|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02981 |
PLN02981 |
glucosamine:fructose-6-phosphate aminotransferase |
1-428 |
0e+00 |
|
glucosamine:fructose-6-phosphate aminotransferase
Pssm-ID: 215531 [Multi-domain] Cd Length: 680 Bit Score: 553.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080037 1 MCGIFAYMNYRVPKTRKEIFETLIRGLQRLEYRGYDSAGVAIDgNNHEVKERHIHLVKKRGKVKALDEELYK---QDSMD 77
Cdd:PLN02981 1 MCGIFAYLNYNVPRERRFILEVLFNGLRRLEYRGYDSAGIAID-NDPSLESSSPLVFREEGKIESLVRSVYEevaETDLN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080037 78 LKVEFETHFGIAHTRWATHGVPNAVNSHPQRSDKDNEFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIAKLIKYVF 157
Cdd:PLN02981 80 LDLVFENHAGIAHTRWATHGPPAPRNSHPQSSGPGNEFLVVHNGIITNYEVLKETLLRHGFTFESDTDTEVIPKLAKFVF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080037 158 D--NRETEDITFSTLVERVIQQLEGAFALVFKSIHYPGEAVATRRGSPLLIGVrskyKLSTEQipvlyptcnienvknic 235
Cdd:PLN02981 160 DklNEEEGDVTFSQVVMEVMRQLEGAYALIFKSPHYPNELVACKRGSPLLLGV----KELPEE----------------- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080037 236 KTRMKRLDSSTCLHAVGDKAVEFFFASDASAIIEHTNRVIFLEDDDIAAVADGKLSIHRVKRSATDDPS---------RA 306
Cdd:PLN02981 219 KNSSAVFTSEGFLTKNRDKPKEFFLASDASAVVEHTKRVLVIEDNEVVHLKDGGVGIYKFENEKGRGGGglsrpasveRA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080037 307 IQTLQMELQQIMKGNFSAFMQKEIFEQPESVFNTMRGRV----NFETNTVLLGGLKDHLKEIRRCRRLIVIGCGTSYHAA 382
Cdd:PLN02981 299 LSTLEMEVEQIMKGNYDHYMQKEIHEQPESLTTTMRGRLirggSGKAKRVLLGGLKDHLKTIRRSRRIVFIGCGTSYNAA 378
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1907080037 383 VATRQVLEELTELPVMVELASDFLDRNTPVFRDDVCFFISQSG-TSD 428
Cdd:PLN02981 379 LAARPILEELSGVPVTMELASDLLDRQGPIYREDTAVFVSQSGeTAD 425
|
|
| GlmS |
COG0449 |
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ... |
1-428 |
4.59e-139 |
|
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase domains [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440218 [Multi-domain] Cd Length: 610 Bit Score: 412.10 E-value: 4.59e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080037 1 MCGIFAYMnyrvpkTRKEIFETLIRGLQRLEYRGYDSAGVAIdgnnheVKERHIHLVKKRGKVKALDEELYKQDsmdlkv 80
Cdd:COG0449 1 MCGIVGYI------GKRDAAPILLEGLKRLEYRGYDSAGIAV------LDDGGLEVRKAVGKLANLEEKLAEEP------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080037 81 eFETHFGIAHTRWATHGVPNAVNSHPQRSDkDNEFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIAKLIKYVFDnr 160
Cdd:COG0449 63 -LSGTIGIGHTRWATHGAPSDENAHPHTSC-SGRIAVVHNGIIENYAELREELEAKGHTFKSETDTEVIAHLIEEYLK-- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080037 161 etEDITFSTLVERVIQQLEGAFALVFKSIHYPGEAVATRRGSPLLIGvrskyklsteqipvlyptcnienvknicktrmk 240
Cdd:COG0449 139 --GGGDLLEAVRKALKRLEGAYALAVISADEPDRIVAARKGSPLVIG--------------------------------- 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080037 241 rldsstclhaVGDKavEFFFASDASAIIEHTNRVIFLEDDDIAAVADGKLSIHRVKRSATDdpsRAIQTLQMELQQIMKG 320
Cdd:COG0449 184 ----------LGEG--ENFLASDVPALLPYTRRVIYLEDGEIAVLTRDGVEIYDLDGEPVE---REVKTVDWDAEAAEKG 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080037 321 NFSAFMQKEIFEQPESVFNTMRGRVNfETNTVLLGGLKDHLKEIRRCRRLIVIGCGTSYHAAVATRQVLEELTELPVMVE 400
Cdd:COG0449 249 GYPHFMLKEIHEQPEAIRDTLRGRLD-EDGRVVLDELNLAAEDLRNIDRIYIVACGTSYHAGLVGKYLIEELARIPVEVE 327
|
410 420
....*....|....*....|....*....
gi 1907080037 401 LASDFLDRNTPVFRDDVCFFISQSG-TSD 428
Cdd:COG0449 328 IASEFRYRDPVVDPGTLVIAISQSGeTAD 356
|
|
| PTZ00394 |
PTZ00394 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
1-428 |
5.51e-131 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 173585 [Multi-domain] Cd Length: 670 Bit Score: 393.47 E-value: 5.51e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080037 1 MCGIFAYMNYRVPKTRKEIFETLIRGLQRLEYRGYDSAGVAIDGNNHEVKE----------RHIhLVKKRGKVKALDEEL 70
Cdd:PTZ00394 1 MCGIFGYANHNVPRTVEQILNVLLDGIQKVEYRGYDSAGLAIDANIGSEKEdgtaasaptpRPC-VVRSVGNISQLREKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080037 71 YKQDS----MDLKVEFETHFGIAHTRWATHGVPNAVNSHPQRSDkDNEFVVIHNGIITNYKDLRKFLESKGYEFESETDT 146
Cdd:PTZ00394 80 FSEAVaatlPPMDATTSHHVGIAHTRWATHGGVCERNCHPQQSN-NGEFTIVHNGIVTNYMTLKELLKEEGYHFSSDTDT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080037 147 ETIAKLIKYVFDNRETedITFSTLVERVIQQLEGAFALVFKSIHYPGEAVATRRGSPLLIGVRskyklsteqipvlyptc 226
Cdd:PTZ00394 159 EVISVLSEYLYTRKGI--HNFADLALEVSRMVEGSYALLVKSVYFPGQLAASRKGSPLMVGIR----------------- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080037 227 nienvknicktrmkRLDSSTCL-----HAVGD--KAVEFFFASDASAIIEHTNRVIFLEDDDIAAVADGKLSIHRVKRSA 299
Cdd:PTZ00394 220 --------------RTDDRGCVmklqtYDLTDlsGPLEVFFSSDVNSFAEYTREVVFLEDGDIAHYCDGALRFYNAAERQ 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080037 300 TDDPSRAIQTLQMELQQIMKGNFSAFMQKEIFEQPESVFNTMRGRVNFETNTVLLGGLKDH-LKEIRRCRRLIVIGCGTS 378
Cdd:PTZ00394 286 RSIVKREVQHLDAKPEGLSKGNYPHFMLKEIYEQPESVISSMHGRIDFSSGTVQLSGFTQQsIRAILTSRRILFIACGTS 365
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1907080037 379 YHAAVATRQVLEELTELPVMVELASDFLDRNTPVFRDDVCFFISQSG-TSD 428
Cdd:PTZ00394 366 LNSCLAVRPLFEELVPLPISVENASDFLDRRPRIQRDDVCFFVSQSGeTAD 416
|
|
| PRK00331 |
PRK00331 |
isomerizing glutamine--fructose-6-phosphate transaminase; |
1-428 |
1.53e-127 |
|
isomerizing glutamine--fructose-6-phosphate transaminase;
Pssm-ID: 234729 [Multi-domain] Cd Length: 604 Bit Score: 382.08 E-value: 1.53e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080037 1 MCGIFAYMNYRvpktrkEIFETLIRGLQRLEYRGYDSAGVAIdgnnheVKERHIHLVKKRGKVKALDEELyKQDSMdlkv 80
Cdd:PRK00331 1 MCGIVGYVGQR------NAAEILLEGLKRLEYRGYDSAGIAV------LDDGGLEVRKAVGKVANLEAKL-EEEPL---- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080037 81 efETHFGIAHTRWATHGVPNAVNSHPQRsDKDNEFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIAKLIKYVFDNr 160
Cdd:PRK00331 64 --PGTTGIGHTRWATHGKPTERNAHPHT-DCSGRIAVVHNGIIENYAELKEELLAKGHVFKSETDTEVIAHLIEEELKE- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080037 161 etediTFSTL--VERVIQQLEGAFALVFKSIHYPGEAVATRRGSPLLIGvrskyklsteqipvlyptcnienvknicktr 238
Cdd:PRK00331 140 -----GGDLLeaVRKALKRLEGAYALAVIDKDEPDTIVAARNGSPLVIG------------------------------- 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080037 239 mkrldsstclhaVGDKavEFFFASDASAIIEHTNRVIFLEDDDIAAVADGKLSIHrvkrSATDDP-SRAIQTLQMELQQI 317
Cdd:PRK00331 184 ------------LGEG--ENFLASDALALLPYTRRVIYLEDGEIAVLTRDGVEIF----DFDGNPvEREVYTVDWDASAA 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080037 318 MKGNFSAFMQKEIFEQPESVFNTMRGRVNFetntvlLGGLKDHLKEIRRCRRLIVIGCGTSYHAAVATRQVLEELTELPV 397
Cdd:PRK00331 246 EKGGYRHFMLKEIYEQPEAIRDTLEGRLDE------LGEGELADEDLKKIDRIYIVACGTSYHAGLVAKYLIESLAGIPV 319
|
410 420 430
....*....|....*....|....*....|..
gi 1907080037 398 MVELASDFLDRNTPVFRDDVCFFISQSG-TSD 428
Cdd:PRK00331 320 EVEIASEFRYRDPVLSPKTLVIAISQSGeTAD 351
|
|
| GFAT |
cd00714 |
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ... |
2-285 |
1.61e-114 |
|
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus of glucosamine-6P synthase (GlmS, or GFAT in humans). The glutaminase domain catalyzes amide nitrogen transfer from glutamine to the appropriate substrate. In this process, glutamine is hydrolyzed to glutamic acid and ammonia. In humans, GFAT catalyzes the first and rate-limiting step of hexosamine metabolism, the conversion of D-fructose-6P (Fru6P) into D-glucosamine-6P using L-glutamine as a nitrogen source. The end product of this pathway, UDP-N-acetyl glucosamine, is a major building block of the bacterial peptidoglycan and fungal chitin.
Pssm-ID: 238366 [Multi-domain] Cd Length: 215 Bit Score: 335.19 E-value: 1.61e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080037 2 CGIFAYMNYRvpktrkEIFETLIRGLQRLEYRGYDSAGVAIDGNNHevkerhIHLVKKRGKVKALDEELYKQDSmdlkve 81
Cdd:cd00714 1 CGIVGYIGKR------EAVDILLEGLKRLEYRGYDSAGIAVIGDGS------LEVVKAVGKVANLEEKLAEKPL------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080037 82 fETHFGIAHTRWATHGVPNAVNSHPQRSDkDNEFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIAKLIKYVFDnre 161
Cdd:cd00714 63 -SGHVGIGHTRWATHGEPTDVNAHPHRSC-DGEIAVVHNGIIENYAELKEELEAKGYKFESETDTEVIAHLIEYYYD--- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080037 162 tEDITFSTLVERVIQQLEGAFALVFKSIHYPGEAVATRRGSPLLIGVrskyklsteqipvlyptcnienvknicktrmkr 241
Cdd:cd00714 138 -GGLDLLEAVKKALKRLEGAYALAVISKDEPDEIVAARNGSPLVIGI--------------------------------- 183
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1907080037 242 ldsstclhavgdKAVEFFFASDASAIIEHTNRVIFLEDDDIAAV 285
Cdd:cd00714 184 ------------GDGENFVASDAPALLEHTRRVIYLEDGDIAVI 215
|
|
| glmS |
TIGR01135 |
glucosamine--fructose-6-phosphate aminotransferase (isomerizing); The member from ... |
2-428 |
1.02e-106 |
|
glucosamine--fructose-6-phosphate aminotransferase (isomerizing); The member from Methanococcus jannaschii contains an intein. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan, Central intermediary metabolism, Amino sugars]
Pssm-ID: 273462 [Multi-domain] Cd Length: 607 Bit Score: 328.83 E-value: 1.02e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080037 2 CGIFAYMnyrvpkTRKEIFETLIRGLQRLEYRGYDSAGVAIdgnnheVKERHIHLVKKRGKVKALDEELYKQdsmdlkvE 81
Cdd:TIGR01135 1 CGIVGYI------GQRDAVPILLEGLKRLEYRGYDSAGIAV------VDEGKLFVRKAVGKVAELANKLGEK-------P 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080037 82 FETHFGIAHTRWATHGVPNAVNSHPQRsDKDNEFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIAKLIKYVFdnRE 161
Cdd:TIGR01135 62 LPGGVGIGHTRWATHGKPTDENAHPHT-DEGGRIAVVHNGIIENYAELREELEARGHVFSSDTDTEVIAHLIEEEL--RE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080037 162 TEDITFStlVERVIQQLEGAFALVFKSIHYPGEAVATRRGSPLLIGvrskyklsteqipvlyptcnienvknicktrmkr 241
Cdd:TIGR01135 139 GGDLLEA--VQKALKQLRGAYALAVLHADHPETLVAARSGSPLIVG---------------------------------- 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080037 242 ldsstclhaVGDKavEFFFASDASAIIEHTNRVIFLEDDDIAAVADGKLSIHrvkrSATDDP-SRAIQTLQMELQQIMKG 320
Cdd:TIGR01135 183 ---------LGDG--ENFVASDVTALLPYTRRVIYLEDGDIAILTKDGVEIY----NFEGAPvQREVRVIDWDLDAAEKG 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080037 321 NFSAFMQKEIFEQPESVFNTMRGRVNFETNTVLLGGLKDHLKEIrrcRRLIVIGCGTSYHAAVATRQVLEELTELPVMVE 400
Cdd:TIGR01135 248 GYRHFMLKEIYEQPRALRDTLEGRIEENGGVFEELGAEELLKNI---DRIQIVACGTSYHAGLVAKYLIERLAGIPVEVE 324
|
410 420
....*....|....*....|....*....
gi 1907080037 401 LASDFLDRNTPVFRDDVCFFISQSG-TSD 428
Cdd:TIGR01135 325 IASEFRYRKPVVDKDTLVIAISQSGeTAD 353
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
1-428 |
7.54e-67 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 225.29 E-value: 7.54e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080037 1 MCGIFAYMnyrvpkTRKEIFETLIRGLQRLEYRGYDSAGVA-IDGNNHEVKERHIHLVKKRGKVKALDEELykqdsmdLK 79
Cdd:PTZ00295 24 CCGIVGYL------GNEDASKILLEGIEILQNRGYDSCGIStISSGGELKTTKYASDGTTSDSIEILKEKL-------LD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080037 80 VEFETHFGIAHTRWATHGVPNAVNSHPQrSDKDNEFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIAKLIKYVFDN 159
Cdd:PTZ00295 91 SHKNSTIGIAHTRWATHGGKTDENAHPH-CDYKKRIALVHNGTIENYVELKSELIAKGIKFRSETDSEVIANLIGLELDQ 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080037 160 REtediTFSTLVERVIQQLEGAFALVFKSIHYPGEAVATRRGSPLLIGVRSKyklsteqipvlyptcnienvknicktrm 239
Cdd:PTZ00295 170 GE----DFQEAVKSAISRLQGTWGLCIIHKDNPDSLIVARNGSPLLVGIGDD---------------------------- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080037 240 krldsstclhavgdkavEFFFASDASAIIEHTNRVIFLEDDDIAavadgklSIHRVKRSATDDPSRAIQtLQMELQQIMK 319
Cdd:PTZ00295 218 -----------------SIYVASEPSAFAKYTNEYISLKDGEIA-------ELSLENVNDLYTQRRVEK-IPEEVIEKSP 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080037 320 GNFSAFMQKEIFEQPESVFNTM--RGRVNFETNTVLLGGLKDHLKEIRRCRRLIVIGCGTSYHAAVATRQVLEELTEL-P 396
Cdd:PTZ00295 273 EPYPHWTLKEIFEQPIALSRALnnGGRLSGYNNRVKLGGLDQYLEELLNIKNLILVGCGTSYYAALFAASIMQKLKCFnT 352
|
410 420 430
....*....|....*....|....*....|....*
gi 1907080037 397 VMVELASDF-LDRNTpvfRDDVCF-FISQSG-TSD 428
Cdd:PTZ00295 353 VQVIDASELtLYRLP---DEDAGViFISQSGeTLD 384
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
2-283 |
8.82e-55 |
|
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide nitrogen transfer from glutamine to the appropriate substrate. In this process, glutamine is hydrolyzed to glutamic acid and ammonia. This domain is related to members of the Ntn (N-terminal nucleophile) hydrolase superfamily and is found at the N-terminus of enzymes such as glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), beta lactam synthetase (beta-LS) and glutamate synthase (GltS). GLMS catalyzes the formation of glucosamine 6-phosphate from fructose 6-phosphate and glutamine in amino sugar synthesis. GPATase catalyzes the first step in purine biosynthesis, an amide transfer from glutamine to PRPP, resulting in phosphoribosylamine, pyrophosphate and glutamate. Asparagine synthetase B synthesizes asparagine from aspartate and glutamine. Beta-LS catalyzes the formation of the beta-lactam ring in the beta-lactamase inhibitor clavulanic acid. GltS synthesizes L-glutamate from 2-oxoglutarate and L-glutamine. These enzymes are generally dimers, but GPATase also exists as a homotetramer.
Pssm-ID: 238212 [Multi-domain] Cd Length: 220 Bit Score: 181.88 E-value: 8.82e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080037 2 CGIFAYMNYRVPKTRKEIfeTLIRGLQRLEYRGYDSAGVAIDGNnhevkeRHIHLVKKRGKVKALDEELykqdsmdLKVE 81
Cdd:cd00352 1 CGIFGIVGADGAASLLLL--LLLRGLAALEHRGPDGAGIAVYDG------DGLFVEKRAGPVSDVALDL-------LDEP 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080037 82 FETHFGIAHTRWATHGVPNAVNSHPQRSDkDNEFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIAKLIKYVFDNRE 161
Cdd:cd00352 66 LKSGVALGHVRLATNGLPSEANAQPFRSE-DGRIALVHNGEIYNYRELREELEARGYRFEGESDSEVILHLLERLGREGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080037 162 TEDitfstLVERVIQQLEGAFALVFKSIHyPGEAVATRRG---SPLLIGVRskyklsteqipvlyptcnienvknicktr 238
Cdd:cd00352 145 LFE-----AVEDALKRLDGPFAFALWDGK-PDRLFAARDRfgiRPLYYGIT----------------------------- 189
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1907080037 239 mkrldsstclhavgdKAVEFFFASDASAIIEHT-NRVIFLEDDDIA 283
Cdd:cd00352 190 ---------------KDGGLVFASEPKALLALPfKGVRRLPPGELL 220
|
|
| PurF |
COG0034 |
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ... |
1-186 |
5.52e-24 |
|
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; Glutamine phosphoribosylpyrophosphate amidotransferase is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439804 [Multi-domain] Cd Length: 464 Bit Score: 103.95 E-value: 5.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080037 1 MCGIFAYMNyrvpktRKEIFETLIRGLQRLEYRGYDSAG-VAIDGNnhevkerHIHLVKKRGKVKaldeELYKQDSMDlk 79
Cdd:COG0034 7 ECGVFGIYG------HEDVAQLTYYGLYALQHRGQESAGiATSDGG-------RFHLHKGMGLVS----DVFDEEDLE-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080037 80 vEFETHFGIAHTRWATHGVPNAVNSHP-QRSDKDNEFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIAKLIKyvfd 158
Cdd:COG0034 68 -RLKGNIAIGHVRYSTTGSSSLENAQPfYVNSPFGSIALAHNGNLTNAEELREELEEEGAIFQTTSDTEVILHLIA---- 142
|
170 180
....*....|....*....|....*...
gi 1907080037 159 nRETEDITFSTLVERVIQQLEGAFALVF 186
Cdd:COG0034 143 -RELTKEDLEEAIKEALRRVKGAYSLVI 169
|
|
| GPATase_N |
cd00715 |
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ... |
2-186 |
1.03e-23 |
|
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the N-terminus of glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase) . The glutaminase domain catalyzes amide nitrogen transfer from glutamine to the appropriate substrate. In this process, glutamine is hydrolyzed to glutamic acid and ammonia. GPATase catalyzes the first step in purine biosynthesis, an amide transfer from glutamine to PRPP, resulting in phosphoribosylamine, pyrophosphate and glutamate. GPATase crystalizes as a homotetramer, but can also exist as a homdimer.
Pssm-ID: 238367 [Multi-domain] Cd Length: 252 Bit Score: 99.46 E-value: 1.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080037 2 CGIFAYMNyrvpktRKEIFETLIRGLQRLEYRGYDSAGVAIDGNNHevkerhIHLVKKRGKVkaldEELYKQDSMDlkvE 81
Cdd:cd00715 1 CGVFGIYG------AEDAARLTYLGLYALQHRGQESAGIATSDGKR------FHTHKGMGLV----SDVFDEEKLR---R 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080037 82 FETHFGIAHTRWATHGVPNAVNSHPQRSD-KDNEFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIAKLIKyvfdnR 160
Cdd:cd00715 62 LPGNIAIGHVRYSTAGSSSLENAQPFVVNsPLGGIALAHNGNLVNAKELREELEEEGRIFQTTSDSEVILHLIA-----R 136
|
170 180
....*....|....*....|....*.
gi 1907080037 161 ETEDITFSTLVERVIQQLEGAFALVF 186
Cdd:cd00715 137 SLAKDDLFEAIIDALERVKGAYSLVI 162
|
|
| SIS_GlmS_GlmD_1 |
cd05008 |
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
369-427 |
2.81e-21 |
|
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and Glucosamine-6-phosphate deaminase (GlmD). The SIS domain is found in many phosphosugar isomerases and phosphosugar binding proteins. GlmS contains a N-terminal glutaminase domain and two C-terminal SIS domains and catalyzes the first step in hexosamine metabolism, converting fructose 6-phosphate into glucosamine 6-phosphate using glutamine as nitrogen source. The glutaminase domain hydrolyzes glutamine to glutamate and ammonia. Ammonia is transferred through a channel to the isomerase domain for glucosamine 6-phosphate synthesis. The end product of the pathway is N-acetylglucosamine, which plays multiple roles in eukaryotic cells including being a building block of bacterial and fungal cell walls. In the absence of glutamine, GlmS catalyzes the isomerization of fructose 6-phosphate into glucose 6- phosphate (PGI-like activity). Glucosamine-6-phosphate deaminase (GlmD) contains two SIS domains and catalyzes the deamination and isomerization of glucosamine-6-phosphate into fructose-6-phosphate with the release of ammonia; in presence of high ammonia concentration, GlmD can catalyze the reverse reaction.
Pssm-ID: 240141 [Multi-domain] Cd Length: 126 Bit Score: 89.09 E-value: 2.81e-21
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907080037 369 RLIVIGCGTSYHAAVATRQVLEELTELPVMVELASDFLDRNTPVFRDDVCFFISQSGTS 427
Cdd:cd05008 1 RILIVGCGTSYHAALVAKYLLERLAGIPVEVEAASEFRYRRPLLDEDTLVIAISQSGET 59
|
|
| purF |
TIGR01134 |
amidophosphoribosyltransferase; Alternate name: glutamine phosphoribosylpyrophosphate (PRPP) ... |
2-217 |
9.67e-19 |
|
amidophosphoribosyltransferase; Alternate name: glutamine phosphoribosylpyrophosphate (PRPP) amidotransferase. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 273461 [Multi-domain] Cd Length: 442 Bit Score: 88.15 E-value: 9.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080037 2 CGIFAYMNyrvpkTRKEIFETLIRGLQRLEYRGYDSAGVAIDGNNHevkerhIHLVKKRGKVKaldeELYKQDSMDlkvE 81
Cdd:TIGR01134 1 CGVVGIYG-----QEEVAASLTYYGLYALQHRGQESAGISVFDGNR------FRLHKGNGLVS----DVFNEEHLQ---R 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080037 82 FETHFGIAHTRWATHGVPNAVNSHPQRSDKDNEFVVI-HNGIITNYKDLRKFLESKGYEFESETDTETIAKLIKyvfdNR 160
Cdd:TIGR01134 63 LKGNVGIGHVRYSTAGSSGLENAQPFVVNSPYGGLALaHNGNLVNADELRRELEEEGRHFNTTSDSEVLLHLLA----HN 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907080037 161 ETEDITFSTLVERVIQQLEGAFALVFKSIHypgEAVATR--RG-SPLLIGVR-SKYKLSTE 217
Cdd:TIGR01134 139 DESKDDLFDAVARVLERVRGAYALVLMTED---GLVAVRdpHGiRPLVLGRRgDGYVVASE 196
|
|
| PLN02440 |
PLN02440 |
amidophosphoribosyltransferase |
1-210 |
5.64e-18 |
|
amidophosphoribosyltransferase
Pssm-ID: 215241 [Multi-domain] Cd Length: 479 Bit Score: 85.88 E-value: 5.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080037 1 MCGIFAYmnYRVPKTRKEIFEtlirGLQRLEYRGYDSAG-VAIDGNNhevkerhIHLVKKRGKVKaldeELYKQDSMDlk 79
Cdd:PLN02440 1 ECGVVGI--FGDPEASRLCYL----GLHALQHRGQEGAGiVTVDGNR-------LQSITGNGLVS----DVFDESKLD-- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080037 80 vEFETHFGIAHTRWATHGVPNAVNSHPqrsdkdneFV---------VIHNGIITNYKDLRKFLESKGYEFESETDTETIA 150
Cdd:PLN02440 62 -QLPGDIAIGHVRYSTAGASSLKNVQP--------FVanyrfgsigVAHNGNLVNYEELRAKLEENGSIFNTSSDTEVLL 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907080037 151 KLIkyvfdnreTEDI--TFSTLVERVIQQLEGAFALVFKSihyPGEAVATR-----RgsPLLIGVRS 210
Cdd:PLN02440 133 HLI--------AISKarPFFSRIVDACEKLKGAYSMVFLT---EDKLVAVRdphgfR--PLVMGRRS 186
|
|
| GATase_6 |
pfam13522 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
82-186 |
5.32e-16 |
|
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain found in a variety of enzymes, such as asparagine synthetase and glutamine--fructose-6-phosphate transaminase.
Pssm-ID: 433279 [Multi-domain] Cd Length: 130 Bit Score: 74.26 E-value: 5.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080037 82 FETHFGIAHTRWATHGVPNAVNsHPQRSdKDNEFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIAKLIKYvfdnre 161
Cdd:pfam13522 8 VEGGVALGHVRLAIVDLPDAGN-QPMLS-RDGRLVLVHNGEIYNYGELREELADLGHAFRSRSDTEVLLALYEE------ 79
|
90 100
....*....|....*....|....*
gi 1907080037 162 teditfstLVERVIQQLEGAFALVF 186
Cdd:pfam13522 80 --------WGEDCLERLRGMFAFAI 96
|
|
| PRK05793 |
PRK05793 |
amidophosphoribosyltransferase; Provisional |
26-185 |
3.99e-15 |
|
amidophosphoribosyltransferase; Provisional
Pssm-ID: 235611 [Multi-domain] Cd Length: 469 Bit Score: 77.38 E-value: 3.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080037 26 GLQRLEYRGYDSAGVAI-DGnnhevkeRHIHLVKKRGKV-KALDEELYKqdsmdlkvEFETHFGIAHTRWATHGVPNAVN 103
Cdd:PRK05793 35 GLYALQHRGQESAGIAVsDG-------EKIKVHKGMGLVsEVFSKEKLK--------GLKGNSAIGHVRYSTTGASDLDN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080037 104 SHPQRSDKDNEFVVI-HNGIITNYKDLRKFLESKGYEFESETDTETIAKLI----KYVFDNreteditfsTLVErVIQQL 178
Cdd:PRK05793 100 AQPLVANYKLGSIAIaHNGNLVNADVIRELLEDGGRIFQTSIDSEVILNLIarsaKKGLEK---------ALVD-AIQAI 169
|
....*..
gi 1907080037 179 EGAFALV 185
Cdd:PRK05793 170 KGSYALV 176
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
363-425 |
9.33e-15 |
|
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars. Presumably the SIS domains bind to the end-product of the pathway.
Pssm-ID: 426230 [Multi-domain] Cd Length: 131 Bit Score: 70.79 E-value: 9.33e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907080037 363 EIRRCRRLIVIGCGTSYHAAVATRQVLEELTELPVMVELASDFLDR-NTPVFRDDVCFFISQSG 425
Cdd:pfam01380 1 LLAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGvLALVDEDDLVIAISYSG 64
|
|
| GlxB |
cd01907 |
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ... |
2-155 |
3.14e-14 |
|
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine amidotransferase-like protein of unknown function found in bacteria and archaea. GlxB has a structural fold similar to that of other class II glutamine amidotransferases including glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), beta lactam synthetase (beta-LS) and glutamate synthase (GltS). The GlxB fold is also somewhat similar to the Ntn (N-terminal nucleophile) hydrolase fold of the proteasomal alpha and beta subunits.
Pssm-ID: 238888 [Multi-domain] Cd Length: 249 Bit Score: 72.30 E-value: 3.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080037 2 CGIFAYMNyrvPKTRKEIFETLIRGLQRLEYRG-YDSAGVAIDGNNHEvkerhihLVKKRGKvkalDEELYKQ------- 73
Cdd:cd01907 1 CGIFGIMS---KDGEPFVGALLVEMLDAMQERGpGDGAGFALYGDPDA-------FVYSSGK----DMEVFKGvgypedi 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080037 74 -DSMDLKvEFETHFGIAHTRWATHGVPNAVNSHPqrsdkdneF-----VVIHNGIITNYKDLRKFLESKGYEFESETDTE 147
Cdd:cd01907 67 aRRYDLE-EYKGYHWIAHTRQPTNSAVWWYGAHP--------FsigdiAVVHNGEISNYGSNREYLERFGYKFETETDTE 137
|
....*...
gi 1907080037 148 TIAKLIKY 155
Cdd:cd01907 138 VIAYYLDL 145
|
|
| GATase_7 |
pfam13537 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
90-185 |
7.64e-14 |
|
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain found in a variety of enzymes such as asparagine synthetase and glutamine-fructose-6-phosphate transaminase.
Pssm-ID: 433289 [Multi-domain] Cd Length: 123 Bit Score: 67.93 E-value: 7.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080037 90 HTRWATHGVPNAvnSHPQRSDKDNEFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIAKLIKYVFdnreteditfst 169
Cdd:pfam13537 1 HRRLSIIDLEGG--AQPMVSSEDGRYVIVFNGEIYNYRELRAELEAKGYRFRTHSDTEVILHLYEAEW------------ 66
|
90
....*....|....*.
gi 1907080037 170 lVERVIQQLEGAFALV 185
Cdd:pfam13537 67 -GEDCVDRLNGMFAFA 81
|
|
| AgaS |
COG2222 |
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ... |
328-427 |
6.52e-13 |
|
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441824 [Multi-domain] Cd Length: 336 Bit Score: 69.54 E-value: 6.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080037 328 KEIFEQPESVfntmrgRVNFETNTVLLGGLKDHLKEIRRcRRLIVIGCGTSYHAAVATRQVLEELTELPVMVELASDFLD 407
Cdd:COG2222 2 REIAQQPEAW------RRALAALAAAIAALLARLRAKPP-RRVVLVGAGSSDHAAQAAAYLLERLLGIPVAALAPSELVV 74
|
90 100
....*....|....*....|.
gi 1907080037 408 RNTPVFRD-DVCFFISQSGTS 427
Cdd:COG2222 75 YPAYLKLEgTLVVAISRSGNS 95
|
|
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
1-152 |
1.52e-12 |
|
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; Asparagine synthetase B (glutamine-hydrolyzing) is part of the Pathway/BioSystem: Asparagine biosynthesis
Pssm-ID: 440136 [Multi-domain] Cd Length: 558 Bit Score: 69.48 E-value: 1.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080037 1 MCGIFAYMNYRVPKTRkeifETLIRGLQRLEYRGYDSAGVAIDGnnhevkerhihlvkkrgkvkaldeelykqdsmdlkv 80
Cdd:COG0367 1 MCGIAGIIDFDGGADR----EVLERMLDALAHRGPDGSGIWVDG------------------------------------ 40
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907080037 81 efetHFGIAHTRWAThgVPNAVNSHpQ-RSDKDNEFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIAKL 152
Cdd:COG0367 41 ----GVALGHRRLSI--IDLSEGGH-QpMVSEDGRYVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHA 106
|
|
| AsnB |
cd00712 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ... |
2-152 |
2.54e-12 |
|
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine synthetase B catalyses the ATP-dependent conversion of aspartate to asparagine. This enzyme is a homodimer, with each monomer composed of a glutaminase domain and a synthetase domain. The N-terminal glutaminase domain hydrolyzes glutamine to glutamic acid and ammonia.
Pssm-ID: 238364 [Multi-domain] Cd Length: 220 Bit Score: 66.04 E-value: 2.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080037 2 CGIFAYMNYRvpkTRKEIFETLIRGLQRLEYRGYDSAGVAIDGNnhevkerhihlvkkrgkvkaldeelykqdsmdlkve 81
Cdd:cd00712 1 CGIAGIIGLD---GASVDRATLERMLDALAHRGPDGSGIWIDEG------------------------------------ 41
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907080037 82 fethFGIAHTRWATHGVpnavnSH---PQRSDkDNEFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIAKL 152
Cdd:cd00712 42 ----VALGHRRLSIIDL-----SGgaqPMVSE-DGRLVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHL 105
|
|
| asn_synth_AEB |
TIGR01536 |
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing ... |
83-186 |
3.36e-08 |
|
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing asparagine synthase. A poorly conserved C-terminal extension was removed from the model. Bacterial members of the family tend to have a long, poorly conserved insert lacking from archaeal and eukaryotic sequences. Multiple isozymes have been demonstrated, such as in Bacillus subtilis. Long-branch members of the phylogenetic tree (which typically were also second or third candidate members from their genomes) were removed from the seed alignment and score below trusted cutoff. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 273676 [Multi-domain] Cd Length: 466 Bit Score: 55.42 E-value: 3.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080037 83 ETHFGIAHTRWATHGVPNAVnsHPQRSDKDnEFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIAKLIkyvfdnRET 162
Cdd:TIGR01536 39 DGNAILGHRRLAIIDLSGGA--QPMSNEGK-TYVIVFNGEIYNHEELREELEAKGYTFQTDSDTEVILHLY------EEW 109
|
90 100
....*....|....*....|....
gi 1907080037 163 EditfstlvERVIQQLEGAFALVF 186
Cdd:TIGR01536 110 G--------EECVDRLDGMFAFAL 125
|
|
| PTZ00077 |
PTZ00077 |
asparagine synthetase-like protein; Provisional |
1-154 |
3.41e-08 |
|
asparagine synthetase-like protein; Provisional
Pssm-ID: 185431 [Multi-domain] Cd Length: 586 Bit Score: 55.88 E-value: 3.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080037 1 MCGIFAYMNYrvpKTRKEIFETLIRGL-QRLEYRGYDSAGVAIdgnnhevkerhihlvkkrgkvkaldeelykqdsmdLK 79
Cdd:PTZ00077 1 MCGILAIFNS---KGERHELRRKALELsKRLRHRGPDWSGIIV-----------------------------------LE 42
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907080037 80 VEFETHFGIAHTRWATHGVpnaVNSHPQRSDKDNEFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIAKLIK 154
Cdd:PTZ00077 43 NSPGTYNILAHERLAIVDL---SDGKQPLLDDDETVALMQNGEIYNHWEIRPELEKEGYKFSSNSDCEIIGHLYK 114
|
|
| asnB |
PRK09431 |
asparagine synthetase B; Provisional |
1-185 |
6.67e-07 |
|
asparagine synthetase B; Provisional
Pssm-ID: 236513 [Multi-domain] Cd Length: 554 Bit Score: 51.45 E-value: 6.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080037 1 MCGIFAYmnYRVPKTRKEIFETLIRGLQRLEYRGYDSAGVAIDGNnhevkerhihlvkkrgkvkaldeelykqdsmdlkv 80
Cdd:PRK09431 1 MCGIFGI--LDIKTDADELRKKALEMSRLMRHRGPDWSGIYASDN----------------------------------- 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080037 81 efethfGI-AHTRWATHGVPNavnSHPQRSDKDNEFVVIHNGIITNYKDLRKFLESKgYEFESETDTETIAKLikYvfdn 159
Cdd:PRK09431 44 ------AIlGHERLSIVDVNG---GAQPLYNEDGTHVLAVNGEIYNHQELRAELGDK-YAFQTGSDCEVILAL--Y---- 107
|
170 180
....*....|....*....|....*.
gi 1907080037 160 rETEDITFstlvervIQQLEGAFALV 185
Cdd:PRK09431 108 -QEKGPDF-------LDDLDGMFAFA 125
|
|
| YafJ |
COG0121 |
Predicted glutamine amidotransferase YafJ [General function prediction only]; |
83-153 |
1.46e-06 |
|
Predicted glutamine amidotransferase YafJ [General function prediction only];
Pssm-ID: 439891 [Multi-domain] Cd Length: 248 Bit Score: 49.19 E-value: 1.46e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907080037 83 ETHFGIAHTRWATHGVPNAVNSHPQRSDkdnEFVVIHNGIITNYKDLRKFLESK-----GYEFESETDTETIAKLI 153
Cdd:COG0121 75 KSRLVIAHVRKATVGPVSLENTHPFRGG---RWLFAHNGQLDGFDRLRRRLAEElpdelYFQPVGTTDSELAFALL 147
|
|
| YafJ |
cd01908 |
Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine ... |
88-178 |
7.06e-06 |
|
Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine amidotransferase-like protein of unknown function found in prokaryotes, eukaryotes and archaea. YafJ has a conserved structural fold similar to those of other class II glutamine amidotransferases including glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), beta lactam synthetase (beta-LS) and glutamate synthase (GltS). The YafJ fold is also somewhat similar to the Ntn (N-terminal nucleophile) hydrolase fold of the proteasomal alpha and beta subunits.
Pssm-ID: 238889 [Multi-domain] Cd Length: 257 Bit Score: 47.38 E-value: 7.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080037 88 IAHTRWATHGVPNAVNSHPQRSDkdnEFVVIHNGIITNYKDLR-KFLESKGYEFESETDTETIAKLIkyvFDNRETEDIT 166
Cdd:cd01908 84 LAHVRAATVGPVSLENCHPFTRG---RWLFAHNGQLDGFRLLRrRLLRLLPRLPVGTTDSELAFALL---LSRLLERDPL 157
|
90
....*....|..
gi 1907080037 167 FSTLVERVIQQL 178
Cdd:cd01908 158 DPAELLDAILQT 169
|
|
| SIS |
cd04795 |
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
370-432 |
9.89e-06 |
|
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars.
Pssm-ID: 240112 [Multi-domain] Cd Length: 87 Bit Score: 43.90 E-value: 9.89e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907080037 370 LIVIGCGTSYHAAVATRQVLEELTELPVMVELASDFLDRNTPVF--RDDVCFFISQSGTSDRPKK 432
Cdd:cd04795 1 IFVIGIGGSGAIAAYFALELLELTGIEVVALIATELEHASLLSLlrKGDVVIALSYSGRTEELLA 65
|
|
| PLN02549 |
PLN02549 |
asparagine synthase (glutamine-hydrolyzing) |
1-185 |
7.32e-05 |
|
asparagine synthase (glutamine-hydrolyzing)
Pssm-ID: 178164 [Multi-domain] Cd Length: 578 Bit Score: 45.14 E-value: 7.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080037 1 MCGIFAYMNYRVPKTRKEifeTLIRGL-QRLEYRGYDSAGVAIDGNnhevkerhihlvkkrgkvkaldeelykqdsmdlk 79
Cdd:PLN02549 1 MCGILAVLGCSDDSQAKR---SRVLELsRRLRHRGPDWSGLYGNED---------------------------------- 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080037 80 vefethFGIAHTRWAThgVPNAVNSHPQRSDkDNEFVVIHNGIITNYKDLRKFLESkgYEFESETDTETIAKLIKYVFdn 159
Cdd:PLN02549 44 ------CYLAHERLAI--MDPESGDQPLYNE-DKTIVVTANGEIYNHKELREKLKL--HKFRTGSDCEVIAHLYEEHG-- 110
|
170 180
....*....|....*....|....*.
gi 1907080037 160 reteditfstlvERVIQQLEGAFALV 185
Cdd:PLN02549 111 ------------EEFVDMLDGMFSFV 124
|
|
| SIS_1 |
cd05710 |
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ... |
369-426 |
2.35e-04 |
|
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars.
Pssm-ID: 240214 [Multi-domain] Cd Length: 120 Bit Score: 40.64 E-value: 2.35e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907080037 369 RLIVIGCGTSYHAAVATRQVLEELTELPVMVELASDFLDRNTPVFRDD-VCFFISQSGT 426
Cdd:cd05710 1 NVFFVGCGGSLADMYPAKYFLKKESKLPVFVYNAAEFLHTGPKRLTEKsVVILASHSGN 59
|
|
| GATase_4 |
pfam13230 |
Glutamine amidotransferases class-II; This family captures members that are not found in ... |
81-149 |
2.50e-03 |
|
Glutamine amidotransferases class-II; This family captures members that are not found in pfam00310.
Pssm-ID: 433047 [Multi-domain] Cd Length: 272 Bit Score: 39.62 E-value: 2.50e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080037 81 EFETHFGIAHTRWATHGVPNAVNSHP-QRSDKDNEFVVIHNGIITNYKDLRkfleSKGYEFESETDTETI 149
Cdd:pfam13230 68 PIRSRNVIAHIRKATQGRVTLENTHPfMRELWGRYWIFAHNGDLKGYAPKL----SGRFQPVGSTDSELA 133
|
|
| |
