|
Name |
Accession |
Description |
Interval |
E-value |
| pyrG |
PRK05380 |
CTP synthetase; Validated |
1-546 |
0e+00 |
|
CTP synthetase; Validated
Pssm-ID: 235437 [Multi-domain] Cd Length: 533 Bit Score: 1072.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910291 1 MTKYVFVTGGVVSSLGKGIAAASLAAILESRGLQVTLLKLDPYINVDPGTMSPFQHGEVFVTEDGAETDLDLGHYERFIS 80
Cdd:PRK05380 1 MTKYIFVTGGVVSSLGKGITAASLGRLLKARGLKVTIQKLDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910291 81 ARMRKVNNFTTGQIYESVLRKERRGDYLGKTVQVIPHITNEIQDFVARGAEAAwngatDVAIVEIGGTVGDIESLPFLEA 160
Cdd:PRK05380 81 TNLTKYNNVTTGKIYSSVIEKERRGDYLGKTVQVIPHITDEIKERILAAGTDA-----DVVIVEIGGTVGDIESLPFLEA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910291 161 ARQMSLRMGRNNAAFVHLTLVPYIASAGELKTKPTQHSVQKLREIGIYPNVLLCRADRRIPDDERAKISMFSNVPLDAVI 240
Cdd:PRK05380 156 IRQLRLELGRENVLFIHLTLVPYIAAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEEKRKIALFCNVPEEAVI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910291 241 SVWDVDSIYKIPAMLHKQGVDNIVCEALGLTPPPADLSMWDNLVDALEHPQDSVTIGMVGKYVDLTESYKSLSEALVHAG 320
Cdd:PRK05380 236 SAPDVDSIYEVPLLLHEQGLDDIVLERLGLEAPEPDLSEWEELVERLKNPKGEVTIALVGKYVELPDAYKSVIEALKHAG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910291 321 IHTRSKVNIEYIDSEDIETRG-TDQLKHLDAILVPGGFGKRGTEGKIAAIRYARENGVPYLGICLGMQLAVIEFARHVAG 399
Cdd:PRK05380 316 IANDVKVNIKWIDSEDLEEENvAELLKGVDGILVPGGFGERGIEGKILAIRYARENNIPFLGICLGMQLAVIEFARNVLG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910291 400 LGGANSTEFDPAAPHPVVALITEWMDRegrverrdnsSDLGGTMRKGAQRCPIRPGTRAQSIYGDD-VNERHRHRYEVNN 478
Cdd:PRK05380 396 LEDANSTEFDPDTPHPVIDLMPEQKDV----------SDLGGTMRLGAYPCKLKPGTLAAEIYGKEeIYERHRHRYEVNN 465
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489910291 479 VYVPRLEDAGMVISARTPTENLPEMMELPSHPWFVGVQFHPEFTSTPRDGHPLFSSYIRAALEHKAQR 546
Cdd:PRK05380 466 KYREQLEKAGLVFSGTSPDGRLVEIVELPDHPWFVGVQFHPEFKSRPRRPHPLFAGFVKAALENKKRK 533
|
|
| PyrG |
COG0504 |
CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase ... |
2-547 |
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: 1058.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910291 2 TKYVFVTGGVVSSLGKGIAAASLAAILESRGLQVTLLKLDPYINVDPGTMSPFQHGEVFVTEDGAETDLDLGHYERFISA 81
Cdd:COG0504 1 TKYIFVTGGVVSSLGKGITAASLGRLLKARGLKVTIQKLDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFLDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910291 82 RMRKVNNFTTGQIYESVLRKERRGDYLGKTVQVIPHITNEIQDFVARGAEaawNGATDVAIVEIGGTVGDIESLPFLEAA 161
Cdd:COG0504 81 NLSKANNVTTGQIYSSVIEKERRGDYLGKTVQVIPHITDEIKRRIRRAAE---ESGADVVIVEIGGTVGDIESLPFLEAI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910291 162 RQMSLRMGRNNAAFVHLTLVPYIASAGELKTKPTQHSVQKLREIGIYPNVLLCRADRRIPDDERAKISMFSNVPLDAVIS 241
Cdd:COG0504 158 RQLRLELGRENVLFIHVTLVPYIAAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEIKRKIALFCNVPEEAVIS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910291 242 VWDVDSIYKIPAMLHKQGVDNIVCEALGLTPPPADLSMWDNLVDALEHPQDSVTIGMVGKYVDLTESYKSLSEALVHAGI 321
Cdd:COG0504 238 APDVDSIYEVPLMLHEQGLDEIVLKKLGLEAREPDLSEWEELVERIKNPKKEVTIALVGKYVELPDAYKSVVEALKHAGI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910291 322 HTRSKVNIEYIDSEDIETRGTD-QLKHLDAILVPGGFGKRGTEGKIAAIRYARENGVPYLGICLGMQLAVIEFARHVAGL 400
Cdd:COG0504 318 ANGVKVNIKWIDSEDLEEENAEeLLKGVDGILVPGGFGERGIEGKIAAIRYARENKIPFLGICLGMQLAVIEFARNVLGL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910291 401 GGANSTEFDPAAPHPVVALITEwmdregrverRDNSSDLGGTMRKGAQRCPIRPGTRAQSIYGDD-VNERHRHRYEVNNV 479
Cdd:COG0504 398 EDANSTEFDPNTPHPVIDLMPE----------QKDVSDLGGTMRLGAYPCKLKPGTLAAEAYGKEeISERHRHRYEFNNE 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489910291 480 YVPRLEDAGMVISARTPTENLPEMMELPSHPWFVGVQFHPEFTSTPRDGHPLFSSYIRAALEHKAQRA 547
Cdd:COG0504 468 YREQLEKAGLVFSGTSPDGRLVEIVELPDHPWFVGVQFHPEFKSRPNRPHPLFRGFVKAALEYKKKKK 535
|
|
| PyrG |
TIGR00337 |
CTP synthase; CTP synthase is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. ... |
2-538 |
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: 851.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910291 2 TKYVFVTGGVVSSLGKGIAAASLAAILESRGLQVTLLKLDPYINVDPGTMSPFQHGEVFVTEDGAETDLDLGHYERFISA 81
Cdd:TIGR00337 1 MKYIFVTGGVVSSLGKGITAASLGRLLKARGLNVTIIKIDPYINIDPGTMSPLQHGEVFVTDDGAETDLDLGHYERFLDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910291 82 RMRKVNNFTTGQIYESVLRKERRGDYLGKTVQVIPHITNEIQDFVARGAEaawNGATDVAIVEIGGTVGDIESLPFLEAA 161
Cdd:TIGR00337 81 NLTRDNNITTGKIYSSVIEKERKGDYLGKTVQIIPHITNEIKDRILRVAK---ISGPDVVIVEIGGTVGDIESLPFLEAI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910291 162 RQMSLRMGRNNAAFVHLTLVPYIASAGELKTKPTQHSVQKLREIGIYPNVLLCRADRRIPDDERAKISMFSNVPLDAVIS 241
Cdd:TIGR00337 158 RQFRVEVGRENVLFIHVTLVPYIAAAGEQKTKPTQHSVKELRSLGIQPDIIICRSSRPLDPNTKDKIALFCDVEEEAVIS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910291 242 VWDVDSIYKIPAMLHKQGVDNIVCEALGLTPPPADLSMWDNLVDALEHPQDSVTIGMVGKYVDLTESYKSLSEALVHAGI 321
Cdd:TIGR00337 238 AKDVSSIYEVPLLLLKQGLDDYLCRRLNLNCDEADLSEWEQLVEKFANPKHEVTIGIVGKYVELKDAYLSVIEALKHAGA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910291 322 HTRSKVNIEYIDSEDIETRGTDQLKHLDAILVPGGFGKRGTEGKIAAIRYARENGVPYLGICLGMQLAVIEFARHVAGLG 401
Cdd:TIGR00337 318 KLDTKVNIKWIDSEDLEEEGVEFLKGLDGILVPGGFGERGVEGKILAIKYARENNIPFLGICLGMQLAVIEFARNVAGLE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910291 402 GANSTEFDPAAPHPVVALITEWMDREgrverrdnssDLGGTMRKGAQRCPIRPGTRAQSIYGDD-VNERHRHRYEVNNVY 480
Cdd:TIGR00337 398 GANSTEFDPDTKYPVVDLLPEQKDIS----------DLGGTMRLGLYPCILKPGTLAFKLYGKEeVYERHRHRYEVNNEY 467
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 489910291 481 VPRLEDAGMVISARTPTENLPEMMELPSHPWFVGVQFHPEFTSTPRDGHPLFSSYIRA 538
Cdd:TIGR00337 468 REQIENKGLIVSGTSPDGRLVEIIELPDHPFFVACQFHPEFTSRPNDPHPLFLGFVKA 525
|
|
| PLN02327 |
PLN02327 |
CTP synthase |
2-539 |
0e+00 |
|
CTP synthase
Pssm-ID: 215186 [Multi-domain] Cd Length: 557 Bit Score: 655.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910291 2 TKYVFVTGGVVSSLGKGIAAASLAAILESRGLQVTLLKLDPYINVDPGTMSPFQHGEVFVTEDGAETDLDLGHYERFISA 81
Cdd:PLN02327 1 MKYVLVTGGVVSGLGKGVTASSIGVLLKACGLRVTSIKIDPYLNTDAGTMSPFEHGEVFVLDDGGEVDLDLGNYERFLDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910291 82 RMRKVNNFTTGQIYESVLRKERRGDYLGKTVQVIPHITNEIQDFVARGAEAAWNGAT---DVAIVEIGGTVGDIESLPFL 158
Cdd:PLN02327 81 TLTRDNNITTGKIYQSVIEKERRGDYLGKTVQVVPHITDAIQEWIERVAKIPVDGKEgpaDVCVIELGGTVGDIESMPFI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910291 159 EAARQMSLRMGRNNAAFVHLTLVPYIASAGELKTKPTQHSVQKLREIGIYPNVLLCRADRRIPDDERAKISMFSNVPLDA 238
Cdd:PLN02327 161 EALRQFSFRVGPGNFCLIHVSLVPVLGVVGEQKTKPTQHSVRGLRALGLTPHILACRSTKPLEENVKEKLSQFCHVPAEN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910291 239 VISVWDVDSIYKIPAMLHKQGVDNIVCEALGL--TPPPADLSMWDNLVDALEHPQDSVTIGMVGKYVDLTESYKSLSEAL 316
Cdd:PLN02327 241 ILNLHDVSNIWHVPLLLRDQKAHEAILKVLNLlsVAREPDLEEWTARAESCDNLTEPVRIAMVGKYTGLSDSYLSVLKAL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910291 317 VHAGIHTRSKVNIEYIDSEDIETRGT-----------DQLKHLDAILVPGGFGKRGTEGKIAAIRYARENGVPYLGICLG 385
Cdd:PLN02327 321 LHASVACSRKLVIDWVAASDLEDETAketpdayaaawKLLKGADGILVPGGFGDRGVEGKILAAKYARENKVPYLGICLG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910291 386 MQLAVIEFARHVAGLGGANSTEFDPAAPHPVVALITEwMDREGrverrdnssdLGGTMRKGAQRCPIR-PGTRAQSIYGD 464
Cdd:PLN02327 401 MQIAVIEFARSVLGLKDANSTEFDPETPNPCVIFMPE-GSKTH----------MGGTMRLGSRRTYFQtPDCKSAKLYGN 469
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489910291 465 D--VNERHRHRYEVNNVYVPRLEDAGMVISARTPTENLPEMMELPSHPWFVGVQFHPEFTSTPRDGHPLFSSYIRAA 539
Cdd:PLN02327 470 VsfVDERHRHRYEVNPEMVPRLEKAGLSFVGKDETGRRMEIVELPSHPFFVGVQFHPEFKSRPGKPSPLFLGLIAAA 546
|
|
| CTP_synth_N |
pfam06418 |
CTP synthase N-terminus; This family consists of the N-terminal region of the CTP synthase ... |
3-270 |
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: 519.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910291 3 KYVFVTGGVVSSLGKGIAAASLAAILESRGLQVTLLKLDPYINVDPGTMSPFQHGEVFVTEDGAETDLDLGHYERFISAR 82
Cdd:pfam06418 1 KYIFVTGGVVSGLGKGITAASLGRLLKSRGLKVTIIKIDPYLNVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFLDIN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910291 83 MRKVNNFTTGQIYESVLRKERRGDYLGKTVQVIPHITNEIQDFVARGAEaawNGATDVAIVEIGGTVGDIESLPFLEAAR 162
Cdd:pfam06418 81 LTKDNNITTGKIYQSVIEKERRGDYLGKTVQVIPHITDEIKERIRRVAK---EVGPDVVIVEIGGTVGDIESLPFLEAIR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910291 163 QMSLRMGRNNAAFVHLTLVPYIASAGELKTKPTQHSVQKLREIGIYPNVLLCRADRRIPDDERAKISMFSNVPLDAVISV 242
Cdd:pfam06418 158 QLRLEVGRENVLFIHVTLVPYLKAAGELKTKPTQHSVKELRSIGIQPDIIVCRSERPLDEEVKEKIALFCNVPKEAVISA 237
|
250 260
....*....|....*....|....*...
gi 489910291 243 WDVDSIYKIPAMLHKQGVDNIVCEALGL 270
Cdd:pfam06418 238 PDVSSIYEVPLLLEEQGLDDIILKRLNL 265
|
|
| CTPS_N |
cd03113 |
N-terminal domain of cytidine 5'-triphosphate synthase; Cytidine 5'-triphosphate synthase ... |
3-266 |
3.67e-164 |
|
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: 466.58 E-value: 3.67e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910291 3 KYVFVTGGVVSSLGKGIAAASLAAILESRGLQVTLLKLDPYINVDPGTMSPFQHGEVFVTEDGAETDLDLGHYERFISAR 82
Cdd:cd03113 1 KYIFVTGGVVSGLGKGITASSIGRLLKSRGLRVTAIKIDPYLNVDAGTMSPYEHGEVFVLDDGGETDLDLGNYERFLDVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910291 83 MRKVNNFTTGQIYESVLRKERRGDYLGKTVQVIPHITNEIQDFVARGAEaawNGATDVAIVEIGGTVGDIESLPFLEAAR 162
Cdd:cd03113 81 LTRDNNITTGKIYSEVIEKERRGDYLGKTVQVIPHITDEIKERIRRVAK---IPEPDVCIVEIGGTVGDIESLPFLEALR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910291 163 QMSLRMGRNNAAFVHLTLVPYIASAGELKTKPTQHSVQKLREIGIYPNVLLCRADRRIPDDERAKISMFSNVPLDAVISV 242
Cdd:cd03113 158 QFQFEVGRENFLFIHVTLVPYLEATGEQKTKPTQHSVKELRSLGIQPDIIVCRSEKPLDEETKEKIALFCNVPPEAVISV 237
|
250 260
....*....|....*....|....
gi 489910291 243 WDVDSIYKIPAMLHKQGVDNIVCE 266
Cdd:cd03113 238 HDVSSIYEVPLLLEKQGLDDYILR 261
|
|
| GATase1_CTP_Synthase |
cd01746 |
Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase; ... |
294-536 |
5.92e-132 |
|
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: 383.83 E-value: 5.92e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910291 294 VTIGMVGKYVDLTESYKSLSEALVHAGIHTRSKVNIEYIDSEDIETRGTDQ-LKHLDAILVPGGFGKRGTEGKIAAIRYA 372
Cdd:cd01746 1 VRIALVGKYVELPDAYLSVLEALKHAGIALGVKLEIKWIDSEDLEEENAEEaLKGADGILVPGGFGIRGVEGKILAIKYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910291 373 RENGVPYLGICLGMQLAVIEFARHVAGLGGANSTEFDPAAPHPVVALITEWmdregrverrDNSSDLGGTMRKGAQRCPI 452
Cdd:cd01746 81 RENNIPFLGICLGMQLAVIEFARNVLGLPDANSTEFDPDTPHPVVDLMPEQ----------KGVKDLGGTMRLGAYPVIL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910291 453 RPGTRAQSIYGDD-VNERHRHRYEVNNVYVPRLEDAGMVISARTPTENLPEMMELPSHPWFVGVQFHPEFTSTPRDGHPL 531
Cdd:cd01746 151 KPGTLAHKYYGKDeVEERHRHRYEVNPEYVDELEEAGLRFSGTDPDGGLVEIVELPDHPFFVGTQFHPEFKSRPLKPHPL 230
|
....*
gi 489910291 532 FSSYI 536
Cdd:cd01746 231 FVGFV 235
|
|
| GATase |
pfam00117 |
Glutamine amidotransferase class-I; |
305-538 |
1.46e-41 |
|
Glutamine amidotransferase class-I;
Pssm-ID: 395067 [Multi-domain] Cd Length: 188 Bit Score: 147.77 E-value: 1.46e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910291 305 LTESYKSLSEALVHAGIHTRSKVNIEYIDSEDIETRGTDqlkhLDAILVPGGFGKRGT-EGKIAAIRYARENGVPYLGIC 383
Cdd:pfam00117 2 LIDNGDSFTYNLARALRELGVEVTVVPNDTPAEEILEEN----PDGIILSGGPGSPGAaGGAIEAIREARELKIPILGIC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910291 384 LGMQLAVIEFArhvaglgganstefdpaaphpvvalitewmdreGRVERRDNSSDLGGTMRKGAQRCPIRPGTraqsiyG 463
Cdd:pfam00117 78 LGHQLLALAFG---------------------------------GKVVKAKKFGHHGKNSPVGDDGCGLFYGL------P 118
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489910291 464 DDVNERHRHRYEVNNVYVPrledAGMVISARTPTENLPEMMELPSHPWFvGVQFHPEFTSTPRDGHPLFSSYIRA 538
Cdd:pfam00117 119 NVFIVRRYHSYAVDPDTLP----DGLEVTATSENDGTIMGIRHKKLPIF-GVQFHPESILTPHGPEILFNFFIKA 188
|
|
| PRK06186 |
PRK06186 |
hypothetical protein; Validated |
296-542 |
8.81e-39 |
|
hypothetical protein; Validated
Pssm-ID: 180452 [Multi-domain] Cd Length: 229 Bit Score: 141.64 E-value: 8.81e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910291 296 IGMVGKYVDLTESYKSLSEALVHAGIHTRSKVNIEYIDSEDIetRGTDQLKHLDAI-LVPGGfGKRGTEGKIAAIRYARE 374
Cdd:PRK06186 4 IALVGDYNPDVTAHQAIPLALDLAAAVLGLPVDYEWLPTPEI--TDPEDLAGFDGIwCVPGS-PYRNDDGALTAIRFARE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910291 375 NGVPYLGICLGMQLAVIEFARHVAGLGGANSTEFDPAAPHPVVA-LITEWMDREGRVErrdnssdlggtmrkgaqrcpIR 453
Cdd:PRK06186 81 NGIPFLGTCGGFQHALLEYARNVLGWADAAHAETDPEGDRPVIApLSCSLVEKTGDIR--------------------LR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910291 454 PGTRAQSIYG-DDVNERHRHRYEVNNVYVPRLEDAGMVISARTPtENLPEMMELPSHPWFVGVQFHPEFTSTPRDGHPLF 532
Cdd:PRK06186 141 PGSLIARAYGtLEIEEGYHCRYGVNPEFVAALESGDLRVTGWDE-DGDVRAVELPGHPFFVATLFQPERAALAGRPPPLV 219
|
250
....*....|
gi 489910291 533 SSYIRAALEH 542
Cdd:PRK06186 220 RAFLRAARAA 229
|
|
| PuuD |
COG2071 |
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ... |
318-542 |
2.34e-16 |
|
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: 78.29 E-value: 2.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910291 318 HAGIHTRSKVNIEYIDS-----------------EDIEtrgtDQLKHLDAILVPGG-------FGKRGTEGK-------- 365
Cdd:COG2071 7 TAGGYPAHYLPEDYVRAvraagglpvllppvgdeEDLD----ELLDRLDGLVLTGGadvdpalYGEEPHPELgpidperd 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910291 366 ---IAAIRYARENGVPYLGICLGMQLAViefarhVAgLGG----ANSTEFDPAAPHpvvalitewmdregrveRRDNSSD 438
Cdd:COG2071 83 afeLALIRAALERGKPVLGICRGMQLLN------VA-LGGtlyqDLPDQVPGALDH-----------------RQPAPRY 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910291 439 LGgtmRKGAQrcpIRPGTRAQSIYGDDvnerhrhRYEVNNVY---VPRLEDaGMVISARTPtENLPEMMELPSHPWFVGV 515
Cdd:COG2071 139 AP---RHTVE---IEPGSRLARILGEE-------EIRVNSLHhqaVKRLGP-GLRVSARAP-DGVIEAIESPGAPFVLGV 203
|
250 260
....*....|....*....|....*...
gi 489910291 516 QFHPEF-TSTPRDGHPLFSSYIRAALEH 542
Cdd:COG2071 204 QWHPEWlAASDPLSRRLFEAFVEAARAR 231
|
|
| GATase1 |
cd01653 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
296-404 |
1.78e-15 |
|
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: 72.63 E-value: 1.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910291 296 IGMVGKYVDLTESYKSLSEALVHAGihtrskVNIEYIDSEDIETRGTDQLKHLDAILVPGGFG----KRGTEGKIAAIRY 371
Cdd:cd01653 1 VAVLLFPGFEELELASPLDALREAG------AEVDVVSPDGGPVESDVDLDDYDGLILPGGPGtpddLARDEALLALLRE 74
|
90 100 110
....*....|....*....|....*....|...
gi 489910291 372 ARENGVPYLGICLGMQLAVIEFARHVAGLGGAN 404
Cdd:cd01653 75 AAAAGKPILGICLGAQLLVLGVQFHPEAIDGAE 107
|
|
| GAT_1 |
cd03128 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
296-388 |
3.28e-13 |
|
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: 65.30 E-value: 3.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910291 296 IGMVGKYVDLTESYKSLSEALVHAGihtrskVNIEYIDSEDIETRGTDQLKHLDAILVPGGFG----KRGTEGKIAAIRY 371
Cdd:cd03128 1 VAVLLFGGSEELELASPLDALREAG------AEVDVVSPDGGPVESDVDLDDYDGLILPGGPGtpddLAWDEALLALLRE 74
|
90
....*....|....*..
gi 489910291 372 ARENGVPYLGICLGMQL 388
Cdd:cd03128 75 AAAAGKPVLGICLGAQL 91
|
|
| Peptidase_C26 |
pfam07722 |
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ... |
333-520 |
8.15e-12 |
|
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: 64.97 E-value: 8.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910291 333 DSEDIETrgtdQLKHLDAILVPGG-------FGKRGTEG-----------KIAAIRYARENGVPYLGICLGMQLAViefa 394
Cdd:pfam07722 48 DPEDAAA----ILDRLDGLLLTGGpnvdphfYGEEPSESggpydpardayELALIRAALARGKPILGICRGFQLLN---- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910291 395 rhVAgLGGanSTefdpaapHPVVALITEWMD-REGRVERRDNssdlggtmrkGAQRCPIRPGTRAQSIYGD---DVNERH 470
Cdd:pfam07722 120 --VA-LGG--TL-------YQDIQEQPGFTDhREHCQVAPYA----------PSHAVNVEPGSLLASLLGSeefRVNSLH 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489910291 471 RHRyevnnvyVPRLeDAGMVISARTPtENLPEMMELPSHPWFV-GVQFHPE 520
Cdd:pfam07722 178 HQA-------IDRL-APGLRVEAVAP-DGTIEAIESPNAKGFAlGVQWHPE 219
|
|
| GuaA1 |
COG0518 |
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ... |
366-524 |
3.81e-08 |
|
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: 54.18 E-value: 3.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910291 366 IAAIRYARENGVPYLGICLGMQLAviefARHvagLGGAnstefdpAAPHPVvalitewmdRE---GRVERRDNSSDLGGt 442
Cdd:COG0518 72 PALIREAFELGKPVLGICYGAQLL----AHA---LGGK-------VEPGPG---------REigwAPVELTEADPLFAG- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910291 443 mrkgaqrcpIRPGTRAQsiygddvnerHRHRYEVnnVYVPrledAGMVISARTP-TENlpEMMELPSHpwFVGVQFHPEF 521
Cdd:COG0518 128 ---------LPDEFTVW----------MSHGDTV--TELP----EGAEVLASSDnCPN--QAFRYGRR--VYGVQFHPEV 178
|
...
gi 489910291 522 TST 524
Cdd:COG0518 179 THT 181
|
|
| GATase1_2 |
cd01745 |
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ... |
333-521 |
1.80e-07 |
|
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group contains a subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain. GATase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. Glutamine amidotransferases (GATase) includes the triad family of amidotransferases which have a conserved Cys-His-Glu catalytic triad in the glutaminase active site. In this subgroup this triad is conserved. GATase activity can be found in a range of biosynthetic enzymes, including: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase , anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. Glutamine amidotransferase (GATase) domains can occur either as single polypeptides, as in glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.
Pssm-ID: 153216 [Multi-domain] Cd Length: 189 Bit Score: 51.42 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910291 333 DSEDIEtrgtDQLKHLDAILVPGG--------FGKRGTEGK----------IAAIRYARENGVPYLGICLGMQ-LAVIef 393
Cdd:cd01745 43 DEEDLE----QYLELLDGLLLTGGgdvdpplyGEEPHPELGpidperdafeLALLRAALERGKPILGICRGMQlLNVA-- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910291 394 arhvaglgganstefdpaaphpvvalitewmdregrverrdnssdLGGTMRkgaqrcpirpgtraQSIYgddVNErhRHR 473
Cdd:cd01745 117 ---------------------------------------------LGGTLY--------------QDIR---VNS--LHH 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489910291 474 YEVNnvyvpRLEDaGMVISARTPtENLPEMMELPSHPWFVGVQFHPEF 521
Cdd:cd01745 133 QAIK-----RLAD-GLRVEARAP-DGVIEAIESPDRPFVLGVQWHPEW 173
|
|
| guaA_Nterm |
TIGR00888 |
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ... |
343-537 |
8.55e-06 |
|
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine de novo biosynthesis is well-conserved. However, it appears to split into two separate polypeptide chains in most of the Archaea. This N-terminal region would be the smaller subunit. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 129966 [Multi-domain] Cd Length: 188 Bit Score: 46.54 E-value: 8.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910291 343 DQLKHLD--AILVPGGFGKRGTEGKIAAIRYARENGVPYLGICLGMQLAVIEFARHVaglGGANSTEFDPAaphpvvali 420
Cdd:TIGR00888 35 EEIREKNpkGIILSGGPSSVYAENAPRADEKIFELGVPVLGICYGMQLMAKQLGGEV---GRAEKREYGKA--------- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910291 421 tewmdregRVERRDNSSDLGGTMRKgaqrcpirpgtraQSIY---GDDVNErhrhryevnnvyVPRledaGMVISARTPt 497
Cdd:TIGR00888 103 --------ELEILDEDDLFRGLPDE-------------STVWmshGDKVKE------------LPE----GFKVLATSD- 144
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489910291 498 eNLP-EMMELPSHPWFvGVQFHPEFTSTpRDGHPLFSSYIR 537
Cdd:TIGR00888 145 -NCPvAAMAHEEKPIY-GVQFHPEVTHT-EYGNELLENFVY 182
|
|
| GATase1_IGP_Synthase |
cd01748 |
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ... |
329-388 |
1.81e-05 |
|
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: 45.57 E-value: 1.81e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489910291 329 IEYIDSEDIETRGTDQLKHLDAILVPG-G-FG----KRGTEGKIAAIRYARENGVPYLGICLGMQL 388
Cdd:cd01748 18 LERLGAEVIITSDPEEILSADKLILPGvGaFGdamaNLRERGLIEALKEAIASGKPFLGICLGMQL 83
|
|
| hisH |
PRK13141 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
330-388 |
2.37e-05 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 237288 [Multi-domain] Cd Length: 205 Bit Score: 45.51 E-value: 2.37e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489910291 330 EYIDSEDIETRGTDQLKHLDAILVPG--GFG-------KRGTegkIAAIRYARENGVPYLGICLGMQL 388
Cdd:PRK13141 20 ERLGAEAVITSDPEEILAADGVILPGvgAFPdamanlrERGL---DEVIKEAVASGKPLLGICLGMQL 84
|
|
| IMP_synth_hisH |
TIGR01855 |
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model ... |
329-520 |
2.46e-05 |
|
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model represents the glutamine amidotransferase subunit (or domain, in eukaryotic systems) of imidazole glycerol phosphate synthase. This subunit catalyzes step 5 of histidine biosynthesis from PRPP. The other subunit, the cyclase, catalyzes step 6. [Amino acid biosynthesis, Histidine family]
Pssm-ID: 273836 [Multi-domain] Cd Length: 196 Bit Score: 45.39 E-value: 2.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910291 329 IEYIDSEDIETRGTDQLKHLDAILVPG--GFG---KRGTEGKIAAI-RYARENGVPYLGICLGMQLAvieFARhvaglgg 402
Cdd:TIGR01855 18 LKRVGAEPVVVKDSKEAELADKLILPGvgAFGaamARLRENGLDLFvELVVRLGKPVLGICLGMQLL---FER------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910291 403 anSTEFDpaaPHPVVALItewmdrEGRVER--RDNSSDLGGTMRKGAQRCPIRPGTRAQSIYgddvnerhrhrYEVNNVY 480
Cdd:TIGR01855 88 --SEEGG---GVPGLGLI------KGNVVKleARKVPHMGWNEVHPVKESPLLNGIDEGAYF-----------YFVHSYY 145
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489910291 481 VPRLEDAgmVISARTPTENLPEMMELPShpwFVGVQFHPE 520
Cdd:TIGR01855 146 AVCEEEA--VLAYADYGEKFPAAVQKGN---IFGTQFHPE 180
|
|
| hisH |
PRK13181 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
326-401 |
5.95e-05 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 183878 [Multi-domain] Cd Length: 199 Bit Score: 44.09 E-value: 5.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910291 326 KVNIEYIDSEDIEtrgtdQLKHLDAILVPG--GFGKrGTE-----GKIAAIRYARENGVPYLGICLGMQLavieFARH-- 396
Cdd:PRK13181 21 RLGVEAVVSSDPE-----EIAGADKVILPGvgAFGQ-AMRslresGLDEALKEHVEKKQPVLGICLGMQL----LFESse 90
|
....*...
gi 489910291 397 ---VAGLG 401
Cdd:PRK13181 91 egnVKGLG 98
|
|
| HisH |
COG0118 |
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ... |
310-388 |
1.67e-04 |
|
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: 42.72 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910291 310 KSLSEALVHAGIhtrsKVNIeyidsedieTRGTDQLKHLDAILVPG---------GFGKRGTegkIAAIRYARENGVPYL 380
Cdd:COG0118 14 RSVAKALERLGA----EVVV---------TSDPDEIRAADRLVLPGvgafgdameNLRERGL---DEAIREAVAGGKPVL 77
|
....*...
gi 489910291 381 GICLGMQL 388
Cdd:COG0118 78 GICLGMQL 85
|
|
| PRK13527 |
PRK13527 |
glutamine amidotransferase subunit PdxT; Provisional |
332-386 |
2.13e-04 |
|
glutamine amidotransferase subunit PdxT; Provisional
Pssm-ID: 237412 [Multi-domain] Cd Length: 200 Bit Score: 42.57 E-value: 2.13e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489910291 332 IDSEDIETRGTDQLKHLDAILVPGG-------FGKRgtEGKIAAIRYARENGVPYLGICLGM 386
Cdd:PRK13527 28 IDGEVVEVRRPGDLPDCDALIIPGGesttigrLMKR--EGILDEIKEKIEEGLPILGTCAGL 87
|
|
| hisH |
PRK13146 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
349-417 |
2.41e-04 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 237290 [Multi-domain] Cd Length: 209 Bit Score: 42.46 E-value: 2.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910291 349 DAILVPG---------GFGKRGteGKIAAIRYARENGVPYLGICLGMQL---AVIEFARHvAGLG--GANSTEFDPAAPH 414
Cdd:PRK13146 43 DRVVLPGvgafadcmrGLRAVG--LGEAVIEAVLAAGRPFLGICVGMQLlfeRGLEHGDT-PGLGliPGEVVRFQPDGPA 119
|
...
gi 489910291 415 PVV 417
Cdd:PRK13146 120 LKV 122
|
|
| puuD |
PRK11366 |
gamma-glutamyl-gamma-aminobutyrate hydrolase; Provisional |
345-546 |
3.28e-04 |
|
gamma-glutamyl-gamma-aminobutyrate hydrolase; Provisional
Pssm-ID: 183101 [Multi-domain] Cd Length: 254 Bit Score: 42.58 E-value: 3.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910291 345 LKHLDAILVPGG--------FGKRGTE-----GK----IAAIRYARENGVPYLGICLGMQLAViefarhVAGLGGANSTE 407
Cdd:PRK11366 59 LPKLDGIYLPGSpsnvqphlYGENGDEpdadpGRdllsMALINAALERRIPIFAICRGLQELV------VATGGSLHRKL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910291 408 FDPAAphpvvaLITEWMDREGRVERRDNSS-----DLGGTMRKGAQRCpirpgtraqsiygddvnerhrHRYEVNNVYV- 481
Cdd:PRK11366 133 CEQPE------LLEHREDPELPVEQQYAPShevqvEEGGLLSALLPEC---------------------SNFWVNSLHGq 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489910291 482 -PRLEDAGMVISARTPtENLPEMMELPSHPWFVGVQFHPEFTSTPRD-GHPLFSSYIRAALEHKAQR 546
Cdd:PRK11366 186 gAKVVSPRLRVEARSP-DGLVEAVSVINHPFALGVQWHPEWNSSEYAlSRILFEGFITACQHHIAEK 251
|
|
| PRK12564 |
PRK12564 |
carbamoyl-phosphate synthase small subunit; |
366-532 |
4.19e-04 |
|
carbamoyl-phosphate synthase small subunit;
Pssm-ID: 237139 [Multi-domain] Cd Length: 360 Bit Score: 42.75 E-value: 4.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910291 366 IAAIRYARENGVPYLGICLGMQLavieFARhvaGLG-----------GANstefdpaapHPVVALITewmdreGRVErrd 434
Cdd:PRK12564 238 IEMIRELLEKKIPIFGICLGHQL----LAL---ALGaktykmkfghrGAN---------HPVKDLET------GKVE--- 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910291 435 nssdlggtmrkgaqrcpIrpgTrAQsiygddvNerhrHRYEVNNVYVPrledAGMVISARTPTENLPEMMELPSHPWFvG 514
Cdd:PRK12564 293 -----------------I---T-SQ-------N----HGFAVDEDSLP----ANLEVTHVNLNDGTVEGLRHKDLPAF-S 335
|
170
....*....|....*...
gi 489910291 515 VQFHPEFTSTPRDGHPLF 532
Cdd:PRK12564 336 VQYHPEASPGPHDSAYLF 353
|
|
| CarA |
COG0505 |
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ... |
366-532 |
7.25e-04 |
|
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase small subunit is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 440271 [Multi-domain] Cd Length: 361 Bit Score: 41.93 E-value: 7.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910291 366 IAAIRYARENGVPYLGICLGMQLavieFARhvAgLG-----------GANstefdpaapHPVVALITewmdreGRVErrd 434
Cdd:COG0505 237 IETIRELLGKGIPIFGICLGHQL----LAL--A-LGaktyklkfghrGAN---------HPVKDLET------GRVE--- 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910291 435 nssdlggtmrkgaqrcpIrpgTrAQsiygddvNerhrHRYEVNNvyvPRLEDAGMVISARTPTENLPEMMELPSHPWFvG 514
Cdd:COG0505 292 -----------------I---T-SQ-------N----HGFAVDE---DSLPATDLEVTHVNLNDGTVEGLRHKDLPAF-S 335
|
170
....*....|....*...
gi 489910291 515 VQFHPEFTSTPRDGHPLF 532
Cdd:COG0505 336 VQYHPEASPGPHDSAYLF 353
|
|
| PRK03619 |
PRK03619 |
phosphoribosylformylglycinamidine synthase subunit PurQ; |
317-387 |
1.70e-03 |
|
phosphoribosylformylglycinamidine synthase subunit PurQ;
Pssm-ID: 235140 [Multi-domain] Cd Length: 219 Bit Score: 40.10 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910291 317 VHAgIHTRSKVNIEYIDSEDietrgTDqLKHLDAILVPGGF--GKRGTEGKIAA-------IRYARENGVPYLGICLGMQ 387
Cdd:PRK03619 18 ARA-LRDLLGAEPEYVWHKE-----TD-LDGVDAVVLPGGFsyGDYLRCGAIAAfspimkaVKEFAEKGKPVLGICNGFQ 90
|
|
| hisH |
PRK13143 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
311-388 |
1.81e-03 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 237289 [Multi-domain] Cd Length: 200 Bit Score: 39.85 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910291 311 SLSEALVHAGihtrSKVNIEyIDSEDIETrgtdqlkhLDAILVPG----GFGKRGTEGKIAAIRYARENGVPYLGICLGM 386
Cdd:PRK13143 15 SVSKALERAG----AEVVIT-SDPEEILD--------ADGIVLPGvgafGAAMENLSPLRDVILEAARSGKPFLGICLGM 81
|
..
gi 489910291 387 QL 388
Cdd:PRK13143 82 QL 83
|
|
| GATase1_GMP_Synthase |
cd01742 |
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ... |
374-533 |
1.99e-03 |
|
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase. GMP synthetase is a glutamine amidotransferase from the de novo purine biosynthetic pathway. Glutamine amidotransferase (GATase) activity catalyse the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. GMP synthetase catalyses the amination of the nucleotide precursor xanthosine 5'-monophosphate to form GMP. GMP synthetase belongs to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.
Pssm-ID: 153213 [Multi-domain] Cd Length: 181 Bit Score: 39.44 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910291 374 ENGVPYLGICLGMQLAVIEFARHVaglGGANSTEFDPAaphpvvalitewmdregRVERRDNSSDLGGtmrkgaqrcpir 453
Cdd:cd01742 68 ELGVPVLGICYGMQLIAKALGGKV---ERGDKREYGKA-----------------EIEIDDSSPLFEG------------ 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910291 454 pgtraqsiYGDDVNERHRHRYEVnnVYVPrledAGMVISARTPTeNLPEMMELPSHPWFvGVQFHPEFTSTPRdGHPLFS 533
Cdd:cd01742 116 --------LPDEQTVWMSHGDEV--VKLP----EGFKVIASSDN-CPVAAIANEEKKIY-GVQFHPEVTHTEK-GKEILK 178
|
|
| PRK00758 |
PRK00758 |
GMP synthase subunit A; Validated |
371-536 |
3.41e-03 |
|
GMP synthase subunit A; Validated
Pssm-ID: 179112 [Multi-domain] Cd Length: 184 Bit Score: 38.68 E-value: 3.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910291 371 YARENGVPYLGICLGMQLAVIEFARHVaglGGANSTEFdpaaphpvvALITewmdregrVERRDNSSDLGGtmrkgaqrc 450
Cdd:PRK00758 62 YLKELDVPILGICLGHQLIAKAFGGEV---GRGEYGEY---------ALVE--------VEILDEDDILKG--------- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910291 451 pIRPGTRAQSIYGDDVNErhrhryevnnvyVPRledaGMVISARTPTENLpEMMELPSHPWFvGVQFHPEFTSTPRdGHP 530
Cdd:PRK00758 113 -LPPEIRVWASHADEVKE------------LPD----GFEILARSDICEV-EAMKHKEKPIY-GVQFHPEVAHTEY-GEE 172
|
....*.
gi 489910291 531 LFSSYI 536
Cdd:PRK00758 173 IFKNFL 178
|
|
| GATase1_1 |
cd01741 |
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ... |
366-388 |
3.44e-03 |
|
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group contains a subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain. GATase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. Glutamine amidotransferases (GATase) includes the triad family of amidotransferases which have a conserved Cys-His-Glu catalytic triad in the glutaminase active site. In this subgroup this triad is conserved. GATase activity can be found in a range of biosynthetic enzymes, including: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase , anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. Glutamine amidotransferase (GATase) domains can occur either as single polypeptides, as in glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.
Pssm-ID: 153212 [Multi-domain] Cd Length: 188 Bit Score: 38.77 E-value: 3.44e-03
10 20
....*....|....*....|...
gi 489910291 366 IAAIRYARENGVPYLGICLGMQL 388
Cdd:cd01741 71 KELIRQALAAGKPVLGICLGHQL 93
|
|
| GATase1_CobQ |
cd01750 |
Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ); Type ... |
327-401 |
4.84e-03 |
|
Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ); Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ). CobQ plays a role in cobalamin biosythesis. CobQ catalyses amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide in the biosynthesis of cobalamin. CobQ belongs to the triad family of amidotransferases. Two of the three residues of the catalytic triad that are involved in glutamine binding, hydrolysis and transfer of the resulting ammonia to the acceptor substrate in other triad aminodotransferases are conserved in CobQ.
Pssm-ID: 153221 [Multi-domain] Cd Length: 194 Bit Score: 38.38 E-value: 4.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910291 327 VNIEYIDSedietrgTDQLKHLDAILVPGGfgkRGTEGKIA---------AIRYARENGVPYLGICLGMQL--------A 389
Cdd:cd01750 24 VDVRYVEV-------PEGLGDADLIILPGS---KDTIQDLAwlrkrglaeAIKNYARAGGPVLGICGGYQMlgkyivdpE 93
|
90
....*....|..
gi 489910291 390 VIEFARHVAGLG 401
Cdd:cd01750 94 GVEGPGEIEGLG 105
|
|
| PLN02347 |
PLN02347 |
GMP synthetase |
353-526 |
6.09e-03 |
|
GMP synthetase
Pssm-ID: 215197 [Multi-domain] Cd Length: 536 Bit Score: 39.28 E-value: 6.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910291 353 VPGGFgkrgtegkiaaIRYARENGVPYLGICLGMQLAviefarhVAGLGGanstEFDPAAPHpvvalitEWmdreGRVER 432
Cdd:PLN02347 74 VPEGF-----------FDYCRERGVPVLGICYGMQLI-------VQKLGG----EVKPGEKQ-------EY----GRMEI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910291 433 R-DNSSDLGGTMrkgaqrcpirPGTRAQSIY---GDDVnerhrhryevnnVYVPRledaGMVISARTPTENLPEMMELPS 508
Cdd:PLN02347 121 RvVCGSQLFGDL----------PSGETQTVWmshGDEA------------VKLPE----GFEVVAKSVQGAVVAIENRER 174
|
170
....*....|....*...
gi 489910291 509 HPWfvGVQFHPEFTSTPR 526
Cdd:PLN02347 175 RIY--GLQYHPEVTHSPK 190
|
|
| |
