|
Name |
Accession |
Description |
Interval |
E-value |
| PyrG |
COG0504 |
CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase ... |
3-542 |
0e+00 |
|
CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase (UTP-ammonia lyase) is part of the Pathway/BioSystem: Pyrimidine biosynthesis
Pssm-ID: 440270 [Multi-domain] Cd Length: 535 Bit Score: 997.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080560024 3 TKYIIVTGGVASSLGKGLTAASLGRLLTSRGLKVTMQKLDPYLNVDPGTMNPFQHGEVFVTEDGAETDLDLGHYERFLDR 82
Cdd:COG0504 1 TKYIFVTGGVVSSLGKGITAASLGRLLKARGLKVTIQKLDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFLDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080560024 83 NLSAGGNVTTGKVYSSVIAKERRGEFLGQTVQVIPHITDEIKSRIVAMgnadANGEKPDVVITEIGGTVGDIESQPFLEA 162
Cdd:COG0504 81 NLSKANNVTTGQIYSSVIEKERRGDYLGKTVQVIPHITDEIKRRIRRA----AEESGADVVIVEIGGTVGDIESLPFLEA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080560024 163 ARQVRHDVGRENVFYLHVSLVPYLGPSKELKTKPTQHSVAELRSIGLVPDAVVLRCDRDVPDSLKNKIALMCDIDREGVV 242
Cdd:COG0504 157 IRQLRLELGRENVLFIHVTLVPYIAAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEIKRKIALFCNVPEEAVI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080560024 243 SCPDAPSIYDIPKVLYEEHLDTFIIRRLNLPFRDMDWAVWGDLLERVHNPKGEVTVALVGKYIDLPDAYLSVAEAVRAAG 322
Cdd:COG0504 237 SAPDVDSIYEVPLMLHEQGLDEIVLKKLGLEAREPDLSEWEELVERIKNPKKEVTIALVGKYVELPDAYKSVVEALKHAG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080560024 323 FAHRVKANIRWVASDDCETpEGLKKNMAGVDAIVIPggfggrgiegKIATIRYAKQTGTPLLGICLGMQCVVIEAAR-TA 401
Cdd:COG0504 317 IANGVKVNIKWIDSEDLEE-ENAEELLKGVDGILVPggfgergiegKIAAIRYARENKIPFLGICLGMQLAVIEFARnVL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080560024 402 GVEGASSTEFDENAAEPVIATMEEQlqavSGEADLGGSMRLGSYPAKLAEDSVVARLYGTTDVAERHRHRYEVNNAYRNQ 481
Cdd:COG0504 396 GLEDANSTEFDPNTPHPVIDLMPEQ----KDVSDLGGTMRLGAYPCKLKPGTLAAEAYGKEEISERHRHRYEFNNEYREQ 471
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1080560024 482 LSEAGLVISGTSPDGKLVEFVEYPTdvHPYLVATQAHPELKSRPTNAHPLFDGLIAAALKR 542
Cdd:COG0504 472 LEKAGLVFSGTSPDGRLVEIVELPD--HPWFVGVQFHPEFKSRPNRPHPLFRGFVKAALEY 530
|
|
| pyrG |
PRK05380 |
CTP synthetase; Validated |
3-543 |
0e+00 |
|
CTP synthetase; Validated
Pssm-ID: 235437 [Multi-domain] Cd Length: 533 Bit Score: 991.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080560024 3 TKYIIVTGGVASSLGKGLTAASLGRLLTSRGLKVTMQKLDPYLNVDPGTMNPFQHGEVFVTEDGAETDLDLGHYERFLDR 82
Cdd:PRK05380 2 TKYIFVTGGVVSSLGKGITAASLGRLLKARGLKVTIQKLDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFIDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080560024 83 NLSAGGNVTTGKVYSSVIAKERRGEFLGQTVQVIPHITDEIKSRIVAMGnadangEKPDVVITEIGGTVGDIESQPFLEA 162
Cdd:PRK05380 82 NLTKYNNVTTGKIYSSVIEKERRGDYLGKTVQVIPHITDEIKERILAAG------TDADVVIVEIGGTVGDIESLPFLEA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080560024 163 ARQVRHDVGRENVFYLHVSLVPYLGPSKELKTKPTQHSVAELRSIGLVPDAVVLRCDRDVPDSLKNKIALMCDIDREGVV 242
Cdd:PRK05380 156 IRQLRLELGRENVLFIHLTLVPYIAAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEEKRKIALFCNVPEEAVI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080560024 243 SCPDAPSIYDIPKVLYEEHLDTFIIRRLNLPFRDMDWAVWGDLLERVHNPKGEVTVALVGKYIDLPDAYLSVAEAVRAAG 322
Cdd:PRK05380 236 SAPDVDSIYEVPLLLHEQGLDDIVLERLGLEAPEPDLSEWEELVERLKNPKGEVTIALVGKYVELPDAYKSVIEALKHAG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080560024 323 FAHRVKANIRWVASDDCETpEGLKKNMAGVDAIVIPGGFGGRGIEGKIATIRYAKQTGTPLLGICLGMQCVVIEAAR-TA 401
Cdd:PRK05380 316 IANDVKVNIKWIDSEDLEE-ENVAELLKGVDGILVPGGFGERGIEGKILAIRYARENNIPFLGICLGMQLAVIEFARnVL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080560024 402 GVEGASSTEFDENAAEPVIATMEEQLQAVsgeaDLGGSMRLGSYPAKLAEDSVVARLYGTTDVAERHRHRYEVNNAYRNQ 481
Cdd:PRK05380 395 GLEDANSTEFDPDTPHPVIDLMPEQKDVS----DLGGTMRLGAYPCKLKPGTLAAEIYGKEEIYERHRHRYEVNNKYREQ 470
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1080560024 482 LSEAGLVISGTSPDGKLVEFVEYPtdVHPYLVATQAHPELKSRPTNAHPLFDGLIAAALKRN 543
Cdd:PRK05380 471 LEKAGLVFSGTSPDGRLVEIVELP--DHPWFVGVQFHPEFKSRPRRPHPLFAGFVKAALENK 530
|
|
| PyrG |
TIGR00337 |
CTP synthase; CTP synthase is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. ... |
3-538 |
0e+00 |
|
CTP synthase; CTP synthase is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. The enzyme catalyzes the reaction L-glutamine + H2O + UTP + ATP = CTP + phosphate + ADP + L-glutamate. The enzyme exists as a dimer of identical chains that aggregates as a tetramer. This gene has been found circa 500 bp 5' upstream of enolase in both beta (Nitrosomonas europaea) and gamma (E.coli) subdivisions of proteobacterium (FEMS Microbiol Lett 1998 Aug 1;165(1):153-7). [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273021 [Multi-domain] Cd Length: 525 Bit Score: 786.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080560024 3 TKYIIVTGGVASSLGKGLTAASLGRLLTSRGLKVTMQKLDPYLNVDPGTMNPFQHGEVFVTEDGAETDLDLGHYERFLDR 82
Cdd:TIGR00337 1 MKYIFVTGGVVSSLGKGITAASLGRLLKARGLNVTIIKIDPYINIDPGTMSPLQHGEVFVTDDGAETDLDLGHYERFLDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080560024 83 NLSAGGNVTTGKVYSSVIAKERRGEFLGQTVQVIPHITDEIKSRIVAMgnadANGEKPDVVITEIGGTVGDIESQPFLEA 162
Cdd:TIGR00337 81 NLTRDNNITTGKIYSSVIEKERKGDYLGKTVQIIPHITNEIKDRILRV----AKISGPDVVIVEIGGTVGDIESLPFLEA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080560024 163 ARQVRHDVGRENVFYLHVSLVPYLGPSKELKTKPTQHSVAELRSIGLVPDAVVLRCDRDVPDSLKNKIALMCDIDREGVV 242
Cdd:TIGR00337 157 IRQFRVEVGRENVLFIHVTLVPYIAAAGEQKTKPTQHSVKELRSLGIQPDIIICRSSRPLDPNTKDKIALFCDVEEEAVI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080560024 243 SCPDAPSIYDIPKVLYEEHLDTFIIRRLNLPFRDMDWAVWGDLLERVHNPKGEVTVALVGKYIDLPDAYLSVAEAVRAAG 322
Cdd:TIGR00337 237 SAKDVSSIYEVPLLLLKQGLDDYLCRRLNLNCDEADLSEWEQLVEKFANPKHEVTIGIVGKYVELKDAYLSVIEALKHAG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080560024 323 FAHRVKANIRWVASDDCETPEglKKNMAGVDAIVIPGGFGGRGIEGKIATIRYAKQTGTPLLGICLGMQCVVIEAART-A 401
Cdd:TIGR00337 317 AKLDTKVNIKWIDSEDLEEEG--VEFLKGLDGILVPGGFGERGVEGKILAIKYARENNIPFLGICLGMQLAVIEFARNvA 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080560024 402 GVEGASSTEFDENAAEPVIATMEEQlqavSGEADLGGSMRLGSYPAKLAEDSVVARLYGTTDVAERHRHRYEVNNAYRNQ 481
Cdd:TIGR00337 395 GLEGANSTEFDPDTKYPVVDLLPEQ----KDISDLGGTMRLGLYPCILKPGTLAFKLYGKEEVYERHRHRYEVNNEYREQ 470
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1080560024 482 LSEAGLVISGTSPDGKLVEFVEYPTdvHPYLVATQAHPELKSRPTNAHPLFDGLIAA 538
Cdd:TIGR00337 471 IENKGLIVSGTSPDGRLVEIIELPD--HPFFVACQFHPEFTSRPNDPHPLFLGFVKA 525
|
|
| CTP_synth_N |
pfam06418 |
CTP synthase N-terminus; This family consists of the N-terminal region of the CTP synthase ... |
4-272 |
0e+00 |
|
CTP synthase N-terminus; This family consists of the N-terminal region of the CTP synthase protein (EC:6.3.4.2). This family is found in conjunction with pfam00117 located in the C-terminal region of the protein. CTP synthase catalyzes the synthesis of CTP from UTP by amination of the pyrimidine ring at the 4-position.
Pssm-ID: 461903 Cd Length: 265 Bit Score: 549.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080560024 4 KYIIVTGGVASSLGKGLTAASLGRLLTSRGLKVTMQKLDPYLNVDPGTMNPFQHGEVFVTEDGAETDLDLGHYERFLDRN 83
Cdd:pfam06418 1 KYIFVTGGVVSGLGKGITAASLGRLLKSRGLKVTIIKIDPYLNVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFLDIN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080560024 84 LSAGGNVTTGKVYSSVIAKERRGEFLGQTVQVIPHITDEIKSRIVAMgnadANGEKPDVVITEIGGTVGDIESQPFLEAA 163
Cdd:pfam06418 81 LTKDNNITTGKIYQSVIEKERRGDYLGKTVQVIPHITDEIKERIRRV----AKEVGPDVVIVEIGGTVGDIESLPFLEAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080560024 164 RQVRHDVGRENVFYLHVSLVPYLGPSKELKTKPTQHSVAELRSIGLVPDAVVLRCDRDVPDSLKNKIALMCDIDREGVVS 243
Cdd:pfam06418 157 RQLRLEVGRENVLFIHVTLVPYLKAAGELKTKPTQHSVKELRSIGIQPDIIVCRSERPLDEEVKEKIALFCNVPKEAVIS 236
|
250 260
....*....|....*....|....*....
gi 1080560024 244 CPDAPSIYDIPKVLYEEHLDTFIIRRLNL 272
Cdd:pfam06418 237 APDVSSIYEVPLLLEEQGLDDIILKRLNL 265
|
|
| CTPS_N |
cd03113 |
N-terminal domain of cytidine 5'-triphosphate synthase; Cytidine 5'-triphosphate synthase ... |
4-268 |
6.62e-174 |
|
N-terminal domain of cytidine 5'-triphosphate synthase; Cytidine 5'-triphosphate synthase (CTPS) is a two-domain protein, which consists of an N-terminal synthetase domain and C-terminal glutaminase domain. The enzymes hydrolyze the amide bond of glutamine to ammonia and glutamate at the glutaminase domains and transfer nascent ammonia to the acceptor substrate at the synthetase domain to form an aminated product.
Pssm-ID: 349767 Cd Length: 261 Bit Score: 491.23 E-value: 6.62e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080560024 4 KYIIVTGGVASSLGKGLTAASLGRLLTSRGLKVTMQKLDPYLNVDPGTMNPFQHGEVFVTEDGAETDLDLGHYERFLDRN 83
Cdd:cd03113 1 KYIFVTGGVVSGLGKGITASSIGRLLKSRGLRVTAIKIDPYLNVDAGTMSPYEHGEVFVLDDGGETDLDLGNYERFLDVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080560024 84 LSAGGNVTTGKVYSSVIAKERRGEFLGQTVQVIPHITDEIKSRIVAMgnadANGEKPDVVITEIGGTVGDIESQPFLEAA 163
Cdd:cd03113 81 LTRDNNITTGKIYSEVIEKERRGDYLGKTVQVIPHITDEIKERIRRV----AKIPEPDVCIVEIGGTVGDIESLPFLEAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080560024 164 RQVRHDVGRENVFYLHVSLVPYLGPSKELKTKPTQHSVAELRSIGLVPDAVVLRCDRDVPDSLKNKIALMCDIDREGVVS 243
Cdd:cd03113 157 RQFQFEVGRENFLFIHVTLVPYLEATGEQKTKPTQHSVKELRSLGIQPDIIVCRSEKPLDEETKEKIALFCNVPPEAVIS 236
|
250 260
....*....|....*....|....*
gi 1080560024 244 CPDAPSIYDIPKVLYEEHLDTFIIR 268
Cdd:cd03113 237 VHDVSSIYEVPLLLEKQGLDDYILR 261
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PyrG |
COG0504 |
CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase ... |
3-542 |
0e+00 |
|
CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase (UTP-ammonia lyase) is part of the Pathway/BioSystem: Pyrimidine biosynthesis
Pssm-ID: 440270 [Multi-domain] Cd Length: 535 Bit Score: 997.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080560024 3 TKYIIVTGGVASSLGKGLTAASLGRLLTSRGLKVTMQKLDPYLNVDPGTMNPFQHGEVFVTEDGAETDLDLGHYERFLDR 82
Cdd:COG0504 1 TKYIFVTGGVVSSLGKGITAASLGRLLKARGLKVTIQKLDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFLDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080560024 83 NLSAGGNVTTGKVYSSVIAKERRGEFLGQTVQVIPHITDEIKSRIVAMgnadANGEKPDVVITEIGGTVGDIESQPFLEA 162
Cdd:COG0504 81 NLSKANNVTTGQIYSSVIEKERRGDYLGKTVQVIPHITDEIKRRIRRA----AEESGADVVIVEIGGTVGDIESLPFLEA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080560024 163 ARQVRHDVGRENVFYLHVSLVPYLGPSKELKTKPTQHSVAELRSIGLVPDAVVLRCDRDVPDSLKNKIALMCDIDREGVV 242
Cdd:COG0504 157 IRQLRLELGRENVLFIHVTLVPYIAAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEIKRKIALFCNVPEEAVI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080560024 243 SCPDAPSIYDIPKVLYEEHLDTFIIRRLNLPFRDMDWAVWGDLLERVHNPKGEVTVALVGKYIDLPDAYLSVAEAVRAAG 322
Cdd:COG0504 237 SAPDVDSIYEVPLMLHEQGLDEIVLKKLGLEAREPDLSEWEELVERIKNPKKEVTIALVGKYVELPDAYKSVVEALKHAG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080560024 323 FAHRVKANIRWVASDDCETpEGLKKNMAGVDAIVIPggfggrgiegKIATIRYAKQTGTPLLGICLGMQCVVIEAAR-TA 401
Cdd:COG0504 317 IANGVKVNIKWIDSEDLEE-ENAEELLKGVDGILVPggfgergiegKIAAIRYARENKIPFLGICLGMQLAVIEFARnVL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080560024 402 GVEGASSTEFDENAAEPVIATMEEQlqavSGEADLGGSMRLGSYPAKLAEDSVVARLYGTTDVAERHRHRYEVNNAYRNQ 481
Cdd:COG0504 396 GLEDANSTEFDPNTPHPVIDLMPEQ----KDVSDLGGTMRLGAYPCKLKPGTLAAEAYGKEEISERHRHRYEFNNEYREQ 471
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1080560024 482 LSEAGLVISGTSPDGKLVEFVEYPTdvHPYLVATQAHPELKSRPTNAHPLFDGLIAAALKR 542
Cdd:COG0504 472 LEKAGLVFSGTSPDGRLVEIVELPD--HPWFVGVQFHPEFKSRPNRPHPLFRGFVKAALEY 530
|
|
| pyrG |
PRK05380 |
CTP synthetase; Validated |
3-543 |
0e+00 |
|
CTP synthetase; Validated
Pssm-ID: 235437 [Multi-domain] Cd Length: 533 Bit Score: 991.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080560024 3 TKYIIVTGGVASSLGKGLTAASLGRLLTSRGLKVTMQKLDPYLNVDPGTMNPFQHGEVFVTEDGAETDLDLGHYERFLDR 82
Cdd:PRK05380 2 TKYIFVTGGVVSSLGKGITAASLGRLLKARGLKVTIQKLDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFIDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080560024 83 NLSAGGNVTTGKVYSSVIAKERRGEFLGQTVQVIPHITDEIKSRIVAMGnadangEKPDVVITEIGGTVGDIESQPFLEA 162
Cdd:PRK05380 82 NLTKYNNVTTGKIYSSVIEKERRGDYLGKTVQVIPHITDEIKERILAAG------TDADVVIVEIGGTVGDIESLPFLEA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080560024 163 ARQVRHDVGRENVFYLHVSLVPYLGPSKELKTKPTQHSVAELRSIGLVPDAVVLRCDRDVPDSLKNKIALMCDIDREGVV 242
Cdd:PRK05380 156 IRQLRLELGRENVLFIHLTLVPYIAAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEEKRKIALFCNVPEEAVI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080560024 243 SCPDAPSIYDIPKVLYEEHLDTFIIRRLNLPFRDMDWAVWGDLLERVHNPKGEVTVALVGKYIDLPDAYLSVAEAVRAAG 322
Cdd:PRK05380 236 SAPDVDSIYEVPLLLHEQGLDDIVLERLGLEAPEPDLSEWEELVERLKNPKGEVTIALVGKYVELPDAYKSVIEALKHAG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080560024 323 FAHRVKANIRWVASDDCETpEGLKKNMAGVDAIVIPGGFGGRGIEGKIATIRYAKQTGTPLLGICLGMQCVVIEAAR-TA 401
Cdd:PRK05380 316 IANDVKVNIKWIDSEDLEE-ENVAELLKGVDGILVPGGFGERGIEGKILAIRYARENNIPFLGICLGMQLAVIEFARnVL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080560024 402 GVEGASSTEFDENAAEPVIATMEEQLQAVsgeaDLGGSMRLGSYPAKLAEDSVVARLYGTTDVAERHRHRYEVNNAYRNQ 481
Cdd:PRK05380 395 GLEDANSTEFDPDTPHPVIDLMPEQKDVS----DLGGTMRLGAYPCKLKPGTLAAEIYGKEEIYERHRHRYEVNNKYREQ 470
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1080560024 482 LSEAGLVISGTSPDGKLVEFVEYPtdVHPYLVATQAHPELKSRPTNAHPLFDGLIAAALKRN 543
Cdd:PRK05380 471 LEKAGLVFSGTSPDGRLVEIVELP--DHPWFVGVQFHPEFKSRPRRPHPLFAGFVKAALENK 530
|
|
| PyrG |
TIGR00337 |
CTP synthase; CTP synthase is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. ... |
3-538 |
0e+00 |
|
CTP synthase; CTP synthase is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. The enzyme catalyzes the reaction L-glutamine + H2O + UTP + ATP = CTP + phosphate + ADP + L-glutamate. The enzyme exists as a dimer of identical chains that aggregates as a tetramer. This gene has been found circa 500 bp 5' upstream of enolase in both beta (Nitrosomonas europaea) and gamma (E.coli) subdivisions of proteobacterium (FEMS Microbiol Lett 1998 Aug 1;165(1):153-7). [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273021 [Multi-domain] Cd Length: 525 Bit Score: 786.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080560024 3 TKYIIVTGGVASSLGKGLTAASLGRLLTSRGLKVTMQKLDPYLNVDPGTMNPFQHGEVFVTEDGAETDLDLGHYERFLDR 82
Cdd:TIGR00337 1 MKYIFVTGGVVSSLGKGITAASLGRLLKARGLNVTIIKIDPYINIDPGTMSPLQHGEVFVTDDGAETDLDLGHYERFLDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080560024 83 NLSAGGNVTTGKVYSSVIAKERRGEFLGQTVQVIPHITDEIKSRIVAMgnadANGEKPDVVITEIGGTVGDIESQPFLEA 162
Cdd:TIGR00337 81 NLTRDNNITTGKIYSSVIEKERKGDYLGKTVQIIPHITNEIKDRILRV----AKISGPDVVIVEIGGTVGDIESLPFLEA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080560024 163 ARQVRHDVGRENVFYLHVSLVPYLGPSKELKTKPTQHSVAELRSIGLVPDAVVLRCDRDVPDSLKNKIALMCDIDREGVV 242
Cdd:TIGR00337 157 IRQFRVEVGRENVLFIHVTLVPYIAAAGEQKTKPTQHSVKELRSLGIQPDIIICRSSRPLDPNTKDKIALFCDVEEEAVI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080560024 243 SCPDAPSIYDIPKVLYEEHLDTFIIRRLNLPFRDMDWAVWGDLLERVHNPKGEVTVALVGKYIDLPDAYLSVAEAVRAAG 322
Cdd:TIGR00337 237 SAKDVSSIYEVPLLLLKQGLDDYLCRRLNLNCDEADLSEWEQLVEKFANPKHEVTIGIVGKYVELKDAYLSVIEALKHAG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080560024 323 FAHRVKANIRWVASDDCETPEglKKNMAGVDAIVIPGGFGGRGIEGKIATIRYAKQTGTPLLGICLGMQCVVIEAART-A 401
Cdd:TIGR00337 317 AKLDTKVNIKWIDSEDLEEEG--VEFLKGLDGILVPGGFGERGVEGKILAIKYARENNIPFLGICLGMQLAVIEFARNvA 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080560024 402 GVEGASSTEFDENAAEPVIATMEEQlqavSGEADLGGSMRLGSYPAKLAEDSVVARLYGTTDVAERHRHRYEVNNAYRNQ 481
Cdd:TIGR00337 395 GLEGANSTEFDPDTKYPVVDLLPEQ----KDISDLGGTMRLGLYPCILKPGTLAFKLYGKEEVYERHRHRYEVNNEYREQ 470
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1080560024 482 LSEAGLVISGTSPDGKLVEFVEYPTdvHPYLVATQAHPELKSRPTNAHPLFDGLIAA 538
Cdd:TIGR00337 471 IENKGLIVSGTSPDGRLVEIIELPD--HPFFVACQFHPEFTSRPNDPHPLFLGFVKA 525
|
|
| PLN02327 |
PLN02327 |
CTP synthase |
3-539 |
0e+00 |
|
CTP synthase
Pssm-ID: 215186 [Multi-domain] Cd Length: 557 Bit Score: 585.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080560024 3 TKYIIVTGGVASSLGKGLTAASLGRLLTSRGLKVTMQKLDPYLNVDPGTMNPFQHGEVFVTEDGAETDLDLGHYERFLDR 82
Cdd:PLN02327 1 MKYVLVTGGVVSGLGKGVTASSIGVLLKACGLRVTSIKIDPYLNTDAGTMSPFEHGEVFVLDDGGEVDLDLGNYERFLDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080560024 83 NLSAGGNVTTGKVYSSVIAKERRGEFLGQTVQVIPHITDEIKSRI--VAMGNADANGEKPDVVITEIGGTVGDIESQPFL 160
Cdd:PLN02327 81 TLTRDNNITTGKIYQSVIEKERRGDYLGKTVQVVPHITDAIQEWIerVAKIPVDGKEGPADVCVIELGGTVGDIESMPFI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080560024 161 EAARQVRHDVGRENVFYLHVSLVPYLGPSKELKTKPTQHSVAELRSIGLVPDAVVLRCDRDVPDSLKNKIALMCDIDREG 240
Cdd:PLN02327 161 EALRQFSFRVGPGNFCLIHVSLVPVLGVVGEQKTKPTQHSVRGLRALGLTPHILACRSTKPLEENVKEKLSQFCHVPAEN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080560024 241 VVSCPDAPSIYDIPKVLYEEHLDTFIIRRLNLP--FRDMDWAVWGDLLERVHNPKGEVTVALVGKYIDLPDAYLSVAEAV 318
Cdd:PLN02327 241 ILNLHDVSNIWHVPLLLRDQKAHEAILKVLNLLsvAREPDLEEWTARAESCDNLTEPVRIAMVGKYTGLSDSYLSVLKAL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080560024 319 RAAGFAHRVKANIRWVASDDCE------TPEGLK---KNMAGVDAIVIPGGFGGRGIEGKIATIRYAKQTGTPLLGICLG 389
Cdd:PLN02327 321 LHASVACSRKLVIDWVAASDLEdetakeTPDAYAaawKLLKGADGILVPGGFGDRGVEGKILAAKYARENKVPYLGICLG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080560024 390 MQCVVIEAARTA-GVEGASSTEFDENAAEPVIATMEEqlqaVSGEaDLGGSMRLGSYPAKL-AEDSVVARLYGTTD-VAE 466
Cdd:PLN02327 401 MQIAVIEFARSVlGLKDANSTEFDPETPNPCVIFMPE----GSKT-HMGGTMRLGSRRTYFqTPDCKSAKLYGNVSfVDE 475
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1080560024 467 RHRHRYEVNNAYRNQLSEAGLVISGTSPDGKLVEFVEYPTdvHPYLVATQAHPELKSRPTNAHPLFDGLIAAA 539
Cdd:PLN02327 476 RHRHRYEVNPEMVPRLEKAGLSFVGKDETGRRMEIVELPS--HPFFVGVQFHPEFKSRPGKPSPLFLGLIAAA 546
|
|
| CTP_synth_N |
pfam06418 |
CTP synthase N-terminus; This family consists of the N-terminal region of the CTP synthase ... |
4-272 |
0e+00 |
|
CTP synthase N-terminus; This family consists of the N-terminal region of the CTP synthase protein (EC:6.3.4.2). This family is found in conjunction with pfam00117 located in the C-terminal region of the protein. CTP synthase catalyzes the synthesis of CTP from UTP by amination of the pyrimidine ring at the 4-position.
Pssm-ID: 461903 Cd Length: 265 Bit Score: 549.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080560024 4 KYIIVTGGVASSLGKGLTAASLGRLLTSRGLKVTMQKLDPYLNVDPGTMNPFQHGEVFVTEDGAETDLDLGHYERFLDRN 83
Cdd:pfam06418 1 KYIFVTGGVVSGLGKGITAASLGRLLKSRGLKVTIIKIDPYLNVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFLDIN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080560024 84 LSAGGNVTTGKVYSSVIAKERRGEFLGQTVQVIPHITDEIKSRIVAMgnadANGEKPDVVITEIGGTVGDIESQPFLEAA 163
Cdd:pfam06418 81 LTKDNNITTGKIYQSVIEKERRGDYLGKTVQVIPHITDEIKERIRRV----AKEVGPDVVIVEIGGTVGDIESLPFLEAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080560024 164 RQVRHDVGRENVFYLHVSLVPYLGPSKELKTKPTQHSVAELRSIGLVPDAVVLRCDRDVPDSLKNKIALMCDIDREGVVS 243
Cdd:pfam06418 157 RQLRLEVGRENVLFIHVTLVPYLKAAGELKTKPTQHSVKELRSIGIQPDIIVCRSERPLDEEVKEKIALFCNVPKEAVIS 236
|
250 260
....*....|....*....|....*....
gi 1080560024 244 CPDAPSIYDIPKVLYEEHLDTFIIRRLNL 272
Cdd:pfam06418 237 APDVSSIYEVPLLLEEQGLDDIILKRLNL 265
|
|
| CTPS_N |
cd03113 |
N-terminal domain of cytidine 5'-triphosphate synthase; Cytidine 5'-triphosphate synthase ... |
4-268 |
6.62e-174 |
|
N-terminal domain of cytidine 5'-triphosphate synthase; Cytidine 5'-triphosphate synthase (CTPS) is a two-domain protein, which consists of an N-terminal synthetase domain and C-terminal glutaminase domain. The enzymes hydrolyze the amide bond of glutamine to ammonia and glutamate at the glutaminase domains and transfer nascent ammonia to the acceptor substrate at the synthetase domain to form an aminated product.
Pssm-ID: 349767 Cd Length: 261 Bit Score: 491.23 E-value: 6.62e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080560024 4 KYIIVTGGVASSLGKGLTAASLGRLLTSRGLKVTMQKLDPYLNVDPGTMNPFQHGEVFVTEDGAETDLDLGHYERFLDRN 83
Cdd:cd03113 1 KYIFVTGGVVSGLGKGITASSIGRLLKSRGLRVTAIKIDPYLNVDAGTMSPYEHGEVFVLDDGGETDLDLGNYERFLDVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080560024 84 LSAGGNVTTGKVYSSVIAKERRGEFLGQTVQVIPHITDEIKSRIVAMgnadANGEKPDVVITEIGGTVGDIESQPFLEAA 163
Cdd:cd03113 81 LTRDNNITTGKIYSEVIEKERRGDYLGKTVQVIPHITDEIKERIRRV----AKIPEPDVCIVEIGGTVGDIESLPFLEAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080560024 164 RQVRHDVGRENVFYLHVSLVPYLGPSKELKTKPTQHSVAELRSIGLVPDAVVLRCDRDVPDSLKNKIALMCDIDREGVVS 243
Cdd:cd03113 157 RQFQFEVGRENFLFIHVTLVPYLEATGEQKTKPTQHSVKELRSLGIQPDIIVCRSEKPLDEETKEKIALFCNVPPEAVIS 236
|
250 260
....*....|....*....|....*
gi 1080560024 244 CPDAPSIYDIPKVLYEEHLDTFIIR 268
Cdd:cd03113 237 VHDVSSIYEVPLLLEKQGLDDYILR 261
|
|
| GATase1_CTP_Synthase |
cd01746 |
Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase; ... |
296-536 |
8.76e-104 |
|
Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase; Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase (CTP). CTP is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. CTPs produce CTP from UTP and glutamine and regulate intracellular CTP levels through interactions with four ribonucleotide triphosphates. The enzyme exists as a dimer of identical chains that aggregates as a tetramer. CTP is derived form UTP in three separate steps involving two active sites. In one active site, the UTP O4 oxygen is activated by Mg-ATP-dependent phosphorylation, followed by displacement of the resulting 4-phosphate moiety by ammonia. At a separate site, ammonia is generated via rate limiting glutamine hydrolysis (glutaminase) activity. A gated channel that spans between the glutamine hydrolysis and amidoligase active sites provides a path for ammonia diffusion. CTPs belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.
Pssm-ID: 153217 [Multi-domain] Cd Length: 235 Bit Score: 311.41 E-value: 8.76e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080560024 296 VTVALVGKYIDLPDAYLSVAEAVRAAGFAHRVKANIRWVASDDCEtPEGLKKNMAGVDAIVIPGGFGGRGIEGKIATIRY 375
Cdd:cd01746 1 VRIALVGKYVELPDAYLSVLEALKHAGIALGVKLEIKWIDSEDLE-EENAEEALKGADGILVPGGFGIRGVEGKILAIKY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080560024 376 AKQTGTPLLGICLGMQCVVIEAARTA-GVEGASSTEFDENAAEPVIATMEEQlqavSGEADLGGSMRLGSYPAKLAEDSV 454
Cdd:cd01746 80 ARENNIPFLGICLGMQLAVIEFARNVlGLPDANSTEFDPDTPHPVVDLMPEQ----KGVKDLGGTMRLGAYPVILKPGTL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080560024 455 VARLYGTTDVAERHRHRYEVNNAYRNQLSEAGLVISGTSPDGKLVEFVEYPTdvHPYLVATQAHPELKSRPTNAHPLFDG 534
Cdd:cd01746 156 AHKYYGKDEVEERHRHRYEVNPEYVDELEEAGLRFSGTDPDGGLVEIVELPD--HPFFVGTQFHPEFKSRPLKPHPLFVG 233
|
..
gi 1080560024 535 LI 536
Cdd:cd01746 234 FV 235
|
|
| PRK06186 |
PRK06186 |
hypothetical protein; Validated |
298-542 |
6.59e-29 |
|
hypothetical protein; Validated
Pssm-ID: 180452 [Multi-domain] Cd Length: 229 Bit Score: 114.29 E-value: 6.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080560024 298 VALVGKYIDLPDAYLSVAEAVRAAGFAHRVKANIRWVASDDCETPEGLkknmAGVDAI-VIPGGFGGRGIEGKIAtIRYA 376
Cdd:PRK06186 4 IALVGDYNPDVTAHQAIPLALDLAAAVLGLPVDYEWLPTPEITDPEDL----AGFDGIwCVPGSPYRNDDGALTA-IRFA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080560024 377 KQTGTPLLGICLGMQCVVIEAARTA-GVEGASSTEFDENAAEPVIA----TMEEQLQAVsgeadlggsmrlgsypaKLAE 451
Cdd:PRK06186 79 RENGIPFLGTCGGFQHALLEYARNVlGWADAAHAETDPEGDRPVIAplscSLVEKTGDI-----------------RLRP 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080560024 452 DSVVARLYGTTDVAERHRHRYEVNNAYRNQLSEAGLVISGTSPDGKlVEFVEYPTdvHPYLVATQAHPELKSRPTNAHPL 531
Cdd:PRK06186 142 GSLIARAYGTLEIEEGYHCRYGVNPEFVAALESGDLRVTGWDEDGD-VRAVELPG--HPFFVATLFQPERAALAGRPPPL 218
|
250
....*....|.
gi 1080560024 532 FDGLIAAALKR 542
Cdd:PRK06186 219 VRAFLRAARAA 229
|
|
| GATase |
pfam00117 |
Glutamine amidotransferase class-I; |
307-538 |
1.89e-24 |
|
Glutamine amidotransferase class-I;
Pssm-ID: 395067 [Multi-domain] Cd Length: 188 Bit Score: 100.39 E-value: 1.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080560024 307 LPDAYLSVAEAVRAAGFAHRVKANIRWVASDDCETPEglkknmAGVDAIVI-PGGFGGRGIEGKIATIRYAKQTGTPLLG 385
Cdd:pfam00117 2 LIDNGDSFTYNLARALRELGVEVTVVPNDTPAEEILE------ENPDGIILsGGPGSPGAAGGAIEAIREARELKIPILG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080560024 386 ICLGMQCVVIEAARtagvegasstefdenaaePVIATmeeqlqavSGEADLGGSMRLGSYPAKLaedsvvarLYGTTD-V 464
Cdd:pfam00117 76 ICLGHQLLALAFGG------------------KVVKA--------KKFGHHGKNSPVGDDGCGL--------FYGLPNvF 121
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1080560024 465 AERHRHRYEVNNAyrnqLSEAGLVISGTSPDGKLVEFVEYPTDvhPYlVATQAHPELKSRPTNAHPLFDGLIAA 538
Cdd:pfam00117 122 IVRRYHSYAVDPD----TLPDGLEVTATSENDGTIMGIRHKKL--PI-FGVQFHPESILTPHGPEILFNFFIKA 188
|
|
| PuuD |
COG2071 |
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ... |
370-542 |
1.12e-10 |
|
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: 61.72 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080560024 370 IATIRYAKQTGTPLLGICLGMQcvVIeaartagvegasstefdeNAAepviatmeeqlqavsgeadLGGSM--------- 440
Cdd:COG2071 86 LALIRAALERGKPVLGICRGMQ--LL------------------NVA-------------------LGGTLyqdlpdqvp 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080560024 441 --------RLGSYPAK---LAEDSVVARLYGTTdvaerhrhRYEVnNAYRNQ----LSEaGLVISGTSPDGkLVEFVEYP 505
Cdd:COG2071 127 galdhrqpAPRYAPRHtveIEPGSRLARILGEE--------EIRV-NSLHHQavkrLGP-GLRVSARAPDG-VIEAIESP 195
|
170 180 190
....*....|....*....|....*....|....*...
gi 1080560024 506 TdvHPYLVATQAHPELKSRPTNAH-PLFDGLIAAALKR 542
Cdd:COG2071 196 G--APFVLGVQWHPEWLAASDPLSrRLFEAFVEAARAR 231
|
|
| Peptidase_C26 |
pfam07722 |
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ... |
370-520 |
4.36e-09 |
|
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: 56.88 E-value: 4.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080560024 370 IATIRYAKQTGTPLLGICLGMQCVvieaartagvegasstefdeNAAepVIATMEEQLQAVSGEAD-LGGSMRLGSYPA- 447
Cdd:pfam07722 95 LALIRAALARGKPILGICRGFQLL--------------------NVA--LGGTLYQDIQEQPGFTDhREHCQVAPYAPSh 152
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1080560024 448 --KLAEDSVVARLYGTTDVAERHRHRYEVnnayrNQLSEaGLVISGTSPDGkLVEFVEYPtDVHPYLVATQAHPE 520
Cdd:pfam07722 153 avNVEPGSLLASLLGSEEFRVNSLHHQAI-----DRLAP-GLRVEAVAPDG-TIEAIESP-NAKGFALGVQWHPE 219
|
|
| GATase1 |
cd01653 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
298-395 |
3.15e-08 |
|
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group includes proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA. and, the A4 beta-galactosidase middle domain. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.
Pssm-ID: 153210 [Multi-domain] Cd Length: 115 Bit Score: 51.83 E-value: 3.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080560024 298 VALVGKYIDLPDAYLSVAEAVRAAGFahrvkaNIRWVASDDceTPEGLKKNMAGVDAIVIP----GGFGGRGIEGKIATI 373
Cdd:cd01653 1 VAVLLFPGFEELELASPLDALREAGA------EVDVVSPDG--GPVESDVDLDDYDGLILPggpgTPDDLARDEALLALL 72
|
90 100
....*....|....*....|..
gi 1080560024 374 RYAKQTGTPLLGICLGMQCVVI 395
Cdd:cd01653 73 REAAAAGKPILGICLGAQLLVL 94
|
|
| GAT_1 |
cd03128 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
298-392 |
2.72e-07 |
|
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: 48.74 E-value: 2.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080560024 298 VALVGKYIDLPDAYLSVAEAVRAAGFahrvkaNIRWVASDDceTPEGLKKNMAGVDAIVIP----GGFGGRGIEGKIATI 373
Cdd:cd03128 1 VAVLLFGGSEELELASPLDALREAGA------EVDVVSPDG--GPVESDVDLDDYDGLILPggpgTPDDLAWDEALLALL 72
|
90
....*....|....*....
gi 1080560024 374 RYAKQTGTPLLGICLGMQC 392
Cdd:cd03128 73 REAAAAGKPVLGICLGAQL 91
|
|
| GATase1_2 |
cd01745 |
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ... |
370-536 |
6.15e-04 |
|
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: 41.02 E-value: 6.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080560024 370 IATIRYAKQTGTPLLGICLGMQcvvieaartagvegasstefdenaaepVIATMeeqlqavsgeadLGGSMRLgsypakl 449
Cdd:cd01745 90 LALLRAALERGKPILGICRGMQ---------------------------LLNVA------------LGGTLYQ------- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080560024 450 aedsvvarlygttDVAERHRHRYEVnnayrNQLSEaGLVISGTSPDGkLVEFVEYPTdvHPYLVATQAHPELKsRPTNAH 529
Cdd:cd01745 124 -------------DIRVNSLHHQAI-----KRLAD-GLRVEARAPDG-VIEAIESPD--RPFVLGVQWHPEWL-ADTDPD 180
|
....*....
gi 1080560024 530 --PLFDGLI 536
Cdd:cd01745 181 slKLFEAFV 189
|
|
| hisH |
PRK13141 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
370-391 |
1.26e-03 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 237288 [Multi-domain] Cd Length: 205 Bit Score: 40.11 E-value: 1.26e-03
|
| GATase1_IGP_Synthase |
cd01748 |
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ... |
313-391 |
2.54e-03 |
|
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate synthase (IGPS); Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate synthase (IGPS). IGPS incorporates ammonia derived from glutamine into N1-[(5'-phosphoribulosyl)-formimino]-5-aminoimidazole-4-carboxamide ribonucleotide (PRFAR) to form 5'-(5-aminoimidazole-4-carboxamide) ribonucleotide (AICAR) and imidazole glycerol phosphate (IGP). The glutamine amidotransferase domain generates the ammonia nucleophile which is channeled from the glutaminase active site to the PRFAR active site. IGPS belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.
Pssm-ID: 153219 [Multi-domain] Cd Length: 198 Bit Score: 39.40 E-value: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080560024 313 SVAEAVRAAGFahrvkaNIRWVASddcetPEGLKKnmagVDAIVIP------GGFGGRGIEGKIATIRYAKQTGTPLLGI 386
Cdd:cd01748 13 SVANALERLGA------EVIITSD-----PEEILS----ADKLILPgvgafgDAMANLRERGLIEALKEAIASGKPFLGI 77
|
....*
gi 1080560024 387 CLGMQ 391
Cdd:cd01748 78 CLGMQ 82
|
|
| HisH |
COG0118 |
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ... |
370-391 |
4.16e-03 |
|
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid transport and metabolism]; Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH is part of the Pathway/BioSystem: Histidine biosynthesis
Pssm-ID: 439888 [Multi-domain] Cd Length: 196 Bit Score: 38.48 E-value: 4.16e-03
|
| GuaA1 |
COG0518 |
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ... |
373-411 |
6.25e-03 |
|
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: 38.39 E-value: 6.25e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1080560024 373 IRYAKQTGTPLLGICLGMQcvVIeaARTAG--VEGASSTEF 411
Cdd:COG0518 75 IREAFELGKPVLGICYGAQ--LL--AHALGgkVEPGPGREI 111
|
|
| |
