|
Name |
Accession |
Description |
Interval |
E-value |
| CarA |
COG0505 |
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ... |
35-396 |
0e+00 |
|
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase small subunit is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 440271 [Multi-domain] Cd Length: 361 Bit Score: 618.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788586792 35 DGRVFRGRGFGATGTTLGEAVFTTAMTGYQETLTDPSYHRQLVVATAPQIGNTGWNDEDYESRgnKIWAAGFIIRDLSRI 114
Cdd:COG0505 11 DGTVFEGKSFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVTFTYPHIGNYGVNDEDFESD--RPWVAGLVVRELSRR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788586792 115 PSNWRSERSLEDELKAQGIIGIRQIDTRALVRHLRDNGSIAAGIFSGEDaqqPVDKLVEIVRAQPAMKGADLAREVSTDQ 194
Cdd:COG0505 89 PSNWRSEESLDEYLKEHGIPGISGIDTRALTRHLREKGAMKGVISTGDL---DIEELLEKARAAPGMEGLDLVKEVSTKE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788586792 195 AYVVEAQGEKKARVVAYDLGIKSNTPRELAKRGLEVVVVPANTPYEDIKkEYQPDGVFLSNGPGDPATADEMVAVAKAAL 274
Cdd:COG0505 166 PYEWTEAPGAGFHVVALDFGVKRNILRELAERGCRVTVVPATTSAEEIL-ALNPDGVFLSNGPGDPAALDYAIETIRELL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788586792 275 DDGMPLFGICFGNQILGRALGLNTYKLVFGHRGVNVPVKDHRTGRIFITAQNHGFALEGKAGESFDtpwgeAEVTHTCLN 354
Cdd:COG0505 245 GKGIPIFGICLGHQLLALALGAKTYKLKFGHRGANHPVKDLETGRVEITSQNHGFAVDEDSLPATD-----LEVTHVNLN 319
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2788586792 355 DDVVEGVALKNGMAFSVQYHPESAAGPHDAHSLFDDFLELIQ 396
Cdd:COG0505 320 DGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDRFIELME 361
|
|
| PRK12564 |
PRK12564 |
carbamoyl-phosphate synthase small subunit; |
35-395 |
0e+00 |
|
carbamoyl-phosphate synthase small subunit;
Pssm-ID: 237139 [Multi-domain] Cd Length: 360 Bit Score: 600.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788586792 35 DGRVFRGRGFGATGTTLGEAVFTTAMTGYQETLTDPSYHRQLVVATAPQIGNTGWNDEDYESrgNKIWAAGFIIRDLSRI 114
Cdd:PRK12564 11 DGTVFEGKAFGAEGETVGEVVFNTSMTGYQEILTDPSYAGQIVTFTYPLIGNYGVNREDFES--DRPHAKGLIVRELSDI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788586792 115 PSNWRSERSLEDELKAQGIIGIRQIDTRALVRHLRDNGSIAAGIFSGEDaqqPVDKLVEIVRAQPAMKGADLAREVSTDQ 194
Cdd:PRK12564 89 PSNWRSEMSLDEYLKENGIPGISGIDTRALTRKLREKGAMKGVIATEDF---DAEELLEKARAFPGLLGLDLVKEVSTKE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788586792 195 AYVV-EAQGEKKARVVAYDLGIKSNTPRELAKRGLEVVVVPANTPYEDIKKeYQPDGVFLSNGPGDPATADEMVAVAKAA 273
Cdd:PRK12564 166 PYPWpGPGGELKYKVVAIDFGVKRNILRELAERGCRVTVVPATTTAEEILA-LNPDGVFLSNGPGDPAALDYAIEMIREL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788586792 274 LDDGMPLFGICFGNQILGRALGLNTYKLVFGHRGVNVPVKDHRTGRIFITAQNHGFALEGkagesfDTPWGEAEVTHTCL 353
Cdd:PRK12564 245 LEKKIPIFGICLGHQLLALALGAKTYKMKFGHRGANHPVKDLETGKVEITSQNHGFAVDE------DSLPANLEVTHVNL 318
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2788586792 354 NDDVVEGVALKNGMAFSVQYHPESAAGPHDAHSLFDDFLELI 395
Cdd:PRK12564 319 NDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDEFVELM 360
|
|
| CPSaseIIsmall |
TIGR01368 |
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ... |
35-397 |
0e+00 |
|
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small chain of the glutamine-dependent form (EC 6.3.5.5) of carbamoyl phosphate synthase, CPSase II. The C-terminal domain has glutamine amidotransferase activity. Note that the sequence from the mammalian urea cycle form has lost the active site Cys, resulting in an ammonia-dependent form, CPSase I (EC 6.3.4.16). CPSases of pyrimidine biosynthesis, arginine biosynthesis, and the urea cycle may be encoded by one or by several genes, depending on the species. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273580 [Multi-domain] Cd Length: 357 Bit Score: 519.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788586792 35 DGRVFRGRGFGATGTTLGEAVFTTAMTGYQETLTDPSYHRQLVVATAPQIGNTGWNDEDYESrgNKIWAAGFIIRDLSRI 114
Cdd:TIGR01368 7 DGTVFRGYSFGAEGTVAGEVVFNTGMTGYQEILTDPSYKGQIVVFTYPLIGNYGVNDEDAES--KGIHVSGLVVRELSDR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788586792 115 PSNWRSERSLEDELKAQGIIGIRQIDTRALVRHLRDNGSIAAGIFSGEDaqqPVDKLVEIVRAQPAMKGADLAREVSTDQ 194
Cdd:TIGR01368 85 YSNWRATESLDQFLKRHGIPGIYGVDTRALVKKIREKGTMKGVISTEDS---NDEELVEKARVSPDITGINLVAEVSTKE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788586792 195 AYVVEAQGEKKARVVAYDLGIKSNTPRELAKRGLEVVVVPANTPYEDIKKeYQPDGVFLSNGPGDPATADEMVAVAKAAL 274
Cdd:TIGR01368 162 PYTWGQRGGKGKRVVVIDFGVKRNILRRLVKRGCEVTVVPYDTDAEEIKK-YNPDGIFLSNGPGDPAAVEPAIETIRKLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788586792 275 DDgMPLFGICFGNQILGRALGLNTYKLVFGHRGVNVPVKDHRTGRIFITAQNHGFALEGKAgesfdTPWGEAEVTHTCLN 354
Cdd:TIGR01368 241 EK-IPIFGICLGHQLLALAFGAKTYKMKFGHRGGNHPVKDLITGRVEITSQNHGYAVDPDS-----LPAGDLEVTHVNLN 314
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2788586792 355 DDVVEGVALKNGMAFSVQYHPESAAGPHDAHSLFDDFLELIQK 397
Cdd:TIGR01368 315 DGTVEGIRHKDLPVFSVQYHPEASPGPHDTEYLFDEFIDLMKK 357
|
|
| GATase1_CPSase |
cd01744 |
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ... |
208-392 |
1.09e-94 |
|
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: 281.31 E-value: 1.09e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788586792 208 VVAYDLGIKSNTPRELAKRGLEVVVVPANTPYEDIKKeYQPDGVFLSNGPGDPATADEMVAVAKAALDDGMPLFGICFGN 287
Cdd:cd01744 1 VVVIDFGVKHNILRELLKRGCEVTVVPYNTDAEEILK-LDPDGIFLSNGPGDPALLDEAIKTVRKLLGKKIPIFGICLGH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788586792 288 QILGRALGLNTYKLVFGHRGVNVPVKDHRTGRIFITAQNHGFALEgkaGESFDTPWgeaEVTHTCLNDDVVEGVALKNGM 367
Cdd:cd01744 80 QLLALALGAKTYKMKFGHRGSNHPVKDLITGRVYITSQNHGYAVD---PDSLPGGL---EVTHVNLNDGTVEGIRHKDLP 153
|
170 180
....*....|....*....|....*
gi 2788586792 368 AFSVQYHPESAAGPHDAHSLFDDFL 392
Cdd:cd01744 154 VFSVQFHPEASPGPHDTEYLFDEFL 178
|
|
| CPSase_sm_chain |
pfam00988 |
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ... |
35-158 |
1.89e-75 |
|
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase domain is in the amino terminus of protein. Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00289. The small chain has a GATase domain in the carboxyl terminus. See pfam00117.
Pssm-ID: 460017 [Multi-domain] Cd Length: 126 Bit Score: 230.29 E-value: 1.89e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788586792 35 DGRVFRGRGFGATGTTLGEAVFTTAMTGYQETLTDPSYHRQLVVATAPQIGNTGWNDEDYESrgNKIWAAGFIIRDLSRI 114
Cdd:pfam00988 5 DGTVFEGKSFGAAGSTVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNPEDFES--DKIHVAGLVVREYSDE 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2788586792 115 PSNWRSERSLEDELKAQGIIGIRQIDTRALVRHLRDNGSIAAGI 158
Cdd:pfam00988 83 PSNWRAEESLDEWLKEQGIPGISGVDTRALTRKIREKGAMKGVI 126
|
|
| CPSase_sm_chain |
smart01097 |
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ... |
35-158 |
1.32e-74 |
|
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: 228.41 E-value: 1.32e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788586792 35 DGRVFRGRGFGATGTTLGEAVFTTAMTGYQETLTDPSYHRQLVVATAPQIGNTGWNDEDYESrgNKIWAAGFIIRDLSRI 114
Cdd:smart01097 9 DGTVFEGESFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNDEDFES--DKIQVKGLVVRELSDE 86
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2788586792 115 PSNWRSERSLEDELKAQGIIGIRQIDTRALVRHLRDNGSIAAGI 158
Cdd:smart01097 87 PSNWRSEQSLDEFLKENGIPGISGIDTRALTRKLREKGAMKGVI 130
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CarA |
COG0505 |
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ... |
35-396 |
0e+00 |
|
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase small subunit is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 440271 [Multi-domain] Cd Length: 361 Bit Score: 618.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788586792 35 DGRVFRGRGFGATGTTLGEAVFTTAMTGYQETLTDPSYHRQLVVATAPQIGNTGWNDEDYESRgnKIWAAGFIIRDLSRI 114
Cdd:COG0505 11 DGTVFEGKSFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVTFTYPHIGNYGVNDEDFESD--RPWVAGLVVRELSRR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788586792 115 PSNWRSERSLEDELKAQGIIGIRQIDTRALVRHLRDNGSIAAGIFSGEDaqqPVDKLVEIVRAQPAMKGADLAREVSTDQ 194
Cdd:COG0505 89 PSNWRSEESLDEYLKEHGIPGISGIDTRALTRHLREKGAMKGVISTGDL---DIEELLEKARAAPGMEGLDLVKEVSTKE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788586792 195 AYVVEAQGEKKARVVAYDLGIKSNTPRELAKRGLEVVVVPANTPYEDIKkEYQPDGVFLSNGPGDPATADEMVAVAKAAL 274
Cdd:COG0505 166 PYEWTEAPGAGFHVVALDFGVKRNILRELAERGCRVTVVPATTSAEEIL-ALNPDGVFLSNGPGDPAALDYAIETIRELL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788586792 275 DDGMPLFGICFGNQILGRALGLNTYKLVFGHRGVNVPVKDHRTGRIFITAQNHGFALEGKAGESFDtpwgeAEVTHTCLN 354
Cdd:COG0505 245 GKGIPIFGICLGHQLLALALGAKTYKLKFGHRGANHPVKDLETGRVEITSQNHGFAVDEDSLPATD-----LEVTHVNLN 319
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2788586792 355 DDVVEGVALKNGMAFSVQYHPESAAGPHDAHSLFDDFLELIQ 396
Cdd:COG0505 320 DGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDRFIELME 361
|
|
| PRK12564 |
PRK12564 |
carbamoyl-phosphate synthase small subunit; |
35-395 |
0e+00 |
|
carbamoyl-phosphate synthase small subunit;
Pssm-ID: 237139 [Multi-domain] Cd Length: 360 Bit Score: 600.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788586792 35 DGRVFRGRGFGATGTTLGEAVFTTAMTGYQETLTDPSYHRQLVVATAPQIGNTGWNDEDYESrgNKIWAAGFIIRDLSRI 114
Cdd:PRK12564 11 DGTVFEGKAFGAEGETVGEVVFNTSMTGYQEILTDPSYAGQIVTFTYPLIGNYGVNREDFES--DRPHAKGLIVRELSDI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788586792 115 PSNWRSERSLEDELKAQGIIGIRQIDTRALVRHLRDNGSIAAGIFSGEDaqqPVDKLVEIVRAQPAMKGADLAREVSTDQ 194
Cdd:PRK12564 89 PSNWRSEMSLDEYLKENGIPGISGIDTRALTRKLREKGAMKGVIATEDF---DAEELLEKARAFPGLLGLDLVKEVSTKE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788586792 195 AYVV-EAQGEKKARVVAYDLGIKSNTPRELAKRGLEVVVVPANTPYEDIKKeYQPDGVFLSNGPGDPATADEMVAVAKAA 273
Cdd:PRK12564 166 PYPWpGPGGELKYKVVAIDFGVKRNILRELAERGCRVTVVPATTTAEEILA-LNPDGVFLSNGPGDPAALDYAIEMIREL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788586792 274 LDDGMPLFGICFGNQILGRALGLNTYKLVFGHRGVNVPVKDHRTGRIFITAQNHGFALEGkagesfDTPWGEAEVTHTCL 353
Cdd:PRK12564 245 LEKKIPIFGICLGHQLLALALGAKTYKMKFGHRGANHPVKDLETGKVEITSQNHGFAVDE------DSLPANLEVTHVNL 318
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2788586792 354 NDDVVEGVALKNGMAFSVQYHPESAAGPHDAHSLFDDFLELI 395
Cdd:PRK12564 319 NDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDEFVELM 360
|
|
| CPSaseIIsmall |
TIGR01368 |
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ... |
35-397 |
0e+00 |
|
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small chain of the glutamine-dependent form (EC 6.3.5.5) of carbamoyl phosphate synthase, CPSase II. The C-terminal domain has glutamine amidotransferase activity. Note that the sequence from the mammalian urea cycle form has lost the active site Cys, resulting in an ammonia-dependent form, CPSase I (EC 6.3.4.16). CPSases of pyrimidine biosynthesis, arginine biosynthesis, and the urea cycle may be encoded by one or by several genes, depending on the species. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273580 [Multi-domain] Cd Length: 357 Bit Score: 519.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788586792 35 DGRVFRGRGFGATGTTLGEAVFTTAMTGYQETLTDPSYHRQLVVATAPQIGNTGWNDEDYESrgNKIWAAGFIIRDLSRI 114
Cdd:TIGR01368 7 DGTVFRGYSFGAEGTVAGEVVFNTGMTGYQEILTDPSYKGQIVVFTYPLIGNYGVNDEDAES--KGIHVSGLVVRELSDR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788586792 115 PSNWRSERSLEDELKAQGIIGIRQIDTRALVRHLRDNGSIAAGIFSGEDaqqPVDKLVEIVRAQPAMKGADLAREVSTDQ 194
Cdd:TIGR01368 85 YSNWRATESLDQFLKRHGIPGIYGVDTRALVKKIREKGTMKGVISTEDS---NDEELVEKARVSPDITGINLVAEVSTKE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788586792 195 AYVVEAQGEKKARVVAYDLGIKSNTPRELAKRGLEVVVVPANTPYEDIKKeYQPDGVFLSNGPGDPATADEMVAVAKAAL 274
Cdd:TIGR01368 162 PYTWGQRGGKGKRVVVIDFGVKRNILRRLVKRGCEVTVVPYDTDAEEIKK-YNPDGIFLSNGPGDPAAVEPAIETIRKLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788586792 275 DDgMPLFGICFGNQILGRALGLNTYKLVFGHRGVNVPVKDHRTGRIFITAQNHGFALEGKAgesfdTPWGEAEVTHTCLN 354
Cdd:TIGR01368 241 EK-IPIFGICLGHQLLALAFGAKTYKMKFGHRGGNHPVKDLITGRVEITSQNHGYAVDPDS-----LPAGDLEVTHVNLN 314
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2788586792 355 DDVVEGVALKNGMAFSVQYHPESAAGPHDAHSLFDDFLELIQK 397
Cdd:TIGR01368 315 DGTVEGIRHKDLPVFSVQYHPEASPGPHDTEYLFDEFIDLMKK 357
|
|
| PRK12838 |
PRK12838 |
carbamoyl phosphate synthase small subunit; Reviewed |
35-397 |
2.52e-143 |
|
carbamoyl phosphate synthase small subunit; Reviewed
Pssm-ID: 183784 [Multi-domain] Cd Length: 354 Bit Score: 411.98 E-value: 2.52e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788586792 35 DGRVFRGRGFGATGTTLGEAVFTTAMTGYQETLTDPSYHRQLVVATAPQIGNTGWNDEDYESRgnKIWAAGFIIRDLSRI 114
Cdd:PRK12838 9 DGTVFEGELIGAPIDVTGEIVFNTGMTGYQEVLTDPSYKGQIVVFTYPLIGNYGINADDYESK--QPQVKGVIVYELSRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788586792 115 PSNWRSERSLEDELKAQGIIGIRQIDTRALVRHLRDNGSIAAGIFSGEDaqqpvdklvEIVRAQ--PAMKGADLAREVST 192
Cdd:PRK12838 87 GSHYRAKQSLDDFLKEWNIPGISGVDTRALVKHIREKGTMKASITTTDD---------AHAFDQikALVLPKNVVAQVST 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788586792 193 DQAYVVEAQGEKkarVVAYDLGIKSNTPRELAKRGLEVVVVPANTPYEDIkKEYQPDGVFLSNGPGDPATADEMVAVAKa 272
Cdd:PRK12838 158 KEPYTYGNGGKH---VALIDFGYKKSILRSLSKRGCKVTVLPYDTSLEEI-KNLNPDGIVLSNGPGDPKELQPYLPEIK- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788586792 273 ALDDGMPLFGICFGNQILGRALGLNTYKLVFGHRGVNVPVKDHRTGRIFITAQNHGFALEgkaGESFD-TPWgeaEVTHT 351
Cdd:PRK12838 233 KLISSYPILGICLGHQLIALALGADTEKLPFGHRGANHPVIDLTTGRVWMTSQNHGYVVD---EDSLDgTPL---SVRFF 306
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 2788586792 352 CLNDDVVEGVALKNGMAFSVQYHPESAAGPHDAHSLFDDFLELIQK 397
Cdd:PRK12838 307 NVNDGSIEGLRHKKKPVLSVQFHPEAHPGPHDAEYIFDEFLEMMEK 352
|
|
| carA |
CHL00197 |
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional |
35-397 |
6.75e-116 |
|
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
Pssm-ID: 214392 [Multi-domain] Cd Length: 382 Bit Score: 343.32 E-value: 6.75e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788586792 35 DGRVFRGRGFGATGTTLGEAVFTTAMTGYQETLTDPSYHRQLVVATAPQIGNTGWNDEDYESrgNKIWAAGFIIRDLSRI 114
Cdd:CHL00197 13 DGTYYRGWSFSNPITTIGEVVFNTGMTGYQEIITDPSYFEQIVTFTYPEIGNTGINLEDIES--VKIQVKGIIAKNICKS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788586792 115 PSNWRSERSLEDELKAQGIIGIRQIDTRALVRHLRDNGSIaAGIFSGE--DAQQPVDKLVEIvraqPAMKGADLAREVST 192
Cdd:CHL00197 91 SSNWRQQESLVSYLQRHKIPFIFGIDTRALTQHLRRFGTM-NGCISNQnlNLSYLRAKIKES----PHMPSSDLIPRVTT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788586792 193 DQ--------------AYVVEAQGEKKARVVAYDLGIKSNTPRELAKRGLEVVVVPANTPYEDIKKeYQPDGVFLSNGPG 258
Cdd:CHL00197 166 SSyyewdekshpsfylADNKRPHSSYQLKIIVIDFGVKYNILRRLKSFGCSITVVPATSPYQDILS-YQPDGILLSNGPG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788586792 259 DPATADEMVAVAKAALDDGMPLFGICFGNQILGRALGLNTYKLVFGHRGVNVPVKDHRtgRIFITAQNHGFALEgkaGES 338
Cdd:CHL00197 245 DPSAIHYGIKTVKKLLKYNIPIFGICMGHQILSLALEAKTFKLKFGHRGLNHPSGLNQ--QVEITSQNHGFAVN---LES 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2788586792 339 FDTpwGEAEVTHTCLNDDVVEGVALKNGMAFSVQYHPESAAGPHDAHSLFDDFLELIQK 397
Cdd:CHL00197 320 LAK--NKFYITHFNLNDGTVAGISHSPKPYFSVQYHPEASPGPHDADYLFEYFIEIIKH 376
|
|
| PLN02771 |
PLN02771 |
carbamoyl-phosphate synthase (glutamine-hydrolyzing) |
35-388 |
5.30e-100 |
|
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
Pssm-ID: 178370 [Multi-domain] Cd Length: 415 Bit Score: 303.82 E-value: 5.30e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788586792 35 DGRVFRGRGFGATGTTLGEAVFTTAMTGYQETLTDPSYHRQLVVATAPQIGNTGWNDEDYESRgnKIWAAGFIIRDLSRI 114
Cdd:PLN02771 63 DGSVWKAKSFGARGTQVGEVVFNTSLTGYQEILTDPSYAGQFVLMTNPHIGNTGVNFDDEESR--QCFLAGLVIRSLSIS 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788586792 115 PSNWRSERSLEDELKAQGIIGIRQIDTRALVRHLRDNGSIaAGIFSGEDAQQPvDKLVEIVRAQPaMKGADLAREVSTDQ 194
Cdd:PLN02771 141 TSNWRCTKTLGDYLAERNIMGIYDVDTRAITRRLREDGSL-IGVLSTEDSKTD-EELLKMSRSWD-IVGIDLISGVSCKS 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788586792 195 AYV------------VEAQGEKKARVVAYDLGIKSNTPRELAKRGLEVVVVPANTPYEDIKKeYQPDGVFLSNGPGDPAT 262
Cdd:PLN02771 218 PYEwvdktnpewdfnTNSRDGESYHVIAYDFGIKHNILRRLASYGCKITVVPSTWPASEALK-MKPDGVLFSNGPGDPSA 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788586792 263 ADEMVAVAKAALDDgMPLFGICFGNQILGRALGLNTYKLVFGHRGVNVPVKDHRTGRIFITAQNHGFALEGKAgesfdTP 342
Cdd:PLN02771 297 VPYAVETVKELLGK-VPVFGICMGHQLLGQALGGKTFKMKFGHHGGNHPVRNNRTGRVEISAQNHNYAVDPAS-----LP 370
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 2788586792 343 WGeAEVTHTCLNDDVVEGVALKNGMAFSVQYHPESAAGPHDAHSLF 388
Cdd:PLN02771 371 EG-VEVTHVNLNDGSCAGLAFPALNVMSLQYHPEASPGPHDSDNAF 415
|
|
| GATase1_CPSase |
cd01744 |
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ... |
208-392 |
1.09e-94 |
|
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: 281.31 E-value: 1.09e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788586792 208 VVAYDLGIKSNTPRELAKRGLEVVVVPANTPYEDIKKeYQPDGVFLSNGPGDPATADEMVAVAKAALDDGMPLFGICFGN 287
Cdd:cd01744 1 VVVIDFGVKHNILRELLKRGCEVTVVPYNTDAEEILK-LDPDGIFLSNGPGDPALLDEAIKTVRKLLGKKIPIFGICLGH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788586792 288 QILGRALGLNTYKLVFGHRGVNVPVKDHRTGRIFITAQNHGFALEgkaGESFDTPWgeaEVTHTCLNDDVVEGVALKNGM 367
Cdd:cd01744 80 QLLALALGAKTYKMKFGHRGSNHPVKDLITGRVYITSQNHGYAVD---PDSLPGGL---EVTHVNLNDGTVEGIRHKDLP 153
|
170 180
....*....|....*....|....*
gi 2788586792 368 AFSVQYHPESAAGPHDAHSLFDDFL 392
Cdd:cd01744 154 VFSVQFHPEASPGPHDTEYLFDEFL 178
|
|
| CPSase_sm_chain |
pfam00988 |
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ... |
35-158 |
1.89e-75 |
|
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase domain is in the amino terminus of protein. Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00289. The small chain has a GATase domain in the carboxyl terminus. See pfam00117.
Pssm-ID: 460017 [Multi-domain] Cd Length: 126 Bit Score: 230.29 E-value: 1.89e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788586792 35 DGRVFRGRGFGATGTTLGEAVFTTAMTGYQETLTDPSYHRQLVVATAPQIGNTGWNDEDYESrgNKIWAAGFIIRDLSRI 114
Cdd:pfam00988 5 DGTVFEGKSFGAAGSTVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNPEDFES--DKIHVAGLVVREYSDE 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2788586792 115 PSNWRSERSLEDELKAQGIIGIRQIDTRALVRHLRDNGSIAAGI 158
Cdd:pfam00988 83 PSNWRAEESLDEWLKEQGIPGISGVDTRALTRKIREKGAMKGVI 126
|
|
| CPSase_sm_chain |
smart01097 |
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ... |
35-158 |
1.32e-74 |
|
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: 228.41 E-value: 1.32e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788586792 35 DGRVFRGRGFGATGTTLGEAVFTTAMTGYQETLTDPSYHRQLVVATAPQIGNTGWNDEDYESrgNKIWAAGFIIRDLSRI 114
Cdd:smart01097 9 DGTVFEGESFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNDEDFES--DKIQVKGLVVRELSDE 86
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2788586792 115 PSNWRSERSLEDELKAQGIIGIRQIDTRALVRHLRDNGSIAAGI 158
Cdd:smart01097 87 PSNWRSEQSLDEFLKENGIPGISGIDTRALTRKLREKGAMKGVI 130
|
|
| GATase |
pfam00117 |
Glutamine amidotransferase class-I; |
208-394 |
1.81e-52 |
|
Glutamine amidotransferase class-I;
Pssm-ID: 395067 [Multi-domain] Cd Length: 188 Bit Score: 173.58 E-value: 1.81e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788586792 208 VVAYDLGIKSNTPRELAKRGLEVVVVPANTPYEDIKKEYqPDGVFLSNGPGDPATADEMVAVAKAALDDGMPLFGICFGN 287
Cdd:pfam00117 2 LIDNGDSFTYNLARALRELGVEVTVVPNDTPAEEILEEN-PDGIILSGGPGSPGAAGGAIEAIREARELKIPILGICLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788586792 288 QILGRALGLNTYKL-VFGHRGVNVPVKDHR------TGRIFITAQNHGFALEGKAGESfdtpwgEAEVTHTCLNDDVVEG 360
Cdd:pfam00117 81 QLLALAFGGKVVKAkKFGHHGKNSPVGDDGcglfygLPNVFIVRRYHSYAVDPDTLPD------GLEVTATSENDGTIMG 154
|
170 180 190
....*....|....*....|....*....|....
gi 2788586792 361 VALKNGMAFSVQYHPESAAGPHDAHSLFDDFLEL 394
Cdd:pfam00117 155 IRHKKLPIFGVQFHPESILTPHGPEILFNFFIKA 188
|
|
| GATase1_Anthranilate_Synthase |
cd01743 |
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ... |
223-392 |
5.79e-19 |
|
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase (ASase). This group contains proteins similar to para-aminobenzoate (PABA) synthase and ASase. These enzymes catalyze similar reactions and produce similar products, PABA and ortho-aminobenzoate (anthranilate). Each enzyme is composed of non-identical subunits: a glutamine amidotransferase subunit (component II) and a subunit that produces an aminobenzoate products (component I). ASase catalyses the synthesis of anthranilate from chorismate and glutamine and is a tetrameric protein comprising two copies each of components I and II. Component II of ASase belongs to the family of triad GTases which hydrolyze glutamine and transfer nascent ammonia between the active sites. In some bacteria, such as Escherichia coli, component II can be much larger than in other organisms, due to the presence of phosphoribosyl-anthranilate transferase (PRTase) activity. PRTase catalyses the second step in tryptophan biosynthesis and results in the addition of 5-phosphoribosyl-1-pyrophosphate to anthranilate to create N-5'-phosphoribosyl-anthranilate. In E.coli, the first step in the conversion of chorismate to PABA involves two proteins: PabA and PabB which co-operate to transfer the amide nitrogen of glutamine to chorismate forming 4-amino-4 deoxychorismate (ADC). PabA acts as a glutamine amidotransferase, supplying an amino group to PabB, which carries out the amination reaction. A third protein PabC then mediates elimination of pyruvate and aromatization to give PABA. Several organisms have bipartite proteins containing fused domains homologous to PabA and PabB commonly called PABA synthases. These hybrid PABA synthases may produce ADC and not PABA.
Pssm-ID: 153214 [Multi-domain] Cd Length: 184 Bit Score: 84.12 E-value: 5.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788586792 223 LAKRGLEVVVVPANTPYEDIKKEYQPDGVFLSNGPGDPATADEMVAVAKaALDDGMPLFGICFGNQILGRALGLNTYKLV 302
Cdd:cd01743 18 LRELGAEVVVVRNDEITLEELELLNPDAIVISPGPGHPEDAGISLEIIR-ALAGKVPILGVCLGHQAIAEAFGGKVVRAP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788586792 303 FGHRGVNVPVKDHRTGRIFITAQN------HGFALEgkagesfDTPWGEAEVTHTCLNDDVVEGVALKNGMAFSVQYHPE 376
Cdd:cd01743 97 EPMHGKTSEIHHDGSGLFKGLPQPftvgryHSLVVD-------PDPLPDLLEVTASTEDGVIMALRHRDLPIYGVQFHPE 169
|
170
....*....|....*.
gi 2788586792 377 SAAGPHdAHSLFDDFL 392
Cdd:cd01743 170 SILTEY-GLRLLENFL 184
|
|
| PRK05670 |
PRK05670 |
anthranilate synthase component II; Provisional |
221-394 |
1.69e-11 |
|
anthranilate synthase component II; Provisional
Pssm-ID: 235552 [Multi-domain] Cd Length: 189 Bit Score: 62.84 E-value: 1.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788586792 221 RELakrGLEVVVVPANTPYEDIKKEYQPDGVFLSNGPGDPATADEMVAVAKaALDDGMPLFGICFGNQILGRALGlntyk 300
Cdd:PRK05670 20 GEL---GAEVVVYRNDEITLEEIEALNPDAIVLSPGPGTPAEAGISLELIR-EFAGKVPILGVCLGHQAIGEAFG----- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788586792 301 lvfGHRGvnvpvkdhRTGRIF------ITAQNHG-FA-LEGK---------AGESFDTPwGEAEVTHTClNDDVVEGVAL 363
Cdd:PRK05670 91 ---GKVV--------RAKEIMhgktspIEHDGSGiFAgLPNPftvtryhslVVDRESLP-DCLEVTAWT-DDGEIMGVRH 157
|
170 180 190
....*....|....*....|....*....|.
gi 2788586792 364 KNGMAFSVQYHPESAAGPHdAHSLFDDFLEL 394
Cdd:PRK05670 158 KELPIYGVQFHPESILTEH-GHKLLENFLEL 187
|
|
| GATase1_1 |
cd01741 |
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ... |
221-376 |
1.91e-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: 56.87 E-value: 1.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788586792 221 RELAKRGLEVVV--VPANTPYEDIKKeyqPDGVFLSNGPGDPATADE--MVAVA---KAALDDGMPLFGICFGNQILGRA 293
Cdd:cd01741 21 REAGAETIEIDVvdVYAGELLPDLDD---YDGLVILGGPMSVDEDDYpwLKKLKeliRQALAAGKPVLGICLGHQLLARA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788586792 294 LG----LNTYKLVFGHRGVNVpVKDHRTGRIFITAQNHGFALEGKaGESFD------TPWGEAEVTHtclnddvVEGVAL 363
Cdd:cd01741 98 LGgkvgRNPKGWEIGWFPVTL-TEAGKADPLFAGLPDEFPVFHWH-GDTVVelppgaVLLASSEACP-------NQAFRY 168
|
170
....*....|...
gi 2788586792 364 KNGmAFSVQYHPE 376
Cdd:cd01741 169 GDR-ALGLQFHPE 180
|
|
| GATase1 |
cd01653 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
223-290 |
4.83e-09 |
|
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: 53.76 E-value: 4.83e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2788586792 223 LAKRGLEVVVVPANTPYEDIKKE-YQPDGVFLSNGPGDPATAD---EMVAVAKAALDDGMPLFGICFGNQIL 290
Cdd:cd01653 21 LREAGAEVDVVSPDGGPVESDVDlDDYDGLILPGGPGTPDDLArdeALLALLREAAAAGKPILGICLGAQLL 92
|
|
| PRK07765 |
PRK07765 |
aminodeoxychorismate/anthranilate synthase component II; |
249-377 |
5.85e-09 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181107 [Multi-domain] Cd Length: 214 Bit Score: 55.83 E-value: 5.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788586792 249 DGVFLSNGPGDPATADEMVAVAKAALDDGMPLFGICFGNQILGRALGLNTYK---LVFG------HRGVNV------Pvk 313
Cdd:PRK07765 48 DGVLLSPGPGTPERAGASIDMVRACAAAGTPLLGVCLGHQAIGVAFGATVDRapeLLHGktssvhHTGVGVlaglpdP-- 125
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2788586792 314 dhrtgriFITAQNHGFALEGkagesfDTPWGEAEVT-HTclNDDVVEGVALKNGMAFSVQYHPES 377
Cdd:PRK07765 126 -------FTATRYHSLTILP------ETLPAELEVTaRT--DSGVIMAVRHRELPIHGVQFHPES 175
|
|
| GATase1_GMP_Synthase |
cd01742 |
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ... |
221-376 |
8.08e-09 |
|
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: 54.85 E-value: 8.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788586792 221 RELakrGLEVVVVPANTPYEDIKKeYQPDGVFLSNGPgDPATADEMVAVAKAALDDGMPLFGICFGNQILGRALGlntyK 300
Cdd:cd01742 19 REL---GVYSEILPNTTPLEEIKL-KNPKGIILSGGP-SSVYEEDAPRVDPEIFELGVPVLGICYGMQLIAKALG----G 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788586792 301 LV-------FGHRGVNVPVKDHRTGRIFITAQ---NHGFALEgKAGESFDTpwgeAEVTHTCLnddvVEGVALKNGMAFS 370
Cdd:cd01742 90 KVergdkreYGKAEIEIDDSSPLFEGLPDEQTvwmSHGDEVV-KLPEGFKV----IASSDNCP----VAAIANEEKKIYG 160
|
....*.
gi 2788586792 371 VQYHPE 376
Cdd:cd01742 161 VQFHPE 166
|
|
| PRK13566 |
PRK13566 |
anthranilate synthase component I; |
227-377 |
1.24e-08 |
|
anthranilate synthase component I;
Pssm-ID: 237429 [Multi-domain] Cd Length: 720 Bit Score: 56.85 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788586792 227 GLEVVVVPANTPyEDIKKEYQPDGVFLSNGPGDPATADeMVAVAKAALDDGMPLFGICFGNQILGRALGlntyklvfGHR 306
Cdd:PRK13566 550 GAEVTTVRYGFA-EEMLDRVNPDLVVLSPGPGRPSDFD-CKATIDAALARNLPIFGVCLGLQAIVEAFG--------GEL 619
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788586792 307 GV-NVPVkdH-RTGRIFITaqnHGFALEGKAGESF------------DTPWGEAEVTHTcLNDDVVEGVALKNGMAFSVQ 372
Cdd:PRK13566 620 GQlAYPM--HgKPSRIRVR---GPGRLFSGLPEEFtvgryhslfadpETLPDELLVTAE-TEDGVIMAIEHKTLPVAAVQ 693
|
....*
gi 2788586792 373 YHPES 377
Cdd:PRK13566 694 FHPES 698
|
|
| GAT_1 |
cd03128 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
223-290 |
1.31e-08 |
|
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group contains proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA, the A4 beta-galactosidase middle domain and peptidase E. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase (CPSase), cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. Peptidase E is believed to be a serine peptidase having a Ser-His-Glu catalytic triad which differs from the Cys-His-Glu catalytic triad of typical GATase1 domains, by having a Ser in place of the reactive Cys at the nucleophile elbow. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase. Peptidase E has a circular permutation in the common core of a typical GTAse1 domain.
Pssm-ID: 153222 [Multi-domain] Cd Length: 92 Bit Score: 51.82 E-value: 1.31e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2788586792 223 LAKRGLEVVVVPANTPYEDIKKE-YQPDGVFLSNGPGDPATAD---EMVAVAKAALDDGMPLFGICFGNQIL 290
Cdd:cd03128 21 LREAGAEVDVVSPDGGPVESDVDlDDYDGLILPGGPGTPDDLAwdeALLALLREAAAAGKPVLGICLGAQLL 92
|
|
| Peptidase_C26 |
pfam07722 |
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ... |
230-376 |
3.57e-08 |
|
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze the cleavage of the gamma-glutamyl bond in poly-gamma-glutamyl substrates. They are structurally related to pfam00117, but contain extensions in four loops and at the C terminus.
Pssm-ID: 429620 [Multi-domain] Cd Length: 219 Bit Score: 53.41 E-value: 3.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788586792 230 VVVVPANTPYEDIKKEYQP-DGVFLSNGP--------------GDPATA--DEM-VAVAKAALDDGMPLFGICFGNQILG 291
Cdd:pfam07722 40 PVLLPILGDPEDAAAILDRlDGLLLTGGPnvdphfygeepsesGGPYDParDAYeLALIRAALARGKPILGICRGFQLLN 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788586792 292 RALGLNTY------KLVFGHRGVNVPVKDHRT-----------GRIFITAQ---N--HGFALEgKAGESFdtpwgeaEVT 349
Cdd:pfam07722 120 VALGGTLYqdiqeqPGFTDHREHCQVAPYAPShavnvepgsllASLLGSEEfrvNslHHQAID-RLAPGL-------RVE 191
|
170 180
....*....|....*....|....*....
gi 2788586792 350 HTClNDDVVEGVALKNGMAF--SVQYHPE 376
Cdd:pfam07722 192 AVA-PDGTIEAIESPNAKGFalGVQWHPE 219
|
|
| GATase1_2 |
cd01745 |
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ... |
223-391 |
1.25e-07 |
|
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group contains a subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain. GATase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. Glutamine amidotransferases (GATase) includes the triad family of amidotransferases which have a conserved Cys-His-Glu catalytic triad in the glutaminase active site. In this subgroup this triad is conserved. GATase activity can be found in a range of biosynthetic enzymes, including: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase , anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. Glutamine amidotransferase (GATase) domains can occur either as single polypeptides, as in glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.
Pssm-ID: 153216 [Multi-domain] Cd Length: 189 Bit Score: 51.42 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788586792 223 LAKRGLEVVVVPANTPYEDIKKEYQP-DGVFLSNGP-------GDPATADEM----------VAVAKAALDDGMPLFGIC 284
Cdd:cd01745 28 VRKAGGLPVLLPPVDDEEDLEQYLELlDGLLLTGGGdvdpplyGEEPHPELGpidperdafeLALLRAALERGKPILGIC 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788586792 285 FGNQILGRALGLNTYKLVfghrGVNvpvkdhrtgrifitaQNHGFALEgKAGESFdtpwgeaEVTHTClNDDVVEGVALK 364
Cdd:cd01745 108 RGMQLLNVALGGTLYQDI----RVN---------------SLHHQAIK-RLADGL-------RVEARA-PDGVIEAIESP 159
|
170 180
....*....|....*....|....*....
gi 2788586792 365 N-GMAFSVQYHPESAAGPHDAHS-LFDDF 391
Cdd:cd01745 160 DrPFVLGVQWHPEWLADTDPDSLkLFEAF 188
|
|
| guaA |
PRK00074 |
GMP synthase; Reviewed |
232-295 |
4.40e-07 |
|
GMP synthase; Reviewed
Pssm-ID: 234614 [Multi-domain] Cd Length: 511 Bit Score: 51.97 E-value: 4.40e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2788586792 232 VVPANTPYEDIKkEYQPDGVFLSNGPgDPATADEMVAVAKAALDDGMPLFGICFGNQILGRALG 295
Cdd:PRK00074 32 IVPYDISAEEIR-AFNPKGIILSGGP-ASVYEEGAPRADPEIFELGVPVLGICYGMQLMAHQLG 93
|
|
| PabB-fungal |
TIGR01823 |
aminodeoxychorismate synthase, fungal clade; This model represents the fungal clade of a ... |
230-410 |
5.25e-07 |
|
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: 51.83 E-value: 5.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788586792 230 VVVVPANTPYEDIKkEYQP--DGVFLSNGPGDPATADEMVAVAKA---ALDDGMPLFGICFGNQILGRALGLNTYKLvfg 304
Cdd:TIGR01823 35 VTTVHSDTFQDQLL-ELLPlfDAIVVGPGPGNPNNAQDMGIISELwelANLDEVPVLGICLGFQSLCLAQGADISRL--- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788586792 305 hrgvnvPVKDHrtGRIFITAQNHGFALEGKAG-------------ESFDT--PWGEAEVThtclNDDVVEGVALKNGMAF 369
Cdd:TIGR01823 111 ------PTPKH--GQVYEMHTNDAAIFCGLFSvkstryhslyanpEGIDTllPLCLTEDE----EGIILMSAQTKKKPWF 178
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2788586792 370 SVQYHPESAAGPHDAHSLFDDFLELiqkVDFNKSATGNSNK 410
Cdd:TIGR01823 179 GVQYHPESCCSELGSGKLVSNFLKL---AFINNVKTGRWEK 216
|
|
| GuaA1 |
COG0518 |
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ... |
221-295 |
6.78e-07 |
|
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: 49.94 E-value: 6.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788586792 221 RELAKRGLEVVVV--------PANTPYEDikkeyqPDGVFLSNGP-----GDPATADEMvAVAKAALDDGMPLFGICFGN 287
Cdd:COG0518 20 RRLREAGIELDVLrvyageilPYDPDLED------PDGLILSGGPmsvydEDPWLEDEP-ALIREAFELGKPVLGICYGA 92
|
....*...
gi 2788586792 288 QILGRALG 295
Cdd:COG0518 93 QLLAHALG 100
|
|
| PRK00758 |
PRK00758 |
GMP synthase subunit A; Validated |
227-394 |
7.64e-07 |
|
GMP synthase subunit A; Validated
Pssm-ID: 179112 [Multi-domain] Cd Length: 184 Bit Score: 49.08 E-value: 7.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788586792 227 GLEVVVVPANTPYEDIKKEyqPDGVFLSNGPgdpaTADEMVAVAKAALDDGMPLFGICFGNQILGRALGlntyklvfGHR 306
Cdd:PRK00758 23 GVDAKIIPNTTPVEEIKAF--EDGLILSGGP----DIERAGNCPEYLKELDVPILGICLGHQLIAKAFG--------GEV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788586792 307 G---------VNVPVKDHRTgrIFItaqnhGFALEGKAGESfdtpwgeaevtHtclNDDV-----------------VEG 360
Cdd:PRK00758 89 GrgeygeyalVEVEILDEDD--ILK-----GLPPEIRVWAS-----------H---ADEVkelpdgfeilarsdiceVEA 147
|
170 180 190
....*....|....*....|....*....|....
gi 2788586792 361 VALKNGMAFSVQYHPESAAGPHdAHSLFDDFLEL 394
Cdd:PRK00758 148 MKHKEKPIYGVQFHPEVAHTEY-GEEIFKNFLEI 180
|
|
| GATase_3 |
pfam07685 |
CobB/CobQ-like glutamine amidotransferase domain; |
225-368 |
6.80e-05 |
|
CobB/CobQ-like glutamine amidotransferase domain;
Pssm-ID: 429595 [Multi-domain] Cd Length: 189 Bit Score: 43.38 E-value: 6.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788586792 225 KRGLEVVVVPANTPYEDIKKEyqPDGVFLsngPG------DPATADEMVAVA--KAALDDGMPLFGICFGNQILGRAL-- 294
Cdd:pfam07685 22 RYEPAVRVRFVPLPDESLGPD--ADLIIL---PGgkptiqDLALLRNSGMDEaiKEAAEDGGPVLGICGGYQMLGETIed 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788586792 295 -------GLNtyklVFGHRGVNVPVKdhRTGRIFITAQNHGFALEG---KAGESFD----TPWGEAEVTHTCLNDDVVEG 360
Cdd:pfam07685 97 pegvrieGLG----LLDIETVFQKEK--LTGQVVGYLLLEGETVRGyeiHYGRTILgdgaKPLGRVKVGGGNNGEDGKDG 170
|
....*...
gi 2788586792 361 VALKNGMA 368
Cdd:pfam07685 171 AVSGNVFG 178
|
|
| PRK06774 |
PRK06774 |
aminodeoxychorismate synthase component II; |
227-393 |
7.12e-05 |
|
aminodeoxychorismate synthase component II;
Pssm-ID: 180689 [Multi-domain] Cd Length: 191 Bit Score: 43.31 E-value: 7.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788586792 227 GLEVVVVPANT-PYEDIKKeYQPDGVFLSNGPGDPATAD-EMVAVAKAAldDGMPLFGICFGNQILGRALGLNTYKL--- 301
Cdd:PRK06774 23 GTEVMVKRNDElQLTDIEQ-LAPSHLVISPGPCTPNEAGiSLAVIRHFA--DKLPILGVCLGHQALGQAFGARVVRArqv 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788586792 302 --------------VFghRGVNVPVKDHRTGRIFITAQNhgfalegkAGESFD-TPWGEAEVthtclNDDVVEGVALKNG 366
Cdd:PRK06774 100 mhgktsaichsgqgVF--RGLNQPLTVTRYHSLVIAADS--------LPGCFElTAWSERGG-----EMDEIMGIRHRTL 164
|
170 180
....*....|....*....|....*..
gi 2788586792 367 MAFSVQYHPESAAGpHDAHSLFDDFLE 393
Cdd:PRK06774 165 PLEGVQFHPESILS-EQGHQLLDNFLK 190
|
|
| PRK05637 |
PRK05637 |
anthranilate synthase component II; Provisional |
247-381 |
7.36e-05 |
|
anthranilate synthase component II; Provisional
Pssm-ID: 180178 [Multi-domain] Cd Length: 208 Bit Score: 43.68 E-value: 7.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788586792 247 QPDGVFLSNGPGDPATADEMVAVAKAALDDgMPLFGICFGNQIL-------GRALGL---NTYKLVFGHRGVNVPV---- 312
Cdd:PRK05637 44 NPDLICLSPGPGHPRDAGNMMALIDRTLGQ-IPLLGICLGFQALlehhggkVEPCGPvhgTTDNMILTDAGVQSPVfagl 122
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2788586792 313 -----KDHRT--GRIFITAQNHGFAlegkageSFDTPwGEAEVTHTCLND--DVVEGVALKNGMAFSVQYHPESAAGP 381
Cdd:PRK05637 123 atdvePDHPEipGRKVPIARYHSLG-------CVVAP-DGMESLGTCSSEigPVIMAAETTDGKAIGLQFHPESVLSP 192
|
|
| PRK09065 |
PRK09065 |
glutamine amidotransferase; Provisional |
273-295 |
9.36e-05 |
|
glutamine amidotransferase; Provisional
Pssm-ID: 181635 [Multi-domain] Cd Length: 237 Bit Score: 43.41 E-value: 9.36e-05
|
| PRK14607 |
PRK14607 |
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase; |
231-392 |
1.20e-04 |
|
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
Pssm-ID: 237764 [Multi-domain] Cd Length: 534 Bit Score: 44.32 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788586792 231 VVVPANTPYEDIKkEYQPDGVFLSNGPGDPATADEMVAVAKAALDDgMPLFGICFGNQILGRALGLNTYKLVFGHRGVNV 310
Cdd:PRK14607 29 VVRNDEITIEEIE-ALNPSHIVISPGPGRPEEAGISVEVIRHFSGK-VPILGVCLGHQAIGYAFGGKIVHAKRILHGKTS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788586792 311 PVkDHRTGRIFITAQNHGFAL--EGKAGESFDTPwGEAEVTHTClNDDVVEGVALKNGMAFSVQYHPESaAGPHDAHSLF 388
Cdd:PRK14607 107 PI-DHNGKGLFRGIPNPTVATryHSLVVEEASLP-ECLEVTAKS-DDGEIMGIRHKEHPIFGVQFHPES-ILTEEGKRIL 182
|
....
gi 2788586792 389 DDFL 392
Cdd:PRK14607 183 KNFL 186
|
|
| PLN02335 |
PLN02335 |
anthranilate synthase |
240-377 |
1.77e-04 |
|
anthranilate synthase
Pssm-ID: 177969 [Multi-domain] Cd Length: 222 Bit Score: 42.48 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788586792 240 EDIKKEyQPDGVFLSNGPGDPAtaDEMVAVaKAALDDG--MPLFGICFGNQILGRALGLNTYKLVFG--HrGVNVPVKDH 315
Cdd:PLN02335 56 EELKRK-NPRGVLISPGPGTPQ--DSGISL-QTVLELGplVPLFGVCMGLQCIGEAFGGKIVRSPFGvmH-GKSSPVHYD 130
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2788586792 316 RTG---------RIFITAQNHGFALEgkaGESFdtPWGEAEVThTCLNDDVVEGVALKNGMAFS-VQYHPES 377
Cdd:PLN02335 131 EKGeeglfsglpNPFTAGRYHSLVIE---KDTF--PSDELEVT-AWTEDGLIMAARHRKYKHIQgVQFHPES 196
|
|
| GATase1_CobQ |
cd01750 |
Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ); Type ... |
223-294 |
6.01e-04 |
|
Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ); Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ). CobQ plays a role in cobalamin biosythesis. CobQ catalyses amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide in the biosynthesis of cobalamin. CobQ belongs to the triad family of amidotransferases. Two of the three residues of the catalytic triad that are involved in glutamine binding, hydrolysis and transfer of the resulting ammonia to the acceptor substrate in other triad aminodotransferases are conserved in CobQ.
Pssm-ID: 153221 [Multi-domain] Cd Length: 194 Bit Score: 40.69 E-value: 6.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788586792 223 LAKRGLEVVVVPANTPYEDikkeyqPDGVFLsngPGDPATADEMVAVAKAALDD--------GMPLFGICFGNQILGRAL 294
Cdd:cd01750 19 AREPGVDVRYVEVPEGLGD------ADLIIL---PGSKDTIQDLAWLRKRGLAEaiknyaraGGPVLGICGGYQMLGKYI 89
|
|
| PRK07053 |
PRK07053 |
glutamine amidotransferase; Provisional |
260-299 |
2.72e-03 |
|
glutamine amidotransferase; Provisional
Pssm-ID: 235919 [Multi-domain] Cd Length: 234 Bit Score: 39.16 E-value: 2.72e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 2788586792 260 PATADEmVAVAKAALDDGMPLFGICFGNQILGRALGLNTY 299
Cdd:PRK07053 67 PFLAPE-IALLRQRLAAGLPTLGICLGAQLIARALGARVY 105
|
|
| PBP1_ABC_unchar_transporter |
cd06325 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC-type transport systems ... |
221-282 |
6.54e-03 |
|
type 1 periplasmic ligand-binding domain of uncharacterized ABC-type transport systems predicted to be involved in uptake of amino acids, peptides, or inorganic ions; This group includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type transport systems that are predicted to be involved in the uptake of amino acids, peptides, or inorganic ions. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); its ligand specificity has not been determined experimentally.
Pssm-ID: 380548 Cd Length: 282 Bit Score: 38.25 E-value: 6.54e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2788586792 221 RELAKRGLEVVVVPANTPyEDIK------KEYQPDGVFLsngPGDPATADEMVAVAKAALDDGMPLFG 282
Cdd:cd06325 154 AAAKKLGLELVEVPVSSP-ADIEqafaslAGKVADALYV---PTDNTVASARPRIAALALKARIPVIY 217
|
|
| |
