|
Name |
Accession |
Description |
Interval |
E-value |
| GlmS |
COG0449 |
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ... |
1-609 |
0e+00 |
|
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: 1082.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 1 MCGIVGAIAQRDVAEILLEGLRRLEYRGYDSAGLAVVDaEGHMTRLRRLGKVQMLAQAAEEHPLHGGTGIAHTRWATHGE 80
Cdd:COG0449 1 MCGIVGYIGKRDAAPILLEGLKRLEYRGYDSAGIAVLD-DGGLEVRKAVGKLANLEEKLAEEPLSGTIGIGHTRWATHGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 81 PSEVNAHPHVS--EHIVVVHNGIIENHEPLREELKARGYTFVSETDTEVIAHLVNWELKQGGTLREAVLRAIPQLRGAYG 158
Cdd:COG0449 80 PSDENAHPHTScsGRIAVVHNGIIENYAELREELEAKGHTFKSETDTEVIAHLIEEYLKGGGDLLEAVRKALKRLEGAYA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 159 TVIMDSRHPDTLLAARSGSPLVIGLGMGENFIASDQLALLPVTRRFIFLEEGDIAEITRRSVNIFDKTGAEVKRQDIESN 238
Cdd:COG0449 160 LAVISADEPDRIVAARKGSPLVIGLGEGENFLASDVPALLPYTRRVIYLEDGEIAVLTRDGVEIYDLDGEPVEREVKTVD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 239 LQYDAGDKGIYRHYMQKEIYEQPNAIKNTLTGRIS-HGQVDLSELgPNADELLSKVEHIQILACGTSYNSGMVSRYWFES 317
Cdd:COG0449 240 WDAEAAEKGGYPHFMLKEIHEQPEAIRDTLRGRLDeDGRVVLDEL-NLAAEDLRNIDRIYIVACGTSYHAGLVGKYLIEE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 318 LAGIPCDVEIASEFRYRKSAVRRNSLMITLSQSGETADTLAGLRLSKELGyLGSLAICNVPGSSLVRESDLALMTNAGTE 397
Cdd:COG0449 319 LARIPVEVEIASEFRYRDPVVDPGTLVIAISQSGETADTLAALREAKEKG-AKVLAICNVVGSTIARESDAVLYTHAGPE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 398 IGVASTKAFTTQLTVLLMLVAKLSRLKG-LDASIEHDIVHGLQALPSRIEQMLSQDKRIEALAEDFSDKHHALFLGRGDQ 476
Cdd:COG0449 398 IGVASTKAFTTQLAALYLLALYLARARGtLSAEEEAELLEELRKLPEKIEEVLDLEEQIEELAEKYADARNALFLGRGIN 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 477 YPIALEGALKLKEISYIHAEAYAAGELKHGPLALIDADMPVIVVAPNNELLEKLKSNIEEVRARGGQLYVFAEQDAGFVS 556
Cdd:COG0449 478 YPVALEGALKLKEISYIHAEGYAAGELKHGPIALIDEGMPVVAIAPQDELYEKTLSNIQEVKARGGKVIAIADEGDEEVE 557
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 15833925 557 SDNMHIIEMPNVEEVIAPIFYTVPLQLLAYHVALIKGTDVDQPRNLAKSVTVE 609
Cdd:COG0449 558 ELADDVIEVPEVDELLAPILAVVPLQLLAYHVAVLRGTDVDQPRNLAKSVTVE 610
|
|
| PRK00331 |
PRK00331 |
isomerizing glutamine--fructose-6-phosphate transaminase; |
1-609 |
0e+00 |
|
isomerizing glutamine--fructose-6-phosphate transaminase;
Pssm-ID: 234729 [Multi-domain] Cd Length: 604 Bit Score: 1078.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 1 MCGIVGAIAQRDVAEILLEGLRRLEYRGYDSAGLAVVDaEGHMTRLRRLGKVQMLAQAAEEHPLHGGTGIAHTRWATHGE 80
Cdd:PRK00331 1 MCGIVGYVGQRNAAEILLEGLKRLEYRGYDSAGIAVLD-DGGLEVRKAVGKVANLEAKLEEEPLPGTTGIGHTRWATHGK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 81 PSEVNAHPHVS--EHIVVVHNGIIENHEPLREELKARGYTFVSETDTEVIAHLVNWELKQGGTLREAVLRAIPQLRGAYG 158
Cdd:PRK00331 80 PTERNAHPHTDcsGRIAVVHNGIIENYAELKEELLAKGHVFKSETDTEVIAHLIEEELKEGGDLLEAVRKALKRLEGAYA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 159 TVIMDSRHPDTLLAARSGSPLVIGLGMGENFIASDQLALLPVTRRFIFLEEGDIAEITRRSVNIFDKTGAEVKRQDIESN 238
Cdd:PRK00331 160 LAVIDKDEPDTIVAARNGSPLVIGLGEGENFLASDALALLPYTRRVIYLEDGEIAVLTRDGVEIFDFDGNPVEREVYTVD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 239 LQYDAGDKGIYRHYMQKEIYEQPNAIKNTLTGRIshgqvDLSELGPNADELLSKVEHIQILACGTSYNSGMVSRYWFESL 318
Cdd:PRK00331 240 WDASAAEKGGYRHFMLKEIYEQPEAIRDTLEGRL-----DELGEGELADEDLKKIDRIYIVACGTSYHAGLVAKYLIESL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 319 AGIPCDVEIASEFRYRKSAVRRNSLMITLSQSGETADTLAGLRLSKELGyLGSLAICNVPGSSLVRESDLALMTNAGTEI 398
Cdd:PRK00331 315 AGIPVEVEIASEFRYRDPVLSPKTLVIAISQSGETADTLAALRLAKELG-AKTLAICNVPGSTIARESDAVLYTHAGPEI 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 399 GVASTKAFTTQLTVLLMLVAKLSRLKG-LDASIEHDIVHGLQALPSRIEQMLSQDKRIEALAEDFSDKHHALFLGRGDQY 477
Cdd:PRK00331 394 GVASTKAFTAQLAVLYLLALALAKARGtLSAEEEADLVHELRELPALIEQVLDLKEQIEELAEDFADARNALFLGRGVDY 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 478 PIALEGALKLKEISYIHAEAYAAGELKHGPLALIDADMPVIVVAPNNELLEKLKSNIEEVRARGGQLYVFAEQDaGFVSS 557
Cdd:PRK00331 474 PVALEGALKLKEISYIHAEGYAAGELKHGPIALIDEGMPVVAIAPNDELYEKTKSNIQEVKARGARVIVIADEG-DEVAE 552
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 15833925 558 DNMHIIEMPNVEEVIAPIFYTVPLQLLAYHVALIKGTDVDQPRNLAKSVTVE 609
Cdd:PRK00331 553 EADDVIEVPEVHELLAPLLYVVPLQLLAYHVALARGTDVDKPRNLAKSVTVE 604
|
|
| glmS |
TIGR01135 |
glucosamine--fructose-6-phosphate aminotransferase (isomerizing); The member from ... |
2-609 |
0e+00 |
|
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: 1016.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 2 CGIVGAIAQRDVAEILLEGLRRLEYRGYDSAGLAVVDaEGHMTRLRRLGKVQMLAQAAEEHPLHGGTGIAHTRWATHGEP 81
Cdd:TIGR01135 1 CGIVGYIGQRDAVPILLEGLKRLEYRGYDSAGIAVVD-EGKLFVRKAVGKVAELANKLGEKPLPGGVGIGHTRWATHGKP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 82 SEVNAHPHVSEH--IVVVHNGIIENHEPLREELKARGYTFVSETDTEVIAHLVNWELKQGGTLREAVLRAIPQLRGAYGT 159
Cdd:TIGR01135 80 TDENAHPHTDEGgrIAVVHNGIIENYAELREELEARGHVFSSDTDTEVIAHLIEEELREGGDLLEAVQKALKQLRGAYAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 160 VIMDSRHPDTLLAARSGSPLVIGLGMGENFIASDQLALLPVTRRFIFLEEGDIAEITRRSVNIFDKTGAEVKRQDIESNL 239
Cdd:TIGR01135 160 AVLHADHPETLVAARSGSPLIVGLGDGENFVASDVTALLPYTRRVIYLEDGDIAILTKDGVEIYNFEGAPVQREVRVIDW 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 240 QYDAGDKGIYRHYMQKEIYEQPNAIKNTLTGRISHGQVDLSELGpnADELLSKVEHIQILACGTSYNSGMVSRYWFESLA 319
Cdd:TIGR01135 240 DLDAAEKGGYRHFMLKEIYEQPRALRDTLEGRIEENGGVFEELG--AEELLKNIDRIQIVACGTSYHAGLVAKYLIERLA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 320 GIPCDVEIASEFRYRKSAVRRNSLMITLSQSGETADTLAGLRLSKELGyLGSLAICNVPGSSLVRESDLALMTNAGTEIG 399
Cdd:TIGR01135 318 GIPVEVEIASEFRYRKPVVDKDTLVIAISQSGETADTLEALRLAKELG-AKTLGICNVPGSTLVREADHTLYTRAGPEIG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 400 VASTKAFTTQLTVLLMLVAKLSRLKG-LDASIEHDIVHGLQALPSRIEQMLSQDKRIEALAEDFSDKHHALFLGRGDQYP 478
Cdd:TIGR01135 397 VASTKAFTTQLTVLYLLALALAKARGtLSAEEEAELVDALRRLPDLVEQVLLADESIAELAERYADKRNFLFLGRGLGYP 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 479 IALEGALKLKEISYIHAEAYAAGELKHGPLALIDADMPVIVVAPNNELLEKLKSNIEEVRARGGQLYVFAEQDAGFVSSD 558
Cdd:TIGR01135 477 IALEGALKLKEISYIHAEGYPAGELKHGPIALIDEGLPVVAIAPKDSLLEKTKSNVEEVKARGARVIVFAPEDDETIASV 556
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 15833925 559 NMHIIEMPNVEEVIAPIFYTVPLQLLAYHVALIKGTDVDQPRNLAKSVTVE 609
Cdd:TIGR01135 557 ADDVIKLPEVEELLAPIVYTIPLQLLAYHIALAKGTDVDKPRNLAKSVTVE 607
|
|
| PLN02981 |
PLN02981 |
glucosamine:fructose-6-phosphate aminotransferase |
1-609 |
1.22e-174 |
|
glucosamine:fructose-6-phosphate aminotransferase
Pssm-ID: 215531 [Multi-domain] Cd Length: 680 Bit Score: 511.60 E-value: 1.22e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 1 MCGIVGAI------AQRDVAEILLEGLRRLEYRGYDSAGLAVvDAEGHMTR-----LRRLGKVQMLA----QAAEEHPLH 65
Cdd:PLN02981 1 MCGIFAYLnynvprERRFILEVLFNGLRRLEYRGYDSAGIAI-DNDPSLESssplvFREEGKIESLVrsvyEEVAETDLN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 66 GG------TGIAHTRWATHGEPSEVNAHPHVSE---HIVVVHNGIIENHEPLREELKARGYTFVSETDTEVIAHLVNW-- 134
Cdd:PLN02981 80 LDlvfenhAGIAHTRWATHGPPAPRNSHPQSSGpgnEFLVVHNGIITNYEVLKETLLRHGFTFESDTDTEVIPKLAKFvf 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 135 ----ELKQGGTLREAVLRAIPQLRGAYGtVIMDSRH-PDTLLAARSGSPLVIG---LGMGEN------------------ 188
Cdd:PLN02981 160 dklnEEEGDVTFSQVVMEVMRQLEGAYA-LIFKSPHyPNELVACKRGSPLLLGvkeLPEEKNssavftsegfltknrdkp 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 189 ---FIASDQLALLPVTRRFIFLEEGDIAEITRRSVNIF------------DKTGAEVKRQDIESNLQYDAGDKGIYRHYM 253
Cdd:PLN02981 239 kefFLASDASAVVEHTKRVLVIEDNEVVHLKDGGVGIYkfenekgrggggLSRPASVERALSTLEMEVEQIMKGNYDHYM 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 254 QKEIYEQPNAIKNTLTGRISHGQVDLSE---LGPNADEL--LSKVEHIQILACGTSYNSGMVSRYWFESLAGIPCDVEIA 328
Cdd:PLN02981 319 QKEIHEQPESLTTTMRGRLIRGGSGKAKrvlLGGLKDHLktIRRSRRIVFIGCGTSYNAALAARPILEELSGVPVTMELA 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 329 SEFRYRKSAVRRNSLMITLSQSGETADTLAGLRLSKELGYLgSLAICNVPGSSLVRESDLALMTNAGTEIGVASTKAFTT 408
Cdd:PLN02981 399 SDLLDRQGPIYREDTAVFVSQSGETADTLRALEYAKENGAL-CVGITNTVGSAISRGTHCGVHINAGAEIGVASTKAYTS 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 409 QLTVLLMLVAKLSRLKGLDASIEHDIVHGLQALPSRIEQMLSQDKRIEALAEDFSDKHHALFLGRGDQYPIALEGALKLK 488
Cdd:PLN02981 478 QIVAMTMLALALGEDSISSRSRREAIIDGLFDLPNKVREVLKLDQEMKELAELLIDEQSLLVFGRGYNYATALEGALKVK 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 489 EISYIHAEAYAAGELKHGPLALIDADMPVIVVAPNNELLEKLKSNIEEVRARGGQLYVFA-EQDAGFV-SSDNMHIIEMP 566
Cdd:PLN02981 558 EVALMHSEGILAGEMKHGPLALVDETLPIIVIATRDACFSKQQSVIQQLRARKGRLIVICsKGDASSVcPSGGCRVIEVP 637
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 15833925 567 NVEEVIAPIFYTVPLQLLAYHVALIKGTDVDQPRNLAKSVTVE 609
Cdd:PLN02981 638 QVEDCLQPVINIVPLQLLAYHLTVLRGHNVDQPRNLAKSVTTQ 680
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
1-608 |
5.81e-167 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 490.30 E-value: 5.81e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 1 MCGIVGAIAQRDVAEILLEGLRRLEYRGYDSAGLAVVDAEGHM--TRLRRLGK----VQMLAQAAEEHPLHGGTGIAHTR 74
Cdd:PTZ00295 24 CCGIVGYLGNEDASKILLEGIEILQNRGYDSCGISTISSGGELktTKYASDGTtsdsIEILKEKLLDSHKNSTIGIAHTR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 75 WATHGEPSEVNAHPHV--SEHIVVVHNGIIENHEPLREELKARGYTFVSETDTEVIAHLVNWELKQGGTLREAVLRAIPQ 152
Cdd:PTZ00295 104 WATHGGKTDENAHPHCdyKKRIALVHNGTIENYVELKSELIAKGIKFRSETDSEVIANLIGLELDQGEDFQEAVKSAISR 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 153 LRGAYGTVIMDSRHPDTLLAARSGSPLVIGLGMGENFIASDQLALLPVTRRFIFLEEGDIAEITRRSVNIFDKTGAEVK- 231
Cdd:PTZ00295 184 LQGTWGLCIIHKDNPDSLIVARNGSPLLVGIGDDSIYVASEPSAFAKYTNEYISLKDGEIAELSLENVNDLYTQRRVEKi 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 232 -RQDIESNlqydagdKGIYRHYMQKEIYEQPNAIKNTLT--GRISHGQ--VDLSELGPNADELLSkVEHIQILACGTSYN 306
Cdd:PTZ00295 264 pEEVIEKS-------PEPYPHWTLKEIFEQPIALSRALNngGRLSGYNnrVKLGGLDQYLEELLN-IKNLILVGCGTSYY 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 307 SGMVSRYWFESLAGI-PCDVEIASEF-RYRKSavRRNSLMITLSQSGETADTLAGLRLSKELGYLgSLAICNVPGSSLVR 384
Cdd:PTZ00295 336 AALFAASIMQKLKCFnTVQVIDASELtLYRLP--DEDAGVIFISQSGETLDVVRALNLADELNLP-KISVVNTVGSLIAR 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 385 ESDLALMTNAGTEIGVASTKAFTTQLTVLLMLVAKLSRLKGLDASIEH--DIVHGLQALPSRIEQMLSQDKRI-EALAED 461
Cdd:PTZ00295 413 STDCGVYLNAGREVAVASTKAFTSQVTVLSLIALWFAQNKEYSCSNYKcsSLINSLHRLPTYIGMTLKSCEEQcKRIAEK 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 462 FSDKHHALFLGRGDQYPIALEGALKLKEISYIHAEAYAAGELKHGPLALIDAD--MPVIVVAPNNELLEKLKSNIEEVRA 539
Cdd:PTZ00295 493 LKNAKSMFILGKGLGYPIALEGALKIKEITYIHAEGFSGGALKHGPFALIDKEknTPVILIILDDEHKELMINAAEQVKA 572
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15833925 540 RGGQLYVFAEqDAGFVSSDNMHIIEMPNVeEVIAPIFYTVPLQLLAYHVALIKGTDVDQPRNLAKSVTV 608
Cdd:PTZ00295 573 RGAYIIVITD-DEDLVKDFADEIILIPSN-GPLTALLAVIPLQLLAYEIAILRGINPDKPRGLAKTVTV 639
|
|
| PTZ00394 |
PTZ00394 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
1-609 |
6.38e-157 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 173585 [Multi-domain] Cd Length: 670 Bit Score: 465.89 E-value: 6.38e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 1 MCGIVGAIAQ------RDVAEILLEGLRRLEYRGYDSAGLA-----------------------VVDAEGHMTRLRRlgK 51
Cdd:PTZ00394 1 MCGIFGYANHnvprtvEQILNVLLDGIQKVEYRGYDSAGLAidanigsekedgtaasaptprpcVVRSVGNISQLRE--K 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 52 VQMLAQAAEEHPLHGGT----GIAHTRWATHGEPSEVNAHPHVSEH--IVVVHNGIIENHEPLREELKARGYTFVSETDT 125
Cdd:PTZ00394 79 VFSEAVAATLPPMDATTshhvGIAHTRWATHGGVCERNCHPQQSNNgeFTIVHNGIVTNYMTLKELLKEEGYHFSSDTDT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 126 EVIAHLVNWELKQGG--TLREAVLRAIPQLRGAYGTVIMDSRHPDTLLAARSGSPLVIGL-------------------- 183
Cdd:PTZ00394 159 EVISVLSEYLYTRKGihNFADLALEVSRMVEGSYALLVKSVYFPGQLAASRKGSPLMVGIrrtddrgcvmklqtydltdl 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 184 -GMGENFIASDQLALLPVTRRFIFLEEGDIAEI---TRRSVNIFDKTGAEVKRQDIESNLQYDAGDKGIYRHYMQKEIYE 259
Cdd:PTZ00394 239 sGPLEVFFSSDVNSFAEYTREVVFLEDGDIAHYcdgALRFYNAAERQRSIVKREVQHLDAKPEGLSKGNYPHFMLKEIYE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 260 QPNAIKNTLTGRI--SHGQVDLSELGPNADELLSKVEHIQILACGTSYNSGMVSRYWFESLAGIPCDVEIASEFRYRKSA 337
Cdd:PTZ00394 319 QPESVISSMHGRIdfSSGTVQLSGFTQQSIRAILTSRRILFIACGTSLNSCLAVRPLFEELVPLPISVENASDFLDRRPR 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 338 VRRNSLMITLSQSGETADTLAGLRLSKELGYLgSLAICNVPGSSLVRESDLALMTNAGTEIGVASTKAFTTQLTVLLMLV 417
Cdd:PTZ00394 399 IQRDDVCFFVSQSGETADTLMALQLCKEAGAM-CVGITNVVGSSISRLTHYAIHLNAGVEVGVASTKAYTSQVVVLTLVA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 418 AKLSRLKGLDASIEHDIVHGLQALPSRIEQMLS-QDKRIEALAEDFSDKHHALFLGRGDQYPIALEGALKLKEISYIHAE 496
Cdd:PTZ00394 478 LLLSSDSVRLQERRNEIIRGLAELPAAISECLKiTHDPVKALAARLKESSSILVLGRGYDLATAMEAALKVKELSYVHTE 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 497 AYAAGELKHGPLALIDADMPVIVVAPNNELLEKLKSNIEEVRARGGQLYVFAEQDAGFVSSDNMHIIEMPNVEEVIAPIF 576
Cdd:PTZ00394 558 GIHSGELKHGPLALIDETSPVLAMCTHDKHFGLSKSAVQQVKARGGAVVVFATEVDAELKAAASEIVLVPKTVDCLQCVV 637
|
650 660 670
....*....|....*....|....*....|...
gi 15833925 577 YTVPLQLLAYHVALIKGTDVDQPRNLAKSVTVE 609
Cdd:PTZ00394 638 NVIPFQLLAYYMALLRGNNVDCPRNLAKSVTVQ 670
|
|
| GFAT |
cd00714 |
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ... |
2-215 |
7.95e-128 |
|
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: 374.48 E-value: 7.95e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 2 CGIVGAIAQRDVAEILLEGLRRLEYRGYDSAGLAVVDaEGHMTRLRRLGKVQMLAQAAEEHPLHGGTGIAHTRWATHGEP 81
Cdd:cd00714 1 CGIVGYIGKREAVDILLEGLKRLEYRGYDSAGIAVIG-DGSLEVVKAVGKVANLEEKLAEKPLSGHVGIGHTRWATHGEP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 82 SEVNAHPHVSEH--IVVVHNGIIENHEPLREELKARGYTFVSETDTEVIAHLVNWELKQGGTLREAVLRAIPQLRGAYGT 159
Cdd:cd00714 80 TDVNAHPHRSCDgeIAVVHNGIIENYAELKEELEAKGYKFESETDTEVIAHLIEYYYDGGLDLLEAVKKALKRLEGAYAL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15833925 160 VIMDSRHPDTLLAARSGSPLVIGLGMGENFIASDQLALLPVTRRFIFLEEGDIAEI 215
Cdd:cd00714 160 AVISKDEPDEIVAARNGSPLVIGIGDGENFVASDAPALLEHTRRVIYLEDGDIAVI 215
|
|
| AgaS |
COG2222 |
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ... |
255-609 |
3.00e-75 |
|
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: 243.27 E-value: 3.00e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 255 KEIYEQPNAIKNTLtgriSHGQVDLSELgpnADELLSK-VEHIQILACGTSYNSGMVSRYWFESLAGIPCDVEIASEF-R 332
Cdd:COG2222 2 REIAQQPEAWRRAL----AALAAAIAAL---LARLRAKpPRRVVLVGAGSSDHAAQAAAYLLERLLGIPVAALAPSELvV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 333 YRKSAVRRNSLMITLSQSGETADTLAGLRLSKELGYLgSLAICNVPGSSLVRESDLALMTNAGTEIGVASTKAFTTQLTV 412
Cdd:COG2222 75 YPAYLKLEGTLVVAISRSGNSPEVVAALELAKARGAR-TLAITNNPDSPLAEAADRVLPLPAGPEKSVAATKSFTTMLLA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 413 LLMLVAKLSRLKGLDASiehdivhgLQALPSRIEQMLSQDKRIEALAEdFSDKHHALFLGRGDQYPIALEGALKLKEISY 492
Cdd:COG2222 154 LLALLAAWGGDDALLAA--------LDALPAALEAALAADWPAAALAA-LADAERVVFLGRGPLYGLAREAALKLKELSA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 493 IHAEAYAAGELKHGPLALIDADMPVIVVAPNNELLEKLKSNIEEVRARGGQLYVFAEQDAGFVssdnmHIIEMPNVEEVI 572
Cdd:COG2222 225 GHAEAYSAAEFRHGPKSLVDPGTLVVVLASEDPTRELDLDLAAELRALGARVVAIGAEDDAAI-----TLPAIPDLHDAL 299
|
330 340 350
....*....|....*....|....*....|....*..
gi 15833925 573 APIFYTVPLQLLAYHVALIKGTDVDQPRNLAKSVTVE 609
Cdd:COG2222 300 DPLLLLVVAQRLALALALARGLDPDTPRHLNKVVKTV 336
|
|
| SIS_GlmS_GlmD_2 |
cd05009 |
SIS (Sugar ISomerase) domain repeat 2 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
453-607 |
2.92e-69 |
|
SIS (Sugar ISomerase) domain repeat 2 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: 240142 [Multi-domain] Cd Length: 153 Bit Score: 220.98 E-value: 2.92e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 453 KRIEALAEDFSDKHHALFLGRGDQYPIALEGALKLKEISYIHAEAYAAGELKHGPLALIDADMPVIVVAPNNELLEKLKS 532
Cdd:cd05009 1 EDIKELAEKLKEAKSFYVLGRGPNYGTALEGALKLKETSYIHAEAYSAGEFKHGPIALVDEGTPVIFLAPEDRLEEKLES 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15833925 533 NIEEVRARGGQLYVFAeqDAGFVSSDNMHIIEMPNVEEVIAPIFYTVPLQLLAYHVALIKGTDVDQPRNLAKSVT 607
Cdd:cd05009 81 LIKEVKARGAKVIVIT--DDGDAKDLADVVIRVPATVEELSPLLYIVPLQLLAYHLAVARGIDPDKPRNLAKSVT 153
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
2-213 |
5.74e-65 |
|
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: 212.31 E-value: 5.74e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 2 CGIVGAIAQRDVAEILLE----GLRRLEYRGYDSAGLAVVDAEGHMTRlRRLGKVQMLAQAAEEHPLHGGTGIAHTRWAT 77
Cdd:cd00352 1 CGIFGIVGADGAASLLLLlllrGLAALEHRGPDGAGIAVYDGDGLFVE-KRAGPVSDVALDLLDEPLKSGVALGHVRLAT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 78 HGEPSEVNAHPHVSE--HIVVVHNGIIENHEPLREELKARGYTFVSETDTEVIAHLVnWELKQGGTLREAVLRAIPQLRG 155
Cdd:cd00352 80 NGLPSEANAQPFRSEdgRIALVHNGEIYNYRELREELEARGYRFEGESDSEVILHLL-ERLGREGGLFEAVEDALKRLDG 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15833925 156 AYGTVIMDsRHPDTLLAARSG---SPLVIGLGM-GENFIASDQLALLPVT-RRFIFLEEGDIA 213
Cdd:cd00352 159 PFAFALWD-GKPDRLFAARDRfgiRPLYYGITKdGGLVFASEPKALLALPfKGVRRLPPGELL 220
|
|
| SIS_GlmS_GlmD_1 |
cd05008 |
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
295-421 |
3.05e-58 |
|
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: 191.17 E-value: 3.05e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 295 HIQILACGTSYNSGMVSRYWFESLAGIPCDVEIASEFRYRKSAVRRNSLMITLSQSGETADTLAGLRLSKELGYLgSLAI 374
Cdd:cd05008 1 RILIVGCGTSYHAALVAKYLLERLAGIPVEVEAASEFRYRRPLLDEDTLVIAISQSGETADTLAALRLAKEKGAK-TVAI 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 15833925 375 CNVPGSSLVRESDLALMTNAGTEIGVASTKAFTTQLTVLLMLVAKLS 421
Cdd:cd05008 80 TNVVGSTLAREADYVLYLRAGPEISVAATKAFTSQLLALLLLALALA 126
|
|
| PurF |
COG0034 |
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ... |
1-182 |
5.01e-38 |
|
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: 146.71 E-value: 5.01e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 1 MCGIVGAIAQRDVAEILLEGLRRLEYRGYDSAGLAVVDaEGHMTRLRRLGKVqmlAQA-AEEH--PLHGGTGIAHTRWAT 77
Cdd:COG0034 7 ECGVFGIYGHEDVAQLTYYGLYALQHRGQESAGIATSD-GGRFHLHKGMGLV---SDVfDEEDleRLKGNIAIGHVRYST 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 78 HGEPSEVNAHPHVSEH----IVVVHNGIIENHEPLREELKARGYTFVSETDTEVIAHLVNWELKqGGTLREAVLRAIPQL 153
Cdd:COG0034 83 TGSSSLENAQPFYVNSpfgsIALAHNGNLTNAEELREELEEEGAIFQTTSDTEVILHLIARELT-KEDLEEAIKEALRRV 161
|
170 180 190
....*....|....*....|....*....|..
gi 15833925 154 RGAYGTVIMDsrhPDTLLAAR--SG-SPLVIG 182
Cdd:COG0034 162 KGAYSLVILT---GDGLIAARdpNGiRPLVLG 190
|
|
| GPATase_N |
cd00715 |
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ... |
2-226 |
3.91e-37 |
|
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: 138.75 E-value: 3.91e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 2 CGIVGAIAQRDVAEILLEGLRRLEYRGYDSAGLAVVDaEGHMTRLRRLGkvqMLAQAAEEH---PLHGGTGIAHTRWATH 78
Cdd:cd00715 1 CGVFGIYGAEDAARLTYLGLYALQHRGQESAGIATSD-GKRFHTHKGMG---LVSDVFDEEklrRLPGNIAIGHVRYSTA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 79 GEPSEVNAHPHVSEH----IVVVHNGIIENHEPLREELKARGYTFVSETDTEVIAHLVNWELKQgGTLREAVLRAIPQLR 154
Cdd:cd00715 77 GSSSLENAQPFVVNSplggIALAHNGNLVNAKELREELEEEGRIFQTTSDSEVILHLIARSLAK-DDLFEAIIDALERVK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 155 GAYGTVIMdsrHPDTLLAAR--SG-SPLVIG-LGMGENFIASDQLALLPVTRRFIF-LEEGDIAEITR---RSVNIFDKT 226
Cdd:cd00715 156 GAYSLVIM---TADGLIAVRdpHGiRPLVLGkLEGDGYVVASESCALDIIGAEFVRdVEPGEIVVIDDdglESSQRAPKP 232
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
289-419 |
1.60e-34 |
|
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: 127.41 E-value: 1.60e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 289 LLSKVEHIQILACGTSYNSGMVSRYWFESLAGIPCDVEIASEFRYR-KSAVRRNSLMITLSQSGETADTLAGLRLSKELG 367
Cdd:pfam01380 1 LLAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGvLALVDEDDLVIAISYSGETKDLLAAAELAKARG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 15833925 368 yLGSLAICNVPGSSLVRESDLALMTNAGTEIGVASTKAFTTQLTVLLMLVAK 419
Cdd:pfam01380 81 -AKIIAITDSPGSPLAREADHVLYINAGPETGVASTKSITAQLAALDALAVA 131
|
|
| purF |
TIGR01134 |
amidophosphoribosyltransferase; Alternate name: glutamine phosphoribosylpyrophosphate (PRPP) ... |
2-197 |
3.18e-33 |
|
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: 132.44 E-value: 3.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 2 CGIVGAIAQR-DVAEILLEGLRRLEYRGYDSAGLAVVDaeGHMTRLRR-LGKVQMLAQAAEEHPLHGGTGIAHTRWATHG 79
Cdd:TIGR01134 1 CGVVGIYGQEeVAASLTYYGLYALQHRGQESAGISVFD--GNRFRLHKgNGLVSDVFNEEHLQRLKGNVGIGHVRYSTAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 80 EPSEVNAHPHVSE----HIVVVHNGIIENHEPLREELKARGYTFVSETDTEVIAHLVNWELKQGGTLREAVLRAIPQLRG 155
Cdd:TIGR01134 79 SSGLENAQPFVVNspygGLALAHNGNLVNADELRRELEEEGRHFNTTSDSEVLLHLLAHNDESKDDLFDAVARVLERVRG 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15833925 156 AYGTVIMdsrHPDTLLAARS--G-SPLVIGlGMGENF-IASDQLAL 197
Cdd:TIGR01134 159 AYALVLM---TEDGLVAVRDphGiRPLVLG-RRGDGYvVASESCAL 200
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
462-592 |
4.00e-30 |
|
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: 115.09 E-value: 4.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 462 FSDKHHALFLGRGDQYPIALEGALKLKEISYIHAEAYAAGELKHGPLALIDADMPVIVVAPNNELLEKLKsNIEEVRARG 541
Cdd:pfam01380 2 LAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGVLALVDEDDLVIAISYSGETKDLLA-AAELAKARG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 15833925 542 GQLYVFAEQDAGFVSSDNMHIIEMPNVEEVIAPIFYTVPLQLLAYHVALIK 592
Cdd:pfam01380 81 AKIIAITDSPGSPLAREADHVLYINAGPETGVASTKSITAQLAALDALAVA 131
|
|
| PRK05793 |
PRK05793 |
amidophosphoribosyltransferase; Provisional |
2-226 |
5.90e-27 |
|
amidophosphoribosyltransferase; Provisional
Pssm-ID: 235611 [Multi-domain] Cd Length: 469 Bit Score: 114.36 E-value: 5.90e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 2 CGIVGAIA--QRDVAEILLEGLRRLEYRGYDSAGLAVVDAEgHMTRLRRLGKVQMLAQAAEEHPLHGGTGIAHTRWATHG 79
Cdd:PRK05793 15 CGVFGVFSknNIDVASLTYYGLYALQHRGQESAGIAVSDGE-KIKVHKGMGLVSEVFSKEKLKGLKGNSAIGHVRYSTTG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 80 EPSEVNAHPHVSEH----IVVVHNGIIENHEPLREELKARGYTFVSETDTEVIAHLVNWELKQGgtLREAVLRAIPQLRG 155
Cdd:PRK05793 94 ASDLDNAQPLVANYklgsIAIAHNGNLVNADVIRELLEDGGRIFQTSIDSEVILNLIARSAKKG--LEKALVDAIQAIKG 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15833925 156 AYGTVIMDSrhpDTLLAARSGS---PLVIGLGMGENFIASDQLALLPVTRRFIF-LEEGDIAEITR---RSVNIFDKT 226
Cdd:PRK05793 172 SYALVILTE---DKLIGVRDPHgirPLCLGKLGDDYILSSESCALDTIGAEFIRdVEPGEIVIIDEdgiKSIKFAEKT 246
|
|
| GlxB |
cd01907 |
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ... |
2-197 |
7.83e-25 |
|
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: 103.89 E-value: 7.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 2 CGIVGAI---AQRDVAEILLEGLRRLEYRG-YDSAGLAVVDAEG--------HMTRLRRLGKVQMLAQAAEEHPLHGGTG 69
Cdd:cd01907 1 CGIFGIMskdGEPFVGALLVEMLDAMQERGpGDGAGFALYGDPDafvyssgkDMEVFKGVGYPEDIARRYDLEEYKGYHW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 70 IAHTRWATHgepSEVN---AHPHVSEHIVVVHNGIIENHEPLREELKARGYTFVSETDTEVIAHLVNWELKQGGTLREAV 146
Cdd:cd01907 81 IAHTRQPTN---SAVWwygAHPFSIGDIAVVHNGEISNYGSNREYLERFGYKFETETDTEVIAYYLDLLLRKGGLPLEYY 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15833925 147 LRAI----------PQLRGAYGTVIMDSrhPDTLLAARSGS-----------PLVIGLGMGENFIASDQLAL 197
Cdd:cd01907 158 KHIIrmpeeerellLALRLTYRLADLDG--PFTIIVGTPDGfivirdriklrPAVVAETDDYVAIASEECAI 227
|
|
| PLN02440 |
PLN02440 |
amidophosphoribosyltransferase |
1-200 |
1.94e-22 |
|
amidophosphoribosyltransferase
Pssm-ID: 215241 [Multi-domain] Cd Length: 479 Bit Score: 100.91 E-value: 1.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 1 MCGIVGAIAQRDVAEILLEGLRRLEYRGYDSAGlaVVDAEGHMTRLRR-LGKVQMLAQAAEEHPLHGGTGIAHTRWATHG 79
Cdd:PLN02440 1 ECGVVGIFGDPEASRLCYLGLHALQHRGQEGAG--IVTVDGNRLQSITgNGLVSDVFDESKLDQLPGDIAIGHVRYSTAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 80 EPSEVNAHPHVSEH----IVVVHNGIIENHEPLREELKARGYTFVSETDTEVIAHLVNWELKQggTLREAVLRAIPQLRG 155
Cdd:PLN02440 79 ASSLKNVQPFVANYrfgsIGVAHNGNLVNYEELRAKLEENGSIFNTSSDTEVLLHLIAISKAR--PFFSRIVDACEKLKG 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15833925 156 AYGTVIMDSrhpDTLLAARSGS---PLVIGL-GMGENFIASDQLALLPV 200
Cdd:PLN02440 157 AYSMVFLTE---DKLVAVRDPHgfrPLVMGRrSNGAVVFASETCALDLI 202
|
|
| GATase_6 |
pfam13522 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
65-174 |
5.58e-20 |
|
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: 86.21 E-value: 5.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 65 HGGTGIAHTRWATHGEPSEVNaHPHVSE--HIVVVHNGIIENHEPLREELKARGYTFVSETDTEVIAHLvnwelkqggtL 142
Cdd:pfam13522 9 EGGVALGHVRLAIVDLPDAGN-QPMLSRdgRLVLVHNGEIYNYGELREELADLGHAFRSRSDTEVLLAL----------Y 77
|
90 100 110
....*....|....*....|....*....|..
gi 15833925 143 REAVLRAIPQLRGAYGTVIMDSRhPDTLLAAR 174
Cdd:pfam13522 78 EEWGEDCLERLRGMFAFAIWDRR-RRTLFLAR 108
|
|
| GATase_7 |
pfam13537 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
94-199 |
8.45e-17 |
|
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: 76.79 E-value: 8.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 94 IVVVHNGIIENHEPLREELKARGYTFVSETDTEVIAHLVNwelKQGGTlrEAVLRaipqLRGAYGTVIMDSRHpDTLLAA 173
Cdd:pfam13537 24 YVIVFNGEIYNYRELRAELEAKGYRFRTHSDTEVILHLYE---AEWGE--DCVDR----LNGMFAFAIWDRRR-QRLFLA 93
|
90 100 110
....*....|....*....|....*....|
gi 15833925 174 R--SG-SPLVIGLGMGENFI-ASDQLALLP 199
Cdd:pfam13537 94 RdrFGiKPLYYGRDDGGRLLfASELKALLA 123
|
|
| AsnB |
cd00712 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ... |
2-200 |
9.29e-16 |
|
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: 76.44 E-value: 9.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 2 CGIVGAI---AQRDVAEILLEGLRRLEYRGYDSAGLAVvdaeghmtrlrrlgkvqmlaqaaeehplHGGTGIAHTRWATH 78
Cdd:cd00712 1 CGIAGIIgldGASVDRATLERMLDALAHRGPDGSGIWI----------------------------DEGVALGHRRLSII 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 79 GEPSEvnAHPHVSE--HIVVVHNGIIENHEPLREELKARGYTFVSETDTEVIAHLvnweLKQGGTlreavlRAIPQLRGA 156
Cdd:cd00712 53 DLSGG--AQPMVSEdgRLVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHL----YEEWGE------DCLERLNGM 120
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15833925 157 YGTVIMDSRhPDTLLAAR--SGS-PLVIGLGmGENFI-ASDQLALLPV 200
Cdd:cd00712 121 FAFALWDKR-KRRLFLARdrFGIkPLYYGRD-GGGLAfASELKALLAL 166
|
|
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
1-174 |
1.19e-15 |
|
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: 80.27 E-value: 1.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 1 MCGIVGAIAQRDVA--EILLEGLRRLEYRGYDSAGLAVvdaeghmtrlrrlgkvqmlaqaaeehplHGGTGIAHTRWATH 78
Cdd:COG0367 1 MCGIAGIIDFDGGAdrEVLERMLDALAHRGPDGSGIWV----------------------------DGGVALGHRRLSII 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 79 GEPSevNAH-PHVSE--HIVVVHNGIIENHEPLREELKARGYTFVSETDTEVIAHLvnWElkQGGTlreavlRAIPQLRG 155
Cdd:COG0367 53 DLSE--GGHqPMVSEdgRYVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHA--YE--EWGE------DCLERLNG 120
|
170
....*....|....*....
gi 15833925 156 AYGTVIMDSRHpDTLLAAR 174
Cdd:COG0367 121 MFAFAIWDRRE-RRLFLAR 138
|
|
| YafJ |
COG0121 |
Predicted glutamine amidotransferase YafJ [General function prediction only]; |
62-177 |
2.14e-13 |
|
Predicted glutamine amidotransferase YafJ [General function prediction only];
Pssm-ID: 439891 [Multi-domain] Cd Length: 248 Bit Score: 70.38 E-value: 2.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 62 HPLHGGTGIAHTRWATHGEPSEVNAHPHVSEHIVVVHNGIIENHEPLREELKAR-----GYTFVSETDTEVIAHLVNWEL 136
Cdd:COG0121 72 RPIKSRLVIAHVRKATVGPVSLENTHPFRGGRWLFAHNGQLDGFDRLRRRLAEElpdelYFQPVGTTDSELAFALLLSRL 151
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 15833925 137 KQGG-TLREAVLRAIPQLR------GAYGTVIMDsrhPDTLLAARSGS 177
Cdd:COG0121 152 RDGGpDPAEALAEALRELAelarapGRLNLLLSD---GERLYATRYTS 196
|
|
| PTZ00077 |
PTZ00077 |
asparagine synthetase-like protein; Provisional |
1-197 |
9.79e-13 |
|
asparagine synthetase-like protein; Provisional
Pssm-ID: 185431 [Multi-domain] Cd Length: 586 Bit Score: 70.90 E-value: 9.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 1 MCGIVGAIAQRDVAEIL----LEGLRRLEYRGYDSAGLAVVDAEGHMTRLrrlgkvqmlaqaaeehplhggtgIAHTRWA 76
Cdd:PTZ00077 1 MCGILAIFNSKGERHELrrkaLELSKRLRHRGPDWSGIIVLENSPGTYNI-----------------------LAHERLA 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 77 -----THGEPSEVNAHPhvsehIVVVHNGIIENHEPLREELKARGYTFVSETDTEVIAHLvnweLKQGGTlreavlRAIP 151
Cdd:PTZ00077 58 ivdlsDGKQPLLDDDET-----VALMQNGEIYNHWEIRPELEKEGYKFSSNSDCEIIGHL----YKEYGP------KDFW 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15833925 152 -QLRGAYGTVIMDSRHpDTLLAARSG---SPLVIGLGM-GENFIASDQLAL 197
Cdd:PTZ00077 123 nHLDGMFATVIYDMKT-NTFFAARDHigiIPLYIGYAKdGSIWFSSELKAL 172
|
|
| YafJ |
cd01908 |
Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine ... |
62-178 |
1.15e-12 |
|
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: 68.18 E-value: 1.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 62 HPLHGGTGIAHTRWATHGEPSEVNAHPHVSEHIVVVHNGIIENHEPLREEL-KARGYTFVSETDTEVIAHLVnweLKQGG 140
Cdd:cd01908 76 RPIKSPLVLAHVRAATVGPVSLENCHPFTRGRWLFAHNGQLDGFRLLRRRLlRLLPRLPVGTTDSELAFALL---LSRLL 152
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 15833925 141 T--------LREAVLRAIPQLR-----GAYGTVIMDSrhpDTLLAARSGSP 178
Cdd:cd01908 153 ErdpldpaeLLDAILQTLRELAalappGRLNLLLSDG---EYLIATRYASA 200
|
|
| PLN02549 |
PLN02549 |
asparagine synthase (glutamine-hydrolyzing) |
1-197 |
1.51e-12 |
|
asparagine synthase (glutamine-hydrolyzing)
Pssm-ID: 178164 [Multi-domain] Cd Length: 578 Bit Score: 70.18 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 1 MCGIVGAIAQRDVA----EILLEGLRRLEYRGYDSAGLAVvdaeghmtrlrrlgkvqmlaqaaeehplHGGTGIAHTRWA 76
Cdd:PLN02549 1 MCGILAVLGCSDDSqakrSRVLELSRRLRHRGPDWSGLYG----------------------------NEDCYLAHERLA 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 77 THGEPSevNAHPHVSEH--IVVVHNGIIENHEPLREELKArgYTFVSETDTEVIAHLvnWELKQGGTLREavlraipqLR 154
Cdd:PLN02549 53 IMDPES--GDQPLYNEDktIVVTANGEIYNHKELREKLKL--HKFRTGSDCEVIAHL--YEEHGEEFVDM--------LD 118
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15833925 155 GAYGTVIMDSRHpDTLLAARSG---SPLVIGLGM-GENFIASDQLAL 197
Cdd:PLN02549 119 GMFSFVLLDTRD-NSFIAARDHigiTPLYIGWGLdGSVWFASEMKAL 164
|
|
| asnB |
PRK09431 |
asparagine synthetase B; Provisional |
1-202 |
7.07e-12 |
|
asparagine synthetase B; Provisional
Pssm-ID: 236513 [Multi-domain] Cd Length: 554 Bit Score: 68.01 E-value: 7.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 1 MCGIVGAIAQRDVAEIL----LEGLRRLEYRGYDSAGLAVVDAeghmtrlrrlgkvqmlaqaaeehplhggtGI-AHTRW 75
Cdd:PRK09431 1 MCGIFGILDIKTDADELrkkaLEMSRLMRHRGPDWSGIYASDN-----------------------------AIlGHERL 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 76 A----THGepsevnAHPHVSEH--IVVVHNGIIENHEPLREELKARgYTFVSETDTEVIAHLvnwelkqggtLREAVLRA 149
Cdd:PRK09431 52 SivdvNGG------AQPLYNEDgtHVLAVNGEIYNHQELRAELGDK-YAFQTGSDCEVILAL----------YQEKGPDF 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15833925 150 IPQLRGAYGTVIMDSRHpDTLLAARsgSPL-VIGLGMGEN-----FIASDQLALLPVTR 202
Cdd:PRK09431 115 LDDLDGMFAFALYDSEK-DAYLIAR--DPIgIIPLYYGYDehgnlYFASEMKALVPVCK 170
|
|
| SIS |
cd04795 |
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
296-375 |
5.29e-11 |
|
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: 58.92 E-value: 5.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 296 IQILACGTSYNSGMVSRYWFESLAGIPCDVEIASEFRY--RKSAVRRNSLMITLSQSGETADTLAGLRLSKELGyLGSLA 373
Cdd:cd04795 1 IFVIGIGGSGAIAAYFALELLELTGIEVVALIATELEHasLLSLLRKGDVVIALSYSGRTEELLAALEIAKELG-IPVIA 79
|
..
gi 15833925 374 IC 375
Cdd:cd04795 80 IT 81
|
|
| SIS_1 |
cd05710 |
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ... |
295-420 |
1.57e-10 |
|
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: 58.74 E-value: 1.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 295 HIQILACGTSYNSGMVSRYWFESLAGIPCDVEIASEFRYRK-SAVRRNSLMITLSQSGETADTLAGLRLSKELGYLgSLA 373
Cdd:cd05710 1 NVFFVGCGGSLADMYPAKYFLKKESKLPVFVYNAAEFLHTGpKRLTEKSVVILASHSGNTKETVAAAKFAKEKGAT-VIG 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 15833925 374 ICNVPGSSLVRESDLALMTNAGteigvasTKAFTTQLTVLLMLVAKL 420
Cdd:cd05710 80 LTDDEDSPLAKLADYVIVYGFE-------IDAVEEKYLLLYMLALRL 119
|
|
| asn_synth_AEB |
TIGR01536 |
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing ... |
95-174 |
1.56e-09 |
|
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: 60.43 E-value: 1.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 95 VVVHNGIIENHEPLREELKARGYTFVSETDTEVIAHLVnweLKQGGtlreavlRAIPQLRGAYGTVIMDSRHpDTLLAAR 174
Cdd:TIGR01536 69 VIVFNGEIYNHEELREELEAKGYTFQTDSDTEVILHLY---EEWGE-------ECVDRLDGMFAFALWDSEK-GELFLAR 137
|
|
| SIS |
cd04795 |
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
469-556 |
1.74e-08 |
|
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: 51.99 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 469 LFLGRGDQYPIALEGALKLKEISYIHAEAYAAGELKHGP-LALIDADMPVIVVAPNNElLEKLKSNIEEVRARGGQLYVF 547
Cdd:cd04795 2 FVIGIGGSGAIAAYFALELLELTGIEVVALIATELEHASlLSLLRKGDVVIALSYSGR-TEELLAALEIAKELGIPVIAI 80
|
....*....
gi 15833925 548 AeqDAGFVS 556
Cdd:cd04795 81 T--DALAVS 87
|
|
| frlB |
PRK11382 |
fructoselysine 6-phosphate deglycase; |
287-600 |
9.03e-08 |
|
fructoselysine 6-phosphate deglycase;
Pssm-ID: 183111 [Multi-domain] Cd Length: 340 Bit Score: 54.24 E-value: 9.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 287 DELLSK-VEHIQILACGTSYNSGMVSRYWFESLAGIPCDVEIASEF----RYRKSAvrrNSLMITLSQSGETADTLAGLR 361
Cdd:PRK11382 37 EEMVKRdIDRIYFVACGSPLNAAQTAKHLADRFSDLQVYAISGWEFcdntPYRLDD---RCAVIGVSDYGKTEEVIKALE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 362 LSKELGYLgSLAICNVPGSSLVRESDLALMTNAGT--EIGVASTKAFTTQLTVLLMLVAKLSRLKgldasiehdivHGLQ 439
Cdd:PRK11382 114 LGRACGAL-TAAFTKRADSPITSAAEFSIDYQADCiwEIHLLLCYSVVLEMITRLAPNAEIGKIK-----------NDLK 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 440 ALPSRIEQML-SQDKRIEALAEDFSDKHHALFLGRGDQYPIAL-EGALKLKEISYIHAEAYAAGELKHGPLALIDADMPV 517
Cdd:PRK11382 182 QLPNALGHLVrTWEEKGRQLGELASQWPMIYTVAAGPLRPLGYkEGIVTLMEFTWTHGCVIESGEFRHGPLEIVEPGVPF 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 518 IVVAPNNELLEKLKSNIEEVRARggqlyvfaeqdagfvsSDNMHIIEMPNVEE----VIAPIFYTVPLQLLAYHVALIKG 593
Cdd:PRK11382 262 LFLLGNDESRHTTERAINFVKQR----------------TDNVIVIDYAEISQglhpWLAPFLMFVPMEWLCYYLSIYKD 325
|
....*..
gi 15833925 594 TDVDQPR 600
Cdd:PRK11382 326 HNPDERR 332
|
|
| SIS_RpiR |
cd05013 |
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ... |
288-419 |
3.47e-07 |
|
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many phosphosugar isomerases and phosphosugar binding proteins. In E. coli, rpiR negatively regulates the expression of rpiB gene. Both rpiB and rpiA are ribose phosphate isomerases that catalyze the reversible reactions of ribose 5-phosphate into ribulose 5-phosphate.
Pssm-ID: 240144 [Multi-domain] Cd Length: 139 Bit Score: 49.53 E-value: 3.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 288 ELLSKVEHIQILACGTSYNSGM-VSRYWFesLAGIPCDVEIAS-EFRYRKSAVRRNSLMITLSQSGETADTLAGLRLSKE 365
Cdd:cd05013 8 DLLAKARRIYIFGVGSSGLVAEyLAYKLL--RLGKPVVLLSDPhLQLMSAANLTPGDVVIAISFSGETKETVEAAEIAKE 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 15833925 366 LGyLGSLAICNVPGSSLVRESDLALMTNA-GTEIGVASTKAFTTQLTVLLMLVAK 419
Cdd:cd05013 86 RG-AKVIAITDSANSPLAKLADIVLLVSSeEGDFRSSAFSSRIAQLALIDALFLA 139
|
|
| GATase_4 |
pfam13230 |
Glutamine amidotransferases class-II; This family captures members that are not found in ... |
55-166 |
1.29e-05 |
|
Glutamine amidotransferases class-II; This family captures members that are not found in pfam00310.
Pssm-ID: 433047 [Multi-domain] Cd Length: 272 Bit Score: 47.32 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 55 LAQAAEEHPLHGGTGIAHTRWATHGEPSEVNAHPHVSE----HIVVVHNGIIENHEPLREELkargYTFVSETDTEVI-A 129
Cdd:pfam13230 60 IAELVRRYPIRSRNVIAHIRKATQGRVTLENTHPFMRElwgrYWIFAHNGDLKGYAPKLSGR----FQPVGSTDSELAfC 135
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 15833925 130 HLVNWELKQGGTLRE------AVLRAIPQLRGAYGT---VIMDSRH 166
Cdd:pfam13230 136 WLLDRLASRFPYARPsagelfRALRELAREIAAHGTfnfLLSDGRD 181
|
|
| SIS_AgaS_like |
cd05010 |
AgaS-like protein. AgaS contains a SIS (Sugar ISomerase) domain which is found in many ... |
470-599 |
8.56e-05 |
|
AgaS-like protein. AgaS contains a SIS (Sugar ISomerase) domain which is found in many phosphosugar isomerases and phosphosugar binding proteins. AgaS is a putative isomerase in Escherichia coli. It is similar to the glucosamine-6-phosphate synthases (GlmS) which catalyzes the first step in hexosamine metabolism, converting fructose 6-phosphate into glucosamine 6-phosphate using glutamine as nitrogen source.
Pssm-ID: 240143 [Multi-domain] Cd Length: 151 Bit Score: 43.00 E-value: 8.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 470 FLGRGDQYPIALEGALKLKEIS--YIHAEAYAAGELKHGPLALIDADMPVIVVAPNNELLEKLKSN-IEEVRARGGQLYV 546
Cdd:cd05010 3 YLGSGPLAGLAREAALKVLELTagKVATVYDSPLGFRHGPKSLVDDDTLVVVFVSNDPYTRQYDLDlLKELRRDGIAARV 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 15833925 547 FA---EQDAGFVSSDNMHIIEMPNVEEV-IAPIfYTVPLQLLAYHVALIKGTDVDQP 599
Cdd:cd05010 83 IAispESDAGIEDNSHYYLPGSRDLDDVyLAFP-YILYAQLFALFNSIALGLTPDNP 138
|
|
| SIS_Etherase |
cd05007 |
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ... |
324-416 |
1.31e-03 |
|
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ISomerase) domain. The SIS domain is found in many phosphosugar isomerases and phosphosugar binding proteins. The bacterial cell wall sugar N-acetylmuramic acid carries a unique D-lactyl ether substituent at the C3 position. The etherase catalyzes the cleavage of the lactyl ether bond of N-acetylmuramic acid 6-phosphate.
Pssm-ID: 240140 [Multi-domain] Cd Length: 257 Bit Score: 40.97 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 324 DVEIASEFRYRKSAVRRNSLMITLSQSGETADTLAGLRLSKELGYLgSLAICNVPGSSLVRESDLALMTNAGTEIGVAST 403
Cdd:cd05007 102 DDEEAGAADLQAINLTERDVVIGIAASGRTPYVLGALRYARARGAL-TIGIACNPGSPLLQLADIAIALITGPEVVAGST 180
|
90
....*....|....*
gi 15833925 404 --KAFTTQLTVLLML 416
Cdd:cd05007 181 rlKAGTAQKLALNML 195
|
|
| murQ |
PRK05441 |
N-acetylmuramic acid-6-phosphate etherase; Reviewed |
338-416 |
5.10e-03 |
|
N-acetylmuramic acid-6-phosphate etherase; Reviewed
Pssm-ID: 235467 [Multi-domain] Cd Length: 299 Bit Score: 39.38 E-value: 5.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833925 338 VRRNSLMITLSQSGETADTLAGLRLSKELGYLgSLAICNVPGSSLVRESDLALMTNAGTEIGVAST--KAFTTQLTVLLM 415
Cdd:PRK05441 129 LTAKDVVVGIAASGRTPYVIGALEYARERGAL-TIGISCNPGSPLSKEADIAIEVVVGPEVLTGSTrmKAGTAQKLVLNM 207
|
.
gi 15833925 416 L 416
Cdd:PRK05441 208 I 208
|
|
| |
