|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02327 |
PLN02327 |
CTP synthase |
1-524 |
0e+00 |
|
CTP synthase
Pssm-ID: 215186 [Multi-domain] Cd Length: 557 Bit Score: 984.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513425 1 MKSIGYRVSAIKIDPYLNIDAGTMSPFEHGEVFVLDDGGEVDLDLGNYERFLDVTLTRDNNLTTGKVYSAVIEAERRGDY 80
Cdd:PLN02327 27 LKACGLRVTSIKIDPYLNTDAGTMSPFEHGEVFVLDDGGEVDLDLGNYERFLDVTLTRDNNITTGKIYQSVIEKERRGDY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513425 81 LGKTVQVVPHITNEIQNWMERVAAIPVDGNGAEPDICIVELGGTVGDIESAPFVEALRQFQFRVGKENFVLVHVSLVPVI 160
Cdd:PLN02327 107 LGKTVQVVPHITDAIQEWIERVAKIPVDGKEGPADVCVIELGGTVGDIESMPFIEALRQFSFRVGPGNFCLIHVSLVPVL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513425 161 GVVGEQKTKPTQHTVKELRAAGLSPDFLVCRAEEPLLPATKDKLALFCHVEPSHVLSAHDVSNIYRVPLMLNEQGVTEMI 240
Cdd:PLN02327 187 GVVGEQKTKPTQHSVRGLRALGLTPHILACRSTKPLEENVKEKLSQFCHVPAENILNLHDVSNIWHVPLLLRDQKAHEAI 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513425 241 AEKLNLEIPESRPLFDDWVEMADRVDSLQKTINIAMVGKYTGLTDSYLSVIKALQHSAFKVGAKMEISWVEAASLEAKFE 320
Cdd:PLN02327 267 LKVLNLLSVAREPDLEEWTARAESCDNLTEPVRIAMVGKYTGLSDSYLSVLKALLHASVACSRKLVIDWVAASDLEDETA 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513425 321 EKNAKKYAESWAALKAAHGVLVPGGFGIRGIEGKILAAQYARENGVPYLGVCLGLQVAVIEFARNVLGLEGANSTEFDDK 400
Cdd:PLN02327 347 KETPDAYAAAWKLLKGADGILVPGGFGDRGVEGKILAAKYARENKVPYLGICLGMQIAVIEFARSVLGLKDANSTEFDPE 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513425 401 TPHPTVIFMPEGSKTHMGATMRLGSRQTNLHTEDCHAFRLYGGAKKIHERHRHRYEVNPDMIADLEAAGLRFVGKDTEAQ 480
Cdd:PLN02327 427 TPNPCVIFMPEGSKTHMGGTMRLGSRRTYFQTPDCKSAKLYGNVSFVDERHRHRYEVNPEMVPRLEKAGLSFVGKDETGR 506
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 663513425 481 RMEIIELADHPYYFGTQYHPEFKSRPNRPSPPFLGLVEAAFKRL 524
Cdd:PLN02327 507 RMEIVELPSHPFFVGVQFHPEFKSRPGKPSPLFLGLIAAASGQL 550
|
|
| PyrG |
COG0504 |
CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase ... |
1-523 |
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: 863.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513425 1 MKSIGYRVSAIKIDPYLNIDAGTMSPFEHGEVFVLDDGGEVDLDLGNYERFLDVTLTRDNNLTTGKVYSAVIEAERRGDY 80
Cdd:COG0504 27 LKARGLKVTIQKLDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFLDINLSKANNVTTGQIYSSVIEKERRGDY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513425 81 LGKTVQVVPHITNEIQNWMERVAAipvdgnGAEPDICIVELGGTVGDIESAPFVEALRQFQFRVGKENFVLVHVSLVPVI 160
Cdd:COG0504 107 LGKTVQVIPHITDEIKRRIRRAAE------ESGADVVIVEIGGTVGDIESLPFLEAIRQLRLELGRENVLFIHVTLVPYI 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513425 161 GVVGEQKTKPTQHTVKELRAAGLSPDFLVCRAEEPLLPATKDKLALFCHVEPSHVLSAHDVSNIYRVPLMLNEQGVTEMI 240
Cdd:COG0504 181 AAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEIKRKIALFCNVPEEAVISAPDVDSIYEVPLMLHEQGLDEIV 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513425 241 AEKLNLEIPEsrPLFDDWVEMADRVDSLQKTINIAMVGKYTGLTDSYLSVIKALQHSAFKVGAKMEISWVEAaslEaKFE 320
Cdd:COG0504 261 LKKLGLEARE--PDLSEWEELVERIKNPKKEVTIALVGKYVELPDAYKSVVEALKHAGIANGVKVNIKWIDS---E-DLE 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513425 321 EKNAKKYaeswaaLKAAHGVLVPGGFGIRGIEGKILAAQYARENGVPYLGVCLGLQVAVIEFARNVLGLEGANSTEFDDK 400
Cdd:COG0504 335 EENAEEL------LKGVDGILVPGGFGERGIEGKIAAIRYARENKIPFLGICLGMQLAVIEFARNVLGLEDANSTEFDPN 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513425 401 TPHPTVIFMPE-GSKTHMGATMRLGSRQTNLhTEDCHAFRLYgGAKKIHERHRHRYEVNPDMIADLEAAGLRFVGKDTEA 479
Cdd:COG0504 409 TPHPVIDLMPEqKDVSDLGGTMRLGAYPCKL-KPGTLAAEAY-GKEEISERHRHRYEFNNEYREQLEKAGLVFSGTSPDG 486
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 663513425 480 QRMEIIELADHPYYFGTQYHPEFKSRPNRPSPPFLGLVEAAFKR 523
Cdd:COG0504 487 RLVEIVELPDHPWFVGVQFHPEFKSRPNRPHPLFRGFVKAALEY 530
|
|
| PyrG |
TIGR00337 |
CTP synthase; CTP synthase is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. ... |
1-519 |
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: 797.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513425 1 MKSIGYRVSAIKIDPYLNIDAGTMSPFEHGEVFVLDDGGEVDLDLGNYERFLDVTLTRDNNLTTGKVYSAVIEAERRGDY 80
Cdd:TIGR00337 27 LKARGLNVTIIKIDPYINIDPGTMSPLQHGEVFVTDDGAETDLDLGHYERFLDTNLTRDNNITTGKIYSSVIEKERKGDY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513425 81 LGKTVQVVPHITNEIQNWMERVAAIpvdgngAEPDICIVELGGTVGDIESAPFVEALRQFQFRVGKENFVLVHVSLVPVI 160
Cdd:TIGR00337 107 LGKTVQIIPHITNEIKDRILRVAKI------SGPDVVIVEIGGTVGDIESLPFLEAIRQFRVEVGRENVLFIHVTLVPYI 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513425 161 GVVGEQKTKPTQHTVKELRAAGLSPDFLVCRAEEPLLPATKDKLALFCHVEPSHVLSAHDVSNIYRVPLMLNEQGVTEMI 240
Cdd:TIGR00337 181 AAAGEQKTKPTQHSVKELRSLGIQPDIIICRSSRPLDPNTKDKIALFCDVEEEAVISAKDVSSIYEVPLLLLKQGLDDYL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513425 241 AEKLNLEIPESRplFDDWVEMADRVDSLQKTINIAMVGKYTGLTDSYLSVIKALQHSAFKVGAKMEISWVEAASLEakfe 320
Cdd:TIGR00337 261 CRRLNLNCDEAD--LSEWEQLVEKFANPKHEVTIGIVGKYVELKDAYLSVIEALKHAGAKLDTKVNIKWIDSEDLE---- 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513425 321 eknakkyAESWAALKAAHGVLVPGGFGIRGIEGKILAAQYARENGVPYLGVCLGLQVAVIEFARNVLGLEGANSTEFDDK 400
Cdd:TIGR00337 335 -------EEGVEFLKGLDGILVPGGFGERGVEGKILAIKYARENNIPFLGICLGMQLAVIEFARNVAGLEGANSTEFDPD 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513425 401 TPHPTVIFMPE-GSKTHMGATMRLGSRQTNLhTEDCHAFRLYgGAKKIHERHRHRYEVNPDMIADLEAAGLRFVGKDTEA 479
Cdd:TIGR00337 408 TKYPVVDLLPEqKDISDLGGTMRLGLYPCIL-KPGTLAFKLY-GKEEVYERHRHRYEVNNEYREQIENKGLIVSGTSPDG 485
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 663513425 480 QRMEIIELADHPYYFGTQYHPEFKSRPNRPSPPFLGLVEA 519
Cdd:TIGR00337 486 RLVEIIELPDHPFFVACQFHPEFTSRPNDPHPLFLGFVKA 525
|
|
| CTP_synth_N |
pfam06418 |
CTP synthase N-terminus; This family consists of the N-terminal region of the CTP synthase ... |
1-246 |
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: 509.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513425 1 MKSIGYRVSAIKIDPYLNIDAGTMSPFEHGEVFVLDDGGEVDLDLGNYERFLDVTLTRDNNLTTGKVYSAVIEAERRGDY 80
Cdd:pfam06418 26 LKSRGLKVTIIKIDPYLNVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFLDINLTKDNNITTGKIYQSVIEKERRGDY 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513425 81 LGKTVQVVPHITNEIQNWMERVAAIpvdgngAEPDICIVELGGTVGDIESAPFVEALRQFQFRVGKENFVLVHVSLVPVI 160
Cdd:pfam06418 106 LGKTVQVIPHITDEIKERIRRVAKE------VGPDVVIVEIGGTVGDIESLPFLEAIRQLRLEVGRENVLFIHVTLVPYL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513425 161 GVVGEQKTKPTQHTVKELRAAGLSPDFLVCRAEEPLLPATKDKLALFCHVEPSHVLSAHDVSNIYRVPLMLNEQGVTEMI 240
Cdd:pfam06418 180 KAAGELKTKPTQHSVKELRSIGIQPDIIVCRSERPLDEEVKEKIALFCNVPKEAVISAPDVSSIYEVPLLLEEQGLDDII 259
|
....*.
gi 663513425 241 AEKLNL 246
Cdd:pfam06418 260 LKRLNL 265
|
|
| CTPS_N |
cd03113 |
N-terminal domain of cytidine 5'-triphosphate synthase; Cytidine 5'-triphosphate synthase ... |
1-242 |
1.66e-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: 492.00 E-value: 1.66e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513425 1 MKSIGYRVSAIKIDPYLNIDAGTMSPFEHGEVFVLDDGGEVDLDLGNYERFLDVTLTRDNNLTTGKVYSAVIEAERRGDY 80
Cdd:cd03113 26 LKSRGLRVTAIKIDPYLNVDAGTMSPYEHGEVFVLDDGGETDLDLGNYERFLDVNLTRDNNITTGKIYSEVIEKERRGDY 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513425 81 LGKTVQVVPHITNEIQNWMERVAAIPvdgngaEPDICIVELGGTVGDIESAPFVEALRQFQFRVGKENFVLVHVSLVPVI 160
Cdd:cd03113 106 LGKTVQVIPHITDEIKERIRRVAKIP------EPDVCIVEIGGTVGDIESLPFLEALRQFQFEVGRENFLFIHVTLVPYL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513425 161 GVVGEQKTKPTQHTVKELRAAGLSPDFLVCRAEEPLLPATKDKLALFCHVEPSHVLSAHDVSNIYRVPLMLNEQGVTEMI 240
Cdd:cd03113 180 EATGEQKTKPTQHSVKELRSLGIQPDIIVCRSEKPLDEETKEKIALFCNVPPEAVISVHDVSSIYEVPLLLEKQGLDDYI 259
|
..
gi 663513425 241 AE 242
Cdd:cd03113 260 LR 261
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02327 |
PLN02327 |
CTP synthase |
1-524 |
0e+00 |
|
CTP synthase
Pssm-ID: 215186 [Multi-domain] Cd Length: 557 Bit Score: 984.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513425 1 MKSIGYRVSAIKIDPYLNIDAGTMSPFEHGEVFVLDDGGEVDLDLGNYERFLDVTLTRDNNLTTGKVYSAVIEAERRGDY 80
Cdd:PLN02327 27 LKACGLRVTSIKIDPYLNTDAGTMSPFEHGEVFVLDDGGEVDLDLGNYERFLDVTLTRDNNITTGKIYQSVIEKERRGDY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513425 81 LGKTVQVVPHITNEIQNWMERVAAIPVDGNGAEPDICIVELGGTVGDIESAPFVEALRQFQFRVGKENFVLVHVSLVPVI 160
Cdd:PLN02327 107 LGKTVQVVPHITDAIQEWIERVAKIPVDGKEGPADVCVIELGGTVGDIESMPFIEALRQFSFRVGPGNFCLIHVSLVPVL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513425 161 GVVGEQKTKPTQHTVKELRAAGLSPDFLVCRAEEPLLPATKDKLALFCHVEPSHVLSAHDVSNIYRVPLMLNEQGVTEMI 240
Cdd:PLN02327 187 GVVGEQKTKPTQHSVRGLRALGLTPHILACRSTKPLEENVKEKLSQFCHVPAENILNLHDVSNIWHVPLLLRDQKAHEAI 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513425 241 AEKLNLEIPESRPLFDDWVEMADRVDSLQKTINIAMVGKYTGLTDSYLSVIKALQHSAFKVGAKMEISWVEAASLEAKFE 320
Cdd:PLN02327 267 LKVLNLLSVAREPDLEEWTARAESCDNLTEPVRIAMVGKYTGLSDSYLSVLKALLHASVACSRKLVIDWVAASDLEDETA 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513425 321 EKNAKKYAESWAALKAAHGVLVPGGFGIRGIEGKILAAQYARENGVPYLGVCLGLQVAVIEFARNVLGLEGANSTEFDDK 400
Cdd:PLN02327 347 KETPDAYAAAWKLLKGADGILVPGGFGDRGVEGKILAAKYARENKVPYLGICLGMQIAVIEFARSVLGLKDANSTEFDPE 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513425 401 TPHPTVIFMPEGSKTHMGATMRLGSRQTNLHTEDCHAFRLYGGAKKIHERHRHRYEVNPDMIADLEAAGLRFVGKDTEAQ 480
Cdd:PLN02327 427 TPNPCVIFMPEGSKTHMGGTMRLGSRRTYFQTPDCKSAKLYGNVSFVDERHRHRYEVNPEMVPRLEKAGLSFVGKDETGR 506
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 663513425 481 RMEIIELADHPYYFGTQYHPEFKSRPNRPSPPFLGLVEAAFKRL 524
Cdd:PLN02327 507 RMEIVELPSHPFFVGVQFHPEFKSRPGKPSPLFLGLIAAASGQL 550
|
|
| PyrG |
COG0504 |
CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase ... |
1-523 |
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: 863.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513425 1 MKSIGYRVSAIKIDPYLNIDAGTMSPFEHGEVFVLDDGGEVDLDLGNYERFLDVTLTRDNNLTTGKVYSAVIEAERRGDY 80
Cdd:COG0504 27 LKARGLKVTIQKLDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFLDINLSKANNVTTGQIYSSVIEKERRGDY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513425 81 LGKTVQVVPHITNEIQNWMERVAAipvdgnGAEPDICIVELGGTVGDIESAPFVEALRQFQFRVGKENFVLVHVSLVPVI 160
Cdd:COG0504 107 LGKTVQVIPHITDEIKRRIRRAAE------ESGADVVIVEIGGTVGDIESLPFLEAIRQLRLELGRENVLFIHVTLVPYI 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513425 161 GVVGEQKTKPTQHTVKELRAAGLSPDFLVCRAEEPLLPATKDKLALFCHVEPSHVLSAHDVSNIYRVPLMLNEQGVTEMI 240
Cdd:COG0504 181 AAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEIKRKIALFCNVPEEAVISAPDVDSIYEVPLMLHEQGLDEIV 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513425 241 AEKLNLEIPEsrPLFDDWVEMADRVDSLQKTINIAMVGKYTGLTDSYLSVIKALQHSAFKVGAKMEISWVEAaslEaKFE 320
Cdd:COG0504 261 LKKLGLEARE--PDLSEWEELVERIKNPKKEVTIALVGKYVELPDAYKSVVEALKHAGIANGVKVNIKWIDS---E-DLE 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513425 321 EKNAKKYaeswaaLKAAHGVLVPGGFGIRGIEGKILAAQYARENGVPYLGVCLGLQVAVIEFARNVLGLEGANSTEFDDK 400
Cdd:COG0504 335 EENAEEL------LKGVDGILVPGGFGERGIEGKIAAIRYARENKIPFLGICLGMQLAVIEFARNVLGLEDANSTEFDPN 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513425 401 TPHPTVIFMPE-GSKTHMGATMRLGSRQTNLhTEDCHAFRLYgGAKKIHERHRHRYEVNPDMIADLEAAGLRFVGKDTEA 479
Cdd:COG0504 409 TPHPVIDLMPEqKDVSDLGGTMRLGAYPCKL-KPGTLAAEAY-GKEEISERHRHRYEFNNEYREQLEKAGLVFSGTSPDG 486
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 663513425 480 QRMEIIELADHPYYFGTQYHPEFKSRPNRPSPPFLGLVEAAFKR 523
Cdd:COG0504 487 RLVEIVELPDHPWFVGVQFHPEFKSRPNRPHPLFRGFVKAALEY 530
|
|
| pyrG |
PRK05380 |
CTP synthetase; Validated |
1-523 |
0e+00 |
|
CTP synthetase; Validated
Pssm-ID: 235437 [Multi-domain] Cd Length: 533 Bit Score: 857.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513425 1 MKSIGYRVSAIKIDPYLNIDAGTMSPFEHGEVFVLDDGGEVDLDLGNYERFLDVTLTRDNNLTTGKVYSAVIEAERRGDY 80
Cdd:PRK05380 28 LKARGLKVTIQKLDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFIDTNLTKYNNVTTGKIYSSVIEKERRGDY 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513425 81 LGKTVQVVPHITNEIQNWMERVAAipvdgngaEPDICIVELGGTVGDIESAPFVEALRQFQFRVGKENFVLVHVSLVPVI 160
Cdd:PRK05380 108 LGKTVQVIPHITDEIKERILAAGT--------DADVVIVEIGGTVGDIESLPFLEAIRQLRLELGRENVLFIHLTLVPYI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513425 161 GVVGEQKTKPTQHTVKELRAAGLSPDFLVCRAEEPLLPATKDKLALFCHVEPSHVLSAHDVSNIYRVPLMLNEQGVTEMI 240
Cdd:PRK05380 180 AAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEEKRKIALFCNVPEEAVISAPDVDSIYEVPLLLHEQGLDDIV 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513425 241 AEKLNLEIPEsrPLFDDWVEMADRVDSLQKTINIAMVGKYTGLTDSYLSVIKALQHSAFKVGAKMEISWVEAasleAKFE 320
Cdd:PRK05380 260 LERLGLEAPE--PDLSEWEELVERLKNPKGEVTIALVGKYVELPDAYKSVIEALKHAGIANDVKVNIKWIDS----EDLE 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513425 321 EKNAKKYaeswaaLKAAHGVLVPGGFGIRGIEGKILAAQYARENGVPYLGVCLGLQVAVIEFARNVLGLEGANSTEFDDK 400
Cdd:PRK05380 334 EENVAEL------LKGVDGILVPGGFGERGIEGKILAIRYARENNIPFLGICLGMQLAVIEFARNVLGLEDANSTEFDPD 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513425 401 TPHPTVIFMPE-GSKTHMGATMRLGSRQTNLhTEDCHAFRLYgGAKKIHERHRHRYEVNPDMIADLEAAGLRFVGKDTEA 479
Cdd:PRK05380 408 TPHPVIDLMPEqKDVSDLGGTMRLGAYPCKL-KPGTLAAEIY-GKEEIYERHRHRYEVNNKYREQLEKAGLVFSGTSPDG 485
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 663513425 480 QRMEIIELADHPYYFGTQYHPEFKSRPNRPSPPFLGLVEAAFKR 523
Cdd:PRK05380 486 RLVEIVELPDHPWFVGVQFHPEFKSRPRRPHPLFAGFVKAALEN 529
|
|
| PyrG |
TIGR00337 |
CTP synthase; CTP synthase is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. ... |
1-519 |
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: 797.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513425 1 MKSIGYRVSAIKIDPYLNIDAGTMSPFEHGEVFVLDDGGEVDLDLGNYERFLDVTLTRDNNLTTGKVYSAVIEAERRGDY 80
Cdd:TIGR00337 27 LKARGLNVTIIKIDPYINIDPGTMSPLQHGEVFVTDDGAETDLDLGHYERFLDTNLTRDNNITTGKIYSSVIEKERKGDY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513425 81 LGKTVQVVPHITNEIQNWMERVAAIpvdgngAEPDICIVELGGTVGDIESAPFVEALRQFQFRVGKENFVLVHVSLVPVI 160
Cdd:TIGR00337 107 LGKTVQIIPHITNEIKDRILRVAKI------SGPDVVIVEIGGTVGDIESLPFLEAIRQFRVEVGRENVLFIHVTLVPYI 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513425 161 GVVGEQKTKPTQHTVKELRAAGLSPDFLVCRAEEPLLPATKDKLALFCHVEPSHVLSAHDVSNIYRVPLMLNEQGVTEMI 240
Cdd:TIGR00337 181 AAAGEQKTKPTQHSVKELRSLGIQPDIIICRSSRPLDPNTKDKIALFCDVEEEAVISAKDVSSIYEVPLLLLKQGLDDYL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513425 241 AEKLNLEIPESRplFDDWVEMADRVDSLQKTINIAMVGKYTGLTDSYLSVIKALQHSAFKVGAKMEISWVEAASLEakfe 320
Cdd:TIGR00337 261 CRRLNLNCDEAD--LSEWEQLVEKFANPKHEVTIGIVGKYVELKDAYLSVIEALKHAGAKLDTKVNIKWIDSEDLE---- 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513425 321 eknakkyAESWAALKAAHGVLVPGGFGIRGIEGKILAAQYARENGVPYLGVCLGLQVAVIEFARNVLGLEGANSTEFDDK 400
Cdd:TIGR00337 335 -------EEGVEFLKGLDGILVPGGFGERGVEGKILAIKYARENNIPFLGICLGMQLAVIEFARNVAGLEGANSTEFDPD 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513425 401 TPHPTVIFMPE-GSKTHMGATMRLGSRQTNLhTEDCHAFRLYgGAKKIHERHRHRYEVNPDMIADLEAAGLRFVGKDTEA 479
Cdd:TIGR00337 408 TKYPVVDLLPEqKDISDLGGTMRLGLYPCIL-KPGTLAFKLY-GKEEVYERHRHRYEVNNEYREQIENKGLIVSGTSPDG 485
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 663513425 480 QRMEIIELADHPYYFGTQYHPEFKSRPNRPSPPFLGLVEA 519
Cdd:TIGR00337 486 RLVEIIELPDHPFFVACQFHPEFTSRPNDPHPLFLGFVKA 525
|
|
| CTP_synth_N |
pfam06418 |
CTP synthase N-terminus; This family consists of the N-terminal region of the CTP synthase ... |
1-246 |
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: 509.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513425 1 MKSIGYRVSAIKIDPYLNIDAGTMSPFEHGEVFVLDDGGEVDLDLGNYERFLDVTLTRDNNLTTGKVYSAVIEAERRGDY 80
Cdd:pfam06418 26 LKSRGLKVTIIKIDPYLNVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFLDINLTKDNNITTGKIYQSVIEKERRGDY 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513425 81 LGKTVQVVPHITNEIQNWMERVAAIpvdgngAEPDICIVELGGTVGDIESAPFVEALRQFQFRVGKENFVLVHVSLVPVI 160
Cdd:pfam06418 106 LGKTVQVIPHITDEIKERIRRVAKE------VGPDVVIVEIGGTVGDIESLPFLEAIRQLRLEVGRENVLFIHVTLVPYL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513425 161 GVVGEQKTKPTQHTVKELRAAGLSPDFLVCRAEEPLLPATKDKLALFCHVEPSHVLSAHDVSNIYRVPLMLNEQGVTEMI 240
Cdd:pfam06418 180 KAAGELKTKPTQHSVKELRSIGIQPDIIVCRSERPLDEEVKEKIALFCNVPKEAVISAPDVSSIYEVPLLLEEQGLDDII 259
|
....*.
gi 663513425 241 AEKLNL 246
Cdd:pfam06418 260 LKRLNL 265
|
|
| CTPS_N |
cd03113 |
N-terminal domain of cytidine 5'-triphosphate synthase; Cytidine 5'-triphosphate synthase ... |
1-242 |
1.66e-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: 492.00 E-value: 1.66e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513425 1 MKSIGYRVSAIKIDPYLNIDAGTMSPFEHGEVFVLDDGGEVDLDLGNYERFLDVTLTRDNNLTTGKVYSAVIEAERRGDY 80
Cdd:cd03113 26 LKSRGLRVTAIKIDPYLNVDAGTMSPYEHGEVFVLDDGGETDLDLGNYERFLDVNLTRDNNITTGKIYSEVIEKERRGDY 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513425 81 LGKTVQVVPHITNEIQNWMERVAAIPvdgngaEPDICIVELGGTVGDIESAPFVEALRQFQFRVGKENFVLVHVSLVPVI 160
Cdd:cd03113 106 LGKTVQVIPHITDEIKERIRRVAKIP------EPDVCIVEIGGTVGDIESLPFLEALRQFQFEVGRENFLFIHVTLVPYL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513425 161 GVVGEQKTKPTQHTVKELRAAGLSPDFLVCRAEEPLLPATKDKLALFCHVEPSHVLSAHDVSNIYRVPLMLNEQGVTEMI 240
Cdd:cd03113 180 EATGEQKTKPTQHSVKELRSLGIQPDIIVCRSEKPLDEETKEKIALFCNVPPEAVISVHDVSSIYEVPLLLEKQGLDDYI 259
|
..
gi 663513425 241 AE 242
Cdd:cd03113 260 LR 261
|
|
| GATase1_CTP_Synthase |
cd01746 |
Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase; ... |
272-517 |
2.67e-136 |
|
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: 393.84 E-value: 2.67e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513425 272 INIAMVGKYTGLTDSYLSVIKALQHSAFKVGAKMEISWVEAASLEAKfeeknakkyaESWAALKAAHGVLVPGGFGIRGI 351
Cdd:cd01746 1 VRIALVGKYVELPDAYLSVLEALKHAGIALGVKLEIKWIDSEDLEEE----------NAEEALKGADGILVPGGFGIRGV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513425 352 EGKILAAQYARENGVPYLGVCLGLQVAVIEFARNVLGLEGANSTEFDDKTPHPTVIFMPEG-SKTHMGATMRLGSRQTNL 430
Cdd:cd01746 71 EGKILAIKYARENNIPFLGICLGMQLAVIEFARNVLGLPDANSTEFDPDTPHPVVDLMPEQkGVKDLGGTMRLGAYPVIL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513425 431 HTEDChaFRLYGGAKKIHERHRHRYEVNPDMIADLEAAGLRFVGKDTEAQRMEIIELADHPYYFGTQYHPEFKSRPNRPS 510
Cdd:cd01746 151 KPGTL--AHKYYGKDEVEERHRHRYEVNPEYVDELEEAGLRFSGTDPDGGLVEIVELPDHPFFVGTQFHPEFKSRPLKPH 228
|
....*..
gi 663513425 511 PPFLGLV 517
Cdd:cd01746 229 PLFVGFV 235
|
|
| GATase |
pfam00117 |
Glutamine amidotransferase class-I; |
283-519 |
2.49e-40 |
|
Glutamine amidotransferase class-I;
Pssm-ID: 395067 [Multi-domain] Cd Length: 188 Bit Score: 143.92 E-value: 2.49e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513425 283 LTDSYLSVIKALQHSAFKVGAKMEISWVEAASLEAKFEEknakkyaeswaalkaAHGVLVPGGFGIRGI-EGKILAAQYA 361
Cdd:pfam00117 2 LIDNGDSFTYNLARALRELGVEVTVVPNDTPAEEILEEN---------------PDGIILSGGPGSPGAaGGAIEAIREA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513425 362 RENGVPYLGVCLGLQVAVIEFARNVLgleganstefddktphptvifmPEGSKTHMGATMRLGSRQTNLhtedchafrLY 441
Cdd:pfam00117 67 RELKIPILGICLGHQLLALAFGGKVV----------------------KAKKFGHHGKNSPVGDDGCGL---------FY 115
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 663513425 442 GGAKKIHERHRHRYEVNPdmiaDLEAAGLRFVGKDTEA-QRMEIIELaDHPyYFGTQYHPEFKSRPNRPSPPFLGLVEA 519
Cdd:pfam00117 116 GLPNVFIVRRYHSYAVDP----DTLPDGLEVTATSENDgTIMGIRHK-KLP-IFGVQFHPESILTPHGPEILFNFFIKA 188
|
|
| PRK06186 |
PRK06186 |
hypothetical protein; Validated |
271-520 |
2.26e-32 |
|
hypothetical protein; Validated
Pssm-ID: 180452 [Multi-domain] Cd Length: 229 Bit Score: 123.92 E-value: 2.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513425 271 TINIAMVGKYTGLTDSYLSVIKALQHSAFKVGAKMEISWVEAASLEAKfeeknakkyaeswAALKAAHGV-LVPGGfGIR 349
Cdd:PRK06186 1 TLRIALVGDYNPDVTAHQAIPLALDLAAAVLGLPVDYEWLPTPEITDP-------------EDLAGFDGIwCVPGS-PYR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513425 350 GIEGKILAAQYARENGVPYLGVCLGLQVAVIEFARNVLGLEGANSTEFDDKTPHPtVIfmpegskTHMGATMRlGSRQTN 429
Cdd:PRK06186 67 NDDGALTAIRFARENGIPFLGTCGGFQHALLEYARNVLGWADAAHAETDPEGDRP-VI-------APLSCSLV-EKTGDI 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513425 430 LHTEDCHAFRLYgGAKKIHERHRHRYEVNPDMIADLEAAGLRFVGKDtEAQRMEIIELADHPYYFGTQYHPEFKSRPNRP 509
Cdd:PRK06186 138 RLRPGSLIARAY-GTLEIEEGYHCRYGVNPEFVAALESGDLRVTGWD-EDGDVRAVELPGHPFFVATLFQPERAALAGRP 215
|
250
....*....|.
gi 663513425 510 SPPFLGLVEAA 520
Cdd:PRK06186 216 PPLVRAFLRAA 226
|
|
| GATase1 |
cd01653 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
274-380 |
2.24e-07 |
|
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: 49.52 E-value: 2.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513425 274 IAMVGKYTGLTDSYLSVIKALQHSAFkvgakmEISWVEAASLEAkfeeknakkyaESWAALKAAHGVLVPGGFG----IR 349
Cdd:cd01653 1 VAVLLFPGFEELELASPLDALREAGA------EVDVVSPDGGPV-----------ESDVDLDDYDGLILPGGPGtpddLA 63
|
90 100 110
....*....|....*....|....*....|.
gi 663513425 350 GIEGKILAAQYARENGVPYLGVCLGLQVAVI 380
Cdd:cd01653 64 RDEALLALLREAAAAGKPILGICLGAQLLVL 94
|
|
| GAT_1 |
cd03128 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
274-377 |
2.11e-06 |
|
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: 46.04 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513425 274 IAMVGKYTGLTDSYLSVIKALQHSAFkvgakmEISWVeaasleakfeeKNAKKYAESWAALKAAHGVLVPGGFG----IR 349
Cdd:cd03128 1 VAVLLFGGSEELELASPLDALREAGA------EVDVV-----------SPDGGPVESDVDLDDYDGLILPGGPGtpddLA 63
|
90 100
....*....|....*....|....*...
gi 663513425 350 GIEGKILAAQYARENGVPYLGVCLGLQV 377
Cdd:cd03128 64 WDEALLALLREAAAAGKPVLGICLGAQL 91
|
|
| hisH |
PRK13143 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
289-377 |
3.69e-03 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 237289 [Multi-domain] Cd Length: 200 Bit Score: 38.70 E-value: 3.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513425 289 SVIKALQHsafkVGAKMEISwveaasleakfeeKNAKkyaeswaALKAAHGVLVPG--GFG-----IRGIEGKILAAqya 361
Cdd:PRK13143 15 SVSKALER----AGAEVVIT-------------SDPE-------EILDADGIVLPGvgAFGaamenLSPLRDVILEA--- 67
|
90
....*....|....*.
gi 663513425 362 RENGVPYLGVCLGLQV 377
Cdd:PRK13143 68 ARSGKPFLGICLGMQL 83
|
|
| |
