdd:PRK12838 288 GYVVDEDSLD-GTPLSVRFFNVNDGSIEGLRHKKKP-----VLSVQFHPEAHPGPHDAEYIFDEFLEMM 350
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 232-423 4.71e-92

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: 276.68  E-value: 4.71e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157 232 VALMDFGCKANILRSLLRRGASVTVLPWDYDFNKV-RDGFDGLFLSNGPGSPYSIEPALNMARKAVAEWdRPIFGICMGH 310
Cdd:cd01744    1 VVVIDFGVKHNILRELLKRGCEVTVVPYNTDAEEIlKLDPDGIFLSNGPGDPALLDEAIKTVRKLLGKK-IPIFGICLGH 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157 311 QVIGIAAGVEAYRMKFGNRGHNQPVVALKSagnfvkrGRVYITSQNHGYALTPDESkwPQGWQPWFVNANDSSVEGIIRT 390
Cdd:cd01744   80 QLLALALGAKTYKMKFGHRGSNHPVKDLIT-------GRVYITSQNHGYAVDPDSL--PGGLEVTHVNLNDGTVEGIRHK 150

                        170       180       190
                 ....*....|....*....|....*....|...
gi 808366157 391 ELneqraMVWGVQFHPEHAGGPEDTNGIFEDFV 423
Cdd:cd01744  151 DL-----PVFSVQFHPEASPGPHDTEYLFDEFL 178
carA CHL00197
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
 38-433 7.69e-74

carbamoyl-phosphate synthase arginine-specific small subunit; Provisional


Pssm-ID: 214392 [Multi-domain]  Cd Length: 382  Bit Score: 237.39  E-value: 7.69e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157  38 KPATLHLKSGESFTGRSFGAPRSVFGETVFTTSITSYTESLTDPSYQGQILTFTQPLMGNYGVpdNGSTQspvehpadvd 117
Cdd:CHL00197   5 IPAILVLEDGTYYRGWSFSNPITTIGEVVFNTGMTGYQEIITDPSYFEQIVTFTYPEIGNTGI--NLEDI---------- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157 118 vgaflESNKVQAAGVIVSNLAERFSHYLAKESLATWCARHNVPGLFGVDTRAITSLLRDQGSTLGAllvgdghdkapAVG 197
Cdd:CHL00197  73 -----ESVKIQVKGIIAKNICKSSSNWRQQESLVSYLQRHKIPFIFGIDTRALTQHLRRFGTMNGC-----------ISN 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157 198 DYIDP-------------MAENLIAKVSTKEPY----VLHP-VGGAKAARAH------VALMDFGCKANILRSLLRRGAS 253
Cdd:CHL00197 137 QNLNLsylrakikesphmPSSDLIPRVTTSSYYewdeKSHPsFYLADNKRPHssyqlkIIVIDFGVKYNILRRLKSFGCS 216

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157 254 VTVLPWDYDFNKVRD-GFDGLFLSNGPGSPysiePALNMARKAVAEW---DRPIFGICMGHQVIGIAAGVEAYRMKFGNR 329
Cdd:CHL00197 217 ITVVPATSPYQDILSyQPDGILLSNGPGDP----SAIHYGIKTVKKLlkyNIPIFGICMGHQILSLALEAKTFKLKFGHR 292

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157 330 GHNQPvVALKSagnfvkrgRVYITSQNHGYALTPdESKWPQGWQPWFVNANDSSVEGIirtelNEQRAMVWGVQFHPEHA 409
Cdd:CHL00197 293 GLNHP-SGLNQ--------QVEITSQNHGFAVNL-ESLAKNKFYITHFNLNDGTVAGI-----SHSPKPYFSVQYHPEAS 357

                        410       420
                 ....*....|....*....|....
gi 808366157 410 GGPEDTNGIFEDFVEEVVRIKGSQ 433
Cdd:CHL00197 358 PGPHDADYLFEYFIEIIKHSKSSK 381
PLN02771 PLN02771
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
 13-419 1.07e-68

carbamoyl-phosphate synthase (glutamine-hydrolyzing)


Pssm-ID: 178370 [Multi-domain]  Cd Length: 415  Bit Score: 224.86  E-value: 1.07e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157  13 RTGAIRSLATHASAGPITYTDAP------ASKPATLHLKSGESFTGRSFGAPRSVFGETVFTTSITSYTESLTDPSYQGQ 86
Cdd:PLN02771  24 RRGGVRVSVIRCSSSPLTSDGAGvverpwKTSDARLVLEDGSVWKAKSFGARGTQVGEVVFNTSLTGYQEILTDPSYAGQ 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157  87 ILTFTQPLMGNYGV-PDNGstqspvehpadvdvgaflESNKVQAAGVIVSNLAERFSHYLAKESLATWCARHNVPGLFGV 165
Cdd:PLN02771 104 FVLMTNPHIGNTGVnFDDE------------------ESRQCFLAGLVIRSLSISTSNWRCTKTLGDYLAERNIMGIYDV 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157 166 DTRAITSLLRDQGSTLGALLVGDGH--DKAPAVGDYIDPMAENLIAKVSTKEPYV-LHPVG--------GAKAARAHVAL 234
Cdd:PLN02771 166 DTRAITRRLREDGSLIGVLSTEDSKtdEELLKMSRSWDIVGIDLISGVSCKSPYEwVDKTNpewdfntnSRDGESYHVIA 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157 235 MDFGCKANILRSLLRRGASVTVLPWDYDFNK-VRDGFDGLFLSNGPGSPYSIEPALNMARKAVAEwdRPIFGICMGHQVI 313
Cdd:PLN02771 246 YDFGIKHNILRRLASYGCKITVVPSTWPASEaLKMKPDGVLFSNGPGDPSAVPYAVETVKELLGK--VPVFGICMGHQLL 323

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157 314 GIAAGVEAYRMKFGNRGHNQPVVALKSagnfvkrGRVYITSQNHGYALTPdeSKWPQGWQPWFVNANDSSVEGIIRTELN 393
Cdd:PLN02771 324 GQALGGKTFKMKFGHHGGNHPVRNNRT-------GRVEISAQNHNYAVDP--ASLPEGVEVTHVNLNDGSCAGLAFPALN 394

                        410       420
                 ....*....|....*....|....*.
gi 808366157 394 eqramVWGVQFHPEHAGGPEDTNGIF 419
Cdd:PLN02771 395 -----VMSLQYHPEASPGPHDSDNAF 415
CPSase_sm_chain pfam00988
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 42-184 5.14e-64

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: 202.94  E-value: 5.14e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157   42 LHLKSGESFTGRSFGAPRSVFGETVFTTSITSYTESLTDPSYQGQILTFTQPLMGNYGVPDNgstqspvehpadvdvgaF 121
Cdd:pfam00988   1 LVLEDGTVFEGKSFGAAGSTVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNPE-----------------D 63

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 808366157  122 LESNKVQAAGVIVSNLAERFSHYLAKESLATWCARHNVPGLFGVDTRAITSLLRDQGSTLGAL 184
Cdd:pfam00988  64 FESDKIHVAGLVVREYSDEPSNWRAEESLDEWLKEQGIPGISGVDTRALTRKIREKGAMKGVI 126
CPSase_sm_chain smart01097
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ...
 38-184 1.05e-62

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: 199.52  E-value: 1.05e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157    38 KPATLHLKSGESFTGRSFGAPRSVFGETVFTTSITSYTESLTDPSYQGQILTFTQPLMGNYGVPDNgstqspvehpaDVd 117
Cdd:smart01097   1 MKAYLVLEDGTVFEGESFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNDE-----------DF- 68

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 808366157   118 vgaflESNKVQAAGVIVSNLAERFSHYLAKESLATWCARHNVPGLFGVDTRAITSLLRDQGSTLGAL 184
Cdd:smart01097  69 -----ESDKIQVKGLVVRELSDEPSNWRSEQSLDEFLKENGIPGISGIDTRALTRKLREKGAMKGVI 130
GATase pfam00117
Glutamine amidotransferase class-I;
233-424 8.41e-52

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 173.19  E-value: 8.41e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157  233 ALMDFGC--KANILRSLLRRGASVTVLPWDYDFNKVRDG-FDGLFLSNGPGSPYSIEPALNMARKAVaEWDRPIFGICMG 309
Cdd:pfam00117   1 LLIDNGDsfTYNLARALRELGVEVTVVPNDTPAEEILEEnPDGIILSGGPGSPGAAGGAIEAIREAR-ELKIPILGICLG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157  310 HQVIGIAAGVEAYRMK-FGNRGHNQPVVaLKSAGNFVKRGRVYITSQNHGYALTPDESkwPQGWQPWFVNANDSSVEGII 388
Cdd:pfam00117  80 HQLLALAFGGKVVKAKkFGHHGKNSPVG-DDGCGLFYGLPNVFIVRRYHSYAVDPDTL--PDGLEVTATSENDGTIMGIR 156

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 808366157  389 RTELneqraMVWGVQFHPEHAGGPEDTNGIFEDFVE 424
Cdd:pfam00117 157 HKKL-----PIFGVQFHPESILTPHGPEILFNFFIK 187
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 242-407 3.79e-12

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: 64.86  E-value: 3.79e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157 242 NILRSLLRRGASVTVLPWD--YDFNKVRDGFDGLFLSNGPGSPySIEPALNMARKAVAEwDRPIFGICMGHQVIGIAAGV 319
Cdd:cd01743   13 NLVQYLRELGAEVVVVRNDeiTLEELELLNPDAIVISPGPGHP-EDAGISLEIIRALAG-KVPILGVCLGHQAIAEAFGG 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157 320 EAYRMKFGNRGHnQPVVALKSAGNF------VKRGRvYitsqnHGYALTPDESKwpqgwQPWFVNAndSSVEGIIRTELN 393
Cdd:cd01743   91 KVVRAPEPMHGK-TSEIHHDGSGLFkglpqpFTVGR-Y-----HSLVVDPDPLP-----DLLEVTA--STEDGVIMALRH 156

                        170
                 ....*....|....
gi 808366157 394 EQRAmVWGVQFHPE 407
Cdd:cd01743  157 RDLP-IYGVQFHPE 169
GATase1_GMP_Synthase cd01742
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ...
 232-407 9.64e-11

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: 60.63  E-value: 9.64e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157 232 VALMDFGCKAN--ILRSLLRRGASVTVLPWDYDFNKVRD-GFDGLFLSNGPGSPYsiEPALNMARKAVAEWDRPIFGICM 308
Cdd:cd01742    1 ILILDFGSQYThlIARRVRELGVYSEILPNTTPLEEIKLkNPKGIILSGGPSSVY--EEDAPRVDPEIFELGVPVLGICY 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157 309 GHQVIGIAAGVEAYRMKFGNRGHNQPVVALKSA--GNFVKRGRVYItsqNHGyaltpDE-SKWPQGWQpwfVNAN--DSS 383
Cdd:cd01742   79 GMQLIAKALGGKVERGDKREYGKAEIEIDDSSPlfEGLPDEQTVWM---SHG-----DEvVKLPEGFK---VIASsdNCP 147

                        170       180
                 ....*....|....*....|....
gi 808366157 384 VEGIirtELNEQRamVWGVQFHPE 407
Cdd:cd01742  148 VAAI---ANEEKK--IYGVQFHPE 166
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 243-407 1.82e-10

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: 60.73  E-value: 1.82e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157 243 ILRSLLRRGASVTV--------LPWDYDFnkvrDGFDGLFLSNGPGSPYS----IEPALNMARKAVAEwDRPIFGICMGH 310
Cdd:COG0518   18 IARRLREAGIELDVlrvyageiLPYDPDL----EDPDGLILSGGPMSVYDedpwLEDEPALIREAFEL-GKPVLGICYGA 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157 311 QVIGIAAGVEAYRMKFGNRGHnQPVVALKSA---GNFVKRGRVYitsQNHGYALTpdesKWPQGWQPWFVNANDsSVEGI 387
Cdd:COG0518   93 QLLAHALGGKVEPGPGREIGW-APVELTEADplfAGLPDEFTVW---MSHGDTVT----ELPEGAEVLASSDNC-PNQAF 163

                        170       180
                 ....*....|....*....|
gi 808366157 388 IrtelNEQRamVWGVQFHPE 407
Cdd:COG0518  164 R----YGRR--VYGVQFHPE 177
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 232-313 3.62e-10

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


Pssm-ID: 153210 [Multi-domain]  Cd Length: 115  Bit Score: 57.22  E-value: 3.62e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157 232 VALMDFGCK-----ANILRSLLRRGASVTVLPWDYDFNKVR---DGFDGLFLSNGPGSPYSIE--PALNMARKAVAEWDR 301
Cdd:cd01653    1 VAVLLFPGFeelelASPLDALREAGAEVDVVSPDGGPVESDvdlDDYDGLILPGGPGTPDDLArdEALLALLREAAAAGK 80

                         90
                 ....*....|..
gi 808366157 302 PIFGICMGHQVI 313
Cdd:cd01653   81 PILGICLGAQLL 92
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 232-313 1.33e-09

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


Pssm-ID: 153222 [Multi-domain]  Cd Length: 92  Bit Score: 54.90  E-value: 1.33e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157 232 VALMDFGCK-----ANILRSLLRRGASVTVLPWDYDFNKVR---DGFDGLFLSNGPGSPYSIE--PALNMARKAVAEWDR 301
Cdd:cd03128    1 VAVLLFGGSeelelASPLDALREAGAEVDVVSPDGGPVESDvdlDDYDGLILPGGPGTPDDLAwdEALLALLREAAAAGK 80

                         90
                 ....*....|..
gi 808366157 302 PIFGICMGHQVI 313
Cdd:cd03128   81 PVLGICLGAQLL 92
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 231-423 3.16e-09

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: 56.48  E-value: 3.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157 231 HVALMDFGCKANILRSLLRRGASVTVL-PWDYDFNKVRDGFDGLFLSngpGSPYS--------IEPALNMARKAVAEwDR 301
Cdd:cd01741    7 HDTPEGPGLFEDLLREAGAETIEIDVVdVYAGELLPDLDDYDGLVIL---GGPMSvdeddypwLKKLKELIRQALAA-GK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157 302 PIFGICMGHQVIGIAAGVEAYRMKFGNRGHNQPV------VALKSAGNFVKRGRVYITSQNHGYALtpdeskwPQGWQPW 375
Cdd:cd01741   83 PVLGICLGHQLLARALGGKVGRNPKGWEIGWFPVtlteagKADPLFAGLPDEFPVFHWHGDTVVEL-------PPGAVLL 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 808366157 376 FVNAnDSSVEGIIRTELneqramVWGVQFHPEHAggpedtngIFEDFV 423
Cdd:cd01741  156 ASSE-ACPNQAFRYGDR------ALGLQFHPEER--------LLRNFL 188
guaA_Nterm TIGR00888
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ...
 232-430 1.24e-08

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: 54.63  E-value: 1.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157  232 VALMDFGCKAN--ILRSLLRRGASVTVLPWDYDFNKVRDgFD--GLFLSNGPGSPY---SIEPAlnmarKAVAEWDRPIF 304
Cdd:TIGR00888   1 ILVLDFGSQYTqlIARRLRELGVYSELVPNTTPLEEIRE-KNpkGIILSGGPSSVYaenAPRAD-----EKIFELGVPVL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157  305 GICMGHQVIGIAAGVEayrmkfgnrghnqpvVALKSAGNFvKRGRVYITSQNHGYALTPDESK-W----------PQGWQ 373
Cdd:TIGR00888  75 GICYGMQLMAKQLGGE---------------VGRAEKREY-GKAELEILDEDDLFRGLPDESTvWmshgdkvkelPEGFK 138

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 808366157  374 PWFVNANdSSVEGIIrtelNEQRAmVWGVQFHPE--HAggpEDTNGIFEDFVEEVVRIK 430
Cdd:TIGR00888 139 VLATSDN-CPVAAMA----HEEKP-IYGVQFHPEvtHT---EYGNELLENFVYDVCGCE 188
PRK00758 PRK00758
GMP synthase subunit A; Validated
 231-424 1.34e-08

GMP synthase subunit A; Validated


Pssm-ID: 179112 [Multi-domain]  Cd Length: 184  Bit Score: 54.47  E-value: 1.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157 231 HVALMDFGCKAN--ILRSLLRRGASVTVLPWDYDFNKVRDGFDGLFLSNGPgspySIEPALNmARKAVAEWDRPIFGICM 308
Cdd:PRK00758   1 KIVVVDNGGQYNhlIHRTLRYLGVDAKIIPNTTPVEEIKAFEDGLILSGGP----DIERAGN-CPEYLKELDVPILGICL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157 309 GHQVIGIAAGVEAYRMKFGNRG--------HNQPVVALKSagnfvkRGRVYitsQNHGyaltpDE-SKWPQGwqpwFVNA 379
Cdd:PRK00758  76 GHQLIAKAFGGEVGRGEYGEYAlveveildEDDILKGLPP------EIRVW---ASHA-----DEvKELPDG----FEIL 137

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 808366157 380 NDSS---VEGIIRTELNeqramVWGVQFHPEHA---GGPEdtngIFEDFVE 424
Cdd:PRK00758 138 ARSDiceVEAMKHKEKP-----IYGVQFHPEVAhteYGEE----IFKNFLE 179
PRK07765 PRK07765
aminodeoxychorismate/anthranilate synthase component II;
262-318 1.53e-08

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181107 [Multi-domain]  Cd Length: 214  Bit Score: 54.67  E-value: 1.53e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 808366157 262 DFNKVRDGFDGLFLSNGPGSPYSIEPALNMARkAVAEWDRPIFGICMGHQVIGIAAG 318
Cdd:PRK07765  39 DEAAVAAQFDGVLLSPGPGTPERAGASIDMVR-ACAAAGTPLLGVCLGHQAIGVAFG 94
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 242-423 3.12e-08

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


Pssm-ID: 153216 [Multi-domain]  Cd Length: 189  Bit Score: 53.35  E-value: 3.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157 242 NILRSLLRRGASVTVLPWDYDFNKVR---DGFDGLFLSNGP------------GSPYSIEPA-----LNMARKAVAEwDR 301
Cdd:cd01745   23 YYVDAVRKAGGLPVLLPPVDDEEDLEqylELLDGLLLTGGGdvdpplygeephPELGPIDPErdafeLALLRAALER-GK 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157 302 PIFGICMGHQVIGIAAGVEAYRMKFGNRGHNQpvvALKSAGNFVKRGRVyitsqnhgyaltpdeskwpqgwqpwfvnAND 381
Cdd:cd01745  102 PILGICRGMQLLNVALGGTLYQDIRVNSLHHQ---AIKRLADGLRVEAR----------------------------APD 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 808366157 382 SSVEGIirtElNEQRAMVWGVQFHPE-HAGGPEDTNGIFEDFV 423
Cdd:cd01745  151 GVIEAI---E-SPDRPFVLGVQWHPEwLADTDPDSLKLFEAFV 189
PabB-fungal TIGR01823
aminodeoxychorismate synthase, fungal clade; This model represents the fungal clade of a ...
 252-422 3.62e-08

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


Pssm-ID: 273821 [Multi-domain]  Cd Length: 742  Bit Score: 56.07  E-value: 3.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157  252 ASVTVLPWD-YDFNKVRD--GFDGLFLSNGPGSPYSIEPALNMARK-AVAEWDR-PIFGICMGHQVIGIAAGVEAYRMKF 326
Cdd:TIGR01823  33 VHVTTVHSDtFQDQLLELlpLFDAIVVGPGPGNPNNAQDMGIISELwELANLDEvPVLGICLGFQSLCLAQGADISRLPT 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157  327 GNRGHNQPVVALKSA---GNFVKRGRVYitsqnHGYALTPDEskwPQGWQPWFVNANDssvEGIIRTELNEQRAMVWGVQ 403
Cdd:TIGR01823 113 PKHGQVYEMHTNDAAifcGLFSVKSTRY-----HSLYANPEG---IDTLLPLCLTEDE---EGIILMSAQTKKKPWFGVQ 181

                         170
                  ....*....|....*....
gi 808366157  404 FHPEHAGGPEDTNGIFEDF 422
Cdd:TIGR01823 182 YHPESCCSELGSGKLVSNF 200
PRK14607 PRK14607
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
273-431 1.04e-07

bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;


Pssm-ID: 237764 [Multi-domain]  Cd Length: 534  Bit Score: 54.34  E-value: 1.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157 273 LFLSNGPGSPYSIEPALNMARKAVAEWdrPIFGICMGHQVIGIAAGVEAYRMKFGNRGHNQPVVaLKSAGNFVKRGRVYI 352
Cdd:PRK14607  48 IVISPGPGRPEEAGISVEVIRHFSGKV--PILGVCLGHQAIGYAFGGKIVHAKRILHGKTSPID-HNGKGLFRGIPNPTV 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157 353 TSQNHgyALTPDESKWPQGWQPwFVNANDSSVEGIIRTELNeqramVWGVQFHPEHAgGPEDTNGIFEDFV---EEVVRI 429
Cdd:PRK14607 125 ATRYH--SLVVEEASLPECLEV-TAKSDDGEIMGIRHKEHP-----IFGVQFHPESI-LTEEGKRILKNFLnyqREEIDI 195


                 ..
gi 808366157 430 KG 431
Cdd:PRK14607 196 KS 197
PuuD COG2071
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ...
 241-428 1.25e-07

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: 52.48  E-value: 1.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157 241 ANILRSLLRRGASVTVLPWDYDFNKVR---DGFDGLFLSNGP--------GSP----YSIEPA-----LNMARKAVAEwD 300
Cdd:COG2071   18 EDYVRAVRAAGGLPVLLPPVGDEEDLDellDRLDGLVLTGGAdvdpalygEEPhpelGPIDPErdafeLALIRAALER-G 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157 301 RPIFGICMGHQVIGIAAG----VEAYRMKFGNRGHNQPVVAlksagnFVKRGRVYITSQNHGYALTPDESkwpqgwqpWF 376
Cdd:COG2071   97 KPVLGICRGMQLLNVALGgtlyQDLPDQVPGALDHRQPAPR------YAPRHTVEIEPGSRLARILGEEE--------IR 162

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 808366157 377 VN-------------------ANDSSVEGIirtELNEQRAMVwGVQFHPEH--AGGPEDTNgIFEDFVEEVVR 428
Cdd:COG2071  163 VNslhhqavkrlgpglrvsarAPDGVIEAI---ESPGAPFVL-GVQWHPEWlaASDPLSRR-LFEAFVEAARA 230
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 241-407 1.83e-06

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: 48.11  E-value: 1.83e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157 241 ANILRSLlrrGASVTVLPWD-YDFNKVRD-GFDGLFLSNGPGSPYS---IEPALNMARKAVaewdrPIFGICMGHQVIGI 315
Cdd:COG0512   15 VQYLGEL---GAEVVVVRNDeITLEEIEAlAPDGIVLSPGPGTPEEagiSLEVIRAFAGKI-----PILGVCLGHQAIGE 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157 316 AAGVEAYRMK-----------------FgnRGHNQPVVAlksagnfvkrGRvYitsqnHgyALTPDESKWPQGWQpwfVN 378
Cdd:COG0512   87 AFGGKVVRAPepmhgktspithdgsglF--AGLPNPFTA----------TR-Y-----H--SLVVDRETLPDELE---VT 143

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 808366157 379 AndSSVEGIIrtelneqraM--------VWGVQFHPE 407
Cdd:COG0512  144 A--WTEDGEI---------MgirhrelpIEGVQFHPE 169
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 268-407 2.15e-06

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


Pssm-ID: 429620 [Multi-domain]  Cd Length: 219  Bit Score: 48.41  E-value: 2.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157  268 DGFDGLFLSNGPG---SPYSIEP-----ALNMAR--------KAVAEWDRPIFGICMGHQVIGIAAGVEAY---RMKFGN 328
Cdd:pfam07722  57 DRLDGLLLTGGPNvdpHFYGEEPsesggPYDPARdayelaliRAALARGKPILGICRGFQLLNVALGGTLYqdiQEQPGF 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157  329 RGHNQPVVALKSAG----NFVKRGRVY-ITSQN-------HGYALTpdesKWPQGWQPWFVnANDSSVEGIirtELNEQR 396
Cdd:pfam07722 137 TDHREHCQVAPYAPshavNVEPGSLLAsLLGSEefrvnslHHQAID----RLAPGLRVEAV-APDGTIEAI---ESPNAK 208

                         170
                  ....*....|.
gi 808366157  397 AMVWGVQFHPE 407
Cdd:pfam07722 209 GFALGVQWHPE 219
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 244-407 2.78e-06

anthranilate synthase component II; Provisional


Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 47.82  E-value: 2.78e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157 244 LRSLlrrGASVTVLPWD----YDFNKVRDgfDGLFLSNGPGSPYSI---EPALNMARKAVaewdrPIFGICMGHQVIGIA 316
Cdd:PRK05670  19 LGEL---GAEVVVYRNDeitlEEIEALNP--DAIVLSPGPGTPAEAgisLELIREFAGKV-----PILGVCLGHQAIGEA 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157 317 agveayrmkFGnrghnqpvvalksaGNFVKRGRVY------ITSQNHG-YA-------------LTPDESKWPQGWQpwf 376
Cdd:PRK05670  89 ---------FG--------------GKVVRAKEIMhgktspIEHDGSGiFAglpnpftvtryhsLVVDRESLPDCLE--- 142

                        170       180       190
                 ....*....|....*....|....*....|...
gi 808366157 377 VNA--NDSSVEGIIRTELNeqramVWGVQFHPE 407
Cdd:PRK05670 143 VTAwtDDGEIMGVRHKELP-----IYGVQFHPE 170
PRK13566 PRK13566
anthranilate synthase component I;
208-407 6.01e-06

anthranilate synthase component I;


Pssm-ID: 237429 [Multi-domain]  Cd Length: 720  Bit Score: 48.76  E-value: 6.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157 208 IAKVSTKEPYVLHPVGGAKAARAHVALMDF-GCKANILRSLLRR-GASVTVLPWDYDFNKV-RDGFDGLFLSNGPGSPYs 284
Cdd:PRK13566 505 LRGAKPKNLSAEEPDAAAVGEGKRVLLVDHeDSFVHTLANYFRQtGAEVTTVRYGFAEEMLdRVNPDLVVLSPGPGRPS- 583

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157 285 iEPALNMARKAVAEWDRPIFGICMGHQVIGIAAGVE----AYRM--KFGNRGHNQPVVALKSAGNFVKRGRvYitsqnhg 358
Cdd:PRK13566 584 -DFDCKATIDAALARNLPIFGVCLGLQAIVEAFGGElgqlAYPMhgKPSRIRVRGPGRLFSGLPEEFTVGR-Y------- 654

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 808366157 359 YALTPDESKWPQGWQpwfVNAndSSVEGIIRTeLNEQRAMVWGVQFHPE 407
Cdd:PRK13566 655 HSLFADPETLPDELL---VTA--ETEDGVIMA-IEHKTLPVAAVQFHPE 697
trpG_papA TIGR00566
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ...
 242-407 7.17e-05

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: 43.62  E-value: 7.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157  242 NILRSLLRRGASVTVLPWDYDFNKVRDGFDGLFLSNGPGSPYSIEPALNMARKAVAEWDRPIFGICMGHQVIGIAAG--- 318
Cdd:TIGR00566  14 NLVQYFCELGAEVVVKRNDSLTLQEIEALLPLLIVISPGPCTPNEAGISLEAIRHFAGKLPILGVCLGHQAMGQAFGgdv 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157  319 VEAYRMKFG---NRGHNQPVVALKSAGNFVkrgrvyiTSQNHGYALTPDESkwpqgwqPWFVNANDSSVEGI----IRTe 391
Cdd:TIGR00566  94 VRANTVMHGktsEIEHNGAGIFRGLFNPLT-------ATRYHSLVVEPETL-------PTCFPVTAWEEENIeimaIRH- 158

                         170
                  ....*....|....*..
gi 808366157  392 lneqRAMVW-GVQFHPE 407
Cdd:TIGR00566 159 ----RDLPLeGVQFHPE 171
guaA PRK00074
GMP synthase; Reviewed
 256-431 7.80e-05

GMP synthase; Reviewed


Pssm-ID: 234614 [Multi-domain]  Cd Length: 511  Bit Score: 45.04  E-value: 7.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157 256 VLPWDYDFNKVRD-GFDGLFLSNGPGSPYSIE-PALNmarKAVAEWDRPIFGICMGHQVIGIAAG--VEayrmkfgnRGH 331
Cdd:PRK00074  32 IVPYDISAEEIRAfNPKGIILSGGPASVYEEGaPRAD---PEIFELGVPVLGICYGMQLMAHQLGgkVE--------RAG 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157 332 nqpvvalksagnfvKR--GRVYITSQNHGyAL---TPDESK-W----------PQGWQpwfVNA-NDSSVEGIIRtelNE 394
Cdd:PRK00074 101 --------------KReyGRAELEVDNDS-PLfkgLPEEQDvWmshgdkvtelPEGFK---VIAsTENCPIAAIA---NE 159

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 808366157 395 QRAMvWGVQFHPE--HAggpEDTNGIFEDFVEEVVRIKG 431
Cdd:PRK00074 160 ERKF-YGVQFHPEvtHT---PQGKKLLENFVFDICGCKG 194
PLN02335 PLN02335
anthranilate synthase
 272-335 1.74e-04

anthranilate synthase


Pssm-ID: 177969 [Multi-domain]  Cd Length: 222  Bit Score: 42.86  E-value: 1.74e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 808366157 272 GLFLSNGPGSPYSIEPALNMARKAVAEWdrPIFGICMGHQVIGIAAGVEAYRMKFG-NRGHNQPV 335
Cdd:PLN02335  65 GVLISPGPGTPQDSGISLQTVLELGPLV--PLFGVCMGLQCIGEAFGGKIVRSPFGvMHGKSSPV 127
ASKHA_NBD_Kae1_TsaD cd24031
nucleotide-binding domain (NBD) of the Kae1/TsaD family tRNA N6-adenosine ...
 217-343 4.75e-04

nucleotide-binding domain (NBD) of the Kae1/TsaD family tRNA N6-adenosine threonylcarbamoyltransferase; tRNA N6-adenosine threonylcarbamoyltransferase (EC 2.3.1.234), also called N6-L-threonylcarbamoyladenine synthase, t(6)A synthase, t(6)A37 threonylcarbamoyladenosine biosynthesis protein, or tRNA threonylcarbamoyladenosine biosynthesis protein, is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. It is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. The family includes different orthologous of tRNA N6-adenosine threonylcarbamoyltransferase, such as bacterial kinase-associated endopeptidase 1 (Kae1) and TsaD (also known as YgjD) protein, mammalian O-sialoglycoprotein endopeptidase (OSGEP) and yeast protein Kae1, as well as mammalian OSGEP-like protein 1 (OSGEPL1) and yeast protein Qri7, which are the mitochondrial versions of the universal Kae1/TsaD (also known as YgjD) protein and essential for mitochondrial genome maintenance.


Pssm-ID: 466881  Cd Length: 304  Bit Score: 42.08  E-value: 4.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157 217 YVLHPVGG---AKAARAHVALMdfgckanilRSLLRRGASVTvlpwdydfNKVRDGFDGLFLSNGPGSPYSIEPALNMAR 293
Cdd:cd24031   30 YVTPKAGGivpEEAARHHARKI---------VPLIQEALKES--------GLTAKDIDLIAYTQGPGLGGALRVGATVAR 92

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 808366157 294 KAVAEWDRPIFGI--CMGHqvigiaagVEAYRMKFGNRghnQPVVALKSAGN 343
Cdd:cd24031   93 TLAVAWNKPIIGVnhCIGH--------LEIPKLNTPAF---PPVALYVSGGN 133
PRK08007 PRK08007
aminodeoxychorismate synthase component 2;
273-407 2.98e-03

aminodeoxychorismate synthase component 2;


Pssm-ID: 181194 [Multi-domain]  Cd Length: 187  Bit Score: 38.74  E-value: 2.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157 273 LFLSNGPGSPYSIEPALNMARKAVAEWdrPIFGICMGHQVIGIAAGVEAYRMKFGNRGHNQPVvalKSAGNFVKRGRVYI 352
Cdd:PRK08007  47 IVISPGPCTPDEAGISLDVIRHYAGRL--PILGVCLGHQAMAQAFGGKVVRAAKVMHGKTSPI---THNGEGVFRGLANP 121

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 808366157 353 TSQNHGYALTPDESKWPQGWQpwfVNANDSSVE--GIIRTELNEQramvwGVQFHPE 407
Cdd:PRK08007 122 LTVTRYHSLVVEPDSLPACFE---VTAWSETREimGIRHRQWDLE-----GVQFHPE 170
PRK06774 PRK06774
aminodeoxychorismate synthase component II;
273-407 3.15e-03

aminodeoxychorismate synthase component II;


Pssm-ID: 180689 [Multi-domain]  Cd Length: 191  Bit Score: 38.69  E-value: 3.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808366157 273 LFLSNGPGSPYSIEPALNMARKAVAEWdrPIFGICMGHQVIGIAAGVEAYRMKFGNRGHNQpvvALKSAGNFVKRGRVYI 352
Cdd:PRK06774  47 LVISPGPCTPNEAGISLAVIRHFADKL--PILGVCLGHQALGQAFGARVVRARQVMHGKTS---AICHSGQGVFRGLNQP 121

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 808366157 353 TSQNHGYALTPDESKWPQGWQPWFVNANDSSVEGIIrtELNEQRAMVWGVQFHPE 407
Cdd:PRK06774 122 LTVTRYHSLVIAADSLPGCFELTAWSERGGEMDEIM--GIRHRTLPLEGVQFHPE 174
PLN02889 PLN02889
oxo-acid-lyase/anthranilate synthase
 270-320 7.42e-03

oxo-acid-lyase/anthranilate synthase


Pssm-ID: 215481 [Multi-domain]  Cd Length: 918  Bit Score: 39.06  E-value: 7.42e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 808366157 270 FDGLFLSNGPGSPY---SIEPALNMARKAVaewDRPIFGICMGHQVIGIAAGVE 320
Cdd:PLN02889 132 FDNIVISPGPGSPTcpaDIGICLRLLLECR---DIPILGVCLGHQALGYVHGAR 182
 
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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