|
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: 1078.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 1 MCGIVGAVAQRDVAEILINGLHRLEYRGYDSAGVAVINkQNELQRIRCLGKVKALDEAVSEKPLIGGTGIAHTRWATHGE 80
Cdd:COG0449 1 MCGIVGYIGKRDAAPILLEGLKRLEYRGYDSAGIAVLD-DGGLEVRKAVGKLANLEEKLAEEPLSGTIGIGHTRWATHGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 81 PSETNAHPHSS--GTFAVVHNGIIENHEELRELLKSRGYVFLSQTDTEVIAHLVEWEMRSTDSLLEAVQKSVKQLTGAYG 158
Cdd:COG0449 80 PSDENAHPHTScsGRIAVVHNGIIENYAELREELEAKGHTFKSETDTEVIAHLIEEYLKGGGDLLEAVRKALKRLEGAYA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 159 MVVMDSRHPEHLVAARSGSPLVIGLGIGENFLASDQLALLSVTRRFIFLEEGDIAEITRRTVDIYDTHGNKAKREIHESN 238
Cdd:COG0449 160 LAVISADEPDRIVAARKGSPLVIGLGEGENFLASDVPALLPYTRRVIYLEDGEIAVLTRDGVEIYDLDGEPVEREVKTVD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 239 LENDAAEKGKFRHFMQKEIYEQPTALINTMEGRINHENVIVDSIGNGAKGILEKVEHIQIVACGTSYNAGMVARYWFESL 318
Cdd:COG0449 240 WDAEAAEKGGYPHFMLKEIHEQPEAIRDTLRGRLDEDGRVVLDELNLAAEDLRNIDRIYIVACGTSYHAGLVGKYLIEEL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 319 AGVSCDVEIASEFRYRKFVTRPNSLLITLSQSGETADTLAALRLAKEKGyMAALTICNVAGSSLVRESDLAFMTRAGVEV 398
Cdd:COG0449 320 ARIPVEVEIASEFRYRDPVVDPGTLVIAISQSGETADTLAALREAKEKG-AKVLAICNVVGSTIARESDAVLYTHAGPEI 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 399 GVASTKAFTTQLAALLMLVTALGKVKGHISVEKEREIIKAMQSLPAEIEKALAFDREIEALAEDFAEKHHALFLGRGAFY 478
Cdd:COG0449 399 GVASTKAFTTQLAALYLLALYLARARGTLSAEEEAELLEELRKLPEKIEEVLDLEEQIEELAEKYADARNALFLGRGINY 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 479 PIAVEASLKLKEISYIHAEAYAAGELKHGPLALIDADMPVIVVAPNNELLEKVKSNIEEVRARGGQLYVFADKEAGFTPS 558
Cdd:COG0449 479 PVALEGALKLKEISYIHAEGYAAGELKHGPIALIDEGMPVVAIAPQDELYEKTLSNIQEVKARGGKVIAIADEGDEEVEE 558
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 491949326 559 EGMKIITMPKVNDIVAPIFYTIPMQLLSYYVALIKGTDVDQPRNLAKSVTVE 610
Cdd:COG0449 559 LADDVIEVPEVDELLAPILAVVPLQLLAYHVAVLRGTDVDQPRNLAKSVTVE 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: 1065.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 1 MCGIVGAVAQRDVAEILINGLHRLEYRGYDSAGVAVINkQNELQRIRCLGKVKALDEAVSEKPLIGGTGIAHTRWATHGE 80
Cdd:PRK00331 1 MCGIVGYVGQRNAAEILLEGLKRLEYRGYDSAGIAVLD-DGGLEVRKAVGKVANLEAKLEEEPLPGTTGIGHTRWATHGK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 81 PSETNAHPH--SSGTFAVVHNGIIENHEELRELLKSRGYVFLSQTDTEVIAHLVEWEMRSTDSLLEAVQKSVKQLTGAYG 158
Cdd:PRK00331 80 PTERNAHPHtdCSGRIAVVHNGIIENYAELKEELLAKGHVFKSETDTEVIAHLIEEELKEGGDLLEAVRKALKRLEGAYA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 159 MVVMDSRHPEHLVAARSGSPLVIGLGIGENFLASDQLALLSVTRRFIFLEEGDIAEITRRTVDIYDTHGNKAKREIHESN 238
Cdd:PRK00331 160 LAVIDKDEPDTIVAARNGSPLVIGLGEGENFLASDALALLPYTRRVIYLEDGEIAVLTRDGVEIFDFDGNPVEREVYTVD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 239 LENDAAEKGKFRHFMQKEIYEQPTALINTMEGRINHenvivDSIGNGAKGILEKVEHIQIVACGTSYNAGMVARYWFESL 318
Cdd:PRK00331 240 WDASAAEKGGYRHFMLKEIYEQPEAIRDTLEGRLDE-----LGEGELADEDLKKIDRIYIVACGTSYHAGLVAKYLIESL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 319 AGVSCDVEIASEFRYRKFVTRPNSLLITLSQSGETADTLAALRLAKEKGyMAALTICNVAGSSLVRESDLAFMTRAGVEV 398
Cdd:PRK00331 315 AGIPVEVEIASEFRYRDPVLSPKTLVIAISQSGETADTLAALRLAKELG-AKTLAICNVPGSTIARESDAVLYTHAGPEI 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 399 GVASTKAFTTQLAALLMLVTALGKVKGHISVEKEREIIKAMQSLPAEIEKALAFDREIEALAEDFAEKHHALFLGRGAFY 478
Cdd:PRK00331 394 GVASTKAFTAQLAVLYLLALALAKARGTLSAEEEADLVHELRELPALIEQVLDLKEQIEELAEDFADARNALFLGRGVDY 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 479 PIAVEASLKLKEISYIHAEAYAAGELKHGPLALIDADMPVIVVAPNNELLEKVKSNIEEVRARGGQLYVFADkEAGFTPS 558
Cdd:PRK00331 474 PVALEGALKLKEISYIHAEGYAAGELKHGPIALIDEGMPVVAIAPNDELYEKTKSNIQEVKARGARVIVIAD-EGDEVAE 552
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 491949326 559 EGMKIITMPKVNDIVAPIFYTIPMQLLSYYVALIKGTDVDQPRNLAKSVTVE 610
Cdd:PRK00331 553 EADDVIEVPEVHELLAPLLYVVPLQLLAYHVALARGTDVDKPRNLAKSVTVE 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: 952.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 2 CGIVGAVAQRDVAEILINGLHRLEYRGYDSAGVAVINKQnELQRIRCLGKVKALDEAVSEKPLIGGTGIAHTRWATHGEP 81
Cdd:TIGR01135 1 CGIVGYIGQRDAVPILLEGLKRLEYRGYDSAGIAVVDEG-KLFVRKAVGKVAELANKLGEKPLPGGVGIGHTRWATHGKP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 82 SETNAHPH--SSGTFAVVHNGIIENHEELRELLKSRGYVFLSQTDTEVIAHLVEWEMRSTDSLLEAVQKSVKQLTGAYGM 159
Cdd:TIGR01135 80 TDENAHPHtdEGGRIAVVHNGIIENYAELREELEARGHVFSSDTDTEVIAHLIEEELREGGDLLEAVQKALKQLRGAYAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 160 VVMDSRHPEHLVAARSGSPLVIGLGIGENFLASDQLALLSVTRRFIFLEEGDIAEITRRTVDIYDTHGNKAKREIHESNL 239
Cdd:TIGR01135 160 AVLHADHPETLVAARSGSPLIVGLGDGENFVASDVTALLPYTRRVIYLEDGDIAILTKDGVEIYNFEGAPVQREVRVIDW 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 240 ENDAAEKGKFRHFMQKEIYEQPTALINTMEGRINHENVIVDSIGngAKGILEKVEHIQIVACGTSYNAGMVARYWFESLA 319
Cdd:TIGR01135 240 DLDAAEKGGYRHFMLKEIYEQPRALRDTLEGRIEENGGVFEELG--AEELLKNIDRIQIVACGTSYHAGLVAKYLIERLA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 320 GVSCDVEIASEFRYRKFVTRPNSLLITLSQSGETADTLAALRLAKEKGyMAALTICNVAGSSLVRESDLAFMTRAGVEVG 399
Cdd:TIGR01135 318 GIPVEVEIASEFRYRKPVVDKDTLVIAISQSGETADTLEALRLAKELG-AKTLGICNVPGSTLVREADHTLYTRAGPEIG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 400 VASTKAFTTQLAALLMLVTALGKVKGHISVEKEREIIKAMQSLPAEIEKALAFDREIEALAEDFAEKHHALFLGRGAFYP 479
Cdd:TIGR01135 397 VASTKAFTTQLTVLYLLALALAKARGTLSAEEEAELVDALRRLPDLVEQVLLADESIAELAERYADKRNFLFLGRGLGYP 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 480 IAVEASLKLKEISYIHAEAYAAGELKHGPLALIDADMPVIVVAPNNELLEKVKSNIEEVRARGGQLYVFADKEAGFTPSE 559
Cdd:TIGR01135 477 IALEGALKLKEISYIHAEGYPAGELKHGPIALIDEGLPVVAIAPKDSLLEKTKSNVEEVKARGARVIVFAPEDDETIASV 556
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 491949326 560 GMKIITMPKVNDIVAPIFYTIPMQLLSYYVALIKGTDVDQPRNLAKSVTVE 610
Cdd:TIGR01135 557 ADDVIKLPEVEELLAPIVYTIPLQLLAYHIALAKGTDVDKPRNLAKSVTVE 607
|
|
| PLN02981 |
PLN02981 |
glucosamine:fructose-6-phosphate aminotransferase |
1-610 |
3.82e-173 |
|
glucosamine:fructose-6-phosphate aminotransferase
Pssm-ID: 215531 [Multi-domain] Cd Length: 680 Bit Score: 507.75 E-value: 3.82e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 1 MCGIVGAV------AQRDVAEILINGLHRLEYRGYDSAGVAVINKQNELQR----IRCLGKVKAL----DEAVSEKPLIG 66
Cdd:PLN02981 1 MCGIFAYLnynvprERRFILEVLFNGLRRLEYRGYDSAGIAIDNDPSLESSsplvFREEGKIESLvrsvYEEVAETDLNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 67 G------TGIAHTRWATHGEPSETNAHPHSSGT---FAVVHNGIIENHEELRELLKSRGYVFLSQTDTEVIAHLVEW--- 134
Cdd:PLN02981 81 DlvfenhAGIAHTRWATHGPPAPRNSHPQSSGPgneFLVVHNGIITNYEVLKETLLRHGFTFESDTDTEVIPKLAKFvfd 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 135 ---EMRSTDSLLEAVQKSVKQLTGAYGMVVMDSRHPEHLVAARSGSPLVIG---LGIGEN-------------------- 188
Cdd:PLN02981 161 klnEEEGDVTFSQVVMEVMRQLEGAYALIFKSPHYPNELVACKRGSPLLLGvkeLPEEKNssavftsegfltknrdkpke 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 189 -FLASDQLALLSVTRRFIFLEEGDIAEITRRTVDIYDTHGNKAKREIHES------------NLENDAAEKGKFRHFMQK 255
Cdd:PLN02981 241 fFLASDASAVVEHTKRVLVIEDNEVVHLKDGGVGIYKFENEKGRGGGGLSrpasveralstlEMEVEQIMKGNYDHYMQK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 256 EIYEQPTALINTMEGRinhenVIVDSIGNgAKGIL--EKVEH---------IQIVACGTSYNAGMVARYWFESLAGVSCD 324
Cdd:PLN02981 321 EIHEQPESLTTTMRGR-----LIRGGSGK-AKRVLlgGLKDHlktirrsrrIVFIGCGTSYNAALAARPILEELSGVPVT 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 325 VEIASEFRYRKFVTRPNSLLITLSQSGETADTLAALRLAKEKGYMaALTICNVAGSSLVRESDLAFMTRAGVEVGVASTK 404
Cdd:PLN02981 395 MELASDLLDRQGPIYREDTAVFVSQSGETADTLRALEYAKENGAL-CVGITNTVGSAISRGTHCGVHINAGAEIGVASTK 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 405 AFTTQLAALLMLVTALGkvKGHISVEKERE-IIKAMQSLPAEIEKALAFDREIEALAEDFAEKHHALFLGRGAFYPIAVE 483
Cdd:PLN02981 474 AYTSQIVAMTMLALALG--EDSISSRSRREaIIDGLFDLPNKVREVLKLDQEMKELAELLIDEQSLLVFGRGYNYATALE 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 484 ASLKLKEISYIHAEAYAAGELKHGPLALIDADMPVIVVAPNNELLEKVKSNIEEVRARGGQLYVFADK--EAGFTPSEGM 561
Cdd:PLN02981 552 GALKVKEVALMHSEGILAGEMKHGPLALVDETLPIIVIATRDACFSKQQSVIQQLRARKGRLIVICSKgdASSVCPSGGC 631
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 491949326 562 KIITMPKVNDIVAPIFYTIPMQLLSYYVALIKGTDVDQPRNLAKSVTVE 610
Cdd:PLN02981 632 RVIEVPQVEDCLQPVINIVPLQLLAYHLTVLRGHNVDQPRNLAKSVTTQ 680
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
1-609 |
8.37e-168 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 492.61 E-value: 8.37e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 1 MCGIVGAVAQRDVAEILINGLHRLEYRGYDSAGVAVINKQNELQRIRCLGKVKALD-----EAVSEKPLIGGT-GIAHTR 74
Cdd:PTZ00295 24 CCGIVGYLGNEDASKILLEGIEILQNRGYDSCGISTISSGGELKTTKYASDGTTSDsieilKEKLLDSHKNSTiGIAHTR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 75 WATHGEPSETNAHPHS--SGTFAVVHNGIIENHEELRELLKSRGYVFLSQTDTEVIAHLVEWEMRSTDSLLEAVQKSVKQ 152
Cdd:PTZ00295 104 WATHGGKTDENAHPHCdyKKRIALVHNGTIENYVELKSELIAKGIKFRSETDSEVIANLIGLELDQGEDFQEAVKSAISR 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 153 LTGAYGMVVMDSRHPEHLVAARSGSPLVIGLGIGENFLASDQLALLSVTRRFIFLEEGDIAEITRRTVDIYDTHGN--KA 230
Cdd:PTZ00295 184 LQGTWGLCIIHKDNPDSLIVARNGSPLLVGIGDDSIYVASEPSAFAKYTNEYISLKDGEIAELSLENVNDLYTQRRveKI 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 231 KREIHESNLEndaaekgKFRHFMQKEIYEQPTALINTME--GRI--NHENVIVDSIGNGAKGILeKVEHIQIVACGTSYN 306
Cdd:PTZ00295 264 PEEVIEKSPE-------PYPHWTLKEIFEQPIALSRALNngGRLsgYNNRVKLGGLDQYLEELL-NIKNLILVGCGTSYY 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 307 AGMVARYWFESLAGV-SCDVEIASEF-RYRkfVTRPNSLLITLSQSGETADTLAALRLAKEKGyMAALTICNVAGSSLVR 384
Cdd:PTZ00295 336 AALFAASIMQKLKCFnTVQVIDASELtLYR--LPDEDAGVIFISQSGETLDVVRALNLADELN-LPKISVVNTVGSLIAR 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 385 ESDLAFMTRAGVEVGVASTKAFTTQLAALLMLVTALGKVK-GHISVEKEREIIKAMQSLPAEIEKALAFDREI-EALAED 462
Cdd:PTZ00295 413 STDCGVYLNAGREVAVASTKAFTSQVTVLSLIALWFAQNKeYSCSNYKCSSLINSLHRLPTYIGMTLKSCEEQcKRIAEK 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 463 FAEKHHALFLGRGAFYPIAVEASLKLKEISYIHAEAYAAGELKHGPLALIDAD--MPVIVVAPNNELLEKVKSNIEEVRA 540
Cdd:PTZ00295 493 LKNAKSMFILGKGLGYPIALEGALKIKEITYIHAEGFSGGALKHGPFALIDKEknTPVILIILDDEHKELMINAAEQVKA 572
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 541 RGGQLYVFADKEAgfTPSEGM-KIITMPKvNDIVAPIFYTIPMQLLSYYVALIKGTDVDQPRNLAKSVTV 609
Cdd:PTZ00295 573 RGAYIIVITDDED--LVKDFAdEIILIPS-NGPLTALLAVIPLQLLAYEIAILRGINPDKPRGLAKTVTV 639
|
|
| PTZ00394 |
PTZ00394 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
1-610 |
5.71e-155 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 173585 [Multi-domain] Cd Length: 670 Bit Score: 460.88 E-value: 5.71e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 1 MCGIVGAVAQ------RDVAEILINGLHRLEYRGYDSAGVAV---INKQNELQR-----------IRCLGKVKALDE--- 57
Cdd:PTZ00394 1 MCGIFGYANHnvprtvEQILNVLLDGIQKVEYRGYDSAGLAIdanIGSEKEDGTaasaptprpcvVRSVGNISQLREkvf 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 58 ----AVSEKPLIGGT----GIAHTRWATHGEPSETNAHPHSS--GTFAVVHNGIIENHEELRELLKSRGYVFLSQTDTEV 127
Cdd:PTZ00394 81 seavAATLPPMDATTshhvGIAHTRWATHGGVCERNCHPQQSnnGEFTIVHNGIVTNYMTLKELLKEEGYHFSSDTDTEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 128 IAHLVEW--EMRSTDSLLEAVQKSVKQLTGAYGMVVMDSRHPEHLVAARSGSPLVIGL---------------------G 184
Cdd:PTZ00394 161 ISVLSEYlyTRKGIHNFADLALEVSRMVEGSYALLVKSVYFPGQLAASRKGSPLMVGIrrtddrgcvmklqtydltdlsG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 185 IGENFLASDQLALLSVTRRFIFLEEGDIAEITRRTVDIYDTHGNKA---KREIHESNLENDAAEKGKFRHFMQKEIYEQP 261
Cdd:PTZ00394 241 PLEVFFSSDVNSFAEYTREVVFLEDGDIAHYCDGALRFYNAAERQRsivKREVQHLDAKPEGLSKGNYPHFMLKEIYEQP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 262 TALINTMEGRINHE--NVIVDSIGNGAKGILEKVEHIQIVACGTSYNAGMVARYWFESLAGVSCDVEIASEFRYRKFVTR 339
Cdd:PTZ00394 321 ESVISSMHGRIDFSsgTVQLSGFTQQSIRAILTSRRILFIACGTSLNSCLAVRPLFEELVPLPISVENASDFLDRRPRIQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 340 PNSLLITLSQSGETADTLAALRLAKEKGYMAaLTICNVAGSSLVRESDLAFMTRAGVEVGVASTKAFTTQLAALLMLVTA 419
Cdd:PTZ00394 401 RDDVCFFVSQSGETADTLMALQLCKEAGAMC-VGITNVVGSSISRLTHYAIHLNAGVEVGVASTKAYTSQVVVLTLVALL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 420 LGKVKGHISvEKEREIIKAMQSLPAEIEKALAFDRE-IEALAEDFAEKHHALFLGRGAFYPIAVEASLKLKEISYIHAEA 498
Cdd:PTZ00394 480 LSSDSVRLQ-ERRNEIIRGLAELPAAISECLKITHDpVKALAARLKESSSILVLGRGYDLATAMEAALKVKELSYVHTEG 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 499 YAAGELKHGPLALIDADMPVIVVAPNNELLEKVKSNIEEVRARGGQLYVFADKEAGFTPSEGMKIITMPKVNDIVAPIFY 578
Cdd:PTZ00394 559 IHSGELKHGPLALIDETSPVLAMCTHDKHFGLSKSAVQQVKARGGAVVVFATEVDAELKAAASEIVLVPKTVDCLQCVVN 638
|
650 660 670
....*....|....*....|....*....|..
gi 491949326 579 TIPMQLLSYYVALIKGTDVDQPRNLAKSVTVE 610
Cdd:PTZ00394 639 VIPFQLLAYYMALLRGNNVDCPRNLAKSVTVQ 670
|
|
| GFAT |
cd00714 |
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ... |
2-215 |
7.43e-128 |
|
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus of glucosamine-6P synthase (GlmS, or GFAT in humans). The glutaminase domain catalyzes amide nitrogen transfer from glutamine to the appropriate substrate. In this process, glutamine is hydrolyzed to glutamic acid and ammonia. In humans, GFAT catalyzes the first and rate-limiting step of hexosamine metabolism, the conversion of D-fructose-6P (Fru6P) into D-glucosamine-6P using L-glutamine as a nitrogen source. The end product of this pathway, UDP-N-acetyl glucosamine, is a major building block of the bacterial peptidoglycan and fungal chitin.
Pssm-ID: 238366 [Multi-domain] Cd Length: 215 Bit Score: 374.48 E-value: 7.43e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 2 CGIVGAVAQRDVAEILINGLHRLEYRGYDSAGVAVINKqNELQRIRCLGKVKALDEAVSEKPLIGGTGIAHTRWATHGEP 81
Cdd:cd00714 1 CGIVGYIGKREAVDILLEGLKRLEYRGYDSAGIAVIGD-GSLEVVKAVGKVANLEEKLAEKPLSGHVGIGHTRWATHGEP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 82 SETNAHPHSS--GTFAVVHNGIIENHEELRELLKSRGYVFLSQTDTEVIAHLVEWEMRSTDSLLEAVQKSVKQLTGAYGM 159
Cdd:cd00714 80 TDVNAHPHRScdGEIAVVHNGIIENYAELKEELEAKGYKFESETDTEVIAHLIEYYYDGGLDLLEAVKKALKRLEGAYAL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 491949326 160 VVMDSRHPEHLVAARSGSPLVIGLGIGENFLASDQLALLSVTRRFIFLEEGDIAEI 215
Cdd:cd00714 160 AVISKDEPDEIVAARNGSPLVIGIGDGENFVASDAPALLEHTRRVIYLEDGDIAVI 215
|
|
| AgaS |
COG2222 |
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ... |
255-610 |
1.81e-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: 251.74 E-value: 1.81e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 255 KEIYEQPTALINTMEgrinhenVIVDSIGNGAKGILEK-VEHIQIVACGTSYNAGMVARYWFESLAGVSCDVEIASEF-R 332
Cdd:COG2222 2 REIAQQPEAWRRALA-------ALAAAIAALLARLRAKpPRRVVLVGAGSSDHAAQAAAYLLERLLGIPVAALAPSELvV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 333 YRKFVTRPNSLLITLSQSGETADTLAALRLAKEKG-YMAALTicNVAGSSLVRESDLAFMTRAGVEVGVASTKAFTTQLA 411
Cdd:COG2222 75 YPAYLKLEGTLVVAISRSGNSPEVVAALELAKARGaRTLAIT--NNPDSPLAEAADRVLPLPAGPEKSVAATKSFTTMLL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 412 ALLMLVTALGKvkghisvekEREIIKAMQSLPAEIEKALAFDREIEALAEdFAEKHHALFLGRGAFYPIAVEASLKLKEI 491
Cdd:COG2222 153 ALLALLAAWGG---------DDALLAALDALPAALEAALAADWPAAALAA-LADAERVVFLGRGPLYGLAREAALKLKEL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 492 SYIHAEAYAAGELKHGPLALIDADMPVIVVAPNNELLEKVKSNIEEVRARGGQLYVFADKEAGFTPsegmkIITMPKVND 571
Cdd:COG2222 223 SAGHAEAYSAAEFRHGPKSLVDPGTLVVVLASEDPTRELDLDLAAELRALGARVVAIGAEDDAAIT-----LPAIPDLHD 297
|
330 340 350
....*....|....*....|....*....|....*....
gi 491949326 572 IVAPIFYTIPMQLLSYYVALIKGTDVDQPRNLAKSVTVE 610
Cdd:COG2222 298 ALDPLLLLVVAQRLALALALARGLDPDTPRHLNKVVKTV 336
|
|
| SIS_GlmS_GlmD_2 |
cd05009 |
SIS (Sugar ISomerase) domain repeat 2 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
455-608 |
1.35e-66 |
|
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: 214.05 E-value: 1.35e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 455 EIEALAEDFAEKHHALFLGRGAFYPIAVEASLKLKEISYIHAEAYAAGELKHGPLALIDADMPVIVVAPNNELLEKVKSN 534
Cdd:cd05009 2 DIKELAEKLKEAKSFYVLGRGPNYGTALEGALKLKETSYIHAEAYSAGEFKHGPIALVDEGTPVIFLAPEDRLEEKLESL 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491949326 535 IEEVRARGGQLYVFADKEAGFtpSEGMKIITMPKVNDIVAPIFYTIPMQLLSYYVALIKGTDVDQPRNLAKSVT 608
Cdd:cd05009 82 IKEVKARGAKVIVITDDGDAK--DLADVVIRVPATVEELSPLLYIVPLQLLAYHLAVARGIDPDKPRNLAKSVT 153
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
2-213 |
4.76e-64 |
|
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: 210.00 E-value: 4.76e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 2 CGIVGAVAQRDVAEILI----NGLHRLEYRGYDSAGVAVINkQNELQRIRCLGKVKALDEAVSEKPLIGGTGIAHTRWAT 77
Cdd:cd00352 1 CGIFGIVGADGAASLLLllllRGLAALEHRGPDGAGIAVYD-GDGLFVEKRAGPVSDVALDLLDEPLKSGVALGHVRLAT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 78 HGEPSETNAHPHSS--GTFAVVHNGIIENHEELRELLKSRGYVFLSQTDTEVIAHLVEWEMRSTDsLLEAVQKSVKQLTG 155
Cdd:cd00352 80 NGLPSEANAQPFRSedGRIALVHNGEIYNYRELREELEARGYRFEGESDSEVILHLLERLGREGG-LFEAVEDALKRLDG 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491949326 156 AYGMVVMDsRHPEHLVAARSG---SPLVIGLGI-GENFLASDQLALLSVT-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 |
4.34e-58 |
|
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and Glucosamine-6-phosphate deaminase (GlmD). The SIS domain is found in many phosphosugar isomerases and phosphosugar binding proteins. GlmS contains a N-terminal glutaminase domain and two C-terminal SIS domains and catalyzes the first step in hexosamine metabolism, converting fructose 6-phosphate into glucosamine 6-phosphate using glutamine as nitrogen source. The glutaminase domain hydrolyzes glutamine to glutamate and ammonia. Ammonia is transferred through a channel to the isomerase domain for glucosamine 6-phosphate synthesis. The end product of the pathway is N-acetylglucosamine, which plays multiple roles in eukaryotic cells including being a building block of bacterial and fungal cell walls. In the absence of glutamine, GlmS catalyzes the isomerization of fructose 6-phosphate into glucose 6- phosphate (PGI-like activity). Glucosamine-6-phosphate deaminase (GlmD) contains two SIS domains and catalyzes the deamination and isomerization of glucosamine-6-phosphate into fructose-6-phosphate with the release of ammonia; in presence of high ammonia concentration, GlmD can catalyze the reverse reaction.
Pssm-ID: 240141 [Multi-domain] Cd Length: 126 Bit Score: 190.79 E-value: 4.34e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 295 HIQIVACGTSYNAGMVARYWFESLAGVSCDVEIASEFRYRKFVTRPNSLLITLSQSGETADTLAALRLAKEKGYMaALTI 374
Cdd:cd05008 1 RILIVGCGTSYHAALVAKYLLERLAGIPVEVEAASEFRYRRPLLDEDTLVIAISQSGETADTLAALRLAKEKGAK-TVAI 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 491949326 375 CNVAGSSLVRESDLAFMTRAGVEVGVASTKAFTTQLAALLMLVTALG 421
Cdd:cd05008 80 TNVVGSTLAREADYVLYLRAGPEISVAATKAFTSQLLALLLLALALA 126
|
|
| PurF |
COG0034 |
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ... |
1-182 |
9.91e-39 |
|
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: 148.63 E-value: 9.91e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 1 MCGIVGAVAQRDVAEILINGLHRLEYRGYDSAGVAVINKqNELQRIRCLGKVK-ALDEAVSEKpLIGGTGIAHTRWATHG 79
Cdd:COG0034 7 ECGVFGIYGHEDVAQLTYYGLYALQHRGQESAGIATSDG-GRFHLHKGMGLVSdVFDEEDLER-LKGNIAIGHVRYSTTG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 80 EPSETNAHP----HSSGTFAVVHNGIIENHEELRELLKSRGYVFLSQTDTEVIAHLVEWEMRSTDsLLEAVQKSVKQLTG 155
Cdd:COG0034 85 SSSLENAQPfyvnSPFGSIALAHNGNLTNAEELREELEEEGAIFQTTSDTEVILHLIARELTKED-LEEAIKEALRRVKG 163
|
170 180 190
....*....|....*....|....*....|
gi 491949326 156 AYGMVVMDsrhPEHLVAAR--SG-SPLVIG 182
Cdd:COG0034 164 AYSLVILT---GDGLIAARdpNGiRPLVLG 190
|
|
| GPATase_N |
cd00715 |
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ... |
2-217 |
1.46e-37 |
|
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the N-terminus of glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase) . The glutaminase domain catalyzes amide nitrogen transfer from glutamine to the appropriate substrate. In this process, glutamine is hydrolyzed to glutamic acid and ammonia. GPATase catalyzes the first step in purine biosynthesis, an amide transfer from glutamine to PRPP, resulting in phosphoribosylamine, pyrophosphate and glutamate. GPATase crystalizes as a homotetramer, but can also exist as a homdimer.
Pssm-ID: 238367 [Multi-domain] Cd Length: 252 Bit Score: 139.90 E-value: 1.46e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 2 CGIVGAVAQRDVAEILINGLHRLEYRGYDSAGVAVINkQNELQRIRCLGKVK-ALDEAVSEKpLIGGTGIAHTRWATHGE 80
Cdd:cd00715 1 CGVFGIYGAEDAARLTYLGLYALQHRGQESAGIATSD-GKRFHTHKGMGLVSdVFDEEKLRR-LPGNIAIGHVRYSTAGS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 81 PSETNAHP----HSSGTFAVVHNGIIENHEELRELLKSRGYVFLSQTDTEVIAHLVEWEMRStDSLLEAVQKSVKQLTGA 156
Cdd:cd00715 79 SSLENAQPfvvnSPLGGIALAHNGNLVNAKELREELEEEGRIFQTTSDSEVILHLIARSLAK-DDLFEAIIDALERVKGA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491949326 157 YGMVVMdsrHPEHLVAAR--SG-SPLVIG-LGIGENFLASDQLALLSVTRRFIF-LEEGDIAEITR 217
Cdd:cd00715 158 YSLVIM---TADGLIAVRdpHGiRPLVLGkLEGDGYVVASESCALDIIGAEFVRdVEPGEIVVIDD 220
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
289-419 |
1.09e-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: 125.10 E-value: 1.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 289 ILEKVEHIQIVACGTSYNAGMVARYWFESLAGVSCDVEIASEFRYR-KFVTRPNSLLITLSQSGETADTLAALRLAKEKG 367
Cdd:pfam01380 1 LLAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGvLALVDEDDLVIAISYSGETKDLLAAAELAKARG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 491949326 368 yMAALTICNVAGSSLVRESDLAFMTRAGVEVGVASTKAFTTQLAALLMLVTA 419
Cdd:pfam01380 81 -AKIIAITDSPGSPLAREADHVLYINAGPETGVASTKSITAQLAALDALAVA 131
|
|
| purF |
TIGR01134 |
amidophosphoribosyltransferase; Alternate name: glutamine phosphoribosylpyrophosphate (PRPP) ... |
2-197 |
2.61e-30 |
|
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: 123.97 E-value: 2.61e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 2 CGIVGAVAQR-DVAEILINGLHRLEYRGYDSAGVAVINKQNELQRiRCLGKVKALDEAVSEKPLIGGTGIAHTRWATHGE 80
Cdd:TIGR01134 1 CGVVGIYGQEeVAASLTYYGLYALQHRGQESAGISVFDGNRFRLH-KGNGLVSDVFNEEHLQRLKGNVGIGHVRYSTAGS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 81 PSETNAHPHSSGTF----AVVHNGIIENHEELRELLKSRGYVFLSQTDTEVIAHLVEWEMRSTDSLLEAVQKSVKQLTGA 156
Cdd:TIGR01134 80 SGLENAQPFVVNSPygglALAHNGNLVNADELRRELEEEGRHFNTTSDSEVLLHLLAHNDESKDDLFDAVARVLERVRGA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 491949326 157 YGMVVMdsrHPEHLVAARS--G-SPLVIGlGIGENF-LASDQLAL 197
Cdd:TIGR01134 160 YALVLM---TEDGLVAVRDphGiRPLVLG-RRGDGYvVASESCAL 200
|
|
| PRK05793 |
PRK05793 |
amidophosphoribosyltransferase; Provisional |
2-215 |
1.71e-28 |
|
amidophosphoribosyltransferase; Provisional
Pssm-ID: 235611 [Multi-domain] Cd Length: 469 Bit Score: 118.98 E-value: 1.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 2 CGIVGAVA--QRDVAEILINGLHRLEYRGYDSAGVAVINKQnELQRIRCLGKVKaldEAVSE---KPLIGGTGIAHTRWA 76
Cdd:PRK05793 15 CGVFGVFSknNIDVASLTYYGLYALQHRGQESAGIAVSDGE-KIKVHKGMGLVS---EVFSKeklKGLKGNSAIGHVRYS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 77 THGEPSETNAHP----HSSGTFAVVHNGIIENHEELRELLKSRGYVFLSQTDTEVIAHLVEWEMRStdSLLEAVQKSVKQ 152
Cdd:PRK05793 91 TTGASDLDNAQPlvanYKLGSIAIAHNGNLVNADVIRELLEDGGRIFQTSIDSEVILNLIARSAKK--GLEKALVDAIQA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491949326 153 LTGAYGMVVMDSrhpEHLVAARSGS---PLVIGLGIGENFLASDQLALLSVTRRFIF-LEEGDIAEI 215
Cdd:PRK05793 169 IKGSYALVILTE---DKLIGVRDPHgirPLCLGKLGDDYILSSESCALDTIGAEFIRdVEPGEIVII 232
|
|
| PLN02440 |
PLN02440 |
amidophosphoribosyltransferase |
1-182 |
6.48e-26 |
|
amidophosphoribosyltransferase
Pssm-ID: 215241 [Multi-domain] Cd Length: 479 Bit Score: 111.31 E-value: 6.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 1 MCGIVGAVAQRDVAEILINGLHRLEYRGYDSAGVAVINkQNELQRIRCLGKVKALDEAVSEKPLIGGTGIAHTRWATHGE 80
Cdd:PLN02440 1 ECGVVGIFGDPEASRLCYLGLHALQHRGQEGAGIVTVD-GNRLQSITGNGLVSDVFDESKLDQLPGDIAIGHVRYSTAGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 81 PSETNAHP----HSSGTFAVVHNGIIENHEELRELLKSRGYVFLSQTDTEVIAHLVEWEMRSTdsLLEAVQKSVKQLTGA 156
Cdd:PLN02440 80 SSLKNVQPfvanYRFGSIGVAHNGNLVNYEELRAKLEENGSIFNTSSDTEVLLHLIAISKARP--FFSRIVDACEKLKGA 157
|
170 180
....*....|....*....|....*....
gi 491949326 157 YGMVVMDSrhpEHLVAARSGS---PLVIG 182
Cdd:PLN02440 158 YSMVFLTE---DKLVAVRDPHgfrPLVMG 183
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
463-593 |
7.91e-26 |
|
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: 102.76 E-value: 7.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 463 FAEKHHALFLGRGAFYPIAVEASLKLKEISYIHAEAYAAGELKHGPLALIDADMPVIVVAPNNELLEKVKsNIEEVRARG 542
Cdd:pfam01380 2 LAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGVLALVDEDDLVIAISYSGETKDLLA-AAELAKARG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 491949326 543 GQLYVFADKEAGFTPSEGMKIITMPKVNDIVAPIFYTIPMQLLSYYVALIK 593
Cdd:pfam01380 81 AKIIAITDSPGSPLAREADHVLYINAGPETGVASTKSITAQLAALDALAVA 131
|
|
| GlxB |
cd01907 |
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ... |
2-203 |
1.90e-22 |
|
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: 96.95 E-value: 1.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 2 CGIVGAV---AQRDVAEILINGLHRLEYRG-YDSAGVAVINkqneLQRIRCLGKVKALD--------EAVSEK---PLIG 66
Cdd:cd01907 1 CGIFGIMskdGEPFVGALLVEMLDAMQERGpGDGAGFALYG----DPDAFVYSSGKDMEvfkgvgypEDIARRydlEEYK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 67 GT-GIAHTRWATHGEPSETNAHPHSSGTFAVVHNGIIENHEELRELLKSRGYVFLSQTDTEVIAHLVEWEMRSTDSLLEA 145
Cdd:cd01907 77 GYhWIAHTRQPTNSAVWWYGAHPFSIGDIAVVHNGEISNYGSNREYLERFGYKFETETDTEVIAYYLDLLLRKGGLPLEY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 146 VQKSVKQ-------------------LTGAYGMVVMdsrHPEHLVAARSGS---PLVIGLGIGENFLASDQLALLSVTRR 203
Cdd:cd01907 157 YKHIIRMpeeerelllalrltyrladLDGPFTIIVG---TPDGFIVIRDRIklrPAVVAETDDYVAIASEECAIREIPDR 233
|
|
| GATase_6 |
pfam13522 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
66-133 |
7.97e-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: 82.74 E-value: 7.97e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 66 GGTGIAHTRWATHGEPSETNaHPHSS--GTFAVVHNGIIENHEELRELLKSRGYVFLSQTDTEVIAHLVE 133
Cdd:pfam13522 10 GGVALGHVRLAIVDLPDAGN-QPMLSrdGRLVLVHNGEIYNYGELREELADLGHAFRSRSDTEVLLALYE 78
|
|
| GATase_7 |
pfam13537 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
72-198 |
5.58e-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: 5.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 72 HTRWATHGepSETNAHP---HSSGTFAVVHNGIIENHEELRELLKSRGYVFLSQTDTEVIAHLVEwemrstdslLEAVQK 148
Cdd:pfam13537 1 HRRLSIID--LEGGAQPmvsSEDGRYVIVFNGEIYNYRELRAELEAKGYRFRTHSDTEVILHLYE---------AEWGED 69
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 491949326 149 SVKQLTGAYGMVVMDSRHPEhLVAAR--SG-SPLVIGLGIGENFL-ASDQLALL 198
Cdd:pfam13537 70 CVDRLNGMFAFAIWDRRRQR-LFLARdrFGiKPLYYGRDDGGRLLfASELKALL 122
|
|
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
1-174 |
3.89e-14 |
|
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: 75.26 E-value: 3.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 1 MCGIVGAVAQRDVA--EILINGLHRLEYRGYDSAGVAVinkqnelqrirclgkvkalDEAVsekpliggtGIAHTRWATH 78
Cdd:COG0367 1 MCGIAGIIDFDGGAdrEVLERMLDALAHRGPDGSGIWV-------------------DGGV---------ALGHRRLSII 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 79 GePSETNAHPHSS--GTFAVVHNGIIENHEELRELLKSRGYVFLSQTDTEVIAHL-VEWEmrstdslleavQKSVKQLTG 155
Cdd:COG0367 53 D-LSEGGHQPMVSedGRYVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHAyEEWG-----------EDCLERLNG 120
|
170
....*....|....*....
gi 491949326 156 AYGMVVMDSRHpEHLVAAR 174
Cdd:COG0367 121 MFAFAIWDRRE-RRLFLAR 138
|
|
| AsnB |
cd00712 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ... |
2-131 |
4.43e-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: 71.82 E-value: 4.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 2 CGIVGAV---AQRDVAEILINGLHRLEYRGYDSAGVAVInkqnelqrirclgkvkaldeavsekpliGGTGIAHTRWATH 78
Cdd:cd00712 1 CGIAGIIgldGASVDRATLERMLDALAHRGPDGSGIWID----------------------------EGVALGHRRLSII 52
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 491949326 79 GEpsETNAHPHSS--GTFAVVHNGIIENHEELRELLKSRGYVFLSQTDTEVIAHL 131
Cdd:cd00712 53 DL--SGGAQPMVSedGRLVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHL 105
|
|
| YafJ |
cd01908 |
Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine ... |
63-178 |
1.62e-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: 67.80 E-value: 1.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 63 PLIGGTGIAHTRWATHGEPSETNAHPHSSGTFAVVHNGIIENHEELRE-LLKSRGYVFLSQTDTEVIAHLV--EWEMR-- 137
Cdd:cd01908 77 PIKSPLVLAHVRAATVGPVSLENCHPFTRGRWLFAHNGQLDGFRLLRRrLLRLLPRLPVGTTDSELAFALLlsRLLERdp 156
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 491949326 138 -STDSLLEAVQKSVKQLT-----GAYGMVVMDSrhpEHLVAARSGSP 178
Cdd:cd01908 157 lDPAELLDAILQTLRELAalappGRLNLLLSDG---EYLIATRYASA 200
|
|
| YafJ |
COG0121 |
Predicted glutamine amidotransferase YafJ [General function prediction only]; |
67-177 |
4.09e-12 |
|
Predicted glutamine amidotransferase YafJ [General function prediction only];
Pssm-ID: 439891 [Multi-domain] Cd Length: 248 Bit Score: 66.53 E-value: 4.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 67 GTGIAHTRWATHGEPSETNAHPHSSGTFAVVHNGIIENHEELRELLKSRGYVFL-----SQTDTEVIAHLV--EWEMRST 139
Cdd:COG0121 77 RLVIAHVRKATVGPVSLENTHPFRGGRWLFAHNGQLDGFDRLRRRLAEELPDELyfqpvGTTDSELAFALLlsRLRDGGP 156
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 491949326 140 DsLLEAVQKSVKQLT------GAYGMVVMDsrhPEHLVAARSGS 177
Cdd:COG0121 157 D-PAEALAEALRELAelarapGRLNLLLSD---GERLYATRYTS 196
|
|
| SIS_1 |
cd05710 |
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ... |
295-396 |
8.49e-12 |
|
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: 62.21 E-value: 8.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 295 HIQIVACGTSYNAGMVARYWFESLAGVSCDVEIASEFRYR--KFVTrPNSLLITLSQSGETADTLAALRLAKEKGymaAL 372
Cdd:cd05710 1 NVFFVGCGGSLADMYPAKYFLKKESKLPVFVYNAAEFLHTgpKRLT-EKSVVILASHSGNTKETVAAAKFAKEKG---AT 76
|
90 100
....*....|....*....|....*.
gi 491949326 373 TICNV--AGSSLVRESDLAFMTRAGV 396
Cdd:cd05710 77 VIGLTddEDSPLAKLADYVIVYGFEI 102
|
|
| PLN02549 |
PLN02549 |
asparagine synthase (glutamine-hydrolyzing) |
1-197 |
1.03e-11 |
|
asparagine synthase (glutamine-hydrolyzing)
Pssm-ID: 178164 [Multi-domain] Cd Length: 578 Bit Score: 67.87 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 1 MCGIVGAVAQRDVA---EILINGL-HRLEYRGYDSAGVAVInkqnelqrirclgkvkaldeavsekpliGGTGIAHTRWA 76
Cdd:PLN02549 1 MCGILAVLGCSDDSqakRSRVLELsRRLRHRGPDWSGLYGN----------------------------EDCYLAHERLA 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 77 THGEPSETNAHPHSSGTFAVVHNGIIENHEELRELLKSrgYVFLSQTDTEVIAHLVEwemrstdsllEAVQKSVKQLTGA 156
Cdd:PLN02549 53 IMDPESGDQPLYNEDKTIVVTANGEIYNHKELREKLKL--HKFRTGSDCEVIAHLYE----------EHGEEFVDMLDGM 120
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 491949326 157 YGMVVMDSRHpEHLVAARSG---SPLVIGLGI-GENFLASDQLAL 197
Cdd:PLN02549 121 FSFVLLDTRD-NSFIAARDHigiTPLYIGWGLdGSVWFASEMKAL 164
|
|
| PTZ00077 |
PTZ00077 |
asparagine synthetase-like protein; Provisional |
1-197 |
4.26e-10 |
|
asparagine synthetase-like protein; Provisional
Pssm-ID: 185431 [Multi-domain] Cd Length: 586 Bit Score: 62.42 E-value: 4.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 1 MCGIVGAVAQRDVAEIL----INGLHRLEYRGYDSAGVAVINKQNELQRIrclgkvkaldeavsekpliggtgIAHTRWA 76
Cdd:PTZ00077 1 MCGILAIFNSKGERHELrrkaLELSKRLRHRGPDWSGIIVLENSPGTYNI-----------------------LAHERLA 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 77 THGepSETNAHP--HSSGTFAVVHNGIIENHEELRELLKSRGYVFLSQTDTEVIAHLVEwemrstdsllEAVQKS-VKQL 153
Cdd:PTZ00077 58 IVD--LSDGKQPllDDDETVALMQNGEIYNHWEIRPELEKEGYKFSSNSDCEIIGHLYK----------EYGPKDfWNHL 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 491949326 154 TGAYGMVVMDSRHPEhLVAARSG---SPLVIGLGI-GENFLASDQLAL 197
Cdd:PTZ00077 126 DGMFATVIYDMKTNT-FFAARDHigiIPLYIGYAKdGSIWFSSELKAL 172
|
|
| SIS |
cd04795 |
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
296-367 |
9.54e-09 |
|
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: 52.76 E-value: 9.54e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491949326 296 IQIVACGTSYNAGMVARYWFESLAGVSCDVEIASEFRY--RKFVTRPNSLLITLSQSGETADTLAALRLAKEKG 367
Cdd:cd04795 1 IFVIGIGGSGAIAAYFALELLELTGIEVVALIATELEHasLLSLLRKGDVVIALSYSGRTEELLAALEIAKELG 74
|
|
| SIS_RpiR |
cd05013 |
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ... |
289-416 |
2.76e-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: 53.00 E-value: 2.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 289 ILEKVEHIQIVACGTSynaGMVARYWFESLAGVSCDVEIASEFRYRKFV---TRPNSLLITLSQSGETADTLAALRLAKE 365
Cdd:cd05013 9 LLAKARRIYIFGVGSS---GLVAEYLAYKLLRLGKPVVLLSDPHLQLMSaanLTPGDVVIAISFSGETKETVEAAEIAKE 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 491949326 366 KGyMAALTICNVAGSSLVRESDLAFMTraGVEVGVASTKAFTTQLAALLML 416
Cdd:cd05013 86 RG-AKVIAITDSANSPLAKLADIVLLV--SSEEGDFRSSAFSSRIAQLALI 133
|
|
| frlB |
PRK11382 |
fructoselysine 6-phosphate deglycase; |
293-601 |
2.95e-08 |
|
fructoselysine 6-phosphate deglycase;
Pssm-ID: 183111 [Multi-domain] Cd Length: 340 Bit Score: 55.78 E-value: 2.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 293 VEHIQIVACGTSYNAGMVARYwfesLAGVSCDVEIASEFRYRKFVTRPNSL-----LITLSQSGETADTLAALRLAKEKG 367
Cdd:PRK11382 44 IDRIYFVACGSPLNAAQTAKH----LADRFSDLQVYAISGWEFCDNTPYRLddrcaVIGVSDYGKTEEVIKALELGRACG 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 368 YMAAlTICNVAGSSLVRESDLAFMTRAGV--EVGVASTKAFTTQLAALLMLVTALGKVKGHIsvekeREIIKAMQSLPAE 445
Cdd:PRK11382 120 ALTA-AFTKRADSPITSAAEFSIDYQADCiwEIHLLLCYSVVLEMITRLAPNAEIGKIKNDL-----KQLPNALGHLVRT 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 446 IEKAlafDREIEALAEDFAEKHHalfLGRGAFYPIAV-EASLKLKEISYIHAEAYAAGELKHGPLALIDADMPVIVVAPN 524
Cdd:PRK11382 194 WEEK---GRQLGELASQWPMIYT---VAAGPLRPLGYkEGIVTLMEFTWTHGCVIESGEFRHGPLEIVEPGVPFLFLLGN 267
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491949326 525 NELLEKVKSNIEEVRARGGQLYV--FADKEAGFTPsegmkiitmpkvndIVAPIFYTIPMQLLSYYVALIKGTDVDQPR 601
Cdd:PRK11382 268 DESRHTTERAINFVKQRTDNVIVidYAEISQGLHP--------------WLAPFLMFVPMEWLCYYLSIYKDHNPDERR 332
|
|
| asn_synth_AEB |
TIGR01536 |
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing ... |
91-174 |
4.36e-08 |
|
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing asparagine synthase. A poorly conserved C-terminal extension was removed from the model. Bacterial members of the family tend to have a long, poorly conserved insert lacking from archaeal and eukaryotic sequences. Multiple isozymes have been demonstrated, such as in Bacillus subtilis. Long-branch members of the phylogenetic tree (which typically were also second or third candidate members from their genomes) were removed from the seed alignment and score below trusted cutoff. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 273676 [Multi-domain] Cd Length: 466 Bit Score: 55.80 E-value: 4.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 91 SGTFAVVHNGIIENHEELRELLKSRGYVFLSQTDTEVIAHLVEwemrstdsllEAVQKSVKQLTGAYGMVVMDSRHpEHL 170
Cdd:TIGR01536 65 GKTYVIVFNGEIYNHEELREELEAKGYTFQTDSDTEVILHLYE----------EWGEECVDRLDGMFAFALWDSEK-GEL 133
|
....
gi 491949326 171 VAAR 174
Cdd:TIGR01536 134 FLAR 137
|
|
| RpiR |
COG1737 |
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ... |
294-442 |
4.46e-08 |
|
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains [Transcription];
Pssm-ID: 441343 [Multi-domain] Cd Length: 286 Bit Score: 54.93 E-value: 4.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 294 EHIQIVACGTSYNAGMVARYWFeSLAGVSCDVEIASEFRYRKFVT--RPNSLLITLSQSGETADTLAALRLAKEKGyMAA 371
Cdd:COG1737 135 RRIYIFGVGASAPVAEDLAYKL-LRLGKNVVLLDGDGHLQAESAAllGPGDVVIAISFSGYTRETLEAARLAKERG-AKV 212
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491949326 372 LTICNVAGSSLVRESDLAFMTRAGVEVGVAStkAFTTQLAALLM---LVTALGKVKGHISVEKEREIIKAMQSL 442
Cdd:COG1737 213 IAITDSPLSPLAKLADVVLYVPSEEPTLRSS--AFSSRVAQLALidaLAAAVAQRDGDKARERLERTEALLSEL 284
|
|
| SIS |
cd04795 |
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
470-551 |
1.48e-07 |
|
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: 49.29 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 470 LFLGRGAFYPIAVEASLKLKEISYIHAEAYAAGELKHGP-LALIDADMPVIVVAPNNElLEKVKSNIEEVRARGGQLYVF 548
Cdd:cd04795 2 FVIGIGGSGAIAAYFALELLELTGIEVVALIATELEHASlLSLLRKGDVVIALSYSGR-TEELLAALEIAKELGIPVIAI 80
|
...
gi 491949326 549 ADK 551
Cdd:cd04795 81 TDA 83
|
|
| murQ |
PRK05441 |
N-acetylmuramic acid-6-phosphate etherase; Reviewed |
340-425 |
6.66e-07 |
|
N-acetylmuramic acid-6-phosphate etherase; Reviewed
Pssm-ID: 235467 [Multi-domain] Cd Length: 299 Bit Score: 51.32 E-value: 6.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 340 PNSLLITLSQSGETADTLAALRLAKEKGymaALTIC--NVAGSSLVRESDLAFMTRAGVEVGVAST--KAFTTQLAALLM 415
Cdd:PRK05441 131 AKDVVVGIAASGRTPYVIGALEYARERG---ALTIGisCNPGSPLSKEADIAIEVVVGPEVLTGSTrmKAGTAQKLVLNM 207
|
90
....*....|....
gi 491949326 416 LVTA----LGKVKG 425
Cdd:PRK05441 208 ISTGvmirLGKVYG 221
|
|
| asnB |
PRK09431 |
asparagine synthetase B; Provisional |
1-172 |
1.81e-05 |
|
asparagine synthetase B; Provisional
Pssm-ID: 236513 [Multi-domain] Cd Length: 554 Bit Score: 47.60 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 1 MCGIVGAVAQRDVAEIL----INGLHRLEYRGYDSAGVavinkqnelqrirclgkvkaldeavsekpLIGGTGI-AHTRW 75
Cdd:PRK09431 1 MCGIFGILDIKTDADELrkkaLEMSRLMRHRGPDWSGI-----------------------------YASDNAIlGHERL 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 76 A----THGepsetnAHPHSS--GTFAVVHNGIIENHEELRELLKSRgYVFLSQTDTEVIAHLVEwemrstdsllEAVQKS 149
Cdd:PRK09431 52 SivdvNGG------AQPLYNedGTHVLAVNGEIYNHQELRAELGDK-YAFQTGSDCEVILALYQ----------EKGPDF 114
|
170 180
....*....|....*....|...
gi 491949326 150 VKQLTGAYGMVVMDSRHPEHLVA 172
Cdd:PRK09431 115 LDDLDGMFAFALYDSEKDAYLIA 137
|
|
| SIS_AgaS_like |
cd05010 |
AgaS-like protein. AgaS contains a SIS (Sugar ISomerase) domain which is found in many ... |
471-600 |
1.80e-04 |
|
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: 42.23 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 471 FLGRGAFYPIAVEASLKLKEIS--YIHAEAYAAGELKHGPLALIDADMPVIVVAPNNELLEKVKSN-IEEVRARGGQLYV 547
Cdd:cd05010 3 YLGSGPLAGLAREAALKVLELTagKVATVYDSPLGFRHGPKSLVDDDTLVVVFVSNDPYTRQYDLDlLKELRRDGIAARV 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 491949326 548 FA---DKEAGFTPSEGMKIITMPKVNDI-VAPIFYTIPmQLLSYYVALIKGTDVDQP 600
Cdd:cd05010 83 IAispESDAGIEDNSHYYLPGSRDLDDVyLAFPYILYA-QLFALFNSIALGLTPDNP 138
|
|
| PRK08674 |
PRK08674 |
bifunctional phosphoglucose/phosphomannose isomerase; Validated |
285-451 |
5.60e-03 |
|
bifunctional phosphoglucose/phosphomannose isomerase; Validated
Pssm-ID: 181536 [Multi-domain] Cd Length: 337 Bit Score: 39.19 E-value: 5.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 285 GAKGILEKVEHIQIVACGTSYNAGMVARywfeSLAGVSCDVEIaseFRYRKFVTRP----NSLLITLSQSGETADTLAAL 360
Cdd:PRK08674 26 DLEEDLEKIDNIVISGMGGSGIGGDLLR----ILLFDELKVPV---FVNRDYTLPAfvdeKTLVIAVSYSGNTEETLSAV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949326 361 RLAKEKGymaALTICNVAG---SSLVRESDL-------AFMTRAgvevgvastkAFTTQLAALLMLVTALG-------KV 423
Cdd:PRK08674 99 EQALKRG---AKIIAITSGgklKEMAKEHGLpviivpgGYQPRA----------ALGYLFTPLLKILEKLGlipdksaEV 165
|
170 180
....*....|....*....|....*....
gi 491949326 424 KGHISVEKE-REIIKAMQSLPAEIEKALA 451
Cdd:PRK08674 166 LETKIVLSElAEGLKEKVPTLKNLAKRLA 194
|
|
| |
