|
Name |
Accession |
Description |
Interval |
E-value |
| PyrG |
COG0504 |
CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase ... |
9-551 |
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: 1046.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386803 9 TKHLFVSGGVASSLGKGLTASSLGQLLTARGLHVTMQKLDPYLNVDPGTMNPFQHGEVFVTEDGAETDLDVGHYERFLDR 88
Cdd:COG0504 1 TKYIFVTGGVVSSLGKGITAASLGRLLKARGLKVTIQKLDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFLDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386803 89 NLPGSANVTTGQVYSTVIAKERRGEYLGDTVQVIPHITDEIKRRILAMAQPdadgNRPDVVITEIGGTVGDIESQPFLEA 168
Cdd:COG0504 81 NLSKANNVTTGQIYSSVIEKERRGDYLGKTVQVIPHITDEIKRRIRRAAEE----SGADVVIVEIGGTVGDIESLPFLEA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386803 169 ARQVRHYLGREDVFFLHVSLVPYLAPSGELKTKPTQHSVAALRSIGITPDALILRCDRDVPEALKNKIALMCDVDIDGVI 248
Cdd:COG0504 157 IRQLRLELGRENVLFIHVTLVPYIAAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEIKRKIALFCNVPEEAVI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386803 249 STPDAPSIYDIPKVLHREELDAFVVRRLNLPFRDVDWTEWDDLLRRVHEPHETVRIALVGKYVELSDAYLSVAEALRAGG 328
Cdd:COG0504 237 SAPDVDSIYEVPLMLHEQGLDEIVLKKLGLEAREPDLSEWEELVERIKNPKKEVTIALVGKYVELPDAYKSVVEALKHAG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386803 329 FKHRAKVEICWVASDGCEtTSGAAAALGDVHGVLIPGGFGIRGIEGKIGAIAYARARGLPVLGLCLGLQCIVIEAARSV- 407
Cdd:COG0504 317 IANGVKVNIKWIDSEDLE-EENAEELLKGVDGILVPGGFGERGIEGKIAAIRYARENKIPFLGICLGMQLAVIEFARNVl 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386803 408 GLTNANSAEFDPDTPDPVIATMPDQEEIVageaDLGGTMRLGSYPAVLEPDSVVAQAYQTTQVSERHRHRYEVNNAYRDK 487
Cdd:COG0504 396 GLEDANSTEFDPNTPHPVIDLMPEQKDVS----DLGGTMRLGAYPCKLKPGTLAAEAYGKEEISERHRHRYEFNNEYREQ 471
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 887386803 488 IAESGLRFSGTSPDGHLVEFVEYPpdRHPFVVGTQAHPELKSRPTRPHPLFVAFVGAAIDYKAG 551
Cdd:COG0504 472 LEKAGLVFSGTSPDGRLVEIVELP--DHPWFVGVQFHPEFKSRPNRPHPLFRGFVKAALEYKKK 533
|
|
| pyrG |
PRK05380 |
CTP synthetase; Validated |
9-552 |
0e+00 |
|
CTP synthetase; Validated
Pssm-ID: 235437 [Multi-domain] Cd Length: 533 Bit Score: 1044.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386803 9 TKHLFVSGGVASSLGKGLTASSLGQLLTARGLHVTMQKLDPYLNVDPGTMNPFQHGEVFVTEDGAETDLDVGHYERFLDR 88
Cdd:PRK05380 2 TKYIFVTGGVVSSLGKGITAASLGRLLKARGLKVTIQKLDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFIDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386803 89 NLPGSANVTTGQVYSTVIAKERRGEYLGDTVQVIPHITDEIKRRILAMAqpdadgNRPDVVITEIGGTVGDIESQPFLEA 168
Cdd:PRK05380 82 NLTKYNNVTTGKIYSSVIEKERRGDYLGKTVQVIPHITDEIKERILAAG------TDADVVIVEIGGTVGDIESLPFLEA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386803 169 ARQVRHYLGREDVFFLHVSLVPYLAPSGELKTKPTQHSVAALRSIGITPDALILRCDRDVPEALKNKIALMCDVDIDGVI 248
Cdd:PRK05380 156 IRQLRLELGRENVLFIHLTLVPYIAAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEEKRKIALFCNVPEEAVI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386803 249 STPDAPSIYDIPKVLHREELDAFVVRRLNLPFRDVDWTEWDDLLRRVHEPHETVRIALVGKYVELSDAYLSVAEALRAGG 328
Cdd:PRK05380 236 SAPDVDSIYEVPLLLHEQGLDDIVLERLGLEAPEPDLSEWEELVERLKNPKGEVTIALVGKYVELPDAYKSVIEALKHAG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386803 329 FKHRAKVEICWVASDGCEtTSGAAAALGDVHGVLIPGGFGIRGIEGKIGAIAYARARGLPVLGLCLGLQCIVIEAARSV- 407
Cdd:PRK05380 316 IANDVKVNIKWIDSEDLE-EENVAELLKGVDGILVPGGFGERGIEGKILAIRYARENNIPFLGICLGMQLAVIEFARNVl 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386803 408 GLTNANSAEFDPDTPDPVIATMPDQEEIVageaDLGGTMRLGSYPAVLEPDSVVAQAYQTTQVSERHRHRYEVNNAYRDK 487
Cdd:PRK05380 395 GLEDANSTEFDPDTPHPVIDLMPEQKDVS----DLGGTMRLGAYPCKLKPGTLAAEIYGKEEIYERHRHRYEVNNKYREQ 470
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 887386803 488 IAESGLRFSGTSPDGHLVEFVEYPpdRHPFVVGTQAHPELKSRPTRPHPLFVAFVGAAIDYKAGE 552
Cdd:PRK05380 471 LEKAGLVFSGTSPDGRLVEIVELP--DHPWFVGVQFHPEFKSRPRRPHPLFAGFVKAALENKKRK 533
|
|
| PyrG |
TIGR00337 |
CTP synthase; CTP synthase is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. ... |
9-544 |
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: 805.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386803 9 TKHLFVSGGVASSLGKGLTASSLGQLLTARGLHVTMQKLDPYLNVDPGTMNPFQHGEVFVTEDGAETDLDVGHYERFLDR 88
Cdd:TIGR00337 1 MKYIFVTGGVVSSLGKGITAASLGRLLKARGLNVTIIKIDPYINIDPGTMSPLQHGEVFVTDDGAETDLDLGHYERFLDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386803 89 NLPGSANVTTGQVYSTVIAKERRGEYLGDTVQVIPHITDEIKRRILAMAQPDAdgnrPDVVITEIGGTVGDIESQPFLEA 168
Cdd:TIGR00337 81 NLTRDNNITTGKIYSSVIEKERKGDYLGKTVQIIPHITNEIKDRILRVAKISG----PDVVIVEIGGTVGDIESLPFLEA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386803 169 ARQVRHYLGREDVFFLHVSLVPYLAPSGELKTKPTQHSVAALRSIGITPDALILRCDRDVPEALKNKIALMCDVDIDGVI 248
Cdd:TIGR00337 157 IRQFRVEVGRENVLFIHVTLVPYIAAAGEQKTKPTQHSVKELRSLGIQPDIIICRSSRPLDPNTKDKIALFCDVEEEAVI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386803 249 STPDAPSIYDIPKVLHREELDAFVVRRLNLPFRDVDWTEWDDLLRRVHEPHETVRIALVGKYVELSDAYLSVAEALRAGG 328
Cdd:TIGR00337 237 SAKDVSSIYEVPLLLLKQGLDDYLCRRLNLNCDEADLSEWEQLVEKFANPKHEVTIGIVGKYVELKDAYLSVIEALKHAG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386803 329 FKHRAKVEICWVASDGCETTsgAAAALGDVHGVLIPGGFGIRGIEGKIGAIAYARARGLPVLGLCLGLQCIVIEAARSV- 407
Cdd:TIGR00337 317 AKLDTKVNIKWIDSEDLEEE--GVEFLKGLDGILVPGGFGERGVEGKILAIKYARENNIPFLGICLGMQLAVIEFARNVa 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386803 408 GLTNANSAEFDPDTPDPVIATMPDQEEIVageaDLGGTMRLGSYPAVLEPDSVVAQAYQTTQVSERHRHRYEVNNAYRDK 487
Cdd:TIGR00337 395 GLEGANSTEFDPDTKYPVVDLLPEQKDIS----DLGGTMRLGLYPCILKPGTLAFKLYGKEEVYERHRHRYEVNNEYREQ 470
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 887386803 488 IAESGLRFSGTSPDGHLVEFVEYPpdRHPFVVGTQAHPELKSRPTRPHPLFVAFVGA 544
Cdd:TIGR00337 471 IENKGLIVSGTSPDGRLVEIIELP--DHPFFVACQFHPEFTSRPNDPHPLFLGFVKA 525
|
|
| CTP_synth_N |
pfam06418 |
CTP synthase N-terminus; This family consists of the N-terminal region of the CTP synthase ... |
10-278 |
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: 533.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386803 10 KHLFVSGGVASSLGKGLTASSLGQLLTARGLHVTMQKLDPYLNVDPGTMNPFQHGEVFVTEDGAETDLDVGHYERFLDRN 89
Cdd:pfam06418 1 KYIFVTGGVVSGLGKGITAASLGRLLKSRGLKVTIIKIDPYLNVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFLDIN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386803 90 LPGSANVTTGQVYSTVIAKERRGEYLGDTVQVIPHITDEIKRRILAMAQpdadGNRPDVVITEIGGTVGDIESQPFLEAA 169
Cdd:pfam06418 81 LTKDNNITTGKIYQSVIEKERRGDYLGKTVQVIPHITDEIKERIRRVAK----EVGPDVVIVEIGGTVGDIESLPFLEAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386803 170 RQVRHYLGREDVFFLHVSLVPYLAPSGELKTKPTQHSVAALRSIGITPDALILRCDRDVPEALKNKIALMCDVDIDGVIS 249
Cdd:pfam06418 157 RQLRLEVGRENVLFIHVTLVPYLKAAGELKTKPTQHSVKELRSIGIQPDIIVCRSERPLDEEVKEKIALFCNVPKEAVIS 236
|
250 260
....*....|....*....|....*....
gi 887386803 250 TPDAPSIYDIPKVLHREELDAFVVRRLNL 278
Cdd:pfam06418 237 APDVSSIYEVPLLLEEQGLDDIILKRLNL 265
|
|
| CTPS_N |
cd03113 |
N-terminal domain of cytidine 5'-triphosphate synthase; Cytidine 5'-triphosphate synthase ... |
10-274 |
6.60e-171 |
|
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: 485.07 E-value: 6.60e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386803 10 KHLFVSGGVASSLGKGLTASSLGQLLTARGLHVTMQKLDPYLNVDPGTMNPFQHGEVFVTEDGAETDLDVGHYERFLDRN 89
Cdd:cd03113 1 KYIFVTGGVVSGLGKGITASSIGRLLKSRGLRVTAIKIDPYLNVDAGTMSPYEHGEVFVLDDGGETDLDLGNYERFLDVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386803 90 LPGSANVTTGQVYSTVIAKERRGEYLGDTVQVIPHITDEIKRRILAMAQpdadGNRPDVVITEIGGTVGDIESQPFLEAA 169
Cdd:cd03113 81 LTRDNNITTGKIYSEVIEKERRGDYLGKTVQVIPHITDEIKERIRRVAK----IPEPDVCIVEIGGTVGDIESLPFLEAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386803 170 RQVRHYLGREDVFFLHVSLVPYLAPSGELKTKPTQHSVAALRSIGITPDALILRCDRDVPEALKNKIALMCDVDIDGVIS 249
Cdd:cd03113 157 RQFQFEVGRENFLFIHVTLVPYLEATGEQKTKPTQHSVKELRSLGIQPDIIVCRSEKPLDEETKEKIALFCNVPPEAVIS 236
|
250 260
....*....|....*....|....*
gi 887386803 250 TPDAPSIYDIPKVLHREELDAFVVR 274
Cdd:cd03113 237 VHDVSSIYEVPLLLEKQGLDDYILR 261
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PyrG |
COG0504 |
CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase ... |
9-551 |
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: 1046.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386803 9 TKHLFVSGGVASSLGKGLTASSLGQLLTARGLHVTMQKLDPYLNVDPGTMNPFQHGEVFVTEDGAETDLDVGHYERFLDR 88
Cdd:COG0504 1 TKYIFVTGGVVSSLGKGITAASLGRLLKARGLKVTIQKLDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFLDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386803 89 NLPGSANVTTGQVYSTVIAKERRGEYLGDTVQVIPHITDEIKRRILAMAQPdadgNRPDVVITEIGGTVGDIESQPFLEA 168
Cdd:COG0504 81 NLSKANNVTTGQIYSSVIEKERRGDYLGKTVQVIPHITDEIKRRIRRAAEE----SGADVVIVEIGGTVGDIESLPFLEA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386803 169 ARQVRHYLGREDVFFLHVSLVPYLAPSGELKTKPTQHSVAALRSIGITPDALILRCDRDVPEALKNKIALMCDVDIDGVI 248
Cdd:COG0504 157 IRQLRLELGRENVLFIHVTLVPYIAAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEIKRKIALFCNVPEEAVI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386803 249 STPDAPSIYDIPKVLHREELDAFVVRRLNLPFRDVDWTEWDDLLRRVHEPHETVRIALVGKYVELSDAYLSVAEALRAGG 328
Cdd:COG0504 237 SAPDVDSIYEVPLMLHEQGLDEIVLKKLGLEAREPDLSEWEELVERIKNPKKEVTIALVGKYVELPDAYKSVVEALKHAG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386803 329 FKHRAKVEICWVASDGCEtTSGAAAALGDVHGVLIPGGFGIRGIEGKIGAIAYARARGLPVLGLCLGLQCIVIEAARSV- 407
Cdd:COG0504 317 IANGVKVNIKWIDSEDLE-EENAEELLKGVDGILVPGGFGERGIEGKIAAIRYARENKIPFLGICLGMQLAVIEFARNVl 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386803 408 GLTNANSAEFDPDTPDPVIATMPDQEEIVageaDLGGTMRLGSYPAVLEPDSVVAQAYQTTQVSERHRHRYEVNNAYRDK 487
Cdd:COG0504 396 GLEDANSTEFDPNTPHPVIDLMPEQKDVS----DLGGTMRLGAYPCKLKPGTLAAEAYGKEEISERHRHRYEFNNEYREQ 471
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 887386803 488 IAESGLRFSGTSPDGHLVEFVEYPpdRHPFVVGTQAHPELKSRPTRPHPLFVAFVGAAIDYKAG 551
Cdd:COG0504 472 LEKAGLVFSGTSPDGRLVEIVELP--DHPWFVGVQFHPEFKSRPNRPHPLFRGFVKAALEYKKK 533
|
|
| pyrG |
PRK05380 |
CTP synthetase; Validated |
9-552 |
0e+00 |
|
CTP synthetase; Validated
Pssm-ID: 235437 [Multi-domain] Cd Length: 533 Bit Score: 1044.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386803 9 TKHLFVSGGVASSLGKGLTASSLGQLLTARGLHVTMQKLDPYLNVDPGTMNPFQHGEVFVTEDGAETDLDVGHYERFLDR 88
Cdd:PRK05380 2 TKYIFVTGGVVSSLGKGITAASLGRLLKARGLKVTIQKLDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFIDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386803 89 NLPGSANVTTGQVYSTVIAKERRGEYLGDTVQVIPHITDEIKRRILAMAqpdadgNRPDVVITEIGGTVGDIESQPFLEA 168
Cdd:PRK05380 82 NLTKYNNVTTGKIYSSVIEKERRGDYLGKTVQVIPHITDEIKERILAAG------TDADVVIVEIGGTVGDIESLPFLEA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386803 169 ARQVRHYLGREDVFFLHVSLVPYLAPSGELKTKPTQHSVAALRSIGITPDALILRCDRDVPEALKNKIALMCDVDIDGVI 248
Cdd:PRK05380 156 IRQLRLELGRENVLFIHLTLVPYIAAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEEKRKIALFCNVPEEAVI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386803 249 STPDAPSIYDIPKVLHREELDAFVVRRLNLPFRDVDWTEWDDLLRRVHEPHETVRIALVGKYVELSDAYLSVAEALRAGG 328
Cdd:PRK05380 236 SAPDVDSIYEVPLLLHEQGLDDIVLERLGLEAPEPDLSEWEELVERLKNPKGEVTIALVGKYVELPDAYKSVIEALKHAG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386803 329 FKHRAKVEICWVASDGCEtTSGAAAALGDVHGVLIPGGFGIRGIEGKIGAIAYARARGLPVLGLCLGLQCIVIEAARSV- 407
Cdd:PRK05380 316 IANDVKVNIKWIDSEDLE-EENVAELLKGVDGILVPGGFGERGIEGKILAIRYARENNIPFLGICLGMQLAVIEFARNVl 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386803 408 GLTNANSAEFDPDTPDPVIATMPDQEEIVageaDLGGTMRLGSYPAVLEPDSVVAQAYQTTQVSERHRHRYEVNNAYRDK 487
Cdd:PRK05380 395 GLEDANSTEFDPDTPHPVIDLMPEQKDVS----DLGGTMRLGAYPCKLKPGTLAAEIYGKEEIYERHRHRYEVNNKYREQ 470
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 887386803 488 IAESGLRFSGTSPDGHLVEFVEYPpdRHPFVVGTQAHPELKSRPTRPHPLFVAFVGAAIDYKAGE 552
Cdd:PRK05380 471 LEKAGLVFSGTSPDGRLVEIVELP--DHPWFVGVQFHPEFKSRPRRPHPLFAGFVKAALENKKRK 533
|
|
| PyrG |
TIGR00337 |
CTP synthase; CTP synthase is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. ... |
9-544 |
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: 805.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386803 9 TKHLFVSGGVASSLGKGLTASSLGQLLTARGLHVTMQKLDPYLNVDPGTMNPFQHGEVFVTEDGAETDLDVGHYERFLDR 88
Cdd:TIGR00337 1 MKYIFVTGGVVSSLGKGITAASLGRLLKARGLNVTIIKIDPYINIDPGTMSPLQHGEVFVTDDGAETDLDLGHYERFLDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386803 89 NLPGSANVTTGQVYSTVIAKERRGEYLGDTVQVIPHITDEIKRRILAMAQPDAdgnrPDVVITEIGGTVGDIESQPFLEA 168
Cdd:TIGR00337 81 NLTRDNNITTGKIYSSVIEKERKGDYLGKTVQIIPHITNEIKDRILRVAKISG----PDVVIVEIGGTVGDIESLPFLEA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386803 169 ARQVRHYLGREDVFFLHVSLVPYLAPSGELKTKPTQHSVAALRSIGITPDALILRCDRDVPEALKNKIALMCDVDIDGVI 248
Cdd:TIGR00337 157 IRQFRVEVGRENVLFIHVTLVPYIAAAGEQKTKPTQHSVKELRSLGIQPDIIICRSSRPLDPNTKDKIALFCDVEEEAVI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386803 249 STPDAPSIYDIPKVLHREELDAFVVRRLNLPFRDVDWTEWDDLLRRVHEPHETVRIALVGKYVELSDAYLSVAEALRAGG 328
Cdd:TIGR00337 237 SAKDVSSIYEVPLLLLKQGLDDYLCRRLNLNCDEADLSEWEQLVEKFANPKHEVTIGIVGKYVELKDAYLSVIEALKHAG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386803 329 FKHRAKVEICWVASDGCETTsgAAAALGDVHGVLIPGGFGIRGIEGKIGAIAYARARGLPVLGLCLGLQCIVIEAARSV- 407
Cdd:TIGR00337 317 AKLDTKVNIKWIDSEDLEEE--GVEFLKGLDGILVPGGFGERGVEGKILAIKYARENNIPFLGICLGMQLAVIEFARNVa 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386803 408 GLTNANSAEFDPDTPDPVIATMPDQEEIVageaDLGGTMRLGSYPAVLEPDSVVAQAYQTTQVSERHRHRYEVNNAYRDK 487
Cdd:TIGR00337 395 GLEGANSTEFDPDTKYPVVDLLPEQKDIS----DLGGTMRLGLYPCILKPGTLAFKLYGKEEVYERHRHRYEVNNEYREQ 470
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 887386803 488 IAESGLRFSGTSPDGHLVEFVEYPpdRHPFVVGTQAHPELKSRPTRPHPLFVAFVGA 544
Cdd:TIGR00337 471 IENKGLIVSGTSPDGRLVEIIELP--DHPFFVACQFHPEFTSRPNDPHPLFLGFVKA 525
|
|
| PLN02327 |
PLN02327 |
CTP synthase |
9-545 |
0e+00 |
|
CTP synthase
Pssm-ID: 215186 [Multi-domain] Cd Length: 557 Bit Score: 614.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386803 9 TKHLFVSGGVASSLGKGLTASSLGQLLTARGLHVTMQKLDPYLNVDPGTMNPFQHGEVFVTEDGAETDLDVGHYERFLDR 88
Cdd:PLN02327 1 MKYVLVTGGVVSGLGKGVTASSIGVLLKACGLRVTSIKIDPYLNTDAGTMSPFEHGEVFVLDDGGEVDLDLGNYERFLDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386803 89 NLPGSANVTTGQVYSTVIAKERRGEYLGDTVQVIPHITDEIKRRILAMAQPDADG--NRPDVVITEIGGTVGDIESQPFL 166
Cdd:PLN02327 81 TLTRDNNITTGKIYQSVIEKERRGDYLGKTVQVVPHITDAIQEWIERVAKIPVDGkeGPADVCVIELGGTVGDIESMPFI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386803 167 EAARQVRHYLGREDVFFLHVSLVPYLAPSGELKTKPTQHSVAALRSIGITPDALILRCDRDVPEALKNKIALMCDVDIDG 246
Cdd:PLN02327 161 EALRQFSFRVGPGNFCLIHVSLVPVLGVVGEQKTKPTQHSVRGLRALGLTPHILACRSTKPLEENVKEKLSQFCHVPAEN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386803 247 VISTPDAPSIYDIPKVLHREELDAFVVRRLNLP--FRDVDWTEWDDLLRRVHEPHETVRIALVGKYVELSDAYLSVAEAL 324
Cdd:PLN02327 241 ILNLHDVSNIWHVPLLLRDQKAHEAILKVLNLLsvAREPDLEEWTARAESCDNLTEPVRIAMVGKYTGLSDSYLSVLKAL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386803 325 RAGGFKHRAKVEICWVASDGCE------TTSGAAAA---LGDVHGVLIPGGFGIRGIEGKIGAIAYARARGLPVLGLCLG 395
Cdd:PLN02327 321 LHASVACSRKLVIDWVAASDLEdetakeTPDAYAAAwklLKGADGILVPGGFGDRGVEGKILAAKYARENKVPYLGICLG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386803 396 LQCIVIEAARSV-GLTNANSAEFDPDTPDPVIATMPDqeeivAGEADLGGTMRLGSYPAVLE-PDSVVAQAYQTTQ-VSE 472
Cdd:PLN02327 401 MQIAVIEFARSVlGLKDANSTEFDPETPNPCVIFMPE-----GSKTHMGGTMRLGSRRTYFQtPDCKSAKLYGNVSfVDE 475
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 887386803 473 RHRHRYEVNNAYRDKIAESGLRFSGTSPDGHLVEFVEYPpdRHPFVVGTQAHPELKSRPTRPHPLFVAFVGAA 545
Cdd:PLN02327 476 RHRHRYEVNPEMVPRLEKAGLSFVGKDETGRRMEIVELP--SHPFFVGVQFHPEFKSRPGKPSPLFLGLIAAA 546
|
|
| CTP_synth_N |
pfam06418 |
CTP synthase N-terminus; This family consists of the N-terminal region of the CTP synthase ... |
10-278 |
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: 533.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386803 10 KHLFVSGGVASSLGKGLTASSLGQLLTARGLHVTMQKLDPYLNVDPGTMNPFQHGEVFVTEDGAETDLDVGHYERFLDRN 89
Cdd:pfam06418 1 KYIFVTGGVVSGLGKGITAASLGRLLKSRGLKVTIIKIDPYLNVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFLDIN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386803 90 LPGSANVTTGQVYSTVIAKERRGEYLGDTVQVIPHITDEIKRRILAMAQpdadGNRPDVVITEIGGTVGDIESQPFLEAA 169
Cdd:pfam06418 81 LTKDNNITTGKIYQSVIEKERRGDYLGKTVQVIPHITDEIKERIRRVAK----EVGPDVVIVEIGGTVGDIESLPFLEAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386803 170 RQVRHYLGREDVFFLHVSLVPYLAPSGELKTKPTQHSVAALRSIGITPDALILRCDRDVPEALKNKIALMCDVDIDGVIS 249
Cdd:pfam06418 157 RQLRLEVGRENVLFIHVTLVPYLKAAGELKTKPTQHSVKELRSIGIQPDIIVCRSERPLDEEVKEKIALFCNVPKEAVIS 236
|
250 260
....*....|....*....|....*....
gi 887386803 250 TPDAPSIYDIPKVLHREELDAFVVRRLNL 278
Cdd:pfam06418 237 APDVSSIYEVPLLLEEQGLDDIILKRLNL 265
|
|
| CTPS_N |
cd03113 |
N-terminal domain of cytidine 5'-triphosphate synthase; Cytidine 5'-triphosphate synthase ... |
10-274 |
6.60e-171 |
|
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: 485.07 E-value: 6.60e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386803 10 KHLFVSGGVASSLGKGLTASSLGQLLTARGLHVTMQKLDPYLNVDPGTMNPFQHGEVFVTEDGAETDLDVGHYERFLDRN 89
Cdd:cd03113 1 KYIFVTGGVVSGLGKGITASSIGRLLKSRGLRVTAIKIDPYLNVDAGTMSPYEHGEVFVLDDGGETDLDLGNYERFLDVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386803 90 LPGSANVTTGQVYSTVIAKERRGEYLGDTVQVIPHITDEIKRRILAMAQpdadGNRPDVVITEIGGTVGDIESQPFLEAA 169
Cdd:cd03113 81 LTRDNNITTGKIYSEVIEKERRGDYLGKTVQVIPHITDEIKERIRRVAK----IPEPDVCIVEIGGTVGDIESLPFLEAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386803 170 RQVRHYLGREDVFFLHVSLVPYLAPSGELKTKPTQHSVAALRSIGITPDALILRCDRDVPEALKNKIALMCDVDIDGVIS 249
Cdd:cd03113 157 RQFQFEVGRENFLFIHVTLVPYLEATGEQKTKPTQHSVKELRSLGIQPDIIVCRSEKPLDEETKEKIALFCNVPPEAVIS 236
|
250 260
....*....|....*....|....*
gi 887386803 250 TPDAPSIYDIPKVLHREELDAFVVR 274
Cdd:cd03113 237 VHDVSSIYEVPLLLEKQGLDDYILR 261
|
|
| GATase1_CTP_Synthase |
cd01746 |
Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase; ... |
302-542 |
9.92e-130 |
|
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: 379.20 E-value: 9.92e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386803 302 VRIALVGKYVELSDAYLSVAEALRAGGFKHRAKVEICWVASDGCETtSGAAAALGDVHGVLIPGGFGIRGIEGKIGAIAY 381
Cdd:cd01746 1 VRIALVGKYVELPDAYLSVLEALKHAGIALGVKLEIKWIDSEDLEE-ENAEEALKGADGILVPGGFGIRGVEGKILAIKY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386803 382 ARARGLPVLGLCLGLQCIVIEAARSV-GLTNANSAEFDPDTPDPVIATMPDQEEIVageaDLGGTMRLGSYPAVLEPDSV 460
Cdd:cd01746 80 ARENNIPFLGICLGMQLAVIEFARNVlGLPDANSTEFDPDTPHPVVDLMPEQKGVK----DLGGTMRLGAYPVILKPGTL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386803 461 VAQAYQTTQVSERHRHRYEVNNAYRDKIAESGLRFSGTSPDGHLVEFVEYPpdRHPFVVGTQAHPELKSRPTRPHPLFVA 540
Cdd:cd01746 156 AHKYYGKDEVEERHRHRYEVNPEYVDELEEAGLRFSGTDPDGGLVEIVELP--DHPFFVGTQFHPEFKSRPLKPHPLFVG 233
|
..
gi 887386803 541 FV 542
Cdd:cd01746 234 FV 235
|
|
| PRK06186 |
PRK06186 |
hypothetical protein; Validated |
301-545 |
3.80e-37 |
|
hypothetical protein; Validated
Pssm-ID: 180452 [Multi-domain] Cd Length: 229 Bit Score: 137.79 E-value: 3.80e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386803 301 TVRIALVGKYVELSDAYLSVAEALRAGGFKHRAKVEICWVASDgcetTSGAAAALGDVHGV-LIPGGfGIRGIEGKIGAI 379
Cdd:PRK06186 1 TLRIALVGDYNPDVTAHQAIPLALDLAAAVLGLPVDYEWLPTP----EITDPEDLAGFDGIwCVPGS-PYRNDDGALTAI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386803 380 AYARARGLPVLGLCLGLQCIVIEAARSV-GLTNANSAEFDPDTPDPVIAtmPDQEEIVAGEADLggtmrlgsypaVLEPD 458
Cdd:PRK06186 76 RFARENGIPFLGTCGGFQHALLEYARNVlGWADAAHAETDPEGDRPVIA--PLSCSLVEKTGDI-----------RLRPG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386803 459 SVVAQAYQTTQVSERHRHRYEVNNAYRDKIAESGLRFSGTSPDGHlVEFVEYPpdRHPFVVGTQAHPELKSRPTRPHPLF 538
Cdd:PRK06186 143 SLIARAYGTLEIEEGYHCRYGVNPEFVAALESGDLRVTGWDEDGD-VRAVELP--GHPFFVATLFQPERAALAGRPPPLV 219
|
....*..
gi 887386803 539 VAFVGAA 545
Cdd:PRK06186 220 RAFLRAA 226
|
|
| GATase |
pfam00117 |
Glutamine amidotransferase class-I; |
315-544 |
1.17e-30 |
|
Glutamine amidotransferase class-I;
Pssm-ID: 395067 [Multi-domain] Cd Length: 188 Bit Score: 118.11 E-value: 1.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386803 315 DAYLSVAEALRAGGFKHRAKVEICWVasdgceTTSGAAAALGDVHGVLIPGGFGIRGI-EGKIGAIAYARARGLPVLGLC 393
Cdd:pfam00117 4 DNGDSFTYNLARALRELGVEVTVVPN------DTPAEEILEENPDGIILSGGPGSPGAaGGAIEAIREARELKIPILGIC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386803 394 LGLQCIVIEAARSVGltnansaefdpdtpdpviaTMPDQEeivageaDLGGTMRLGSYPAVLepdsvvaqAYQTTQVS-E 472
Cdd:pfam00117 78 LGHQLLALAFGGKVV-------------------KAKKFG-------HHGKNSPVGDDGCGL--------FYGLPNVFiV 123
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 887386803 473 RHRHRYEVNNayrdKIAESGLRFSGTSPDGHLVEFVEYPPDRhpfVVGTQAHPELKSRPTRPHPLFVAFVGA 544
Cdd:pfam00117 124 RRYHSYAVDP----DTLPDGLEVTATSENDGTIMGIRHKKLP---IFGVQFHPESILTPHGPEILFNFFIKA 188
|
|
| Peptidase_C26 |
pfam07722 |
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ... |
351-526 |
1.81e-10 |
|
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: 61.12 E-value: 1.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386803 351 AAAALGDVHGVLIPGG-------FGIRGIEgKIGAIAYAR------------ARGLPVLGLCLGLQCIVIeaarSVGLTN 411
Cdd:pfam07722 52 AAAILDRLDGLLLTGGpnvdphfYGEEPSE-SGGPYDPARdayelaliraalARGKPILGICRGFQLLNV----ALGGTL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386803 412 ANSAEFDPDTPDPViatMPDQEEIVAgeadlggtmrlGSYPAVLEPDSVVAQAYQTTQVSERHRHRYEVnnayrDKIAEs 491
Cdd:pfam07722 127 YQDIQEQPGFTDHR---EHCQVAPYA-----------PSHAVNVEPGSLLASLLGSEEFRVNSLHHQAI-----DRLAP- 186
|
170 180 190
....*....|....*....|....*....|....*
gi 887386803 492 GLRFSGTSPDGhLVEFVEYpPDRHPFVVGTQAHPE 526
Cdd:pfam07722 187 GLRVEAVAPDG-TIEAIES-PNAKGFALGVQWHPE 219
|
|
| GATase1 |
cd01653 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
304-401 |
3.07e-10 |
|
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group includes proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA. and, the A4 beta-galactosidase middle domain. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.
Pssm-ID: 153210 [Multi-domain] Cd Length: 115 Bit Score: 57.61 E-value: 3.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386803 304 IALVGKYVELSDAYLSVAEALRAGGFKhrakVEICWVASDgcetTSGAAAALGDVHGVLIPGGFG----IRGIEGKIGAI 379
Cdd:cd01653 1 VAVLLFPGFEELELASPLDALREAGAE----VDVVSPDGG----PVESDVDLDDYDGLILPGGPGtpddLARDEALLALL 72
|
90 100
....*....|....*....|..
gi 887386803 380 AYARARGLPVLGLCLGLQCIVI 401
Cdd:cd01653 73 REAAAAGKPILGICLGAQLLVL 94
|
|
| GAT_1 |
cd03128 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
304-399 |
4.44e-09 |
|
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group contains proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA, the A4 beta-galactosidase middle domain and peptidase E. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase (CPSase), cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. Peptidase E is believed to be a serine peptidase having a Ser-His-Glu catalytic triad which differs from the Cys-His-Glu catalytic triad of typical GATase1 domains, by having a Ser in place of the reactive Cys at the nucleophile elbow. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase. Peptidase E has a circular permutation in the common core of a typical GTAse1 domain.
Pssm-ID: 153222 [Multi-domain] Cd Length: 92 Bit Score: 53.74 E-value: 4.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386803 304 IALVGKYVELSDAYLSVAEALRAGGFKhrakVEICWVASDgcetTSGAAAALGDVHGVLIPGGFG----IRGIEGKIGAI 379
Cdd:cd03128 1 VAVLLFGGSEELELASPLDALREAGAE----VDVVSPDGG----PVESDVDLDDYDGLILPGGPGtpddLAWDEALLALL 72
|
90 100
....*....|....*....|
gi 887386803 380 AYARARGLPVLGLCLGLQCI 399
Cdd:cd03128 73 REAAAAGKPVLGICLGAQLL 92
|
|
| GATase1_2 |
cd01745 |
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ... |
379-542 |
1.23e-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: 43.33 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386803 379 IAYARARGLPVLGLCLGLQcivieaarsvgLTNansaefdpdtpdpviatmpdqeeiVAgeadLGGTMrlgsypavlepd 458
Cdd:cd01745 93 LRAALERGKPILGICRGMQ-----------LLN------------------------VA----LGGTL------------ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386803 459 svvaqaYQTTQV-SerhRHRYEVnnayrDKIAEsGLRFSGTSPDGhLVEFVEYPPdrHPFVVGTQAHPELKSRPTRPH-P 536
Cdd:cd01745 122 ------YQDIRVnS---LHHQAI-----KRLAD-GLRVEARAPDG-VIEAIESPD--RPFVLGVQWHPEWLADTDPDSlK 183
|
....*.
gi 887386803 537 LFVAFV 542
Cdd:cd01745 184 LFEAFV 189
|
|
| GATase1_FGAR_AT |
cd01740 |
Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ... |
320-403 |
2.87e-03 |
|
Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ribonucleotide amidotransferase; Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ribonucleotide amidotransferase (FGAR-AT). FGAR-AT catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to formylglycinamidine ribonucleotide (FGAM), ADP, Pi, and glutamate in the fourth step of the purine biosynthetic pathway. FGAR-AT is a glutamine amidotransferase. Glutamine amidotransferase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. FGAR-AT belongs to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site
Pssm-ID: 153211 [Multi-domain] Cd Length: 238 Bit Score: 39.52 E-value: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386803 320 VAEALRAGGFKhrakVEICWVaSDGCEttsgAAAALGDVHGVLIPGGFG----IRGieGKIGA--------IAYARARGL 387
Cdd:cd01740 15 MAYAFELAGFE----AEDVWH-NDLLA----GRKDLDDYDGVVLPGGFSygdyLRA--GAIAAaspllmeeVKEFAERGG 83
|
90
....*....|....*.
gi 887386803 388 PVLGLCLGLQcIVIEA 403
Cdd:cd01740 84 LVLGICNGFQ-ILVEL 98
|
|
| PRK03619 |
PRK03619 |
phosphoribosylformylglycinamidine synthase subunit PurQ; |
355-403 |
4.74e-03 |
|
phosphoribosylformylglycinamidine synthase subunit PurQ;
Pssm-ID: 235140 [Multi-domain] Cd Length: 219 Bit Score: 38.94 E-value: 4.74e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 887386803 355 LGDVHGVLIPGGF--G--IRGiegkiGAIAyARA-----------RGLPVLGLCLGLQcIVIEA 403
Cdd:PRK03619 39 LDGVDAVVLPGGFsyGdyLRC-----GAIA-AFSpimkavkefaeKGKPVLGICNGFQ-ILTEA 95
|
|
| PRK13566 |
PRK13566 |
anthranilate synthase component I; |
379-404 |
9.23e-03 |
|
anthranilate synthase component I;
Pssm-ID: 237429 [Multi-domain] Cd Length: 720 Bit Score: 39.13 E-value: 9.23e-03
10 20
....*....|....*....|....*.
gi 887386803 379 IAYARARGLPVLGLCLGLQCIViEAA 404
Cdd:PRK13566 591 IDAALARNLPIFGVCLGLQAIV-EAF 615
|
|
| |
