|
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: 1074.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 1 MCGIVGAVAQRDIAEILLEGLRRLEYRGYDSAGLAVVDaEGHMTRLRRLGKVQMLAQAAEEHPLHGGTGIAHTRWATHGE 80
Cdd:COG0449 1 MCGIVGYIGKRDAAPILLEGLKRLEYRGYDSAGIAVLD-DGGLEVRKAVGKLANLEEKLAEEPLSGTIGIGHTRWATHGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 81 PSEGNAHPHVS--EHIVVVHNGIIENHEPLREELKARGYTFVSETDTEVIAHLVHWELEQGGTLREAVLRTIPQLRGAYG 158
Cdd:COG0449 80 PSDENAHPHTScsGRIAVVHNGIIENYAELREELEAKGHTFKSETDTEVIAHLIEEYLKGGGDLLEAVRKALKRLEGAYA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 159 TVIMDSRDPSTLLAARSGSPMVIGLGMGENFIASDQLALLPVTRRFIFLEEGDIAEVTRRSVTVFDTKGEQVKRQEIESN 238
Cdd:COG0449 160 LAVISADEPDRIVAARKGSPLVIGLGEGENFLASDVPALLPYTRRVIYLEDGEIAVLTRDGVEIYDLDGEPVEREVKTVD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 239 LQYDAGDKGAYRHYMQKEIYEQPNAIKNTLTGRIS-HGEVDLSELGaNANELLGKVEHIQIVACGTSYNSGMVSRYWFES 317
Cdd:COG0449 240 WDAEAAEKGGYPHFMLKEIHEQPEAIRDTLRGRLDeDGRVVLDELN-LAAEDLRNIDRIYIVACGTSYHAGLVGKYLIEE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 318 LAGVPCDVEIASEFRYRKSAVRRNSLMITLSQSGETADTLAALRLSKELGyLGSLAICNVPGSSLVRESDLALMTKAGTE 397
Cdd:COG0449 319 LARIPVEVEIASEFRYRDPVVDPGTLVIAISQSGETADTLAALREAKEKG-AKVLAICNVVGSTIARESDAVLYTHAGPE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 398 IGVASTKAFTTQLTVLLMLVAKLARLKGE-DASVEHDIVHGLQALPSRIEQMLSQDKRIEALAEDFSDKHHALFLGRGDQ 476
Cdd:COG0449 398 IGVASTKAFTTQLAALYLLALYLARARGTlSAEEEAELLEELRKLPEKIEEVLDLEEQIEELAEKYADARNALFLGRGIN 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 477 YPIALEGALKLKEISYIHAEAYAAGELKHGPLALIDADMPVIVVAPNNELLEKLKSNIEEVRARGGVLYVFADKDAGFAS 556
Cdd:COG0449 478 YPVALEGALKLKEISYIHAEGYAAGELKHGPIALIDEGMPVVAIAPQDELYEKTLSNIQEVKARGGKVIAIADEGDEEVE 557
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 498112425 557 SDNMHIIEMPHVEEVIAPIFYTVPLQLLAYHVALIKGTDVDQPRNLAKSVTVE 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: 1072.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 1 MCGIVGAVAQRDIAEILLEGLRRLEYRGYDSAGLAVVDaEGHMTRLRRLGKVQMLAQAAEEHPLHGGTGIAHTRWATHGE 80
Cdd:PRK00331 1 MCGIVGYVGQRNAAEILLEGLKRLEYRGYDSAGIAVLD-DGGLEVRKAVGKVANLEAKLEEEPLPGTTGIGHTRWATHGK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 81 PSEGNAHPHVS--EHIVVVHNGIIENHEPLREELKARGYTFVSETDTEVIAHLVHWELEQGGTLREAVLRTIPQLRGAYG 158
Cdd:PRK00331 80 PTERNAHPHTDcsGRIAVVHNGIIENYAELKEELLAKGHVFKSETDTEVIAHLIEEELKEGGDLLEAVRKALKRLEGAYA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 159 TVIMDSRDPSTLLAARSGSPMVIGLGMGENFIASDQLALLPVTRRFIFLEEGDIAEVTRRSVTVFDTKGEQVKRQEIESN 238
Cdd:PRK00331 160 LAVIDKDEPDTIVAARNGSPLVIGLGEGENFLASDALALLPYTRRVIYLEDGEIAVLTRDGVEIFDFDGNPVEREVYTVD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 239 LQYDAGDKGAYRHYMQKEIYEQPNAIKNTLTGRIshgevDLSELGANANELLGKVEHIQIVACGTSYNSGMVSRYWFESL 318
Cdd:PRK00331 240 WDASAAEKGGYRHFMLKEIYEQPEAIRDTLEGRL-----DELGEGELADEDLKKIDRIYIVACGTSYHAGLVAKYLIESL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 319 AGVPCDVEIASEFRYRKSAVRRNSLMITLSQSGETADTLAALRLSKELGyLGSLAICNVPGSSLVRESDLALMTKAGTEI 398
Cdd:PRK00331 315 AGIPVEVEIASEFRYRDPVLSPKTLVIAISQSGETADTLAALRLAKELG-AKTLAICNVPGSTIARESDAVLYTHAGPEI 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 399 GVASTKAFTTQLTVLLMLVAKLARLKGE-DASVEHDIVHGLQALPSRIEQMLSQDKRIEALAEDFSDKHHALFLGRGDQY 477
Cdd:PRK00331 394 GVASTKAFTAQLAVLYLLALALAKARGTlSAEEEADLVHELRELPALIEQVLDLKEQIEELAEDFADARNALFLGRGVDY 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 478 PIALEGALKLKEISYIHAEAYAAGELKHGPLALIDADMPVIVVAPNNELLEKLKSNIEEVRARGGVLYVFADKDaGFASS 557
Cdd:PRK00331 474 PVALEGALKLKEISYIHAEGYAAGELKHGPIALIDEGMPVVAIAPNDELYEKTKSNIQEVKARGARVIVIADEG-DEVAE 552
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 498112425 558 DNMHIIEMPHVEEVIAPIFYTVPLQLLAYHVALIKGTDVDQPRNLAKSVTVE 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: 1003.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 2 CGIVGAVAQRDIAEILLEGLRRLEYRGYDSAGLAVVDaEGHMTRLRRLGKVQMLAQAAEEHPLHGGTGIAHTRWATHGEP 81
Cdd:TIGR01135 1 CGIVGYIGQRDAVPILLEGLKRLEYRGYDSAGIAVVD-EGKLFVRKAVGKVAELANKLGEKPLPGGVGIGHTRWATHGKP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 82 SEGNAHPHVSEH--IVVVHNGIIENHEPLREELKARGYTFVSETDTEVIAHLVHWELEQGGTLREAVLRTIPQLRGAYGT 159
Cdd:TIGR01135 80 TDENAHPHTDEGgrIAVVHNGIIENYAELREELEARGHVFSSDTDTEVIAHLIEEELREGGDLLEAVQKALKQLRGAYAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 160 VIMDSRDPSTLLAARSGSPMVIGLGMGENFIASDQLALLPVTRRFIFLEEGDIAEVTRRSVTVFDTKGEQVKRQEIESNL 239
Cdd:TIGR01135 160 AVLHADHPETLVAARSGSPLIVGLGDGENFVASDVTALLPYTRRVIYLEDGDIAILTKDGVEIYNFEGAPVQREVRVIDW 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 240 QYDAGDKGAYRHYMQKEIYEQPNAIKNTLTGRISHGEVDLSELGANanELLGKVEHIQIVACGTSYNSGMVSRYWFESLA 319
Cdd:TIGR01135 240 DLDAAEKGGYRHFMLKEIYEQPRALRDTLEGRIEENGGVFEELGAE--ELLKNIDRIQIVACGTSYHAGLVAKYLIERLA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 320 GVPCDVEIASEFRYRKSAVRRNSLMITLSQSGETADTLAALRLSKELGyLGSLAICNVPGSSLVRESDLALMTKAGTEIG 399
Cdd:TIGR01135 318 GIPVEVEIASEFRYRKPVVDKDTLVIAISQSGETADTLEALRLAKELG-AKTLGICNVPGSTLVREADHTLYTRAGPEIG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 400 VASTKAFTTQLTVLLMLVAKLARLKGE-DASVEHDIVHGLQALPSRIEQMLSQDKRIEALAEDFSDKHHALFLGRGDQYP 478
Cdd:TIGR01135 397 VASTKAFTTQLTVLYLLALALAKARGTlSAEEEAELVDALRRLPDLVEQVLLADESIAELAERYADKRNFLFLGRGLGYP 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 479 IALEGALKLKEISYIHAEAYAAGELKHGPLALIDADMPVIVVAPNNELLEKLKSNIEEVRARGGVLYVFADKDAGFASSD 558
Cdd:TIGR01135 477 IALEGALKLKEISYIHAEGYPAGELKHGPIALIDEGLPVVAIAPKDSLLEKTKSNVEEVKARGARVIVFAPEDDETIASV 556
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 498112425 559 NMHIIEMPHVEEVIAPIFYTVPLQLLAYHVALIKGTDVDQPRNLAKSVTVE 609
Cdd:TIGR01135 557 ADDVIKLPEVEELLAPIVYTIPLQLLAYHIALAKGTDVDKPRNLAKSVTVE 607
|
|
| PLN02981 |
PLN02981 |
glucosamine:fructose-6-phosphate aminotransferase |
1-609 |
1.81e-172 |
|
glucosamine:fructose-6-phosphate aminotransferase
Pssm-ID: 215531 [Multi-domain] Cd Length: 680 Bit Score: 505.83 E-value: 1.81e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 1 MCGIVGAV------AQRDIAEILLEGLRRLEYRGYDSAGLAVvDAEGHMTR-----LRRLGKVQMLA----QAAEEHPLH 65
Cdd:PLN02981 1 MCGIFAYLnynvprERRFILEVLFNGLRRLEYRGYDSAGIAI-DNDPSLESssplvFREEGKIESLVrsvyEEVAETDLN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 66 GG------TGIAHTRWATHGEPSEGNAHPHVSE---HIVVVHNGIIENHEPLREELKARGYTFVSETDTEVIAHLVHW-- 134
Cdd:PLN02981 80 LDlvfenhAGIAHTRWATHGPPAPRNSHPQSSGpgnEFLVVHNGIITNYEVLKETLLRHGFTFESDTDTEVIPKLAKFvf 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 135 ----ELEQGGTLREAVLRTIPQLRGAYGTVIMDSRDPSTLLAARSGSPMVIG---LGMGEN------------------- 188
Cdd:PLN02981 160 dklnEEEGDVTFSQVVMEVMRQLEGAYALIFKSPHYPNELVACKRGSPLLLGvkeLPEEKNssavftsegfltknrdkpk 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 189 --FIASDQLALLPVTRRFIFLEEGDIAEVTRRSVTVFDTKGEQ-------VKRQEIE---SNLQYDAGD--KGAYRHYMQ 254
Cdd:PLN02981 240 efFLASDASAVVEHTKRVLVIEDNEVVHLKDGGVGIYKFENEKgrgggglSRPASVEralSTLEMEVEQimKGNYDHYMQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 255 KEIYEQPNAIKNTLTGRISHGEVDLSE---LGANANEL--LGKVEHIQIVACGTSYNSGMVSRYWFESLAGVPCDVEIAS 329
Cdd:PLN02981 320 KEIHEQPESLTTTMRGRLIRGGSGKAKrvlLGGLKDHLktIRRSRRIVFIGCGTSYNAALAARPILEELSGVPVTMELAS 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 330 EFRYRKSAVRRNSLMITLSQSGETADTLAALRLSKELGYLgSLAICNVPGSSLVRESDLALMTKAGTEIGVASTKAFTTQ 409
Cdd:PLN02981 400 DLLDRQGPIYREDTAVFVSQSGETADTLRALEYAKENGAL-CVGITNTVGSAISRGTHCGVHINAGAEIGVASTKAYTSQ 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 410 LTVLLMLVAKLarlkGEDASVEHD----IVHGLQALPSRIEQMLSQDKRIEALAEDFSDKHHALFLGRGDQYPIALEGAL 485
Cdd:PLN02981 479 IVAMTMLALAL----GEDSISSRSrreaIIDGLFDLPNKVREVLKLDQEMKELAELLIDEQSLLVFGRGYNYATALEGAL 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 486 KLKEISYIHAEAYAAGELKHGPLALIDADMPVIVVAPNNELLEKLKSNIEEVRARGGVLYVFADK--DAGFASSDNMHII 563
Cdd:PLN02981 555 KVKEVALMHSEGILAGEMKHGPLALVDETLPIIVIATRDACFSKQQSVIQQLRARKGRLIVICSKgdASSVCPSGGCRVI 634
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 498112425 564 EMPHVEEVIAPIFYTVPLQLLAYHVALIKGTDVDQPRNLAKSVTVE 609
Cdd:PLN02981 635 EVPQVEDCLQPVINIVPLQLLAYHLTVLRGHNVDQPRNLAKSVTTQ 680
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
1-608 |
4.39e-164 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 482.98 E-value: 4.39e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 1 MCGIVGAVAQRDIAEILLEGLRRLEYRGYDSAGLAVVDAEGHM--TRLRRLGK----VQMLAQAAEEHPLHGGTGIAHTR 74
Cdd:PTZ00295 24 CCGIVGYLGNEDASKILLEGIEILQNRGYDSCGISTISSGGELktTKYASDGTtsdsIEILKEKLLDSHKNSTIGIAHTR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 75 WATHGEPSEGNAHPHV--SEHIVVVHNGIIENHEPLREELKARGYTFVSETDTEVIAHLVHWELEQGGTLREAVLRTIPQ 152
Cdd:PTZ00295 104 WATHGGKTDENAHPHCdyKKRIALVHNGTIENYVELKSELIAKGIKFRSETDSEVIANLIGLELDQGEDFQEAVKSAISR 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 153 LRGAYGTVIMDSRDPSTLLAARSGSPMVIGLGMGENFIASDQLALLPVTRRFIFLEEGDIAEVTRRSVTVFDT--KGEQV 230
Cdd:PTZ00295 184 LQGTWGLCIIHKDNPDSLIVARNGSPLLVGIGDDSIYVASEPSAFAKYTNEYISLKDGEIAELSLENVNDLYTqrRVEKI 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 231 KRQEIESNlqydagdKGAYRHYMQKEIYEQPNAIKNTLT--GRISHGE--VDLSELGANANELLgKVEHIQIVACGTSYN 306
Cdd:PTZ00295 264 PEEVIEKS-------PEPYPHWTLKEIFEQPIALSRALNngGRLSGYNnrVKLGGLDQYLEELL-NIKNLILVGCGTSYY 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 307 SGMVSRYWFESLAGV-PCDVEIASEF-RYRKSavRRNSLMITLSQSGETADTLAALRLSKELGYLgSLAICNVPGSSLVR 384
Cdd:PTZ00295 336 AALFAASIMQKLKCFnTVQVIDASELtLYRLP--DEDAGVIFISQSGETLDVVRALNLADELNLP-KISVVNTVGSLIAR 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 385 ESDLALMTKAGTEIGVASTKAFTTQLTVLLMLVAKLARLKGEDASVEH--DIVHGLQALPSRIEQMLSQDKRI-EALAED 461
Cdd:PTZ00295 413 STDCGVYLNAGREVAVASTKAFTSQVTVLSLIALWFAQNKEYSCSNYKcsSLINSLHRLPTYIGMTLKSCEEQcKRIAEK 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 462 FSDKHHALFLGRGDQYPIALEGALKLKEISYIHAEAYAAGELKHGPLALIDAD--MPVIVVAPNNELLEKLKSNIEEVRA 539
Cdd:PTZ00295 493 LKNAKSMFILGKGLGYPIALEGALKIKEITYIHAEGFSGGALKHGPFALIDKEknTPVILIILDDEHKELMINAAEQVKA 572
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498112425 540 RGGVLYVFADkDAGFASSDNMHIIEMPHVeEVIAPIFYTVPLQLLAYHVALIKGTDVDQPRNLAKSVTV 608
Cdd:PTZ00295 573 RGAYIIVITD-DEDLVKDFADEIILIPSN-GPLTALLAVIPLQLLAYEIAILRGINPDKPRGLAKTVTV 639
|
|
| PTZ00394 |
PTZ00394 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
1-609 |
1.42e-156 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 173585 [Multi-domain] Cd Length: 670 Bit Score: 464.74 E-value: 1.42e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 1 MCGIVGAVAQ------RDIAEILLEGLRRLEYRGYDSAGLA-----------------------VVDAEGHMTRLRRlgK 51
Cdd:PTZ00394 1 MCGIFGYANHnvprtvEQILNVLLDGIQKVEYRGYDSAGLAidanigsekedgtaasaptprpcVVRSVGNISQLRE--K 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 52 VQMLAQAAEEHPLHGGT----GIAHTRWATHGEPSEGNAHPHVSEH--IVVVHNGIIENHEPLREELKARGYTFVSETDT 125
Cdd:PTZ00394 79 VFSEAVAATLPPMDATTshhvGIAHTRWATHGGVCERNCHPQQSNNgeFTIVHNGIVTNYMTLKELLKEEGYHFSSDTDT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 126 EVIAHLVHWELEQGG--TLREAVLRTIPQLRGAYGTVIMDSRDPSTLLAARSGSPMVIGL-------------------- 183
Cdd:PTZ00394 159 EVISVLSEYLYTRKGihNFADLALEVSRMVEGSYALLVKSVYFPGQLAASRKGSPLMVGIrrtddrgcvmklqtydltdl 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 184 -GMGENFIASDQLALLPVTRRFIFLEEGDIAEVTRRSVTVFDTKGEQ---VKRQEIESNLQYDAGDKGAYRHYMQKEIYE 259
Cdd:PTZ00394 239 sGPLEVFFSSDVNSFAEYTREVVFLEDGDIAHYCDGALRFYNAAERQrsiVKREVQHLDAKPEGLSKGNYPHFMLKEIYE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 260 QPNAIKNTLTGRI--SHGEVDLSELGANANELLGKVEHIQIVACGTSYNSGMVSRYWFESLAGVPCDVEIASEFRYRKSA 337
Cdd:PTZ00394 319 QPESVISSMHGRIdfSSGTVQLSGFTQQSIRAILTSRRILFIACGTSLNSCLAVRPLFEELVPLPISVENASDFLDRRPR 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 338 VRRNSLMITLSQSGETADTLAALRLSKELGYLgSLAICNVPGSSLVRESDLALMTKAGTEIGVASTKAFTTQLtVLLMLV 417
Cdd:PTZ00394 399 IQRDDVCFFVSQSGETADTLMALQLCKEAGAM-CVGITNVVGSSISRLTHYAIHLNAGVEVGVASTKAYTSQV-VVLTLV 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 418 AKLarLKGEDASVEH---DIVHGLQALPSRIEQMLS-QDKRIEALAEDFSDKHHALFLGRGDQYPIALEGALKLKEISYI 493
Cdd:PTZ00394 477 ALL--LSSDSVRLQErrnEIIRGLAELPAAISECLKiTHDPVKALAARLKESSSILVLGRGYDLATAMEAALKVKELSYV 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 494 HAEAYAAGELKHGPLALIDADMPVIVVAPNNELLEKLKSNIEEVRARGGVLYVFA-DKDAGFASSDNMhIIEMPHVEEVI 572
Cdd:PTZ00394 555 HTEGIHSGELKHGPLALIDETSPVLAMCTHDKHFGLSKSAVQQVKARGGAVVVFAtEVDAELKAAASE-IVLVPKTVDCL 633
|
650 660 670
....*....|....*....|....*....|....*..
gi 498112425 573 APIFYTVPLQLLAYHVALIKGTDVDQPRNLAKSVTVE 609
Cdd:PTZ00394 634 QCVVNVIPFQLLAYYMALLRGNNVDCPRNLAKSVTVQ 670
|
|
| GFAT |
cd00714 |
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ... |
2-215 |
5.60e-124 |
|
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: 364.46 E-value: 5.60e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 2 CGIVGAVAQRDIAEILLEGLRRLEYRGYDSAGLAVVDaEGHMTRLRRLGKVQMLAQAAEEHPLHGGTGIAHTRWATHGEP 81
Cdd:cd00714 1 CGIVGYIGKREAVDILLEGLKRLEYRGYDSAGIAVIG-DGSLEVVKAVGKVANLEEKLAEKPLSGHVGIGHTRWATHGEP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 82 SEGNAHPHVSEH--IVVVHNGIIENHEPLREELKARGYTFVSETDTEVIAHLVHWELEQGGTLREAVLRTIPQLRGAYGT 159
Cdd:cd00714 80 TDVNAHPHRSCDgeIAVVHNGIIENYAELKEELEAKGYKFESETDTEVIAHLIEYYYDGGLDLLEAVKKALKRLEGAYAL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 498112425 160 VIMDSRDPSTLLAARSGSPMVIGLGMGENFIASDQLALLPVTRRFIFLEEGDIAEV 215
Cdd:cd00714 160 AVISKDEPDEIVAARNGSPLVIGIGDGENFVASDAPALLEHTRRVIYLEDGDIAVI 215
|
|
| AgaS |
COG2222 |
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ... |
255-609 |
1.54e-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: 244.04 E-value: 1.54e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 255 KEIYEQPNAIKNTLtgriSHGEVDLSELGANANELlgKVEHIQIVACGTSYNSGMVSRYWFESLAGVPCDVEIASEF-RY 333
Cdd:COG2222 2 REIAQQPEAWRRAL----AALAAAIAALLARLRAK--PPRRVVLVGAGSSDHAAQAAAYLLERLLGIPVAALAPSELvVY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 334 RKSAVRRNSLMITLSQSGETADTLAALRLSKELGYLgSLAICNVPGSSLVRESDLALMTKAGTEIGVASTKAFTTQLTVL 413
Cdd:COG2222 76 PAYLKLEGTLVVAISRSGNSPEVVAALELAKARGAR-TLAITNNPDSPLAEAADRVLPLPAGPEKSVAATKSFTTMLLAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 414 LMLVAKLARlkgedasvEHDIVHGLQALPSRIEQMLSQDKRIEALAEdFSDKHHALFLGRGDQYPIALEGALKLKEISYI 493
Cdd:COG2222 155 LALLAAWGG--------DDALLAALDALPAALEAALAADWPAAALAA-LADAERVVFLGRGPLYGLAREAALKLKELSAG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 494 HAEAYAAGELKHGPLALIDADMPVIVVAPNNELLEKLKSNIEEVRARGGVLYVFADKDAGfassdNMHIIEMPHVEEVIA 573
Cdd:COG2222 226 HAEAYSAAEFRHGPKSLVDPGTLVVVLASEDPTRELDLDLAAELRALGARVVAIGAEDDA-----AITLPAIPDLHDALD 300
|
330 340 350
....*....|....*....|....*....|....*.
gi 498112425 574 PIFYTVPLQLLAYHVALIKGTDVDQPRNLAKSVTVE 609
Cdd:COG2222 301 PLLLLVVAQRLALALALARGLDPDTPRHLNKVVKTV 336
|
|
| SIS_GlmS_GlmD_2 |
cd05009 |
SIS (Sugar ISomerase) domain repeat 2 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
453-607 |
7.92e-70 |
|
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: 222.52 E-value: 7.92e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 453 KRIEALAEDFSDKHHALFLGRGDQYPIALEGALKLKEISYIHAEAYAAGELKHGPLALIDADMPVIVVAPNNELLEKLKS 532
Cdd:cd05009 1 EDIKELAEKLKEAKSFYVLGRGPNYGTALEGALKLKETSYIHAEAYSAGEFKHGPIALVDEGTPVIFLAPEDRLEEKLES 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498112425 533 NIEEVRARGGVLYVFADKDAGFASSDnmHIIEMPHVEEVIAPIFYTVPLQLLAYHVALIKGTDVDQPRNLAKSVT 607
Cdd:cd05009 81 LIKEVKARGAKVIVITDDGDAKDLAD--VVIRVPATVEELSPLLYIVPLQLLAYHLAVARGIDPDKPRNLAKSVT 153
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
2-213 |
2.15e-63 |
|
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: 208.07 E-value: 2.15e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 2 CGIVGAVAQRDIAEILLE----GLRRLEYRGYDSAGLAVVDAEGHMTRlRRLGKVQMLAQAAEEHPLHGGTGIAHTRWAT 77
Cdd:cd00352 1 CGIFGIVGADGAASLLLLlllrGLAALEHRGPDGAGIAVYDGDGLFVE-KRAGPVSDVALDLLDEPLKSGVALGHVRLAT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 78 HGEPSEGNAHPHVSE--HIVVVHNGIIENHEPLREELKARGYTFVSETDTEVIAHLVHWELEQGGtLREAVLRTIPQLRG 155
Cdd:cd00352 80 NGLPSEANAQPFRSEdgRIALVHNGEIYNYRELREELEARGYRFEGESDSEVILHLLERLGREGG-LFEAVEDALKRLDG 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498112425 156 AYGTVIMDsRDPSTLLAARSG---SPMVIGLGM-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 |
6.26e-59 |
|
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: 192.71 E-value: 6.26e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 295 HIQIVACGTSYNSGMVSRYWFESLAGVPCDVEIASEFRYRKSAVRRNSLMITLSQSGETADTLAALRLSKELGYLgSLAI 374
Cdd:cd05008 1 RILIVGCGTSYHAALVAKYLLERLAGIPVEVEAASEFRYRRPLLDEDTLVIAISQSGETADTLAALRLAKEKGAK-TVAI 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 498112425 375 CNVPGSSLVRESDLALMTKAGTEIGVASTKAFTTQLTVLLMLVAKLA 421
Cdd:cd05008 80 TNVVGSTLAREADYVLYLRAGPEISVAATKAFTSQLLALLLLALALA 126
|
|
| PurF |
COG0034 |
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ... |
1-174 |
5.31e-35 |
|
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: 137.85 E-value: 5.31e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 1 MCGIVGAVAQRDIAEILLEGLRRLEYRGYDSAGLAVVDaEGHMTRLRRLGKVqmlAQA-AEEH--PLHGGTGIAHTRWAT 77
Cdd:COG0034 7 ECGVFGIYGHEDVAQLTYYGLYALQHRGQESAGIATSD-GGRFHLHKGMGLV---SDVfDEEDleRLKGNIAIGHVRYST 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 78 HGEPSEGNAHPHVSEH----IVVVHNGIIENHEPLREELKARGYTFVSETDTEVIAHLVHWELEqGGTLREAVLRTIPQL 153
Cdd:COG0034 83 TGSSSLENAQPFYVNSpfgsIALAHNGNLTNAEELREELEEEGAIFQTTSDTEVILHLIARELT-KEDLEEAIKEALRRV 161
|
170 180
....*....|....*....|.
gi 498112425 154 RGAYGTVIMdsrDPSTLLAAR 174
Cdd:COG0034 162 KGAYSLVIL---TGDGLIAAR 179
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
289-419 |
5.01e-33 |
|
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: 123.18 E-value: 5.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 289 LLGKVEHIQIVACGTSYNSGMVSRYWFESLAGVPCDVEIASEFRYR-KSAVRRNSLMITLSQSGETADTLAALRLSKELG 367
Cdd:pfam01380 1 LLAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGvLALVDEDDLVIAISYSGETKDLLAAAELAKARG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 498112425 368 yLGSLAICNVPGSSLVRESDLALMTKAGTEIGVASTKAFTTQLTVLLMLVAK 419
Cdd:pfam01380 81 -AKIIAITDSPGSPLAREADHVLYINAGPETGVASTKSITAQLAALDALAVA 131
|
|
| GPATase_N |
cd00715 |
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ... |
2-217 |
6.30e-32 |
|
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: 124.11 E-value: 6.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 2 CGIVGAVAQRDIAEILLEGLRRLEYRGYDSAGLAVVDaEGHMTRLRRLGkvqMLAQAAEEH---PLHGGTGIAHTRWATH 78
Cdd:cd00715 1 CGVFGIYGAEDAARLTYLGLYALQHRGQESAGIATSD-GKRFHTHKGMG---LVSDVFDEEklrRLPGNIAIGHVRYSTA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 79 GEPSEGNAHPHVSEH----IVVVHNGIIENHEPLREELKARGYTFVSETDTEVIAHLVHWELEQgGTLREAVLRTIPQLR 154
Cdd:cd00715 77 GSSSLENAQPFVVNSplggIALAHNGNLVNAKELREELEEEGRIFQTTSDSEVILHLIARSLAK-DDLFEAIIDALERVK 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498112425 155 GAYGTVIMdsrDPSTLLAAR--SG-SPMVIG-LGMGENFIASDQLALLPVTRRFIF-LEEGDIAEVTR 217
Cdd:cd00715 156 GAYSLVIM---TADGLIAVRdpHGiRPLVLGkLEGDGYVVASESCALDIIGAEFVRdVEPGEIVVIDD 220
|
|
| purF |
TIGR01134 |
amidophosphoribosyltransferase; Alternate name: glutamine phosphoribosylpyrophosphate (PRPP) ... |
2-197 |
9.52e-31 |
|
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: 125.12 E-value: 9.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 2 CGIVGAVAQR-DIAEILLEGLRRLEYRGYDSAGLAVVDaeGHMTRLRR-LGKVQMLAQAAEEHPLHGGTGIAHTRWATHG 79
Cdd:TIGR01134 1 CGVVGIYGQEeVAASLTYYGLYALQHRGQESAGISVFD--GNRFRLHKgNGLVSDVFNEEHLQRLKGNVGIGHVRYSTAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 80 EPSEGNAHPHVSE----HIVVVHNGIIENHEPLREELKARGYTFVSETDTEVIAHLVHWELEQGGTLREAVLRTIPQLRG 155
Cdd:TIGR01134 79 SSGLENAQPFVVNspygGLALAHNGNLVNADELRRELEEEGRHFNTTSDSEVLLHLLAHNDESKDDLFDAVARVLERVRG 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 498112425 156 AYGTVIMdsrDPSTLLAARS--G-SPMVIGlGMGENF-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 |
2.72e-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: 115.47 E-value: 2.72e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 462 FSDKHHALFLGRGDQYPIALEGALKLKEISYIHAEAYAAGELKHGPLALIDADMPVIVVAPNNELLEKLKsNIEEVRARG 541
Cdd:pfam01380 2 LAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGVLALVDEDDLVIAISYSGETKDLLA-AAELAKARG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 498112425 542 GVLYVFADKDAGFASSDNMHIIEMPHVEEVIAPIFYTVPLQLLAYHVALIK 592
Cdd:pfam01380 81 AKIIAITDSPGSPLAREADHVLYINAGPETGVASTKSITAQLAALDALAVA 131
|
|
| PRK05793 |
PRK05793 |
amidophosphoribosyltransferase; Provisional |
2-224 |
2.27e-24 |
|
amidophosphoribosyltransferase; Provisional
Pssm-ID: 235611 [Multi-domain] Cd Length: 469 Bit Score: 106.66 E-value: 2.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 2 CGIVGAVA--QRDIAEILLEGLRRLEYRGYDSAGLAVVDAEgHMTRLRRLGKVQMLAQAAEEHPLHGGTGIAHTRWATHG 79
Cdd:PRK05793 15 CGVFGVFSknNIDVASLTYYGLYALQHRGQESAGIAVSDGE-KIKVHKGMGLVSEVFSKEKLKGLKGNSAIGHVRYSTTG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 80 EPSEGNAHPHVSEH----IVVVHNGIIENHEPLREELKARGYTFVSETDTEVIAHLVHWELEQGgtLREAVLRTIPQLRG 155
Cdd:PRK05793 94 ASDLDNAQPLVANYklgsIAIAHNGNLVNADVIRELLEDGGRIFQTSIDSEVILNLIARSAKKG--LEKALVDAIQAIKG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 156 AYGTVIMDS------RDPSTLlaarsgSPMVIGLGMGENFIASDQLALLPVTRRFIF-LEEGDI-------------AEV 215
Cdd:PRK05793 172 SYALVILTEdkligvRDPHGI------RPLCLGKLGDDYILSSESCALDTIGAEFIRdVEPGEIviidedgiksikfAEK 245
|
....*....
gi 498112425 216 TRRSVTVFD 224
Cdd:PRK05793 246 TKCQTCAFE 254
|
|
| GlxB |
cd01907 |
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ... |
2-197 |
3.40e-24 |
|
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: 101.96 E-value: 3.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 2 CGIVGAV---AQRDIAEILLEGLRRLEYRG-YDSAGLAVVDAEG--------HMTRLRRLGKVQMLAQAAEEHPLHGGTG 69
Cdd:cd01907 1 CGIFGIMskdGEPFVGALLVEMLDAMQERGpGDGAGFALYGDPDafvyssgkDMEVFKGVGYPEDIARRYDLEEYKGYHW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 70 IAHTRWATHGEPSEGNAHPHVSEHIVVVHNGIIENHEPLREELKARGYTFVSETDTEVIAHLVHWELEQGGTLREAVLRT 149
Cdd:cd01907 81 IAHTRQPTNSAVWWYGAHPFSIGDIAVVHNGEISNYGSNREYLERFGYKFETETDTEVIAYYLDLLLRKGGLPLEYYKHI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498112425 150 I----------PQLRGAYGTVIMDSrdPSTLLAARSGS-----------PMVIGLGMGENFIASDQLAL 197
Cdd:cd01907 161 IrmpeeerellLALRLTYRLADLDG--PFTIIVGTPDGfivirdriklrPAVVAETDDYVAIASEECAI 227
|
|
| GATase_6 |
pfam13522 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
65-174 |
6.99e-22 |
|
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: 91.60 E-value: 6.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 65 HGGTGIAHTRWATHGEPSEGNaHPHVSE--HIVVVHNGIIENHEPLREELKARGYTFVSETDTEVIAHLvhweLEQGGTl 142
Cdd:pfam13522 9 EGGVALGHVRLAIVDLPDAGN-QPMLSRdgRLVLVHNGEIYNYGELREELADLGHAFRSRSDTEVLLAL----YEEWGE- 82
|
90 100 110
....*....|....*....|....*....|..
gi 498112425 143 reavlRTIPQLRGAYGTVIMDSRdPSTLLAAR 174
Cdd:pfam13522 83 -----DCLERLRGMFAFAIWDRR-RRTLFLAR 108
|
|
| PLN02440 |
PLN02440 |
amidophosphoribosyltransferase |
1-233 |
5.99e-21 |
|
amidophosphoribosyltransferase
Pssm-ID: 215241 [Multi-domain] Cd Length: 479 Bit Score: 96.29 E-value: 5.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 1 MCGIVGAVAQRDIAEILLEGLRRLEYRGYDSAGlaVVDAEGHMTRLRR-LGKVQMLAQAAEEHPLHGGTGIAHTRWATHG 79
Cdd:PLN02440 1 ECGVVGIFGDPEASRLCYLGLHALQHRGQEGAG--IVTVDGNRLQSITgNGLVSDVFDESKLDQLPGDIAIGHVRYSTAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 80 EPSEGNAHPHVSEH----IVVVHNGIIENHEPLREELKARGYTFVSETDTEVIAHLVHWELEQggTLREAVLRTIPQLRG 155
Cdd:PLN02440 79 ASSLKNVQPFVANYrfgsIGVAHNGNLVNYEELRAKLEENGSIFNTSSDTEVLLHLIAISKAR--PFFSRIVDACEKLKG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 156 AYGTVIMDS------RDPSTLlaarsgSPMVIGL-GMGENFIASDQLALLPVtrRFIFLEEGDIAEVtrrsvtVFDTKGE 228
Cdd:PLN02440 157 AYSMVFLTEdklvavRDPHGF------RPLVMGRrSNGAVVFASETCALDLI--GATYEREVNPGEV------IVVDKDK 222
|
....*
gi 498112425 229 QVKRQ 233
Cdd:PLN02440 223 GVSSQ 227
|
|
| GATase_7 |
pfam13537 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
72-199 |
6.44e-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: 77.17 E-value: 6.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 72 HTRWATHGepSEGNAHPHVSEH---IVVVHNGIIENHEPLREELKARGYTFVSETDTEVIAHLVHwelEQGGTlrEAVLR 148
Cdd:pfam13537 1 HRRLSIID--LEGGAQPMVSSEdgrYVIVFNGEIYNYRELRAELEAKGYRFRTHSDTEVILHLYE---AEWGE--DCVDR 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 498112425 149 tipqLRGAYGTVIMDSRDPsTLLAAR--SG-SPMVIGLGMGENFI-ASDQLALLP 199
Cdd:pfam13537 74 ----LNGMFAFAIWDRRRQ-RLFLARdrFGiKPLYYGRDDGGRLLfASELKALLA 123
|
|
| AsnB |
cd00712 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ... |
2-174 |
2.13e-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: 78.37 E-value: 2.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 2 CGIVGAVAQRDIA---EILLEGLRRLEYRGYDSAGLAVvdaeghmtrlrrlgkvqmlaqaaeehplHGGTGIAHTRWATH 78
Cdd:cd00712 1 CGIAGIIGLDGASvdrATLERMLDALAHRGPDGSGIWI----------------------------DEGVALGHRRLSII 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 79 GEpsEGNAHPHVSE--HIVVVHNGIIENHEPLREELKARGYTFVSETDTEVIAHLvhweLEQGGTlreavlRTIPQLRGA 156
Cdd:cd00712 53 DL--SGGAQPMVSEdgRLVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHL----YEEWGE------DCLERLNGM 120
|
170
....*....|....*...
gi 498112425 157 YGTVIMDSRDpSTLLAAR 174
Cdd:cd00712 121 FAFALWDKRK-RRLFLAR 137
|
|
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
1-174 |
1.28e-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: 79.88 E-value: 1.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 1 MCGIVGAVA--QRDIAEILLEGLRRLEYRGYDSAGLAVvdaeghmtrlrrlgkvqmlaqaaeehplHGGTGIAHTRWATH 78
Cdd:COG0367 1 MCGIAGIIDfdGGADREVLERMLDALAHRGPDGSGIWV----------------------------DGGVALGHRRLSII 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 79 GEPSEGNAhPHVSE--HIVVVHNGIIENHEPLREELKARGYTFVSETDTEVIAHLvhweLEQGGTlrEAVlrtiPQLRGA 156
Cdd:COG0367 53 DLSEGGHQ-PMVSEdgRYVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHA----YEEWGE--DCL----ERLNGM 121
|
170
....*....|....*...
gi 498112425 157 YGTVIMDSRDpSTLLAAR 174
Cdd:COG0367 122 FAFAIWDRRE-RRLFLAR 138
|
|
| YafJ |
COG0121 |
Predicted glutamine amidotransferase YafJ [General function prediction only]; |
62-177 |
1.79e-13 |
|
Predicted glutamine amidotransferase YafJ [General function prediction only];
Pssm-ID: 439891 [Multi-domain] Cd Length: 248 Bit Score: 70.38 E-value: 1.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 62 HPLHGGTGIAHTRWATHGEPSEGNAHPHVSEHIVVVHNGIIENHEPLREELKAR-----GYTFVSETDTEVIAHLVHWEL 136
Cdd:COG0121 72 RPIKSRLVIAHVRKATVGPVSLENTHPFRGGRWLFAHNGQLDGFDRLRRRLAEElpdelYFQPVGTTDSELAFALLLSRL 151
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 498112425 137 EQGG-TLREAVLRTIPQLR------GAYGTVIMdsrDPSTLLAARSGS 177
Cdd:COG0121 152 RDGGpDPAEALAEALRELAelarapGRLNLLLS---DGERLYATRYTS 196
|
|
| PTZ00077 |
PTZ00077 |
asparagine synthetase-like protein; Provisional |
1-197 |
7.80e-13 |
|
asparagine synthetase-like protein; Provisional
Pssm-ID: 185431 [Multi-domain] Cd Length: 586 Bit Score: 71.28 E-value: 7.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 1 MCGIVGAVAQRDIAEIL----LEGLRRLEYRGYDSAGLAVVDAEGHMTRLrrlgkvqmlaqaaeehplhggtgIAHTRWA 76
Cdd:PTZ00077 1 MCGILAIFNSKGERHELrrkaLELSKRLRHRGPDWSGIIVLENSPGTYNI-----------------------LAHERLA 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 77 THGePSEGnAHPHVS--EHIVVVHNGIIENHEPLREELKARGYTFVSETDTEVIAHLvhweLEQGGTlreavLRTIPQLR 154
Cdd:PTZ00077 58 IVD-LSDG-KQPLLDddETVALMQNGEIYNHWEIRPELEKEGYKFSSNSDCEIIGHL----YKEYGP-----KDFWNHLD 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 498112425 155 GAYGTVIMDSRDpSTLLAARSG---SPMVIGLGM-GENFIASDQLAL 197
Cdd:PTZ00077 127 GMFATVIYDMKT-NTFFAARDHigiIPLYIGYAKdGSIWFSSELKAL 172
|
|
| PLN02549 |
PLN02549 |
asparagine synthase (glutamine-hydrolyzing) |
1-197 |
1.37e-12 |
|
asparagine synthase (glutamine-hydrolyzing)
Pssm-ID: 178164 [Multi-domain] Cd Length: 578 Bit Score: 70.56 E-value: 1.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 1 MCGIVGAVAQRDIA----EILLEGLRRLEYRGYDSAGLAVvdaeghmtrlrrlgkvqmlaqaaeehplHGGTGIAHTRWA 76
Cdd:PLN02549 1 MCGILAVLGCSDDSqakrSRVLELSRRLRHRGPDWSGLYG----------------------------NEDCYLAHERLA 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 77 THgEPSEGNaHPHVSEH--IVVVHNGIIENHEPLREELKArgYTFVSETDTEVIAHLVhwelEQGGtlrEAVLRtipQLR 154
Cdd:PLN02549 53 IM-DPESGD-QPLYNEDktIVVTANGEIYNHKELREKLKL--HKFRTGSDCEVIAHLY----EEHG---EEFVD---MLD 118
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 498112425 155 GAYGTVIMDSRDpSTLLAARSG---SPMVIGLGM-GENFIASDQLAL 197
Cdd:PLN02549 119 GMFSFVLLDTRD-NSFIAARDHigiTPLYIGWGLdGSVWFASEMKAL 164
|
|
| YafJ |
cd01908 |
Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine ... |
62-179 |
3.47e-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: 67.03 E-value: 3.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 62 HPLHGGTGIAHTRWATHGEPSEGNAHPHVSEHIVVVHNGIIENHEPLREEL-KARGYTFVSETDTEVIAHLVhweLEQGG 140
Cdd:cd01908 76 RPIKSPLVLAHVRAATVGPVSLENCHPFTRGRWLFAHNGQLDGFRLLRRRLlRLLPRLPVGTTDSELAFALL---LSRLL 152
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 498112425 141 T--------LREAVLRTIPQLR-----GAYGTVIMDSRdpsTLLAARSGSPM 179
Cdd:cd01908 153 ErdpldpaeLLDAILQTLRELAalappGRLNLLLSDGE---YLIATRYASAP 201
|
|
| SIS_1 |
cd05710 |
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ... |
295-420 |
2.96e-11 |
|
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: 60.67 E-value: 2.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 295 HIQIVACGTSYNSGMVSRYWFESLAGVPCDVEIASEFRYRK-SAVRRNSLMITLSQSGETADTLAALRLSKELGYLgSLA 373
Cdd:cd05710 1 NVFFVGCGGSLADMYPAKYFLKKESKLPVFVYNAAEFLHTGpKRLTEKSVVILASHSGNTKETVAAAKFAKEKGAT-VIG 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 498112425 374 ICNVPGSSLVRESDLALMTKAGteigvasTKAFTTQLTVLLMLVAKL 420
Cdd:cd05710 80 LTDDEDSPLAKLADYVIVYGFE-------IDAVEEKYLLLYMLALRL 119
|
|
| asnB |
PRK09431 |
asparagine synthetase B; Provisional |
1-202 |
4.29e-11 |
|
asparagine synthetase B; Provisional
Pssm-ID: 236513 [Multi-domain] Cd Length: 554 Bit Score: 65.70 E-value: 4.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 1 MCGIVGAVAQRDIAEIL----LEGLRRLEYRGYDSAGLAVVDAeghmtrlrrlgkvqmlaqaaeehplhggtGI-AHTRW 75
Cdd:PRK09431 1 MCGIFGILDIKTDADELrkkaLEMSRLMRHRGPDWSGIYASDN-----------------------------AIlGHERL 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 76 ATHGePSEGnAHPHVSEH--IVVVHNGIIENHEPLREELKARgYTFVSETDTEVIAHLvhweleqggtLREAVLRTIPQL 153
Cdd:PRK09431 52 SIVD-VNGG-AQPLYNEDgtHVLAVNGEIYNHQELRAELGDK-YAFQTGSDCEVILAL----------YQEKGPDFLDDL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 498112425 154 RGAYGTVIMDSrDPSTLLAARsgSPM-VIGLGMGEN-----FIASDQLALLPVTR 202
Cdd:PRK09431 119 DGMFAFALYDS-EKDAYLIAR--DPIgIIPLYYGYDehgnlYFASEMKALVPVCK 170
|
|
| asn_synth_AEB |
TIGR01536 |
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing ... |
4-174 |
1.41e-10 |
|
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: 63.89 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 4 IVGAVAQRDIA----EILLEGLRRLEYRGYDSAGLAVVDaeghmtrlrrlgkvqmlaqaaeehplhGGTGIAHTRWATHG 79
Cdd:TIGR01536 1 IAGFFDLDDKAveedEAIKRMSDTIAHRGPDASGIEYKD---------------------------GNAILGHRRLAIID 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 80 epSEGNAHPHVSE--HIVVVHNGIIENHEPLREELKARGYTFVSETDTEVIAHLvhweLEQGGtlREAVLRtipqLRGAY 157
Cdd:TIGR01536 54 --LSGGAQPMSNEgkTYVIVFNGEIYNHEELREELEAKGYTFQTDSDTEVILHL----YEEWG--EECVDR----LDGMF 121
|
170
....*....|....*..
gi 498112425 158 GTVIMDSRDpSTLLAAR 174
Cdd:TIGR01536 122 AFALWDSEK-GELFLAR 137
|
|
| SIS |
cd04795 |
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
296-375 |
2.18e-10 |
|
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: 57.38 E-value: 2.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 296 IQIVACGTSYNSGMVSRYWFESLAGVPCDVEIASEFRY--RKSAVRRNSLMITLSQSGETADTLAALRLSKELGyLGSLA 373
Cdd:cd04795 1 IFVIGIGGSGAIAAYFALELLELTGIEVVALIATELEHasLLSLLRKGDVVIALSYSGRTEELLAALEIAKELG-IPVIA 79
|
..
gi 498112425 374 IC 375
Cdd:cd04795 80 IT 81
|
|
| frlB |
PRK11382 |
fructoselysine 6-phosphate deglycase; |
276-600 |
8.99e-09 |
|
fructoselysine 6-phosphate deglycase;
Pssm-ID: 183111 [Multi-domain] Cd Length: 340 Bit Score: 57.32 E-value: 8.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 276 EVDLSELGANANELLGK-VEHIQIVACGTSYNSGMVSRYWFESLAGVPCDVEIASEF----RYRKSAvrrNSLMITLSQS 350
Cdd:PRK11382 26 SHDVPLVHAIVEEMVKRdIDRIYFVACGSPLNAAQTAKHLADRFSDLQVYAISGWEFcdntPYRLDD---RCAVIGVSDY 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 351 GETADTLAALRLSKELGYLgSLAICNVPGSSLVRESDLALMTKAGTEIGVASTKAFTtqltVLLMLVAKLARlKGEDASV 430
Cdd:PRK11382 103 GKTEEVIKALELGRACGAL-TAAFTKRADSPITSAAEFSIDYQADCIWEIHLLLCYS----VVLEMITRLAP-NAEIGKI 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 431 EHDivhgLQALPSRIEQML-SQDKRIEALAEDFSDKHHALFLGRGDQYPIAL-EGALKLKEISYIHAEAYAAGELKHGPL 508
Cdd:PRK11382 177 KND----LKQLPNALGHLVrTWEEKGRQLGELASQWPMIYTVAAGPLRPLGYkEGIVTLMEFTWTHGCVIESGEFRHGPL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 509 ALIDADMPVIVVAPNNELLEKLKSNIEEVRARggvlyvfadkdagfasSDNMHIIEMPHVEE----VIAPIFYTVPLQLL 584
Cdd:PRK11382 253 EIVEPGVPFLFLLGNDESRHTTERAINFVKQR----------------TDNVIVIDYAEISQglhpWLAPFLMFVPMEWL 316
|
330
....*....|....*.
gi 498112425 585 AYHVALIKGTDVDQPR 600
Cdd:PRK11382 317 CYYLSIYKDHNPDERR 332
|
|
| SIS |
cd04795 |
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
469-552 |
2.98e-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: 51.22 E-value: 2.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 469 LFLGRGDQYPIALEGALKLKEISYIHAEAYAAGELKHGP-LALIDADMPVIVVAPNNElLEKLKSNIEEVRARGGVLYVF 547
Cdd:cd04795 2 FVIGIGGSGAIAAYFALELLELTGIEVVALIATELEHASlLSLLRKGDVVIALSYSGR-TEELLAALEIAKELGIPVIAI 80
|
....*
gi 498112425 548 ADKDA 552
Cdd:cd04795 81 TDALA 85
|
|
| SIS_RpiR |
cd05013 |
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ... |
284-419 |
7.43e-08 |
|
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: 51.46 E-value: 7.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 284 ANANELLGKVEHIQIVACGTSYNSGM-VSRYWFesLAGVPCDVEIAS-EFRYRKSAVRRNSLMITLSQSGETADTLAALR 361
Cdd:cd05013 4 EKAVDLLAKARRIYIFGVGSSGLVAEyLAYKLL--RLGKPVVLLSDPhLQLMSAANLTPGDVVIAISFSGETKETVEAAE 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 498112425 362 LSKELGyLGSLAICNVPGSSLVRESDLALMTKA-GTEIGVASTKAFTTQLTVLLMLVAK 419
Cdd:cd05013 82 IAKERG-AKVIAITDSANSPLAKLADIVLLVSSeEGDFRSSAFSSRIAQLALIDALFLA 139
|
|
| SIS_AgaS_like |
cd05010 |
AgaS-like protein. AgaS contains a SIS (Sugar ISomerase) domain which is found in many ... |
470-599 |
2.39e-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: 44.54 E-value: 2.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 470 FLGRGDQYPIALEGALKLKEIS--YIHAEAYAAGELKHGPLALIDADMPVIVVAPNNE--------LLEKLKSNieevRA 539
Cdd:cd05010 3 YLGSGPLAGLAREAALKVLELTagKVATVYDSPLGFRHGPKSLVDDDTLVVVFVSNDPytrqydldLLKELRRD----GI 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498112425 540 RGGVLYVFADKDAGFASSDNMHIIEMPHVEEV-IAPIfYTVPLQLLAYHVALIKGTDVDQP 599
Cdd:cd05010 79 AARVIAISPESDAGIEDNSHYYLPGSRDLDDVyLAFP-YILYAQLFALFNSIALGLTPDNP 138
|
|
| SIS_Etherase |
cd05007 |
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ... |
324-416 |
1.66e-04 |
|
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: 43.67 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 324 DVEIASEFRYRKSAVRRNSLMITLSQSGETADTLAALRLSKELGYLgSLAICNVPGSSLVRESDLALMTKAGTEIGVAST 403
Cdd:cd05007 102 DDEEAGAADLQAINLTERDVVIGIAASGRTPYVLGALRYARARGAL-TIGIACNPGSPLLQLADIAIALITGPEVVAGST 180
|
90
....*....|....*
gi 498112425 404 --KAFTTQLTVLLML 416
Cdd:cd05007 181 rlKAGTAQKLALNML 195
|
|
| GATase_4 |
pfam13230 |
Glutamine amidotransferases class-II; This family captures members that are not found in ... |
55-166 |
2.05e-04 |
|
Glutamine amidotransferases class-II; This family captures members that are not found in pfam00310.
Pssm-ID: 433047 [Multi-domain] Cd Length: 272 Bit Score: 43.47 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 55 LAQAAEEHPLHGGTGIAHTRWATHGEPSEGNAHPHVSE----HIVVVHNGIIENHEPLREELkargYTFVSETDTEVI-A 129
Cdd:pfam13230 60 IAELVRRYPIRSRNVIAHIRKATQGRVTLENTHPFMRElwgrYWIFAHNGDLKGYAPKLSGR----FQPVGSTDSELAfC 135
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 498112425 130 HLVHW---ELEQGGTLREAVLRTIPQLR---GAYGT---VIMDSRD 166
Cdd:pfam13230 136 WLLDRlasRFPYARPSAGELFRALRELAreiAAHGTfnfLLSDGRD 181
|
|
| murQ |
PRK05441 |
N-acetylmuramic acid-6-phosphate etherase; Reviewed |
338-416 |
4.43e-03 |
|
N-acetylmuramic acid-6-phosphate etherase; Reviewed
Pssm-ID: 235467 [Multi-domain] Cd Length: 299 Bit Score: 39.38 E-value: 4.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498112425 338 VRRNSLMITLSQSGETADTLAALRLSKELGYLgSLAICNVPGSSLVRESDLALMTKAGTEIGVAST--KAFTTQLTVLLM 415
Cdd:PRK05441 129 LTAKDVVVGIAASGRTPYVIGALEYARERGAL-TIGISCNPGSPLSKEADIAIEVVVGPEVLTGSTrmKAGTAQKLVLNM 207
|
.
gi 498112425 416 L 416
Cdd:PRK05441 208 I 208
|
|
| |
