|
Name |
Accession |
Description |
Interval |
E-value |
| pyrG |
PRK05380 |
CTP synthetase; Validated |
2-542 |
0e+00 |
|
CTP synthetase; Validated
Pssm-ID: 235437 [Multi-domain] Cd Length: 533 Bit Score: 1098.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365319 2 KTNYIFVTGGVVSSLGKGIAAASLAAILEARGLNVTMMKLDPYINVDPGTMSPIQHGEVFVTDDGAETDLDLGHYERFIR 81
Cdd:PRK05380 1 MTKYIFVTGGVVSSLGKGITAASLGRLLKARGLKVTIQKLDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365319 82 TKMTRRNNFTTGRVYSEVLRKERRGDYLGATIQVIPHITNEIKERIIRGGEGHDVVLVEVGGTVGDIESLPFLEAIRQMA 161
Cdd:PRK05380 81 TNLTKYNNVTTGKIYSSVIEKERRGDYLGKTVQVIPHITDEIKERILAAGTDADVVIVEIGGTVGDIESLPFLEAIRQLR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365319 162 AEVGREHTFYLHLTLVPYLAASGEVKTKPTQHSVKELLSIGIQPDALICRSDRVIPANERAKIALFCNVPEKAVISLKDV 241
Cdd:PRK05380 161 LELGRENVLFIHLTLVPYIAAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEEKRKIALFCNVPEEAVISAPDV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365319 242 DSIYKIPALLKSQGLDDYICKRFSLDCPVANLSEWEQVIYEEANPEGEVTIGMVGKYVELPDAYKSVIEALKHGGFKSRV 321
Cdd:PRK05380 241 DSIYEVPLLLHEQGLDDIVLERLGLEAPEPDLSEWEELVERLKNPKGEVTIALVGKYVELPDAYKSVIEALKHAGIANDV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365319 322 AVNIKLIDSQDVETRGV-EILKGLDAILVPGGFGERGVEGKIMAARYARENKIPYLGICLGMQVAMIEFARNVANMEDAN 400
Cdd:PRK05380 321 KVNIKWIDSEDLEEENVaELLKGVDGILVPGGFGERGIEGKILAIRYARENNIPFLGICLGMQLAVIEFARNVLGLEDAN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365319 401 STEFAPDCKYPVIALITEWRDEngnlevrtenSDLGGTMRLGAQPCHLSGDSLVRTLYGKNTITERHRHRYEVNNLLLKR 480
Cdd:PRK05380 401 STEFDPDTPHPVIDLMPEQKDV----------SDLGGTMRLGAYPCKLKPGTLAAEIYGKEEIYERHRHRYEVNNKYREQ 470
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490365319 481 IEDAGLRIAGRSVDNKLVEIIENPNHPWFVACQFHPEFTSTPRDGHPLFAGFVKAAFDYQKG 542
Cdd:PRK05380 471 LEKAGLVFSGTSPDGRLVEIVELPDHPWFVGVQFHPEFKSRPRRPHPLFAGFVKAALENKKR 532
|
|
| PyrG |
COG0504 |
CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase ... |
3-542 |
0e+00 |
|
CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase (UTP-ammonia lyase) is part of the Pathway/BioSystem: Pyrimidine biosynthesis
Pssm-ID: 440270 [Multi-domain] Cd Length: 535 Bit Score: 1080.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365319 3 TNYIFVTGGVVSSLGKGIAAASLAAILEARGLNVTMMKLDPYINVDPGTMSPIQHGEVFVTDDGAETDLDLGHYERFIRT 82
Cdd:COG0504 1 TKYIFVTGGVVSSLGKGITAASLGRLLKARGLKVTIQKLDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFLDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365319 83 KMTRRNNFTTGRVYSEVLRKERRGDYLGATIQVIPHITNEIKERIIRGGE--GHDVVLVEVGGTVGDIESLPFLEAIRQM 160
Cdd:COG0504 81 NLSKANNVTTGQIYSSVIEKERRGDYLGKTVQVIPHITDEIKRRIRRAAEesGADVVIVEIGGTVGDIESLPFLEAIRQL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365319 161 AAEVGREHTFYLHLTLVPYLAASGEVKTKPTQHSVKELLSIGIQPDALICRSDRVIPANERAKIALFCNVPEKAVISLKD 240
Cdd:COG0504 161 RLELGRENVLFIHVTLVPYIAAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEIKRKIALFCNVPEEAVISAPD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365319 241 VDSIYKIPALLKSQGLDDYICKRFSLDCPVANLSEWEQVIYEEANPEGEVTIGMVGKYVELPDAYKSVIEALKHGGFKSR 320
Cdd:COG0504 241 VDSIYEVPLMLHEQGLDEIVLKKLGLEAREPDLSEWEELVERIKNPKKEVTIALVGKYVELPDAYKSVVEALKHAGIANG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365319 321 VAVNIKLIDSQDVETRGV-EILKGLDAILVPGGFGERGVEGKIMAARYARENKIPYLGICLGMQVAMIEFARNVANMEDA 399
Cdd:COG0504 321 VKVNIKWIDSEDLEEENAeELLKGVDGILVPGGFGERGIEGKIAAIRYARENKIPFLGICLGMQLAVIEFARNVLGLEDA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365319 400 NSTEFAPDCKYPVIALITEwrdengnlevRTENSDLGGTMRLGAQPCHLSGDSLVRTLYGKNTITERHRHRYEVNNLLLK 479
Cdd:COG0504 401 NSTEFDPNTPHPVIDLMPE----------QKDVSDLGGTMRLGAYPCKLKPGTLAAEAYGKEEISERHRHRYEFNNEYRE 470
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490365319 480 RIEDAGLRIAGRSVDNKLVEIIENPNHPWFVACQFHPEFTSTPRDGHPLFAGFVKAAFDYQKG 542
Cdd:COG0504 471 QLEKAGLVFSGTSPDGRLVEIVELPDHPWFVGVQFHPEFKSRPNRPHPLFRGFVKAALEYKKK 533
|
|
| PyrG |
TIGR00337 |
CTP synthase; CTP synthase is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. ... |
3-535 |
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: 952.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365319 3 TNYIFVTGGVVSSLGKGIAAASLAAILEARGLNVTMMKLDPYINVDPGTMSPIQHGEVFVTDDGAETDLDLGHYERFIRT 82
Cdd:TIGR00337 1 MKYIFVTGGVVSSLGKGITAASLGRLLKARGLNVTIIKIDPYINIDPGTMSPLQHGEVFVTDDGAETDLDLGHYERFLDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365319 83 KMTRRNNFTTGRVYSEVLRKERRGDYLGATIQVIPHITNEIKERIIRGGE--GHDVVLVEVGGTVGDIESLPFLEAIRQM 160
Cdd:TIGR00337 81 NLTRDNNITTGKIYSSVIEKERKGDYLGKTVQIIPHITNEIKDRILRVAKisGPDVVIVEIGGTVGDIESLPFLEAIRQF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365319 161 AAEVGREHTFYLHLTLVPYLAASGEVKTKPTQHSVKELLSIGIQPDALICRSDRVIPANERAKIALFCNVPEKAVISLKD 240
Cdd:TIGR00337 161 RVEVGRENVLFIHVTLVPYIAAAGEQKTKPTQHSVKELRSLGIQPDIIICRSSRPLDPNTKDKIALFCDVEEEAVISAKD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365319 241 VDSIYKIPALLKSQGLDDYICKRFSLDCPVANLSEWEQVIYEEANPEGEVTIGMVGKYVELPDAYKSVIEALKHGGFKSR 320
Cdd:TIGR00337 241 VSSIYEVPLLLLKQGLDDYLCRRLNLNCDEADLSEWEQLVEKFANPKHEVTIGIVGKYVELKDAYLSVIEALKHAGAKLD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365319 321 VAVNIKLIDSQDVETRGVEILKGLDAILVPGGFGERGVEGKIMAARYARENKIPYLGICLGMQVAMIEFARNVANMEDAN 400
Cdd:TIGR00337 321 TKVNIKWIDSEDLEEEGVEFLKGLDGILVPGGFGERGVEGKILAIKYARENNIPFLGICLGMQLAVIEFARNVAGLEGAN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365319 401 STEFAPDCKYPVIALITEWRDengnlevrteNSDLGGTMRLGAQPCHLSGDSLVRTLYGKNTITERHRHRYEVNNLLLKR 480
Cdd:TIGR00337 401 STEFDPDTKYPVVDLLPEQKD----------ISDLGGTMRLGLYPCILKPGTLAFKLYGKEEVYERHRHRYEVNNEYREQ 470
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 490365319 481 IEDAGLRIAGRSVDNKLVEIIENPNHPWFVACQFHPEFTSTPRDGHPLFAGFVKA 535
Cdd:TIGR00337 471 IENKGLIVSGTSPDGRLVEIIELPDHPFFVACQFHPEFTSRPNDPHPLFLGFVKA 525
|
|
| PLN02327 |
PLN02327 |
CTP synthase |
1-536 |
0e+00 |
|
CTP synthase
Pssm-ID: 215186 [Multi-domain] Cd Length: 557 Bit Score: 649.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365319 1 MKtnYIFVTGGVVSSLGKGIAAASLAAILEARGLNVTMMKLDPYINVDPGTMSPIQHGEVFVTDDGAETDLDLGHYERFI 80
Cdd:PLN02327 1 MK--YVLVTGGVVSGLGKGVTASSIGVLLKACGLRVTSIKIDPYLNTDAGTMSPFEHGEVFVLDDGGEVDLDLGNYERFL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365319 81 RTKMTRRNNFTTGRVYSEVLRKERRGDYLGATIQVIPHITNEIKERIIR-------GGEGH-DVVLVEVGGTVGDIESLP 152
Cdd:PLN02327 79 DVTLTRDNNITTGKIYQSVIEKERRGDYLGKTVQVVPHITDAIQEWIERvakipvdGKEGPaDVCVIELGGTVGDIESMP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365319 153 FLEAIRQMAAEVGREHTFYLHLTLVPYLAASGEVKTKPTQHSVKELLSIGIQPDALICRSDRVIPANERAKIALFCNVPE 232
Cdd:PLN02327 159 FIEALRQFSFRVGPGNFCLIHVSLVPVLGVVGEQKTKPTQHSVRGLRALGLTPHILACRSTKPLEENVKEKLSQFCHVPA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365319 233 KAVISLKDVDSIYKIPALLKSQGLDDYICKRFSLDCPVA--NLSEWEQVIYEEANPEGEVTIGMVGKYVELPDAYKSVIE 310
Cdd:PLN02327 239 ENILNLHDVSNIWHVPLLLRDQKAHEAILKVLNLLSVARepDLEEWTARAESCDNLTEPVRIAMVGKYTGLSDSYLSVLK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365319 311 ALKHGGFKSRVAVNIKLIDSQDVETRGV-----------EILKGLDAILVPGGFGERGVEGKIMAARYARENKIPYLGIC 379
Cdd:PLN02327 319 ALLHASVACSRKLVIDWVAASDLEDETAketpdayaaawKLLKGADGILVPGGFGDRGVEGKILAAKYARENKVPYLGIC 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365319 380 LGMQVAMIEFARNVANMEDANSTEFAPDCKYPVIALITEWRDENgnlevrtensdLGGTMRLGAQPCHL-SGDSLVRTLY 458
Cdd:PLN02327 399 LGMQIAVIEFARSVLGLKDANSTEFDPETPNPCVIFMPEGSKTH-----------MGGTMRLGSRRTYFqTPDCKSAKLY 467
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490365319 459 GK-NTITERHRHRYEVNNLLLKRIEDAGLRIAGRSVDNKLVEIIENPNHPWFVACQFHPEFTSTPRDGHPLFAGFVKAA 536
Cdd:PLN02327 468 GNvSFVDERHRHRYEVNPEMVPRLEKAGLSFVGKDETGRRMEIVELPSHPFFVGVQFHPEFKSRPGKPSPLFLGLIAAA 546
|
|
| CTP_synth_N |
pfam06418 |
CTP synthase N-terminus; This family consists of the N-terminal region of the CTP synthase ... |
5-266 |
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: 526.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365319 5 YIFVTGGVVSSLGKGIAAASLAAILEARGLNVTMMKLDPYINVDPGTMSPIQHGEVFVTDDGAETDLDLGHYERFIRTKM 84
Cdd:pfam06418 2 YIFVTGGVVSGLGKGITAASLGRLLKSRGLKVTIIKIDPYLNVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFLDINL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365319 85 TRRNNFTTGRVYSEVLRKERRGDYLGATIQVIPHITNEIKERIIRGGE--GHDVVLVEVGGTVGDIESLPFLEAIRQMAA 162
Cdd:pfam06418 82 TKDNNITTGKIYQSVIEKERRGDYLGKTVQVIPHITDEIKERIRRVAKevGPDVVIVEIGGTVGDIESLPFLEAIRQLRL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365319 163 EVGREHTFYLHLTLVPYLAASGEVKTKPTQHSVKELLSIGIQPDALICRSDRVIPANERAKIALFCNVPEKAVISLKDVD 242
Cdd:pfam06418 162 EVGRENVLFIHVTLVPYLKAAGELKTKPTQHSVKELRSIGIQPDIIVCRSERPLDEEVKEKIALFCNVPKEAVISAPDVS 241
|
250 260
....*....|....*....|....
gi 490365319 243 SIYKIPALLKSQGLDDYICKRFSL 266
Cdd:pfam06418 242 SIYEVPLLLEEQGLDDIILKRLNL 265
|
|
| CTPS_N |
cd03113 |
N-terminal domain of cytidine 5'-triphosphate synthase; Cytidine 5'-triphosphate synthase ... |
5-262 |
1.14e-166 |
|
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: 472.74 E-value: 1.14e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365319 5 YIFVTGGVVSSLGKGIAAASLAAILEARGLNVTMMKLDPYINVDPGTMSPIQHGEVFVTDDGAETDLDLGHYERFIRTKM 84
Cdd:cd03113 2 YIFVTGGVVSGLGKGITASSIGRLLKSRGLRVTAIKIDPYLNVDAGTMSPYEHGEVFVLDDGGETDLDLGNYERFLDVNL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365319 85 TRRNNFTTGRVYSEVLRKERRGDYLGATIQVIPHITNEIKERIIRGGEGH--DVVLVEVGGTVGDIESLPFLEAIRQMAA 162
Cdd:cd03113 82 TRDNNITTGKIYSEVIEKERRGDYLGKTVQVIPHITDEIKERIRRVAKIPepDVCIVEIGGTVGDIESLPFLEALRQFQF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365319 163 EVGREHTFYLHLTLVPYLAASGEVKTKPTQHSVKELLSIGIQPDALICRSDRVIPANERAKIALFCNVPEKAVISLKDVD 242
Cdd:cd03113 162 EVGRENFLFIHVTLVPYLEATGEQKTKPTQHSVKELRSLGIQPDIIVCRSEKPLDEETKEKIALFCNVPPEAVISVHDVS 241
|
250 260
....*....|....*....|
gi 490365319 243 SIYKIPALLKSQGLDDYICK 262
Cdd:cd03113 242 SIYEVPLLLEKQGLDDYILR 261
|
|
| GATase1_CTP_Synthase |
cd01746 |
Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase; ... |
290-533 |
9.36e-139 |
|
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: 400.78 E-value: 9.36e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365319 290 VTIGMVGKYVELPDAYKSVIEALKHGGFKSRVAVNIKLIDSQDVETRGV-EILKGLDAILVPGGFGERGVEGKIMAARYA 368
Cdd:cd01746 1 VRIALVGKYVELPDAYLSVLEALKHAGIALGVKLEIKWIDSEDLEEENAeEALKGADGILVPGGFGIRGVEGKILAIKYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365319 369 RENKIPYLGICLGMQVAMIEFARNVANMEDANSTEFAPDCKYPVIALITEWRDengnlevrteNSDLGGTMRLGAQPCHL 448
Cdd:cd01746 81 RENNIPFLGICLGMQLAVIEFARNVLGLPDANSTEFDPDTPHPVVDLMPEQKG----------VKDLGGTMRLGAYPVIL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365319 449 SGDSLVRTLYGKNTITERHRHRYEVNNLLLKRIEDAGLRIAGRSVDNKLVEIIENPNHPWFVACQFHPEFTSTPRDGHPL 528
Cdd:cd01746 151 KPGTLAHKYYGKDEVEERHRHRYEVNPEYVDELEEAGLRFSGTDPDGGLVEIVELPDHPFFVGTQFHPEFKSRPLKPHPL 230
|
....*
gi 490365319 529 FAGFV 533
Cdd:cd01746 231 FVGFV 235
|
|
| GATase |
pfam00117 |
Glutamine amidotransferase class-I; |
300-535 |
2.14e-46 |
|
Glutamine amidotransferase class-I;
Pssm-ID: 395067 [Multi-domain] Cd Length: 188 Bit Score: 160.87 E-value: 2.14e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365319 300 ELPDAYKSVIEALKHGGFKSRVAVNIKLIDSQDVETRGVEIlkglDAILVPGGFGERG-VEGKIMAARYARENKIPYLGI 378
Cdd:pfam00117 1 LLIDNGDSFTYNLARALRELGVEVTVVPNDTPAEEILEENP----DGIILSGGPGSPGaAGGAIEAIREARELKIPILGI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365319 379 CLGMQVAMIEFARNVANMEDanstefapdckypvialitewrdengnlevrteNSDLGGTMRLGAQPCHLsgdslvrtLY 458
Cdd:pfam00117 77 CLGHQLLALAFGGKVVKAKK---------------------------------FGHHGKNSPVGDDGCGL--------FY 115
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490365319 459 G-KNTITERHRHRYEVNNLLLKriedAGLRIAGRSVDNKLVEIIENPNHPWFvACQFHPEFTSTPRDGHPLFAGFVKA 535
Cdd:pfam00117 116 GlPNVFIVRRYHSYAVDPDTLP----DGLEVTATSENDGTIMGIRHKKLPIF-GVQFHPESILTPHGPEILFNFFIKA 188
|
|
| PRK06186 |
PRK06186 |
hypothetical protein; Validated |
292-536 |
1.79e-33 |
|
hypothetical protein; Validated
Pssm-ID: 180452 [Multi-domain] Cd Length: 229 Bit Score: 127.00 E-value: 1.79e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365319 292 IGMVGKYVELPDAYKSVIEALKHGGFKSRVAVNIKLIDSQDVetRGVEILKGLDAI-LVPGGfGERGVEGKIMAARYARE 370
Cdd:PRK06186 4 IALVGDYNPDVTAHQAIPLALDLAAAVLGLPVDYEWLPTPEI--TDPEDLAGFDGIwCVPGS-PYRNDDGALTAIRFARE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365319 371 NKIPYLGICLGMQVAMIEFARNVANMEDANSTEFAPDCKYPVIA-LITEWRDENGNLevrtensdlggtmrlgaqpcHLS 449
Cdd:PRK06186 81 NGIPFLGTCGGFQHALLEYARNVLGWADAAHAETDPEGDRPVIApLSCSLVEKTGDI--------------------RLR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365319 450 GDSLVRTLYGKNTITERHRHRYEVNNLLLKRIEDAGLRIAGRSvDNKLVEIIENPNHPWFVACQFHPEFTSTPRDGHPLF 529
Cdd:PRK06186 141 PGSLIARAYGTLEIEEGYHCRYGVNPEFVAALESGDLRVTGWD-EDGDVRAVELPGHPFFVATLFQPERAALAGRPPPLV 219
|
....*..
gi 490365319 530 AGFVKAA 536
Cdd:PRK06186 220 RAFLRAA 226
|
|
| PuuD |
COG2071 |
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ... |
301-536 |
1.08e-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: 79.44 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365319 301 LPDAY-KSVIEAlkhGGfksrVAVnikLIDSQDVETRGVEILKGLDAILVPGG-------FGERGVEGK----------- 361
Cdd:COG2071 16 LPEDYvRAVRAA---GG----LPV---LLPPVGDEEDLDELLDRLDGLVLTGGadvdpalYGEEPHPELgpidperdafe 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365319 362 IMAARYARENKIPYLGICLGMQVAmiefarNVAnmedanstefapdckypvialitewrdengnlevrtensdLGGTM-- 439
Cdd:COG2071 86 LALIRAALERGKPVLGICRGMQLL------NVA----------------------------------------LGGTLyq 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365319 440 ---------------RLGAQPCH---LSGDSLVRTLYGKNTIterhrhryEVNNL---LLKRIEDaGLRIAGRSVDNkLV 498
Cdd:COG2071 120 dlpdqvpgaldhrqpAPRYAPRHtveIEPGSRLARILGEEEI--------RVNSLhhqAVKRLGP-GLRVSARAPDG-VI 189
|
250 260 270
....*....|....*....|....*....|....*....
gi 490365319 499 EIIENPNHPWFVACQFHPEF-TSTPRDGHPLFAGFVKAA 536
Cdd:COG2071 190 EAIESPGAPFVLGVQWHPEWlAASDPLSRRLFEAFVEAA 228
|
|
| GATase1 |
cd01653 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
292-387 |
4.34e-12 |
|
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: 63.00 E-value: 4.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365319 292 IGMVGKYVELPDAYKSVIEALKHGGFksrvavNIKLIDSQDVETRGVEILKGLDAILVPGGFG----ERGVEGKIMAARY 367
Cdd:cd01653 1 VAVLLFPGFEELELASPLDALREAGA------EVDVVSPDGGPVESDVDLDDYDGLILPGGPGtpddLARDEALLALLRE 74
|
90 100
....*....|....*....|
gi 490365319 368 ARENKIPYLGICLGMQVAMI 387
Cdd:cd01653 75 AAAAGKPILGICLGAQLLVL 94
|
|
| GAT_1 |
cd03128 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
292-384 |
2.46e-11 |
|
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: 59.91 E-value: 2.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365319 292 IGMVGKYVELPDAYKSVIEALKHGGFksrvavNIKLIDSQDVETRGVEILKGLDAILVPGGFG----ERGVEGKIMAARY 367
Cdd:cd03128 1 VAVLLFGGSEELELASPLDALREAGA------EVDVVSPDGGPVESDVDLDDYDGLILPGGPGtpddLAWDEALLALLRE 74
|
90
....*....|....*..
gi 490365319 368 ARENKIPYLGICLGMQV 384
Cdd:cd03128 75 AAAAGKPVLGICLGAQL 91
|
|
| GATase1_2 |
cd01745 |
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ... |
292-533 |
8.64e-10 |
|
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: 58.36 E-value: 8.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365319 292 IGMVG-------KYVELPDAYKSVIEALKHGGFksrVAVnikLIDSQDVETRGVEILKGLDAILVPGG--------FGER 356
Cdd:cd01745 1 IGITArlreeegGYERRDYLNQYYVDAVRKAGG---LPV---LLPPVDDEEDLEQYLELLDGLLLTGGgdvdpplyGEEP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365319 357 GVEGK----------IMAARYARENKIPYLGICLGMQvaMIefarNVAnmedanstefapdckypvialitewrdengnl 426
Cdd:cd01745 75 HPELGpidperdafeLALLRAALERGKPILGICRGMQ--LL----NVA-------------------------------- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365319 427 evrtensdLGGTmrlgaqpchLSGDSLVRTLygkntiterhrHRYEVNNLllkrieDAGLRIAGRSVDNkLVEIIENPNH 506
Cdd:cd01745 117 --------LGGT---------LYQDIRVNSL-----------HHQAIKRL------ADGLRVEARAPDG-VIEAIESPDR 161
|
250 260
....*....|....*....|....*...
gi 490365319 507 PWFVACQFHPEFTSTPRDGH-PLFAGFV 533
Cdd:cd01745 162 PFVLGVQWHPEWLADTDPDSlKLFEAFV 189
|
|
| Peptidase_C26 |
pfam07722 |
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ... |
329-517 |
8.07e-08 |
|
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze the cleavage of the gamma-glutamyl bond in poly-gamma-glutamyl substrates. They are structurally related to pfam00117, but contain extensions in four loops and at the C terminus.
Pssm-ID: 429620 [Multi-domain] Cd Length: 219 Bit Score: 53.03 E-value: 8.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365319 329 DSQDVETrgveILKGLDAILVPGG-------FGERGVE--GKIMAAR---------YARENKIPYLGICLGMQVAmiefa 390
Cdd:pfam07722 48 DPEDAAA----ILDRLDGLLLTGGpnvdphfYGEEPSEsgGPYDPARdayelalirAALARGKPILGICRGFQLL----- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365319 391 rNVA---NMedanstefapdckYPVIalitewRDENGNLEVRTENSDLGGtmrLGAQPCHLSGDSLVRTLYGKNTITERH 467
Cdd:pfam07722 119 -NVAlggTL-------------YQDI------QEQPGFTDHREHCQVAPY---APSHAVNVEPGSLLASLLGSEEFRVNS 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490365319 468 RHRYEVNNLllkrieDAGLRIAGRSVDNkLVEIIENPNHPWFV-ACQFHPE 517
Cdd:pfam07722 176 LHHQAIDRL------APGLRVEAVAPDG-TIEAIESPNAKGFAlGVQWHPE 219
|
|
| IMP_synth_hisH |
TIGR01855 |
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model ... |
306-383 |
3.94e-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: 44.62 E-value: 3.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365319 306 KSVIEALKHGGFKSRVavniklidsqdveTRGVEILKGLDAILVPG--GFGE--RGVE--GKIMAARYARENKIPYLGIC 379
Cdd:TIGR01855 12 GSVKRALKRVGAEPVV-------------VKDSKEAELADKLILPGvgAFGAamARLRenGLDLFVELVVRLGKPVLGIC 78
|
....
gi 490365319 380 LGMQ 383
Cdd:TIGR01855 79 LGMQ 82
|
|
| GATase1_IGP_Synthase |
cd01748 |
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ... |
306-384 |
3.95e-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: 44.80 E-value: 3.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365319 306 KSVIEALKHGGFKSRVavniklidsqdveTRGVEILKGLDAILVPG-G-FG-------ERGVEGKImaaRYARENKIPYL 376
Cdd:cd01748 12 RSVANALERLGAEVII-------------TSDPEEILSADKLILPGvGaFGdamanlrERGLIEAL---KEAIASGKPFL 75
|
....*...
gi 490365319 377 GICLGMQV 384
Cdd:cd01748 76 GICLGMQL 83
|
|
| hisH |
PRK13141 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
306-384 |
7.75e-05 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 237288 [Multi-domain] Cd Length: 205 Bit Score: 43.97 E-value: 7.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365319 306 KSVIEALKHGGFKSRVavniklidsqdveTRGVEILKGLDAILVPG--GFG-------ERGVEGKIMAARyarENKIPYL 376
Cdd:PRK13141 13 RSVEKALERLGAEAVI-------------TSDPEEILAADGVILPGvgAFPdamanlrERGLDEVIKEAV---ASGKPLL 76
|
....*...
gi 490365319 377 GICLGMQV 384
Cdd:PRK13141 77 GICLGMQL 84
|
|
| puuD |
PRK11366 |
gamma-glutamyl-gamma-aminobutyrate hydrolase; Provisional |
339-541 |
1.31e-04 |
|
gamma-glutamyl-gamma-aminobutyrate hydrolase; Provisional
Pssm-ID: 183101 [Multi-domain] Cd Length: 254 Bit Score: 43.74 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365319 339 EILKGLDAILVPGG--------FGERGVE-----GK----IMAARYARENKIPYLGICLGMQVAMIEfarnvanmedANS 401
Cdd:PRK11366 57 QLLPKLDGIYLPGSpsnvqphlYGENGDEpdadpGRdllsMALINAALERRIPIFAICRGLQELVVA----------TGG 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365319 402 TEFAPDCKYPVIalitewrdengnLEVRtENSDLggTMRLGAQPCH----LSGDSLVRTLYGKNTiterhrhrYEVNNLL 477
Cdd:PRK11366 127 SLHRKLCEQPEL------------LEHR-EDPEL--PVEQQYAPSHevqvEEGGLLSALLPECSN--------FWVNSLH 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490365319 478 LK--RIEDAGLRIAGRSVDNkLVEIIENPNHPWFVACQFHPEFTSTPRD-GHPLFAGFVKAAFDYQK 541
Cdd:PRK11366 184 GQgaKVVSPRLRVEARSPDG-LVEAVSVINHPFALGVQWHPEWNSSEYAlSRILFEGFITACQHHIA 249
|
|
| SIMIBI |
cd01983 |
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ... |
135-210 |
2.19e-04 |
|
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal recognition particle, MinD, and BioD), consists of signal recognition particle (SRP) GTPases, the assemblage of MinD-like ATPases, which are involved in protein localization, chromosome partitioning, and membrane transport, and a group of metabolic enzymes with kinase or related phosphate transferase activity. Functionally, proteins in this superfamily use the energy from hydrolysis of NTP to transfer electron or ion.
Pssm-ID: 349751 [Multi-domain] Cd Length: 107 Bit Score: 40.88 E-value: 2.19e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490365319 135 DVVLVEVGGTVGDIESLPFleairQMAAEVGREHTFYLHLTLVPYLAASGEVKTKptqhSVKELLSIGIQPDALIC 210
Cdd:cd01983 39 DYVLIDGGGGLETGLLLGT-----IVALLALKKADEVIVVVDPELGSLLEAVKLL----LALLLLGIGIRPDGIVL 105
|
|
| hisH |
PRK13143 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
307-386 |
2.79e-04 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 237289 [Multi-domain] Cd Length: 200 Bit Score: 42.16 E-value: 2.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365319 307 SVIEALKHGGFKSRVavniklidsqdveTRGVEILKGLDAILVPG--GFGErGVEgkiMAARY------ARENKIPYLGI 378
Cdd:PRK13143 15 SVSKALERAGAEVVI-------------TSDPEEILDADGIVLPGvgAFGA-AME---NLSPLrdvileAARSGKPFLGI 77
|
....*...
gi 490365319 379 CLGMQVAM 386
Cdd:PRK13143 78 CLGMQLLF 85
|
|
| hisH |
PRK13181 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
306-384 |
3.36e-04 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 183878 [Multi-domain] Cd Length: 199 Bit Score: 41.77 E-value: 3.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365319 306 KSVIEALKHGGFKSRVavniklidSQDVEtrgveILKGLDAILVPG---------GFGERGVEGKImaaRYARENKIPYL 376
Cdd:PRK13181 13 RSVANALKRLGVEAVV--------SSDPE-----EIAGADKVILPGvgafgqamrSLRESGLDEAL---KEHVEKKQPVL 76
|
....*...
gi 490365319 377 GICLGMQV 384
Cdd:PRK13181 77 GICLGMQL 84
|
|
| HisH |
COG0118 |
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ... |
306-384 |
2.49e-03 |
|
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid transport and metabolism]; Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH is part of the Pathway/BioSystem: Histidine biosynthesis
Pssm-ID: 439888 [Multi-domain] Cd Length: 196 Bit Score: 39.25 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365319 306 KSVIEALKhggfksRVAVNIKLIDSQDVetrgveiLKGLDAILVPG---------GFGERGVEGKImaaRYARENKIPYL 376
Cdd:COG0118 14 RSVAKALE------RLGAEVVVTSDPDE-------IRAADRLVLPGvgafgdameNLRERGLDEAI---REAVAGGKPVL 77
|
....*...
gi 490365319 377 GICLGMQV 384
Cdd:COG0118 78 GICLGMQL 85
|
|
| hisH |
PRK13146 |
imidazole glycerol phosphate synthase subunit HisH; Provisional |
307-384 |
6.08e-03 |
|
imidazole glycerol phosphate synthase subunit HisH; Provisional
Pssm-ID: 237290 [Multi-domain] Cd Length: 209 Bit Score: 38.22 E-value: 6.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365319 307 SVIEALKHGGFKSRVAVniklidsqdveTRGVEILKGLDAILVPG---------GFGERGVEGKIMAARYARENkiPYLG 377
Cdd:PRK13146 16 SAAKALERAGAGADVVV-----------TADPDAVAAADRVVLPGvgafadcmrGLRAVGLGEAVIEAVLAAGR--PFLG 82
|
....*..
gi 490365319 378 ICLGMQV 384
Cdd:PRK13146 83 ICVGMQL 89
|
|
| |
