|
Name |
Accession |
Description |
Interval |
E-value |
| GlmS |
COG0449 |
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ... |
1-610 |
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: 1016.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 1 MCGIVGAVAHRNVTPILLEGLRRLEYRGYDSAGIAVIAaDGSLERVRRPGKLRELEAALESALVEGETGIAHTRWATHGV 80
Cdd:COG0449 1 MCGIVGYIGKRDAAPILLEGLKRLEYRGYDSAGIAVLD-DGGLEVRKAVGKLANLEEKLAEEPLSGTIGIGHTRWATHGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 81 PSERNAHPHV-CRERVAVVHNGIIENHEALRRQLQQKGYEFLSETDTEVVVNQIHDFLEQGFPLLEAVRATVGILEGAYA 159
Cdd:COG0449 80 PSDENAHPHTsCSGRIAVVHNGIIENYAELREELEAKGHTFKSETDTEVIAHLIEEYLKGGGDLLEAVRKALKRLEGAYA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 160 IGVVSTCEPGRLIAARKGSPLVVGLGESENFVASDVFALVGETQRFVFLEEGDLVELTTESVRVYGKDGGRVERPVHETR 239
Cdd:COG0449 160 LAVISADEPDRIVAARKGSPLVIGLGEGENFLASDVPALLPYTRRVIYLEDGEIAVLTRDGVEIYDLDGEPVEREVKTVD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 240 LAPDSVERGEYRHYMQKEIHEQPVAVEKTLSGRIH-QGKVLSAAFGErAEAAFEHVRAVQIVACGTSYHAGKVARYWFEA 318
Cdd:COG0449 240 WDAEAAEKGGYPHFMLKEIHEQPEAIRDTLRGRLDeDGRVVLDELNL-AAEDLRNIDRIYIVACGTSYHAGLVGKYLIEE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 319 LAGLPCSVEVASEFRYRRQVVQPGTLFVTISQSGETADTLAALKAAKELGyAHTLAICNVPESSIVRESDSCLMTRAGPE 398
Cdd:COG0449 319 LARIPVEVEIASEFRYRDPVVDPGTLVIAISQSGETADTLAALREAKEKG-AKVLAICNVVGSTIARESDAVLYTHAGPE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 399 IGVASTKAFTTQLTALLLLVLALGR-RHALAAEQEAKIVRELETLPAQIRHVLQLEDEIAAWAELFGEKHHALYLGRGAQ 477
Cdd:COG0449 398 IGVASTKAFTTQLAALYLLALYLARaRGTLSAEEEAELLEELRKLPEKIEEVLDLEEQIEELAEKYADARNALFLGRGIN 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 478 YPVAMEGALKLKEISYIHAEAYPAGELKHGPLALIDNEMPVVAVAPNNELLEKLKSNLQEVQARGGELYVFADAEAPIEN 557
Cdd:COG0449 478 YPVALEGALKLKEISYIHAEGYAAGELKHGPIALIDEGMPVVAIAPQDELYEKTLSNIQEVKARGGKVIAIADEGDEEVE 557
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 499261848 558 VPGVRILRVAETDEVVAPIVYSVPLQLLAYHVALIKGTDVDQPRNLAKSVTVE 610
Cdd:COG0449 558 ELADDVIEVPEVDELLAPILAVVPLQLLAYHVAVLRGTDVDQPRNLAKSVTVE 610
|
|
| PRK00331 |
PRK00331 |
isomerizing glutamine--fructose-6-phosphate transaminase; |
1-610 |
0e+00 |
|
isomerizing glutamine--fructose-6-phosphate transaminase;
Pssm-ID: 234729 [Multi-domain] Cd Length: 604 Bit Score: 982.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 1 MCGIVGAVAHRNVTPILLEGLRRLEYRGYDSAGIAVIAaDGSLERVRRPGKLRELEAALESALVEGETGIAHTRWATHGV 80
Cdd:PRK00331 1 MCGIVGYVGQRNAAEILLEGLKRLEYRGYDSAGIAVLD-DGGLEVRKAVGKVANLEAKLEEEPLPGTTGIGHTRWATHGK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 81 PSERNAHPHV-CRERVAVVHNGIIENHEALRRQLQQKGYEFLSETDTEVVVNQIHDFLEQGFPLLEAVRATVGILEGAYA 159
Cdd:PRK00331 80 PTERNAHPHTdCSGRIAVVHNGIIENYAELKEELLAKGHVFKSETDTEVIAHLIEEELKEGGDLLEAVRKALKRLEGAYA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 160 IGVVSTCEPGRLIAARKGSPLVVGLGESENFVASDVFALVGETQRFVFLEEGDLVELTTESVRVYGKDGGRVERPVHETR 239
Cdd:PRK00331 160 LAVIDKDEPDTIVAARNGSPLVIGLGEGENFLASDALALLPYTRRVIYLEDGEIAVLTRDGVEIFDFDGNPVEREVYTVD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 240 LAPDSVERGEYRHYMQKEIHEQPVAVEKTLSGRIHqgkvlSAAFGERAEAAFEHVRAVQIVACGTSYHAGKVARYWFEAL 319
Cdd:PRK00331 240 WDASAAEKGGYRHFMLKEIYEQPEAIRDTLEGRLD-----ELGEGELADEDLKKIDRIYIVACGTSYHAGLVAKYLIESL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 320 AGLPCSVEVASEFRYRRQVVQPGTLFVTISQSGETADTLAALKAAKELGyAHTLAICNVPESSIVRESDSCLMTRAGPEI 399
Cdd:PRK00331 315 AGIPVEVEIASEFRYRDPVLSPKTLVIAISQSGETADTLAALRLAKELG-AKTLAICNVPGSTIARESDAVLYTHAGPEI 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 400 GVASTKAFTTQLTALLLLVLALGR-RHALAAEQEAKIVRELETLPAQIRHVLQLEDEIAAWAELFGEKHHALYLGRGAQY 478
Cdd:PRK00331 394 GVASTKAFTAQLAVLYLLALALAKaRGTLSAEEEADLVHELRELPALIEQVLDLKEQIEELAEDFADARNALFLGRGVDY 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 479 PVAMEGALKLKEISYIHAEAYPAGELKHGPLALIDNEMPVVAVAPNNELLEKLKSNLQEVQARGGELYVFADAEAPIENV 558
Cdd:PRK00331 474 PVALEGALKLKEISYIHAEGYAAGELKHGPIALIDEGMPVVAIAPNDELYEKTKSNIQEVKARGARVIVIADEGDEVAEE 553
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 499261848 559 PGVRIlRVAETDEVVAPIVYSVPLQLLAYHVALIKGTDVDQPRNLAKSVTVE 610
Cdd:PRK00331 554 ADDVI-EVPEVHELLAPLLYVVPLQLLAYHVALARGTDVDKPRNLAKSVTVE 604
|
|
| glmS |
TIGR01135 |
glucosamine--fructose-6-phosphate aminotransferase (isomerizing); The member from ... |
2-610 |
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: 870.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 2 CGIVGAVAHRNVTPILLEGLRRLEYRGYDSAGIAVIAaDGSLERVRRPGKLRELEAALESALVEGETGIAHTRWATHGVP 81
Cdd:TIGR01135 1 CGIVGYIGQRDAVPILLEGLKRLEYRGYDSAGIAVVD-EGKLFVRKAVGKVAELANKLGEKPLPGGVGIGHTRWATHGKP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 82 SERNAHPHV-CRERVAVVHNGIIENHEALRRQLQQKGYEFLSETDTEVVVNQIHDFLEQGFPLLEAVRATVGILEGAYAI 160
Cdd:TIGR01135 80 TDENAHPHTdEGGRIAVVHNGIIENYAELREELEARGHVFSSDTDTEVIAHLIEEELREGGDLLEAVQKALKQLRGAYAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 161 GVVSTCEPGRLIAARKGSPLVVGLGESENFVASDVFALVGETQRFVFLEEGDLVELTTESVRVYGKDGGRVERPVHETRL 240
Cdd:TIGR01135 160 AVLHADHPETLVAARSGSPLIVGLGDGENFVASDVTALLPYTRRVIYLEDGDIAILTKDGVEIYNFEGAPVQREVRVIDW 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 241 APDSVERGEYRHYMQKEIHEQPVAVEKTLSGRIHQGKVLSAAFGerAEAAFEHVRAVQIVACGTSYHAGKVARYWFEALA 320
Cdd:TIGR01135 240 DLDAAEKGGYRHFMLKEIYEQPRALRDTLEGRIEENGGVFEELG--AEELLKNIDRIQIVACGTSYHAGLVAKYLIERLA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 321 GLPCSVEVASEFRYRRQVVQPGTLFVTISQSGETADTLAALKAAKELGyAHTLAICNVPESSIVRESDSCLMTRAGPEIG 400
Cdd:TIGR01135 318 GIPVEVEIASEFRYRKPVVDKDTLVIAISQSGETADTLEALRLAKELG-AKTLGICNVPGSTLVREADHTLYTRAGPEIG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 401 VASTKAFTTQLTALLLLVLALGR-RHALAAEQEAKIVRELETLPAQIRHVLQLEDEIAAWAELFGEKHHALYLGRGAQYP 479
Cdd:TIGR01135 397 VASTKAFTTQLTVLYLLALALAKaRGTLSAEEEAELVDALRRLPDLVEQVLLADESIAELAERYADKRNFLFLGRGLGYP 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 480 VAMEGALKLKEISYIHAEAYPAGELKHGPLALIDNEMPVVAVAPNNELLEKLKSNLQEVQARGGELYVFADAEAPIENVP 559
Cdd:TIGR01135 477 IALEGALKLKEISYIHAEGYPAGELKHGPIALIDEGLPVVAIAPKDSLLEKTKSNVEEVKARGARVIVFAPEDDETIASV 556
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 499261848 560 GVRILRVAETDEVVAPIVYSVPLQLLAYHVALIKGTDVDQPRNLAKSVTVE 610
Cdd:TIGR01135 557 ADDVIKLPEVEELLAPIVYTIPLQLLAYHIALAKGTDVDKPRNLAKSVTVE 607
|
|
| PLN02981 |
PLN02981 |
glucosamine:fructose-6-phosphate aminotransferase |
1-610 |
1.53e-162 |
|
glucosamine:fructose-6-phosphate aminotransferase
Pssm-ID: 215531 [Multi-domain] Cd Length: 680 Bit Score: 480.40 E-value: 1.53e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 1 MCGIVGAVAH------RNVTPILLEGLRRLEYRGYDSAGIAvIAADGSLER-----VRRPGKLRELEAALESALVEGE-- 67
Cdd:PLN02981 1 MCGIFAYLNYnvprerRFILEVLFNGLRRLEYRGYDSAGIA-IDNDPSLESssplvFREEGKIESLVRSVYEEVAETDln 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 68 --------TGIAHTRWATHGVPSERNAHPHVCRE--RVAVVHNGIIENHEALRRQLQQKGYEFLSETDTEVV---VNQIH 134
Cdd:PLN02981 80 ldlvfenhAGIAHTRWATHGPPAPRNSHPQSSGPgnEFLVVHNGIITNYEVLKETLLRHGFTFESDTDTEVIpklAKFVF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 135 DFL---EQGFPLLEAVRATVGILEGAYAIGVVSTCEPGRLIAARKGSPLVVG---LGESEN------------------- 189
Cdd:PLN02981 160 DKLneeEGDVTFSQVVMEVMRQLEGAYALIFKSPHYPNELVACKRGSPLLLGvkeLPEEKNssavftsegfltknrdkpk 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 190 --FVASDVFALVGETQRFVFLEEGDLVELTTESVRVYGKDGGRVERPVHETRlaPDSVER--------------GEYRHY 253
Cdd:PLN02981 240 efFLASDASAVVEHTKRVLVIEDNEVVHLKDGGVGIYKFENEKGRGGGGLSR--PASVERalstlemeveqimkGNYDHY 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 254 MQKEIHEQPVAVEKTLSGRIHQG---KVLSAAFGERAE--AAFEHVRAVQIVACGTSYHAGKVARYWFEALAGLPCSVEV 328
Cdd:PLN02981 318 MQKEIHEQPESLTTTMRGRLIRGgsgKAKRVLLGGLKDhlKTIRRSRRIVFIGCGTSYNAALAARPILEELSGVPVTMEL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 329 ASEFRYRRQVVQPGTLFVTISQSGETADTLAALKAAKELGyAHTLAICNVPESSIVRESDSCLMTRAGPEIGVASTKAFT 408
Cdd:PLN02981 398 ASDLLDRQGPIYREDTAVFVSQSGETADTLRALEYAKENG-ALCVGITNTVGSAISRGTHCGVHINAGAEIGVASTKAYT 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 409 TQLTALLLLVLALGRRHALAAEQEAKIVRELETLPAQIRHVLQLEDEIAAWAELFGEKHHALYLGRGAQYPVAMEGALKL 488
Cdd:PLN02981 477 SQIVAMTMLALALGEDSISSRSRREAIIDGLFDLPNKVREVLKLDQEMKELAELLIDEQSLLVFGRGYNYATALEGALKV 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 489 KEISYIHAEAYPAGELKHGPLALIDNEMPVVAVAPNNELLEKLKSNLQEVQARGGELYVFA---DAEAPIENvPGVRILR 565
Cdd:PLN02981 557 KEVALMHSEGILAGEMKHGPLALVDETLPIIVIATRDACFSKQQSVIQQLRARKGRLIVICskgDASSVCPS-GGCRVIE 635
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 499261848 566 VAETDEVVAPIVYSVPLQLLAYHVALIKGTDVDQPRNLAKSVTVE 610
Cdd:PLN02981 636 VPQVEDCLQPVINIVPLQLLAYHLTVLRGHNVDQPRNLAKSVTTQ 680
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
1-609 |
4.46e-149 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 444.46 E-value: 4.46e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 1 MCGIVGAVAHRNVTPILLEGLRRLEYRGYDSAGIAVIAADGSLE-----RVRRPG----KLRELEAALEsalvEGET-GI 70
Cdd:PTZ00295 24 CCGIVGYLGNEDASKILLEGIEILQNRGYDSCGISTISSGGELKttkyaSDGTTSdsieILKEKLLDSH----KNSTiGI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 71 AHTRWATHGVPSERNAHPHV-CRERVAVVHNGIIENHEALRRQLQQKGYEFLSETDTEVVVNQIHDFLEQGFPLLEAVRA 149
Cdd:PTZ00295 100 AHTRWATHGGKTDENAHPHCdYKKRIALVHNGTIENYVELKSELIAKGIKFRSETDSEVIANLIGLELDQGEDFQEAVKS 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 150 TVGILEGAYAIGVVSTCEPGRLIAARKGSPLVVGLGESENFVASDVFALVGETQRFVFLEEGDLVELTTESVRVYgKDGG 229
Cdd:PTZ00295 180 AISRLQGTWGLCIIHKDNPDSLIVARNGSPLLVGIGDDSIYVASEPSAFAKYTNEYISLKDGEIAELSLENVNDL-YTQR 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 230 RVERPVHETRLAPDSvergEYRHYMQKEIHEQPVAVEKTLS--GRIHQGKVLSAAFG-ERAEAAFEHVRAVQIVACGTSY 306
Cdd:PTZ00295 259 RVEKIPEEVIEKSPE----PYPHWTLKEIFEQPIALSRALNngGRLSGYNNRVKLGGlDQYLEELLNIKNLILVGCGTSY 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 307 HAGKVARYWFEALAGLPcSVEV--ASEF---RYRRQVVqpGTLFvtISQSGETADTLAALKAAKELGyAHTLAICNVPES 381
Cdd:PTZ00295 335 YAALFAASIMQKLKCFN-TVQVidASELtlyRLPDEDA--GVIF--ISQSGETLDVVRALNLADELN-LPKISVVNTVGS 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 382 SIVRESDSCLMTRAGPEIGVASTKAFTTQLTA----------LLLLVLALGRRHALaaeqeakiVRELETLPAQIRHVLQ 451
Cdd:PTZ00295 409 LIARSTDCGVYLNAGREVAVASTKAFTSQVTVlslialwfaqNKEYSCSNYKCSSL--------INSLHRLPTYIGMTLK 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 452 L-EDEIAAWAELFGEKHHALYLGRGAQYPVAMEGALKLKEISYIHAEAYPAGELKHGPLALIDNE--MPVVAVAPNNELL 528
Cdd:PTZ00295 481 ScEEQCKRIAEKLKNAKSMFILGKGLGYPIALEGALKIKEITYIHAEGFSGGALKHGPFALIDKEknTPVILIILDDEHK 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 529 EKLKSNLQEVQARGGELYVFADAEAPIENVPGVRILrvAETDEVVAPIVYSVPLQLLAYHVALIKGTDVDQPRNLAKSVT 608
Cdd:PTZ00295 561 ELMINAAEQVKARGAYIIVITDDEDLVKDFADEIIL--IPSNGPLTALLAVIPLQLLAYEIAILRGINPDKPRGLAKTVT 638
|
.
gi 499261848 609 V 609
Cdd:PTZ00295 639 V 639
|
|
| PTZ00394 |
PTZ00394 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
1-610 |
3.12e-147 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 173585 [Multi-domain] Cd Length: 670 Bit Score: 440.85 E-value: 3.12e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 1 MCGIVGAVAH------RNVTPILLEGLRRLEYRGYDSAGIAVIAADGSLER--------------VRRPG---KLREL-- 55
Cdd:PTZ00394 1 MCGIFGYANHnvprtvEQILNVLLDGIQKVEYRGYDSAGLAIDANIGSEKEdgtaasaptprpcvVRSVGnisQLREKvf 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 56 --EAALE----SALVEGETGIAHTRWATHGVPSERNAHPHVCRE-RVAVVHNGIIENHEALRRQLQQKGYEFLSETDTEV 128
Cdd:PTZ00394 81 seAVAATlppmDATTSHHVGIAHTRWATHGGVCERNCHPQQSNNgEFTIVHNGIVTNYMTLKELLKEEGYHFSSDTDTEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 129 VV---------NQIHDFLEQgfpLLEAVRatvgILEGAYAIGVVSTCEPGRLIAARKGSPLVVGL--------------- 184
Cdd:PTZ00394 161 ISvlseylytrKGIHNFADL---ALEVSR----MVEGSYALLVKSVYFPGQLAASRKGSPLMVGIrrtddrgcvmklqty 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 185 ------GESENFVASDVFALVGETQRFVFLEEGDLVELTTESVRVY---GKDGGRVERPVHETRLAPDSVERGEYRHYMQ 255
Cdd:PTZ00394 234 dltdlsGPLEVFFSSDVNSFAEYTREVVFLEDGDIAHYCDGALRFYnaaERQRSIVKREVQHLDAKPEGLSKGNYPHFML 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 256 KEIHEQPVAVEKTLSGRIH--QGKVLSAAFGERAEAAFEHVRAVQIVACGTSYHAGKVARYWFEALAGLPCSVEVASEFR 333
Cdd:PTZ00394 314 KEIYEQPESVISSMHGRIDfsSGTVQLSGFTQQSIRAILTSRRILFIACGTSLNSCLAVRPLFEELVPLPISVENASDFL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 334 YRRQVVQPGTLFVTISQSGETADTLAALKAAKELGyAHTLAICNVPESSIVRESDSCLMTRAGPEIGVASTKAFTTQLTA 413
Cdd:PTZ00394 394 DRRPRIQRDDVCFFVSQSGETADTLMALQLCKEAG-AMCVGITNVVGSSISRLTHYAIHLNAGVEVGVASTKAYTSQVVV 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 414 LLLLVLALGRRHALAAEQEAKIVRELETLPAQIRHVLQL-EDEIAAWAELFGEKHHALYLGRGAQYPVAMEGALKLKEIS 492
Cdd:PTZ00394 473 LTLVALLLSSDSVRLQERRNEIIRGLAELPAAISECLKItHDPVKALAARLKESSSILVLGRGYDLATAMEAALKVKELS 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 493 YIHAEAYPAGELKHGPLALIDNEMPVVAVAPNNELLEKLKSNLQEVQARGGELYVFA-DAEAPIENVpGVRILRVAETDE 571
Cdd:PTZ00394 553 YVHTEGIHSGELKHGPLALIDETSPVLAMCTHDKHFGLSKSAVQQVKARGGAVVVFAtEVDAELKAA-ASEIVLVPKTVD 631
|
650 660 670
....*....|....*....|....*....|....*....
gi 499261848 572 VVAPIVYSVPLQLLAYHVALIKGTDVDQPRNLAKSVTVE 610
Cdd:PTZ00394 632 CLQCVVNVIPFQLLAYYMALLRGNNVDCPRNLAKSVTVQ 670
|
|
| GFAT |
cd00714 |
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ... |
2-216 |
2.18e-119 |
|
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: 352.90 E-value: 2.18e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 2 CGIVGAVAHRNVTPILLEGLRRLEYRGYDSAGIAVIAaDGSLERVRRPGKLRELEAALESALVEGETGIAHTRWATHGVP 81
Cdd:cd00714 1 CGIVGYIGKREAVDILLEGLKRLEYRGYDSAGIAVIG-DGSLEVVKAVGKVANLEEKLAEKPLSGHVGIGHTRWATHGEP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 82 SERNAHPHV-CRERVAVVHNGIIENHEALRRQLQQKGYEFLSETDTEVVVNQIHDFLEQGFPLLEAVRATVGILEGAYAI 160
Cdd:cd00714 80 TDVNAHPHRsCDGEIAVVHNGIIENYAELKEELEAKGYKFESETDTEVIAHLIEYYYDGGLDLLEAVKKALKRLEGAYAL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499261848 161 GVVSTCEPGRLIAARKGSPLVVGLGESENFVASDVFALVGETQRFVFLEEGDLVEL 216
Cdd:cd00714 160 AVISKDEPDEIVAARNGSPLVIGIGDGENFVASDAPALLEHTRRVIYLEDGDIAVI 215
|
|
| AgaS |
COG2222 |
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ... |
256-610 |
6.61e-78 |
|
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: 250.20 E-value: 6.61e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 256 KEIHEQPVAVEKTLsgriHQGKVLSAAFGERAEAAfeHVRAVQIVACGTSYHAGKVARYWFEALAGLPCSVEVASEF-RY 334
Cdd:COG2222 2 REIAQQPEAWRRAL----AALAAAIAALLARLRAK--PPRRVVLVGAGSSDHAAQAAAYLLERLLGIPVAALAPSELvVY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 335 RRQVVQPGTLFVTISQSGETADTLAALKAAKELGyAHTLAICNVPESSIVRESDSCLMTRAGPEIGVASTKAFTTQLTAl 414
Cdd:COG2222 76 PAYLKLEGTLVVAISRSGNSPEVVAALELAKARG-ARTLAITNNPDSPLAEAADRVLPLPAGPEKSVAATKSFTTMLLA- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 415 lllvlalGRRHALAAEQEAKIVRELETLPAQIRHVLQLEDEIAAWAELFGEKHHaLYLGRGAQYPVAMEGALKLKEISYI 494
Cdd:COG2222 154 -------LLALLAAWGGDDALLAALDALPAALEAALAADWPAAALAALADAERV-VFLGRGPLYGLAREAALKLKELSAG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 495 HAEAYPAGELKHGPLALIDNEMPVVAVAPNNELLEKLKSNLQEVQARGGELYVFADaeapiENVPGVRILRVAETDEVVA 574
Cdd:COG2222 226 HAEAYSAAEFRHGPKSLVDPGTLVVVLASEDPTRELDLDLAAELRALGARVVAIGA-----EDDAAITLPAIPDLHDALD 300
|
330 340 350
....*....|....*....|....*....|....*.
gi 499261848 575 PIVYSVPLQLLAYHVALIKGTDVDQPRNLAKSVTVE 610
Cdd:COG2222 301 PLLLLVVAQRLALALALARGLDPDTPRHLNKVVKTV 336
|
|
| SIS_GlmS_GlmD_2 |
cd05009 |
SIS (Sugar ISomerase) domain repeat 2 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
454-608 |
1.57e-65 |
|
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: 211.35 E-value: 1.57e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 454 DEIAAWAELFGEKHHALYLGRGAQYPVAMEGALKLKEISYIHAEAYPAGELKHGPLALIDNEMPVVAVAPNNELLEKLKS 533
Cdd:cd05009 1 EDIKELAEKLKEAKSFYVLGRGPNYGTALEGALKLKETSYIHAEAYSAGEFKHGPIALVDEGTPVIFLAPEDRLEEKLES 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499261848 534 NLQEVQARGGELYVFADAEAPIENvpGVRILRVAETDEVVAPIVYSVPLQLLAYHVALIKGTDVDQPRNLAKSVT 608
Cdd:cd05009 81 LIKEVKARGAKVIVITDDGDAKDL--ADVVIRVPATVEELSPLLYIVPLQLLAYHLAVARGIDPDKPRNLAKSVT 153
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
2-214 |
5.49e-59 |
|
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: 196.52 E-value: 5.49e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 2 CGIVGAVAHRNVTPILLE----GLRRLEYRGYDSAGIAVIAaDGSLERVRRPGKLRELEAALESALVEGETGIAHTRWAT 77
Cdd:cd00352 1 CGIFGIVGADGAASLLLLlllrGLAALEHRGPDGAGIAVYD-GDGLFVEKRAGPVSDVALDLLDEPLKSGVALGHVRLAT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 78 HGVPSERNAHPHV-CRERVAVVHNGIIENHEALRRQLQQKGYEFLSETDTEVVVNQIHDFLEQGFpLLEAVRATVGILEG 156
Cdd:cd00352 80 NGLPSEANAQPFRsEDGRIALVHNGEIYNYRELREELEARGYRFEGESDSEVILHLLERLGREGG-LFEAVEDALKRLDG 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499261848 157 AYAIgVVSTCEPGRLIAARKG---SPLVVGLG-ESENFVASDVFALVGETQRFVF-LEEGDLV 214
Cdd:cd00352 159 PFAF-ALWDGKPDRLFAARDRfgiRPLYYGITkDGGLVFASEPKALLALPFKGVRrLPPGELL 220
|
|
| SIS_GlmS_GlmD_1 |
cd05008 |
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
297-407 |
1.35e-55 |
|
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: 184.24 E-value: 1.35e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 297 VQIVACGTSYHAGKVARYWFEALAGLPCSVEVASEFRYRRQVVQPGTLFVTISQSGETADTLAALKAAKELGyAHTLAIC 376
Cdd:cd05008 2 ILIVGCGTSYHAALVAKYLLERLAGIPVEVEAASEFRYRRPLLDEDTLVIAISQSGETADTLAALRLAKEKG-AKTVAIT 80
|
90 100 110
....*....|....*....|....*....|.
gi 499261848 377 NVPESSIVRESDSCLMTRAGPEIGVASTKAF 407
Cdd:cd05008 81 NVVGSTLAREADYVLYLRAGPEISVAATKAF 111
|
|
| PurF |
COG0034 |
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ... |
1-245 |
3.47e-33 |
|
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: 132.45 E-value: 3.47e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 1 MCGIVGAVAHRNVTPILLEGLRRLEYRGYDSAGIAViAADGSLERVRRPGKLREL--EAALESalVEGETGIAHTRWATH 78
Cdd:COG0034 7 ECGVFGIYGHEDVAQLTYYGLYALQHRGQESAGIAT-SDGGRFHLHKGMGLVSDVfdEEDLER--LKGNIAIGHVRYSTT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 79 GVPSERNAHPHV---CRERVAVVHNGIIENHEALRRQLQQKGYEFLSETDTEVVVNQIHDFLEQGfPLLEAVRATVGILE 155
Cdd:COG0034 84 GSSSLENAQPFYvnsPFGSIALAHNGNLTNAEELREELEEEGAIFQTTSDTEVILHLIARELTKE-DLEEAIKEALRRVK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 156 GAYAIgVVSTcePGRLIAAR--KG-SPLVVGLGESENFVAS--DVFALVGetqrFVFLEE---GDLVELTtesvrvygKD 227
Cdd:COG0034 163 GAYSL-VILT--GDGLIAARdpNGiRPLVLGKLEDGYVVASesCALDILG----AEFVRDvepGEIVVID--------ED 227
|
250 260
....*....|....*....|....*....
gi 499261848 228 GGRVERPVHETRLA-----------PDSV 245
Cdd:COG0034 228 GLRSRQFAEKPRPApcifeyvyfarPDSV 256
|
|
| GPATase_N |
cd00715 |
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ... |
2-246 |
4.02e-29 |
|
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: 116.02 E-value: 4.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 2 CGIVGAVAHRNVTPILLEGLRRLEYRGYDSAGIAViaADGSLERVRR----------PGKLRELEaalesalveGETGIA 71
Cdd:cd00715 1 CGVFGIYGAEDAARLTYLGLYALQHRGQESAGIAT--SDGKRFHTHKgmglvsdvfdEEKLRRLP---------GNIAIG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 72 HTRWATHGVPSERNAHPHVCRER---VAVVHNGIIENHEALRRQLQQKGYEFLSETDTEVVVNQIHDFLEQGfPLLEAVR 148
Cdd:cd00715 70 HVRYSTAGSSSLENAQPFVVNSPlggIALAHNGNLVNAKELREELEEEGRIFQTTSDSEVILHLIARSLAKD-DLFEAII 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 149 ATVGILEGAYAIgVVSTcePGRLIAAR--KG-SPLVVGLGESENFV-ASD--VFALVGETqrFVF-LEEGDLVELTtesv 221
Cdd:cd00715 149 DALERVKGAYSL-VIMT--ADGLIAVRdpHGiRPLVLGKLEGDGYVvASEscALDIIGAE--FVRdVEPGEIVVID---- 219
|
250 260
....*....|....*....|....*
gi 499261848 222 rvygKDGGRVERPVHETRLAPDSVE 246
Cdd:cd00715 220 ----DDGLESSQRAPKPKPAPCIFE 240
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
297-407 |
6.20e-29 |
|
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: 111.62 E-value: 6.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 297 VQIVACGTSYHAGKVARYWFEALAGLPCSVEVASEFRYR-RQVVQPGTLFVTISQSGETADTLAALKAAKELGyAHTLAI 375
Cdd:pfam01380 8 IFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGvLALVDEDDLVIAISYSGETKDLLAAAELAKARG-AKIIAI 86
|
90 100 110
....*....|....*....|....*....|..
gi 499261848 376 CNVPESSIVRESDSCLMTRAGPEIGVASTKAF 407
Cdd:pfam01380 87 TDSPGSPLAREADHVLYINAGPETGVASTKSI 118
|
|
| purF |
TIGR01134 |
amidophosphoribosyltransferase; Alternate name: glutamine phosphoribosylpyrophosphate (PRPP) ... |
2-261 |
3.45e-26 |
|
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: 111.64 E-value: 3.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 2 CGIVGAVAHRNVTPILL-EGLRRLEYRGYDSAGIAViaADGSLERVRR-PGKLRELEAALESALVEGETGIAHTRWATHG 79
Cdd:TIGR01134 1 CGVVGIYGQEEVAASLTyYGLYALQHRGQESAGISV--FDGNRFRLHKgNGLVSDVFNEEHLQRLKGNVGIGHVRYSTAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 80 VPSERNAHPHVCRER---VAVVHNGIIENHEALRRQLQQKGYEFLSETDTEVVVNQIHDFLEQGFPLLEAVRATVGILEG 156
Cdd:TIGR01134 79 SSGLENAQPFVVNSPyggLALAHNGNLVNADELRRELEEEGRHFNTTSDSEVLLHLLAHNDESKDDLFDAVARVLERVRG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 157 AYAIGVVStcePGRLIAARK--G-SPLVVGLGESENFVASDVFAL--VGETQrFVFLEEGDLVELttesvrvygKDGGRV 231
Cdd:TIGR01134 159 AYALVLMT---EDGLVAVRDphGiRPLVLGRRGDGYVVASESCALdiLGAEF-VRDVEPGEVVVI---------FDGGLE 225
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 499261848 232 ERPVHETRLA-----------PDSVERGEYRHYMQKEIHEQ 261
Cdd:TIGR01134 226 SRQCARRPRApcvfeyvyfarPDSVIDGISVYYARKRMGKE 266
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
465-593 |
8.30e-25 |
|
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: 100.07 E-value: 8.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 465 EKHHALYLGRGAQYPVAMEGALKLKEISYIHAEAYPAGELKHGPLALIDNEMPVVAVAPNNELLEKLKsNLQEVQARGGE 544
Cdd:pfam01380 4 KAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGVLALVDEDDLVIAISYSGETKDLLA-AAELAKARGAK 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 499261848 545 LYVFAD-AEAPIENVPGVrILRVAETDEVVAPIVYSVPLQLLAYHVALIK 593
Cdd:pfam01380 83 IIAITDsPGSPLAREADH-VLYINAGPETGVASTKSITAQLAALDALAVA 131
|
|
| PLN02440 |
PLN02440 |
amidophosphoribosyltransferase |
1-198 |
5.67e-23 |
|
amidophosphoribosyltransferase
Pssm-ID: 215241 [Multi-domain] Cd Length: 479 Bit Score: 102.45 E-value: 5.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 1 MCGIVGAVAHRNVTPILLEGLRRLEYRGYDSAGIaVIAADGSLERVRRPGKLREL--EAALESalVEGETGIAHTRWATH 78
Cdd:PLN02440 1 ECGVVGIFGDPEASRLCYLGLHALQHRGQEGAGI-VTVDGNRLQSITGNGLVSDVfdESKLDQ--LPGDIAIGHVRYSTA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 79 GVPSERNAHPHVCRER---VAVVHNGIIENHEALRRQLQQKGYEFLSETDTEVVVNQIHDFLEQgfPLLEAVRATVGILE 155
Cdd:PLN02440 78 GASSLKNVQPFVANYRfgsIGVAHNGNLVNYEELRAKLEENGSIFNTSSDTEVLLHLIAISKAR--PFFSRIVDACEKLK 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499261848 156 GAYAIGVVSTcepGRLIAARKGS---PLVVGLGESENFV-ASDVFAL 198
Cdd:PLN02440 156 GAYSMVFLTE---DKLVAVRDPHgfrPLVMGRRSNGAVVfASETCAL 199
|
|
| GlxB |
cd01907 |
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ... |
2-198 |
4.14e-20 |
|
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: 90.02 E-value: 4.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 2 CGIVGAV---AHRNVTPILLEGLRRLEYRG-YDSAGIA--------VIAADGSLERVRRPGKLRELEAALESALVEGETG 69
Cdd:cd01907 1 CGIFGIMskdGEPFVGALLVEMLDAMQERGpGDGAGFAlygdpdafVYSSGKDMEVFKGVGYPEDIARRYDLEEYKGYHW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 70 IAHTRWATHGVPSERNAHPhVCRERVAVVHNGIIENHEALRRQLQQKGYEFLSETDTEVVVNQIHDFL------------ 137
Cdd:cd01907 81 IAHTRQPTNSAVWWYGAHP-FSIGDIAVVHNGEISNYGSNREYLERFGYKFETETDTEVIAYYLDLLLrkgglpleyykh 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499261848 138 -------EQGFPLLEAVRATVGILEGAYAIgVVSTcePGRLIAAR---KGSPLVVGLGESENFVASDVFAL 198
Cdd:cd01907 160 iirmpeeERELLLALRLTYRLADLDGPFTI-IVGT--PDGFIVIRdriKLRPAVVAETDDYVAIASEECAI 227
|
|
| PRK05793 |
PRK05793 |
amidophosphoribosyltransferase; Provisional |
2-198 |
5.41e-20 |
|
amidophosphoribosyltransferase; Provisional
Pssm-ID: 235611 [Multi-domain] Cd Length: 469 Bit Score: 93.17 E-value: 5.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 2 CGIVGAVA--HRNVTPILLEGLRRLEYRGYDSAGIAViaADGS----------LERVRRPGKLRELEaalesalveGETG 69
Cdd:PRK05793 15 CGVFGVFSknNIDVASLTYYGLYALQHRGQESAGIAV--SDGEkikvhkgmglVSEVFSKEKLKGLK---------GNSA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 70 IAHTRWATHGVPSERNAHPHVCRER---VAVVHNGIIENHEALRRQLQQKGYEFLSETDTEVVVNQIHDFLEQGfpLLEA 146
Cdd:PRK05793 84 IGHVRYSTTGASDLDNAQPLVANYKlgsIAIAHNGNLVNADVIRELLEDGGRIFQTSIDSEVILNLIARSAKKG--LEKA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499261848 147 VRATVGILEGAYAIGVVSTcepGRLIAAR--KG-SPLVVGLGESENFVASDVFAL 198
Cdd:PRK05793 162 LVDAIQAIKGSYALVILTE---DKLIGVRdpHGiRPLCLGKLGDDYILSSESCAL 213
|
|
| GATase_6 |
pfam13522 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
63-194 |
2.11e-19 |
|
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: 84.28 E-value: 2.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 63 LVEGETGIAHTRWATHGVPSERNaHPHVCR-ERVAVVHNGIIENHEALRRQLQQKGYEFLSETDTEVVVNQIHDFLEQGF 141
Cdd:pfam13522 7 WVEGGVALGHVRLAIVDLPDAGN-QPMLSRdGRLVLVHNGEIYNYGELREELADLGHAFRSRSDTEVLLALYEEWGEDCL 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 499261848 142 PLleavratvgiLEGAYAIGVVStCEPGRLIAARKG---SPLVVGLGESENFVASD 194
Cdd:pfam13522 86 ER----------LRGMFAFAIWD-RRRRTLFLARDRlgiKPLYYGILGGGFVFASE 130
|
|
| AsnB |
cd00712 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ... |
2-199 |
6.79e-14 |
|
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: 71.05 E-value: 6.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 2 CGIVGAVAHRNVTP---ILLEGLRRLEYRGYDSAGIaviaadgslervrrpgklreleaalesaLVEGETGIAHTRWATh 78
Cdd:cd00712 1 CGIAGIIGLDGASVdraTLERMLDALAHRGPDGSGI----------------------------WIDEGVALGHRRLSI- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 79 gVPSERNAHPHVCRE-RVAVVHNGIIENHEALRRQLQQKGYEFLSETDTEVVvnqIHDFLEQGfplleavRATVGILEGA 157
Cdd:cd00712 52 -IDLSGGAQPMVSEDgRLVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVI---LHLYEEWG-------EDCLERLNGM 120
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499261848 158 YAIGVVSTcEPGRLIAAR-----KgsPLVVGLGESENFVASDVFALV 199
Cdd:cd00712 121 FAFALWDK-RKRRLFLARdrfgiK--PLYYGRDGGGLAFASELKALL 164
|
|
| YafJ |
COG0121 |
Predicted glutamine amidotransferase YafJ [General function prediction only]; |
33-155 |
1.03e-12 |
|
Predicted glutamine amidotransferase YafJ [General function prediction only];
Pssm-ID: 439891 [Multi-domain] Cd Length: 248 Bit Score: 68.45 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 33 GIAVIAADGSLERVRRPGKLRE-LEAALESALVEGETGIAHTRWATHGVPSERNAHPHVCRERVaVVHNGIIENHEALRR 111
Cdd:COG0121 42 GIGWYEGDGEPRLYRDPLPAWSdPNLRLLARPIKSRLVIAHVRKATVGPVSLENTHPFRGGRWL-FAHNGQLDGFDRLRR 120
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 499261848 112 QLQQKGYEFL-----SETDTEVVVNQIHDFLEQGFP-LLEAVRATVGILE 155
Cdd:COG0121 121 RLAEELPDELyfqpvGTTDSELAFALLLSRLRDGGPdPAEALAEALRELA 170
|
|
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
1-175 |
1.98e-12 |
|
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; Asparagine synthetase B (glutamine-hydrolyzing) is part of the Pathway/BioSystem: Asparagine biosynthesis
Pssm-ID: 440136 [Multi-domain] Cd Length: 558 Bit Score: 69.87 E-value: 1.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 1 MCGIVGAVA--HRNVTPILLEGLRRLEYRGYDSAGIaviaadgslervrrpgklreleaalesaLVEGETGIAHTRWATh 78
Cdd:COG0367 1 MCGIAGIIDfdGGADREVLERMLDALAHRGPDGSGI----------------------------WVDGGVALGHRRLSI- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 79 gVPSERNAH-PHVCRE-RVAVVHNGIIENHEALRRQLQQKGYEFLSETDTEVVVnqiHDFLEQGfplLEAVRAtvgiLEG 156
Cdd:COG0367 52 -IDLSEGGHqPMVSEDgRYVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVIL---HAYEEWG---EDCLER----LNG 120
|
170
....*....|....*....
gi 499261848 157 AYAIGVVSTCEpGRLIAAR 175
Cdd:COG0367 121 MFAFAIWDRRE-RRLFLAR 138
|
|
| GATase_7 |
pfam13537 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
72-175 |
4.97e-12 |
|
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: 63.31 E-value: 4.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 72 HTRWAThgVPSERNAHPHVCRE--RVAVVHNGIIENHEALRRQLQQKGYEFLSETDTEVVVnqihdfleqgfPLLEAV-- 147
Cdd:pfam13537 1 HRRLSI--IDLEGGAQPMVSSEdgRYVIVFNGEIYNYRELRAELEAKGYRFRTHSDTEVIL-----------HLYEAEwg 67
|
90 100
....*....|....*....|....*...
gi 499261848 148 RATVGILEGAYAIGVVSTCEpGRLIAAR 175
Cdd:pfam13537 68 EDCVDRLNGMFAFAIWDRRR-QRLFLAR 94
|
|
| SIS_1 |
cd05710 |
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ... |
300-396 |
9.98e-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: 59.51 E-value: 9.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 300 VACGTSYHAGKVARYWFEALAGLPCSVEVASEFRYRRQV-VQPGTLFVTISQSGETADTLAALKAAKELGyAHTLAICNV 378
Cdd:cd05710 5 VGCGGSLADMYPAKYFLKKESKLPVFVYNAAEFLHTGPKrLTEKSVVILASHSGNTKETVAAAKFAKEKG-ATVIGLTDD 83
|
90
....*....|....*...
gi 499261848 379 PESSIVRESDSCLMTRAG 396
Cdd:cd05710 84 EDSPLAKLADYVIVYGFE 101
|
|
| YafJ |
cd01908 |
Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine ... |
1-179 |
1.04e-10 |
|
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: 62.41 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 1 MCGIVGAVAhrnvTPILLEGL----------RRLEYRGY------DSAGIAVIAADGSLERVRRPGK-------LRELEA 57
Cdd:cd01908 1 MCRLLGYSG----APIPLEPLlirpshsllvQSGGPREMkgtvhaDGWGIGWYEGKGGRPFRYRSPLpawsdinLESLAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 58 ALESALVegetgIAHTRWATHGVPSERNAHPHVcRERVAVVHNGIIENHEALRRQLQQKG-YEFLSETDTEVVVNQIHDF 136
Cdd:cd01908 77 PIKSPLV-----LAHVRAATVGPVSLENCHPFT-RGRWLFAHNGQLDGFRLLRRRLLRLLpRLPVGTTDSELAFALLLSR 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499261848 137 LEQGFP-----LLEAVRATVGILEGAYAIGVVSTC--EPGRLIAARKGSP 179
Cdd:cd01908 151 LLERDPldpaeLLDAILQTLRELAALAPPGRLNLLlsDGEYLIATRYASA 200
|
|
| PTZ00077 |
PTZ00077 |
asparagine synthetase-like protein; Provisional |
1-198 |
1.30e-09 |
|
asparagine synthetase-like protein; Provisional
Pssm-ID: 185431 [Multi-domain] Cd Length: 586 Bit Score: 60.88 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 1 MCGIVGAV-----AHRnVTPILLEGLRRLEYRGYDSAGIAVIAADGSLERVrrpgklreleaalesalvegetgIAHTRW 75
Cdd:PTZ00077 1 MCGILAIFnskgeRHE-LRRKALELSKRLRHRGPDWSGIIVLENSPGTYNI-----------------------LAHERL 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 76 ATHGVPSERnaHP-HVCRERVAVVHNGIIENHEALRRQLQQKGYEFLSETDTEVVVNQIHDFLEQGFPlleavratvGIL 154
Cdd:PTZ00077 57 AIVDLSDGK--QPlLDDDETVALMQNGEIYNHWEIRPELEKEGYKFSSNSDCEIIGHLYKEYGPKDFW---------NHL 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 499261848 155 EGAYAiGVVSTCEPGRLIAARKG---SPLVVGLGES-ENFVASDVFAL 198
Cdd:PTZ00077 126 DGMFA-TVIYDMKTNTFFAARDHigiIPLYIGYAKDgSIWFSSELKAL 172
|
|
| asnB |
PRK09431 |
asparagine synthetase B; Provisional |
1-202 |
1.46e-09 |
|
asparagine synthetase B; Provisional
Pssm-ID: 236513 [Multi-domain] Cd Length: 554 Bit Score: 60.69 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 1 MCGIVGAVAHRNVTPIL----LEGLRRLEYRGYDSAGIaviaadgslervrrpgklreleaalesalVEGETGI-AHTRW 75
Cdd:PRK09431 1 MCGIFGILDIKTDADELrkkaLEMSRLMRHRGPDWSGI-----------------------------YASDNAIlGHERL 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 76 ATHGVpsERNAHPHVCRERVAVVH-NGIIENHEALRRQLQQKgYEFLSETDTEVVVnqiHDFLEQGFPLLEAvratvgiL 154
Cdd:PRK09431 52 SIVDV--NGGAQPLYNEDGTHVLAvNGEIYNHQELRAELGDK-YAFQTGSDCEVIL---ALYQEKGPDFLDD-------L 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499261848 155 EGAYAIGVVSTcEPGRLIAARK--G-SPLVVGLGESENF-VASDVFALVGET 202
Cdd:PRK09431 119 DGMFAFALYDS-EKDAYLIARDpiGiIPLYYGYDEHGNLyFASEMKALVPVC 169
|
|
| SIS_RpiR |
cd05013 |
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ... |
295-391 |
5.47e-09 |
|
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: 54.93 E-value: 5.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 295 RAVQIVACGTSYHagkVARYWFEALAGLPCSVEVASEFRYRRQV---VQPGTLFVTISQSGETADTLAALKAAKELGyAH 371
Cdd:cd05013 14 RRIYIFGVGSSGL---VAEYLAYKLLRLGKPVVLLSDPHLQLMSaanLTPGDVVIAISFSGETKETVEAAEIAKERG-AK 89
|
90 100
....*....|....*....|
gi 499261848 372 TLAICNVPESSIVRESDSCL 391
Cdd:cd05013 90 VIAITDSANSPLAKLADIVL 109
|
|
| asn_synth_AEB |
TIGR01536 |
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing ... |
93-175 |
9.48e-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: 58.11 E-value: 9.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 93 ERVAVVHNGIIENHEALRRQLQQKGYEFLSETDTEVVvnqIHDFLEQGfplleavRATVGILEGAYAIGVVSTcEPGRLI 172
Cdd:TIGR01536 66 KTYVIVFNGEIYNHEELREELEAKGYTFQTDSDTEVI---LHLYEEWG-------EECVDRLDGMFAFALWDS-EKGELF 134
|
...
gi 499261848 173 AAR 175
Cdd:TIGR01536 135 LAR 137
|
|
| RpiR |
COG1737 |
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ... |
285-395 |
1.09e-08 |
|
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains [Transcription];
Pssm-ID: 441343 [Multi-domain] Cd Length: 286 Bit Score: 56.86 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 285 ERAEAAFEHVRAVQIVACGTSYHAGKVARYWFeALAGLPCSVEVASEFRYRRQV--VQPGTLFVTISQSGETADTLAALK 362
Cdd:COG1737 125 ERAVDLLAKARRIYIFGVGASAPVAEDLAYKL-LRLGKNVVLLDGDGHLQAESAalLGPGDVVIAISFSGYTRETLEAAR 203
|
90 100 110
....*....|....*....|....*....|...
gi 499261848 363 AAKELGyAHTLAICNVPESSIVRESDSCLMTRA 395
Cdd:COG1737 204 LAKERG-AKVIAITDSPLSPLAKLADVVLYVPS 235
|
|
| SIS |
cd04795 |
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
297-378 |
6.79e-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: 50.45 E-value: 6.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 297 VQIVACGTSYHAGKVARYWFEALAGLPCSVEVASEFRYRRQVV--QPGTLFVTISQSGETADTLAALKAAKELG---YAH 371
Cdd:cd04795 1 IFVIGIGGSGAIAAYFALELLELTGIEVVALIATELEHASLLSllRKGDVVIALSYSGRTEELLAALEIAKELGipvIAI 80
|
....*..
gi 499261848 372 TLAICNV 378
Cdd:cd04795 81 TDALAVS 87
|
|
| SIS |
cd04795 |
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
470-551 |
7.63e-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: 50.07 E-value: 7.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 470 LYLGRGAQYPVAMEGALKLKEISYIHAEAYPAGELKHGPLALIDNEM-PVVAVAPNNElLEKLKSNLQEVQARGGELYVF 548
Cdd:cd04795 2 FVIGIGGSGAIAAYFALELLELTGIEVVALIATELEHASLLSLLRKGdVVIALSYSGR-TEELLAALEIAKELGIPVIAI 80
|
...
gi 499261848 549 ADA 551
Cdd:cd04795 81 TDA 83
|
|
| frlB |
PRK11382 |
fructoselysine 6-phosphate deglycase; |
297-601 |
1.75e-06 |
|
fructoselysine 6-phosphate deglycase;
Pssm-ID: 183111 [Multi-domain] Cd Length: 340 Bit Score: 50.39 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 297 VQIVACGTSYHAGKVARYWFEALAGLPCSVEVASEF----RYRrqvVQPGTLFVTISQSGETADTLAALkaakELGYAht 372
Cdd:PRK11382 47 IYFVACGSPLNAAQTAKHLADRFSDLQVYAISGWEFcdntPYR---LDDRCAVIGVSDYGKTEEVIKAL----ELGRA-- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 373 laiCNVPESSIVRESDSCLMTRAGPEIGVASTKAFTTQLTALLLLVLALGRRHALAAEQeAKIVRELETLPAQIRHVLQL 452
Cdd:PRK11382 118 ---CGALTAAFTKRADSPITSAAEFSIDYQADCIWEIHLLLCYSVVLEMITRLAPNAEI-GKIKNDLKQLPNALGHLVRT 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 453 -EDEIAAWAELFGEKHHALYLGRGAQYPVAM-EGALKLKEISYIHAEAYPAGELKHGPLALIDNEMPVVAVAPNNELLEK 530
Cdd:PRK11382 194 wEEKGRQLGELASQWPMIYTVAAGPLRPLGYkEGIVTLMEFTWTHGCVIESGEFRHGPLEIVEPGVPFLFLLGNDESRHT 273
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499261848 531 LKSNLQEVQARGGELYVFADAEAPIENVPGvrilrvaetdevVAPIVYSVPLQLLAYHVALIKGTDVDQPR 601
Cdd:PRK11382 274 TERAINFVKQRTDNVIVIDYAEISQGLHPW------------LAPFLMFVPMEWLCYYLSIYKDHNPDERR 332
|
|
| SIS_Etherase |
cd05007 |
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ... |
348-404 |
4.22e-05 |
|
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: 45.59 E-value: 4.22e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 499261848 348 ISQSGETADTLAALKAAKELGyAHTLAICNVPESSIVRESDSCLMTRAGPEIGVAST 404
Cdd:cd05007 125 IAASGRTPYVLGALRYARARG-ALTIGIACNPGSPLLQLADIAIALITGPEVVAGST 180
|
|
| murQ |
PRK05441 |
N-acetylmuramic acid-6-phosphate etherase; Reviewed |
346-406 |
4.78e-05 |
|
N-acetylmuramic acid-6-phosphate etherase; Reviewed
Pssm-ID: 235467 [Multi-domain] Cd Length: 299 Bit Score: 45.54 E-value: 4.78e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499261848 346 VTISQSGETADTLAALKAAKELGyAHTLAICNVPESSIVRESDSCLMTRAGPEIGVAST--KA 406
Cdd:PRK05441 136 VGIAASGRTPYVIGALEYARERG-ALTIGISCNPGSPLSKEADIAIEVVVGPEVLTGSTrmKA 197
|
|
| SIS_PHI |
cd05005 |
Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) ... |
339-391 |
1.02e-04 |
|
Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) superfamily. In the ribulose monophosphate pathway of formaldehyde fixation, hexulose-6-phosphate synthase catalyzes the condensation of ribulose-5-phosphate with formadelhyde to become hexulose-6-phosphate, which is then isomerized to fructose-6-phosphate by PHI.
Pssm-ID: 240138 [Multi-domain] Cd Length: 179 Bit Score: 43.33 E-value: 1.02e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 499261848 339 VQPGTLFVTISQSGETADTLAALKAAKELGyAHTLAICNVPESSIVRESDSCL 391
Cdd:cd05005 73 IGPGDLLIAISGSGETSSVVNAAEKAKKAG-AKVVLITSNPDSPLAKLADVVV 124
|
|
| SIS_AgaS_like |
cd05010 |
AgaS-like protein. AgaS contains a SIS (Sugar ISomerase) domain which is found in many ... |
471-600 |
2.74e-04 |
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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: 41.46 E-value: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 471 YLGRGAQYPVAMEGALKLKEIS--YIHAEAYPAGELKHGPLALIDNEMPVVAVAPNNE--------LLEKLKSNLQ--EV 538
Cdd:cd05010 3 YLGSGPLAGLAREAALKVLELTagKVATVYDSPLGFRHGPKSLVDDDTLVVVFVSNDPytrqydldLLKELRRDGIaaRV 82
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90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499261848 539 QARGGElyvfADAEAPIENVPGVRILRVAETDEVVAPivYSVPLQLLAYHVALIKGTDVDQP 600
Cdd:cd05010 83 IAISPE----SDAGIEDNSHYYLPGSRDLDDVYLAFP--YILYAQLFALFNSIALGLTPDNP 138
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| SIS_PGI_PMI_1 |
cd05017 |
The members of this protein family contain the SIS (Sugar ISomerase) domain and have both the ... |
298-376 |
9.16e-04 |
|
The members of this protein family contain the SIS (Sugar ISomerase) domain and have both the phosphoglucose isomerase (PGI) and the phosphomannose isomerase (PMI) functions. These functions catalyze the reversible reactions of glucose 6-phosphate to fructose 6-phosphate, and mannose 6-phosphate to fructose 6-phosphate, respectively at an equal rate. This protein contains two SIS domains. This alignment is based on the first SIS domain.
Pssm-ID: 240148 [Multi-domain] Cd Length: 119 Bit Score: 39.56 E-value: 9.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499261848 298 QIVACGT--SYHAGKVARYWFEALAGLPCSVeVASEFRYRRqvVQPGTLFVTISQSGETADTLAALKAAKELGyAHTLAI 375
Cdd:cd05017 1 NIVILGMggSGIGGDLLESLLLDEAKIPVYV-VKDYTLPAF--VDRKTLVIAVSYSGNTEETLSAVEQAKERG-AKIVAI 76
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gi 499261848 376 C 376
Cdd:cd05017 77 T 77
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| PRK13937 |
PRK13937 |
phosphoheptose isomerase; Provisional |
331-368 |
8.02e-03 |
|
phosphoheptose isomerase; Provisional
Pssm-ID: 184408 [Multi-domain] Cd Length: 188 Bit Score: 37.91 E-value: 8.02e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 499261848 331 EFRYRRQV---VQPGTLFVTISQSGETADTLAALKAAKELG 368
Cdd:PRK13937 93 ERVFSRQVealGRPGDVLIGISTSGNSPNVLAALEKARELG 133
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