|
Name |
Accession |
Description |
Interval |
E-value |
| GlmS |
COG0449 |
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ... |
1-611 |
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: 1026.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 1 MCGIVGAVAERNITAILLEGLKRLEYRGYDSAGVAVFSNEGIlERRRRSGKVSELEQALAGEPLIGRLGIAHTRWATHGA 80
Cdd:COG0449 1 MCGIVGYIGKRDAAPILLEGLKRLEYRGYDSAGIAVLDDGGL-EVRKAVGKLANLEEKLAEEPLSGTIGIGHTRWATHGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 81 PCERNAHPHFSAN-TLAVVHNGIIENHEALREQLKGLGYVFASDTDTEVIVHLLHHKLKDTADLAVALKAAVKELHGAYG 159
Cdd:COG0449 80 PSDENAHPHTSCSgRIAVVHNGIIENYAELREELEAKGHTFKSETDTEVIAHLIEEYLKGGGDLLEAVRKALKRLEGAYA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 160 LAVINAAQPDRLLAARSGSPLVVGIGLGEHFLASDQLALRQVTDRFMYLEEGDIAEIRRDSVQIWNVDGVSVEREVVQYH 239
Cdd:COG0449 160 LAVISADEPDRIVAARKGSPLVIGLGEGENFLASDVPALLPYTRRVIYLEDGEIAVLTRDGVEIYDLDGEPVEREVKTVD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 240 EGAEAADKGEYRHFMLKEIHEQPKVVQRTLEGRLGQQQVLVHAFGPQAAELFAKVRNVQIVACGTSYHAGMVARYWLEGL 319
Cdd:COG0449 240 WDAEAAEKGGYPHFMLKEIHEQPEAIRDTLRGRLDEDGRVVLDELNLAAEDLRNIDRIYIVACGTSYHAGLVGKYLIEEL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 320 AGIPCQVEVASEFRYRKVVVQPDTLFVSISQSGETADTLAALRNAKELGfLASLAICNVGISSLVRESDLTLLTQAGPEI 399
Cdd:COG0449 320 ARIPVEVEIASEFRYRDPVVDPGTLVIAISQSGETADTLAALREAKEKG-AKVLAICNVVGSTIARESDAVLYTHAGPEI 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 400 GVASTKAFTTQLVALLLLTLSLGQVKGSLEEGVEAQLVEELRRLPTRLGEALAMDGTVEKVAELFAEKHHTLFLGRGAQF 479
Cdd:COG0449 399 GVASTKAFTTQLAALYLLALYLARARGTLSAEEEAELLEELRKLPEKIEEVLDLEEQIEELAEKYADARNALFLGRGINY 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 480 PVAMEGALKLKEISYIHAEAYPAGELKHGPLALVDADMPVVTVAPNNELLEKLKSNLQEVRARGGELIVFADEQAGMKNG 559
Cdd:COG0449 479 PVALEGALKLKEISYIHAEGYAAGELKHGPIALIDEGMPVVAIAPQDELYEKTLSNIQEVKARGGKVIAIADEGDEEVEE 558
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 1499951233 560 EGTHVIAMPHIIDSLAPILYTIPLQLLSYYVAVLKGTDVDQPRNLAKSVTVE 611
Cdd:COG0449 559 LADDVIEVPEVDELLAPILAVVPLQLLAYHVAVLRGTDVDQPRNLAKSVTVE 610
|
|
| PRK00331 |
PRK00331 |
isomerizing glutamine--fructose-6-phosphate transaminase; |
1-611 |
0e+00 |
|
isomerizing glutamine--fructose-6-phosphate transaminase;
Pssm-ID: 234729 [Multi-domain] Cd Length: 604 Bit Score: 1007.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 1 MCGIVGAVAERNITAILLEGLKRLEYRGYDSAGVAVFsNEGILERRRRSGKVSELEQALAGEPLIGRLGIAHTRWATHGA 80
Cdd:PRK00331 1 MCGIVGYVGQRNAAEILLEGLKRLEYRGYDSAGIAVL-DDGGLEVRKAVGKVANLEAKLEEEPLPGTTGIGHTRWATHGK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 81 PCERNAHPHFSAN-TLAVVHNGIIENHEALREQLKGLGYVFASDTDTEVIVHLLHHKLKDTADLAVALKAAVKELHGAYG 159
Cdd:PRK00331 80 PTERNAHPHTDCSgRIAVVHNGIIENYAELKEELLAKGHVFKSETDTEVIAHLIEEELKEGGDLLEAVRKALKRLEGAYA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 160 LAVINAAQPDRLLAARSGSPLVVGIGLGEHFLASDQLALRQVTDRFMYLEEGDIAEIRRDSVQIWNVDGVSVEREVVQYH 239
Cdd:PRK00331 160 LAVIDKDEPDTIVAARNGSPLVIGLGEGENFLASDALALLPYTRRVIYLEDGEIAVLTRDGVEIFDFDGNPVEREVYTVD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 240 EGAEAADKGEYRHFMLKEIHEQPKVVQRTLEGRLGqqqvlVHAFGPQAAELFAKVRNVQIVACGTSYHAGMVARYWLEGL 319
Cdd:PRK00331 240 WDASAAEKGGYRHFMLKEIYEQPEAIRDTLEGRLD-----ELGEGELADEDLKKIDRIYIVACGTSYHAGLVAKYLIESL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 320 AGIPCQVEVASEFRYRKVVVQPDTLFVSISQSGETADTLAALRNAKELGfLASLAICNVGISSLVRESDLTLLTQAGPEI 399
Cdd:PRK00331 315 AGIPVEVEIASEFRYRDPVLSPKTLVIAISQSGETADTLAALRLAKELG-AKTLAICNVPGSTIARESDAVLYTHAGPEI 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 400 GVASTKAFTTQLVALLLLTLSLGQVKGSLEEGVEAQLVEELRRLPTRLGEALAMDGTVEKVAELFAEKHHTLFLGRGAQF 479
Cdd:PRK00331 394 GVASTKAFTAQLAVLYLLALALAKARGTLSAEEEADLVHELRELPALIEQVLDLKEQIEELAEDFADARNALFLGRGVDY 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 480 PVAMEGALKLKEISYIHAEAYPAGELKHGPLALVDADMPVVTVAPNNELLEKLKSNLQEVRARGGELIVFADEqAGMKNG 559
Cdd:PRK00331 474 PVALEGALKLKEISYIHAEGYAAGELKHGPIALIDEGMPVVAIAPNDELYEKTKSNIQEVKARGARVIVIADE-GDEVAE 552
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 1499951233 560 EGTHVIAMPHIIDSLAPILYTIPLQLLSYYVAVLKGTDVDQPRNLAKSVTVE 611
Cdd:PRK00331 553 EADDVIEVPEVHELLAPLLYVVPLQLLAYHVALARGTDVDKPRNLAKSVTVE 604
|
|
| glmS |
TIGR01135 |
glucosamine--fructose-6-phosphate aminotransferase (isomerizing); The member from ... |
2-611 |
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: 878.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 2 CGIVGAVAERNITAILLEGLKRLEYRGYDSAGVAVfSNEGILERRRRSGKVSELEQALAGEPLIGRLGIAHTRWATHGAP 81
Cdd:TIGR01135 1 CGIVGYIGQRDAVPILLEGLKRLEYRGYDSAGIAV-VDEGKLFVRKAVGKVAELANKLGEKPLPGGVGIGHTRWATHGKP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 82 CERNAHPHFSAN-TLAVVHNGIIENHEALREQLKGLGYVFASDTDTEVIVHLLHHKLKDTADLAVALKAAVKELHGAYGL 160
Cdd:TIGR01135 80 TDENAHPHTDEGgRIAVVHNGIIENYAELREELEARGHVFSSDTDTEVIAHLIEEELREGGDLLEAVQKALKQLRGAYAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 161 AVINAAQPDRLLAARSGSPLVVGIGLGEHFLASDQLALRQVTDRFMYLEEGDIAEIRRDSVQIWNVDGVSVEREVVQYHE 240
Cdd:TIGR01135 160 AVLHADHPETLVAARSGSPLIVGLGDGENFVASDVTALLPYTRRVIYLEDGDIAILTKDGVEIYNFEGAPVQREVRVIDW 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 241 GAEAADKGEYRHFMLKEIHEQPKVVQRTLEGRLGQQQVLVHAFGpqAAELFAKVRNVQIVACGTSYHAGMVARYWLEGLA 320
Cdd:TIGR01135 240 DLDAAEKGGYRHFMLKEIYEQPRALRDTLEGRIEENGGVFEELG--AEELLKNIDRIQIVACGTSYHAGLVAKYLIERLA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 321 GIPCQVEVASEFRYRKVVVQPDTLFVSISQSGETADTLAALRNAKELGfLASLAICNVGISSLVRESDLTLLTQAGPEIG 400
Cdd:TIGR01135 318 GIPVEVEIASEFRYRKPVVDKDTLVIAISQSGETADTLEALRLAKELG-AKTLGICNVPGSTLVREADHTLYTRAGPEIG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 401 VASTKAFTTQLVALLLLTLSLGQVKGSLEEGVEAQLVEELRRLPTRLGEALAMDGTVEKVAELFAEKHHTLFLGRGAQFP 480
Cdd:TIGR01135 397 VASTKAFTTQLTVLYLLALALAKARGTLSAEEEAELVDALRRLPDLVEQVLLADESIAELAERYADKRNFLFLGRGLGYP 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 481 VAMEGALKLKEISYIHAEAYPAGELKHGPLALVDADMPVVTVAPNNELLEKLKSNLQEVRARGGELIVFADEQAGMKNGE 560
Cdd:TIGR01135 477 IALEGALKLKEISYIHAEGYPAGELKHGPIALIDEGLPVVAIAPKDSLLEKTKSNVEEVKARGARVIVFAPEDDETIASV 556
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 1499951233 561 GTHVIAMPHIIDSLAPILYTIPLQLLSYYVAVLKGTDVDQPRNLAKSVTVE 611
Cdd:TIGR01135 557 ADDVIKLPEVEELLAPIVYTIPLQLLAYHIALAKGTDVDKPRNLAKSVTVE 607
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
1-610 |
8.09e-163 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 479.90 E-value: 8.09e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 1 MCGIVGAVAERNITAILLEGLKRLEYRGYDSAGVAVFSNEGILE------RRRRSGKVSELEQALAGEPLIGRLGIAHTR 74
Cdd:PTZ00295 24 CCGIVGYLGNEDASKILLEGIEILQNRGYDSCGISTISSGGELKttkyasDGTTSDSIEILKEKLLDSHKNSTIGIAHTR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 75 WATHGAPCERNAHPHFS-ANTLAVVHNGIIENHEALREQLKGLGYVFASDTDTEVIVHLLHHKLKDTADLAVALKAAVKE 153
Cdd:PTZ00295 104 WATHGGKTDENAHPHCDyKKRIALVHNGTIENYVELKSELIAKGIKFRSETDSEVIANLIGLELDQGEDFQEAVKSAISR 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 154 LHGAYGLAVINAAQPDRLLAARSGSPLVVGIGLGEHFLASDQLALRQVTDRFMYLEEGDIAEIRRDsvqiwNVDGVSVER 233
Cdd:PTZ00295 184 LQGTWGLCIIHKDNPDSLIVARNGSPLLVGIGDDSIYVASEPSAFAKYTNEYISLKDGEIAELSLE-----NVNDLYTQR 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 234 EVVQYHEGAEAADKGEYRHFMLKEIHEQPKVVQRTLE--GRLGQQQVLVHAFG-PQAAELFAKVRNVQIVACGTSYHAGM 310
Cdd:PTZ00295 259 RVEKIPEEVIEKSPEPYPHWTLKEIFEQPIALSRALNngGRLSGYNNRVKLGGlDQYLEELLNIKNLILVGCGTSYYAAL 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 311 VARYWLEGLAGI-PCQVEVASEF-RYRkvVVQPDTLFVSISQSGETADTLAALRNAKELGFLaSLAICNVGISSLVRESD 388
Cdd:PTZ00295 339 FAASIMQKLKCFnTVQVIDASELtLYR--LPDEDAGVIFISQSGETLDVVRALNLADELNLP-KISVVNTVGSLIARSTD 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 389 LTLLTQAGPEIGVASTKAFTTQLVALLLLTLSLGQVK-GSLEEGVEAQLVEELRRLPTRLGEAL-AMDGTVEKVAELFAE 466
Cdd:PTZ00295 416 CGVYLNAGREVAVASTKAFTSQVTVLSLIALWFAQNKeYSCSNYKCSSLINSLHRLPTYIGMTLkSCEEQCKRIAEKLKN 495
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 467 KHHTLFLGRGAQFPVAMEGALKLKEISYIHAEAYPAGELKHGPLALVDAD--MPVVTVAPNNELLEKLKSNLQEVRARGG 544
Cdd:PTZ00295 496 AKSMFILGKGLGYPIALEGALKIKEITYIHAEGFSGGALKHGPFALIDKEknTPVILIILDDEHKELMINAAEQVKARGA 575
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1499951233 545 ELIVFADEQAGMKNGeGTHVIAMPHiIDSLAPILYTIPLQLLSYYVAVLKGTDVDQPRNLAKSVTV 610
Cdd:PTZ00295 576 YIIVITDDEDLVKDF-ADEIILIPS-NGPLTALLAVIPLQLLAYEIAILRGINPDKPRGLAKTVTV 639
|
|
| PLN02981 |
PLN02981 |
glucosamine:fructose-6-phosphate aminotransferase |
1-611 |
4.32e-160 |
|
glucosamine:fructose-6-phosphate aminotransferase
Pssm-ID: 215531 [Multi-domain] Cd Length: 680 Bit Score: 474.24 E-value: 4.32e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 1 MCGIVGAV------AERNITAILLEGLKRLEYRGYDSAGVAvFSNEGILERR-----RRSGKVSELE----QALAGEPLI 65
Cdd:PLN02981 1 MCGIFAYLnynvprERRFILEVLFNGLRRLEYRGYDSAGIA-IDNDPSLESSsplvfREEGKIESLVrsvyEEVAETDLN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 66 GRL------GIAHTRWATHGAPCERNAHPHFS--ANTLAVVHNGIIENHEALREQLKGLGYVFASDTDTEVIVHL----- 132
Cdd:PLN02981 80 LDLvfenhaGIAHTRWATHGPPAPRNSHPQSSgpGNEFLVVHNGIITNYEVLKETLLRHGFTFESDTDTEVIPKLakfvf 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 133 --LHHKLKDTADLAVALKaAVKELHGAYGLAVINAAQPDRLLAARSGSPLVVGIGLG----------------------- 187
Cdd:PLN02981 160 dkLNEEEGDVTFSQVVME-VMRQLEGAYALIFKSPHYPNELVACKRGSPLLLGVKELpeeknssavftsegfltknrdkp 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 188 -EHFLASDQLALRQVTDRFMYLEEGDIAEIRRDSVQIWNVDG------------VSVEREVVQYHEGAEAADKGEYRHFM 254
Cdd:PLN02981 239 kEFFLASDASAVVEHTKRVLVIEDNEVVHLKDGGVGIYKFENekgrgggglsrpASVERALSTLEMEVEQIMKGNYDHYM 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 255 LKEIHEQPKVVQRTLEGRLGQ------QQVLVHAFGPQAAELfAKVRNVQIVACGTSYHAGMVARYWLEGLAGIPCQVEV 328
Cdd:PLN02981 319 QKEIHEQPESLTTTMRGRLIRggsgkaKRVLLGGLKDHLKTI-RRSRRIVFIGCGTSYNAALAARPILEELSGVPVTMEL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 329 ASEFRYRKVVVQPDTLFVSISQSGETADTLAALRNAKELGFLAsLAICNVGISSLVRESDLTLLTQAGPEIGVASTKAFT 408
Cdd:PLN02981 398 ASDLLDRQGPIYREDTAVFVSQSGETADTLRALEYAKENGALC-VGITNTVGSAISRGTHCGVHINAGAEIGVASTKAYT 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 409 TQLVALLLLTLSLGQVKGSLEEGVEAqLVEELRRLPTRLGEALAMDGTVEKVAELFAEKHHTLFLGRGAQFPVAMEGALK 488
Cdd:PLN02981 477 SQIVAMTMLALALGEDSISSRSRREA-IIDGLFDLPNKVREVLKLDQEMKELAELLIDEQSLLVFGRGYNYATALEGALK 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 489 LKEISYIHAEAYPAGELKHGPLALVDADMPVVTVAPNNELLEKLKSNLQEVRARGGELIVFADE--QAGMKNGEGTHVIA 566
Cdd:PLN02981 556 VKEVALMHSEGILAGEMKHGPLALVDETLPIIVIATRDACFSKQQSVIQQLRARKGRLIVICSKgdASSVCPSGGCRVIE 635
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 1499951233 567 MPHIIDSLAPILYTIPLQLLSYYVAVLKGTDVDQPRNLAKSVTVE 611
Cdd:PLN02981 636 VPQVEDCLQPVINIVPLQLLAYHLTVLRGHNVDQPRNLAKSVTTQ 680
|
|
| PTZ00394 |
PTZ00394 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
1-611 |
1.67e-143 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 173585 [Multi-domain] Cd Length: 670 Bit Score: 431.22 E-value: 1.67e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 1 MCGIVGAV------AERNITAILLEGLKRLEYRGYDSAGVAVFSNEGILERR--------------RRSGKVSEL----- 55
Cdd:PTZ00394 1 MCGIFGYAnhnvprTVEQILNVLLDGIQKVEYRGYDSAGLAIDANIGSEKEDgtaasaptprpcvvRSVGNISQLrekvf 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 56 --EQALAGEPLIGRL----GIAHTRWATHGAPCERNAHPHFSAN-TLAVVHNGIIENHEALREQLKGLGYVFASDTDTEV 128
Cdd:PTZ00394 81 seAVAATLPPMDATTshhvGIAHTRWATHGGVCERNCHPQQSNNgEFTIVHNGIVTNYMTLKELLKEEGYHFSSDTDTEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 129 IVHLLHH-----KLKDTADLAVALKAavkELHGAYGLAVINAAQPDRLLAARSGSPLVVGI------------------- 184
Cdd:PTZ00394 161 ISVLSEYlytrkGIHNFADLALEVSR---MVEGSYALLVKSVYFPGQLAASRKGSPLMVGIrrtddrgcvmklqtydltd 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 185 --GLGEHFLASDQLALRQVTDRFMYLEEGDIAEIRRDSVQIWNVDGVS---VEREVVQYHEGAEAADKGEYRHFMLKEIH 259
Cdd:PTZ00394 238 lsGPLEVFFSSDVNSFAEYTREVVFLEDGDIAHYCDGALRFYNAAERQrsiVKREVQHLDAKPEGLSKGNYPHFMLKEIY 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 260 EQPKVVQRTLEGRL--GQQQVLVHAFGPQAAELFAKVRNVQIVACGTSYHAGMVARYWLEGLAGIPCQVEVASEFRYRKV 337
Cdd:PTZ00394 318 EQPESVISSMHGRIdfSSGTVQLSGFTQQSIRAILTSRRILFIACGTSLNSCLAVRPLFEELVPLPISVENASDFLDRRP 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 338 VVQPDTLFVSISQSGETADTLAALRNAKELGFLAsLAICNVGISSLVRESDLTLLTQAGPEIGVASTKAFTTQLVALLLL 417
Cdd:PTZ00394 398 RIQRDDVCFFVSQSGETADTLMALQLCKEAGAMC-VGITNVVGSSISRLTHYAIHLNAGVEVGVASTKAYTSQVVVLTLV 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 418 TLSLGQVKGSLEEGvEAQLVEELRRLPTRLGEALAM-DGTVEKVAELFAEKHHTLFLGRGAQFPVAMEGALKLKEISYIH 496
Cdd:PTZ00394 477 ALLLSSDSVRLQER-RNEIIRGLAELPAAISECLKItHDPVKALAARLKESSSILVLGRGYDLATAMEAALKVKELSYVH 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 497 AEAYPAGELKHGPLALVDADMPVVTVAPNNELLEKLKSNLQEVRARGGELIVFADEQAGMKNGEGTHVIAMPHIIDSLAP 576
Cdd:PTZ00394 556 TEGIHSGELKHGPLALIDETSPVLAMCTHDKHFGLSKSAVQQVKARGGAVVVFATEVDAELKAAASEIVLVPKTVDCLQC 635
|
650 660 670
....*....|....*....|....*....|....*
gi 1499951233 577 ILYTIPLQLLSYYVAVLKGTDVDQPRNLAKSVTVE 611
Cdd:PTZ00394 636 VVNVIPFQLLAYYMALLRGNNVDCPRNLAKSVTVQ 670
|
|
| GFAT |
cd00714 |
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ... |
2-216 |
9.77e-120 |
|
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: 353.68 E-value: 9.77e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 2 CGIVGAVAERNITAILLEGLKRLEYRGYDSAGVAVFSNeGILERRRRSGKVSELEQALAGEPLIGRLGIAHTRWATHGAP 81
Cdd:cd00714 1 CGIVGYIGKREAVDILLEGLKRLEYRGYDSAGIAVIGD-GSLEVVKAVGKVANLEEKLAEKPLSGHVGIGHTRWATHGEP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 82 CERNAHPHFSA-NTLAVVHNGIIENHEALREQLKGLGYVFASDTDTEVIVHLLHHKLKDTADLAVALKAAVKELHGAYGL 160
Cdd:cd00714 80 TDVNAHPHRSCdGEIAVVHNGIIENYAELKEELEAKGYKFESETDTEVIAHLIEYYYDGGLDLLEAVKKALKRLEGAYAL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1499951233 161 AVINAAQPDRLLAARSGSPLVVGIGLGEHFLASDQLALRQVTDRFMYLEEGDIAEI 216
Cdd:cd00714 160 AVISKDEPDEIVAARNGSPLVIGIGDGENFVASDAPALLEHTRRVIYLEDGDIAVI 215
|
|
| AgaS |
COG2222 |
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ... |
255-611 |
3.94e-74 |
|
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: 240.57 E-value: 3.94e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 255 LKEIHEQPKVVQRTLEgrlgqqqvlvhAFGPQAAELFAKVR-----NVQIVACGTSYHAGMVARYWLEGLAGIPCQVEVA 329
Cdd:COG2222 1 AREIAQQPEAWRRALA-----------ALAAAIAALLARLRakpprRVVLVGAGSSDHAAQAAAYLLERLLGIPVAALAP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 330 SEF-RYRKVVVQPDTLFVSISQSGETADTLAALRNAKELGFLaSLAICNVGISSLVRESDLTLLTQAGPEIGVASTKAFT 408
Cdd:COG2222 70 SELvVYPAYLKLEGTLVVAISRSGNSPEVVAALELAKARGAR-TLAITNNPDSPLAEAADRVLPLPAGPEKSVAATKSFT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 409 TQLVALLLLTLSLGQvkgsleegvEAQLVEELRRLPTRLGEALAMDGTVEKVAELFAEKHHTlFLGRGAQFPVAMEGALK 488
Cdd:COG2222 149 TMLLALLALLAAWGG---------DDALLAALDALPAALEAALAADWPAAALAALADAERVV-FLGRGPLYGLAREAALK 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 489 LKEISYIHAEAYPAGELKHGPLALVDADMPVVTVAPNNELLEKLKSNLQEVRARGGELIVFADEqagmkNGEGTHVIAMP 568
Cdd:COG2222 219 LKELSAGHAEAYSAAEFRHGPKSLVDPGTLVVVLASEDPTRELDLDLAAELRALGARVVAIGAE-----DDAAITLPAIP 293
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1499951233 569 HIIDSLAPILYTIPLQLLSYYVAVLKGTDVDQPRNLAKSVTVE 611
Cdd:COG2222 294 DLHDALDPLLLLVVAQRLALALALARGLDPDTPRHLNKVVKTV 336
|
|
| SIS_GlmS_GlmD_2 |
cd05009 |
SIS (Sugar ISomerase) domain repeat 2 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
457-609 |
1.56e-67 |
|
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: 216.74 E-value: 1.56e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 457 VEKVAELFAEKHHTLFLGRGAQFPVAMEGALKLKEISYIHAEAYPAGELKHGPLALVDADMPVVTVAPNNELLEKLKSNL 536
Cdd:cd05009 3 IKELAEKLKEAKSFYVLGRGPNYGTALEGALKLKETSYIHAEAYSAGEFKHGPIALVDEGTPVIFLAPEDRLEEKLESLI 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1499951233 537 QEVRARGGELIVFADEQAGMKngEGTHVIAMPHIIDSLAPILYTIPLQLLSYYVAVLKGTDVDQPRNLAKSVT 609
Cdd:cd05009 83 KEVKARGAKVIVITDDGDAKD--LADVVIRVPATVEELSPLLYIVPLQLLAYHLAVARGIDPDKPRNLAKSVT 153
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
2-214 |
2.75e-61 |
|
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: 202.68 E-value: 2.75e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 2 CGIVGAVAERNITAILLE----GLKRLEYRGYDSAGVAVFSNEGILeRRRRSGKVSELEQALAGEPLIGRLGIAHTRWAT 77
Cdd:cd00352 1 CGIFGIVGADGAASLLLLlllrGLAALEHRGPDGAGIAVYDGDGLF-VEKRAGPVSDVALDLLDEPLKSGVALGHVRLAT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 78 HGAPCERNAHPHFSA-NTLAVVHNGIIENHEALREQLKGLGYVFASDTDTEVIVHLLHHKLKDTaDLAVALKAAVKELHG 156
Cdd:cd00352 80 NGLPSEANAQPFRSEdGRIALVHNGEIYNYRELREELEARGYRFEGESDSEVILHLLERLGREG-GLFEAVEDALKRLDG 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1499951233 157 AYGLAVINaAQPDRLLAARSG---SPLVVGIGL-GEHFLASDQLALRQVT-DRFMYLEEGDIA 214
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 ... |
296-407 |
8.01e-53 |
|
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: 176.92 E-value: 8.01e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 296 NVQIVACGTSYHAGMVARYWLEGLAGIPCQVEVASEFRYRKVVVQPDTLFVSISQSGETADTLAALRNAKELGFLaSLAI 375
Cdd:cd05008 1 RILIVGCGTSYHAALVAKYLLERLAGIPVEVEAASEFRYRRPLLDEDTLVIAISQSGETADTLAALRLAKEKGAK-TVAI 79
|
90 100 110
....*....|....*....|....*....|..
gi 1499951233 376 CNVGISSLVRESDLTLLTQAGPEIGVASTKAF 407
Cdd:cd05008 80 TNVVGSTLAREADYVLYLRAGPEISVAATKAF 111
|
|
| PurF |
COG0034 |
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ... |
1-198 |
8.24e-38 |
|
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; Glutamine phosphoribosylpyrophosphate amidotransferase is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439804 [Multi-domain] Cd Length: 464 Bit Score: 145.94 E-value: 8.24e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 1 MCGIVGAVAERNITAILLEGLKRLEYRGYDSAGVAVFSNEGILERRRRsGKVSEL--EQALAGepLIGRLGIAHTRWATH 78
Cdd:COG0034 7 ECGVFGIYGHEDVAQLTYYGLYALQHRGQESAGIATSDGGRFHLHKGM-GLVSDVfdEEDLER--LKGNIAIGHVRYSTT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 79 GAPCERNAHP---HFSANTLAVVHNGIIENHEALREQLKGLGYVFASDTDTEVIVHLLHHKLKDtADLAVALKAAVKELH 155
Cdd:COG0034 84 GSSSLENAQPfyvNSPFGSIALAHNGNLTNAEELREELEEEGAIFQTTSDTEVILHLIARELTK-EDLEEAIKEALRRVK 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1499951233 156 GAYGLAVINaaqPDRLLAAR--SG-SPLVVGIGLGEHFLASDQLAL 198
Cdd:COG0034 163 GAYSLVILT---GDGLIAARdpNGiRPLVLGKLEDGYVVASESCAL 205
|
|
| GPATase_N |
cd00715 |
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ... |
2-201 |
1.92e-35 |
|
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: 133.74 E-value: 1.92e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 2 CGIVGAVAERNITAILLEGLKRLEYRGYDSAGVAVFSNEGILERRRRsGKVSEL--EQALagEPLIGRLGIAHTRWATHG 79
Cdd:cd00715 1 CGVFGIYGAEDAARLTYLGLYALQHRGQESAGIATSDGKRFHTHKGM-GLVSDVfdEEKL--RRLPGNIAIGHVRYSTAG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 80 APCERNAHPhFSANT----LAVVHNGIIENHEALREQLKGLGYVFASDTDTEVIVHLLHHKLKDtADLAVALKAAVKELH 155
Cdd:cd00715 78 SSSLENAQP-FVVNSplggIALAHNGNLVNAKELREELEEEGRIFQTTSDSEVILHLIARSLAK-DDLFEAIIDALERVK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1499951233 156 GAYGLAVINaaqPDRLLAARSGS---PLVVG-IGLGEHFLASDQLALRQV 201
Cdd:cd00715 156 GAYSLVIMT---ADGLIAVRDPHgirPLVLGkLEGDGYVVASESCALDII 202
|
|
| purF |
TIGR01134 |
amidophosphoribosyltransferase; Alternate name: glutamine phosphoribosylpyrophosphate (PRPP) ... |
2-205 |
5.07e-29 |
|
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: 120.12 E-value: 5.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 2 CGIVGAVAERNITAILL-EGLKRLEYRGYDSAGVAVFSNEGILERRRRsGKVSELEQALAGEPLIGRLGIAHTRWATHGA 80
Cdd:TIGR01134 1 CGVVGIYGQEEVAASLTyYGLYALQHRGQESAGISVFDGNRFRLHKGN-GLVSDVFNEEHLQRLKGNVGIGHVRYSTAGS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 81 PCERNAHPhFSANT----LAVVHNGIIENHEALREQLKGLGYVFASDTDTEVIVHLLHHKLKDTADLAVALKAAVKELHG 156
Cdd:TIGR01134 80 SGLENAQP-FVVNSpyggLALAHNGNLVNADELRRELEEEGRHFNTTSDSEVLLHLLAHNDESKDDLFDAVARVLERVRG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1499951233 157 AYGLAVINaaqPDRLLAARS--G-SPLVVGIGLGEHFLASDQLALRQVTDRF 205
Cdd:TIGR01134 159 AYALVLMT---EDGLVAVRDphGiRPLVLGRRGDGYVVASESCALDILGAEF 207
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
290-407 |
8.48e-28 |
|
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: 108.54 E-value: 8.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 290 LFAKVRNVQIVACGTSYHAGMVARYWLEGLAGIPCQVEVASEFRYRKV-VVQPDTLFVSISQSGETADTLAALRNAKELG 368
Cdd:pfam01380 1 LLAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGVLaLVDEDDLVIAISYSGETKDLLAAAELAKARG 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 1499951233 369 fLASLAICNVGISSLVRESDLTLLTQAGPEIGVASTKAF 407
Cdd:pfam01380 81 -AKIIAITDSPGSPLAREADHVLYINAGPETGVASTKSI 118
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
463-594 |
1.22e-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: 105.07 E-value: 1.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 463 LFAEKHHTLFLGRGAQFPVAMEGALKLKEISYIHAEAYPAGELKHGPLALVDADMPVVTVAPNNELLEKLKsNLQEVRAR 542
Cdd:pfam01380 1 LLAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGVLALVDEDDLVIAISYSGETKDLLA-AAELAKAR 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1499951233 543 GGELIVFADEQAGMKNGEGTHVIAMPHIIDSLAPILYTIPLQLLSYYVAVLK 594
Cdd:pfam01380 80 GAKIIAITDSPGSPLAREADHVLYINAGPETGVASTKSITAQLAALDALAVA 131
|
|
| PLN02440 |
PLN02440 |
amidophosphoribosyltransferase |
1-198 |
8.42e-26 |
|
amidophosphoribosyltransferase
Pssm-ID: 215241 [Multi-domain] Cd Length: 479 Bit Score: 110.92 E-value: 8.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 1 MCGIVGAVAERNITAILLEGLKRLEYRGYDSAGVaVFSNEGILERRRRSGKVSELEQALAGEPLIGRLGIAHTRWATHGA 80
Cdd:PLN02440 1 ECGVVGIFGDPEASRLCYLGLHALQHRGQEGAGI-VTVDGNRLQSITGNGLVSDVFDESKLDQLPGDIAIGHVRYSTAGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 81 PCERNAHPhFSAN----TLAVVHNGIIENHEALREQLKGLGYVFASDTDTEVIVHLLHHKLKDTADLAVAlkAAVKELHG 156
Cdd:PLN02440 80 SSLKNVQP-FVANyrfgSIGVAHNGNLVNYEELRAKLEENGSIFNTSSDTEVLLHLIAISKARPFFSRIV--DACEKLKG 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1499951233 157 AY-GLAVINaaqpDRLLAARSGS---PLVVGI-GLGEHFLASDQLAL 198
Cdd:PLN02440 157 AYsMVFLTE----DKLVAVRDPHgfrPLVMGRrSNGAVVFASETCAL 199
|
|
| PRK05793 |
PRK05793 |
amidophosphoribosyltransferase; Provisional |
2-222 |
1.23e-25 |
|
amidophosphoribosyltransferase; Provisional
Pssm-ID: 235611 [Multi-domain] Cd Length: 469 Bit Score: 110.51 E-value: 1.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 2 CGIVGAVAERNITA--ILLEGLKRLEYRGYDSAGVAVfSNEGILERRRRSGKVSELEQALAGEPLIGRLGIAHTRWATHG 79
Cdd:PRK05793 15 CGVFGVFSKNNIDVasLTYYGLYALQHRGQESAGIAV-SDGEKIKVHKGMGLVSEVFSKEKLKGLKGNSAIGHVRYSTTG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 80 APCERNAHP---HFSANTLAVVHNGIIENHEALREQLKGLGYVFASDTDTEVIVHLLHHKLKdtADLAVALKAAVKELHG 156
Cdd:PRK05793 94 ASDLDNAQPlvaNYKLGSIAIAHNGNLVNADVIRELLEDGGRIFQTSIDSEVILNLIARSAK--KGLEKALVDAIQAIKG 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 157 AYGLAVINAaqpDRLLAARSGS---PLVVGIGLGEHFLASDQLALRQVTDRFMY-LEEGDIAEIRRDSVQ 222
Cdd:PRK05793 172 SYALVILTE---DKLIGVRDPHgirPLCLGKLGDDYILSSESCALDTIGAEFIRdVEPGEIVIIDEDGIK 238
|
|
| GlxB |
cd01907 |
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ... |
2-224 |
1.46e-25 |
|
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine amidotransferase-like protein of unknown function found in bacteria and archaea. GlxB has a structural fold similar to that of other class II glutamine amidotransferases including glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), beta lactam synthetase (beta-LS) and glutamate synthase (GltS). The GlxB fold is also somewhat similar to the Ntn (N-terminal nucleophile) hydrolase fold of the proteasomal alpha and beta subunits.
Pssm-ID: 238888 [Multi-domain] Cd Length: 249 Bit Score: 105.81 E-value: 1.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 2 CGIVGAV---AERNITAILLEGLKRLEYRG-YDSAGVAVFSNEGIleRRRRSGKVSELEQALaGEP-----------LIG 66
Cdd:cd01907 1 CGIFGIMskdGEPFVGALLVEMLDAMQERGpGDGAGFALYGDPDA--FVYSSGKDMEVFKGV-GYPediarrydleeYKG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 67 RLGIAHTRWATHGAPCERNAHPhFSANTLAVVHNGIIENHEALREQLKGLGYVFASDTDTEVIVHLLHHKLK-------- 138
Cdd:cd01907 78 YHWIAHTRQPTNSAVWWYGAHP-FSIGDIAVVHNGEISNYGSNREYLERFGYKFETETDTEVIAYYLDLLLRkgglpley 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 139 -----------DTADLAVALKAAVKELHGAYGLAVinaAQPDRLLAARSGS---PLVVGIGLGEHFLASDQLALRQVTDR 204
Cdd:cd01907 157 ykhiirmpeeeRELLLALRLTYRLADLDGPFTIIV---GTPDGFIVIRDRIklrPAVVAETDDYVAIASEECAIREIPDR 233
|
250 260
....*....|....*....|
gi 1499951233 205 fmylEEGDIAEIRRDSVQIW 224
Cdd:cd01907 234 ----DNAKVWEPRPGEYVIW 249
|
|
| GATase_6 |
pfam13522 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
66-194 |
8.49e-20 |
|
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain found in a variety of enzymes, such as asparagine synthetase and glutamine--fructose-6-phosphate transaminase.
Pssm-ID: 433279 [Multi-domain] Cd Length: 130 Bit Score: 85.44 E-value: 8.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 66 GRLGIAHTRWATHGAPCERNaHPHFSAN-TLAVVHNGIIENHEALREQLKGLGYVFASDTDTEVIVHLLHHKLKDTadla 144
Cdd:pfam13522 10 GGVALGHVRLAIVDLPDAGN-QPMLSRDgRLVLVHNGEIYNYGELREELADLGHAFRSRSDTEVLLALYEEWGEDC---- 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1499951233 145 valkaaVKELHGAYGLAVINAAQpDRLLAARSG---SPLVVGIgLGEHFL-ASD 194
Cdd:pfam13522 85 ------LERLRGMFAFAIWDRRR-RTLFLARDRlgiKPLYYGI-LGGGFVfASE 130
|
|
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
1-175 |
4.35e-17 |
|
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: 84.50 E-value: 4.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 1 MCGIVGAVA--ERNITAILLEGLKRLEYRGYDSAGVAVFsnegilerrrrsgkvseleqalagepliGRLGIAHTRWATH 78
Cdd:COG0367 1 MCGIAGIIDfdGGADREVLERMLDALAHRGPDGSGIWVD----------------------------GGVALGHRRLSII 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 79 GaPCERNAHPHFSAN-TLAVVHNGIIENHEALREQLKGLGYVFASDTDTEVIVHLLHHKLKDtadlavalkaAVKELHGA 157
Cdd:COG0367 53 D-LSEGGHQPMVSEDgRYVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHAYEEWGED----------CLERLNGM 121
|
170
....*....|....*...
gi 1499951233 158 YGLAVINAAQpDRLLAAR 175
Cdd:COG0367 122 FAFAIWDRRE-RRLFLAR 138
|
|
| GATase_7 |
pfam13537 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
94-175 |
7.55e-17 |
|
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain found in a variety of enzymes such as asparagine synthetase and glutamine-fructose-6-phosphate transaminase.
Pssm-ID: 433289 [Multi-domain] Cd Length: 123 Bit Score: 76.79 E-value: 7.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 94 TLAVVHNGIIENHEALREQLKGLGYVFASDTDTEVIVHLLHHKlkdtadlavALKAAVKELHGAYGLAVINAAQpDRLLA 173
Cdd:pfam13537 23 RYVIVFNGEIYNYRELRAELEAKGYRFRTHSDTEVILHLYEAE---------WGEDCVDRLNGMFAFAIWDRRR-QRLFL 92
|
..
gi 1499951233 174 AR 175
Cdd:pfam13537 93 AR 94
|
|
| AsnB |
cd00712 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ... |
2-175 |
9.25e-17 |
|
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: 79.52 E-value: 9.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 2 CGIVGAV---AERNITAILLEGLKRLEYRGYDSAGVAVFsnegilerrrrsgkvseleqalagepliGRLGIAHTRWATH 78
Cdd:cd00712 1 CGIAGIIgldGASVDRATLERMLDALAHRGPDGSGIWID----------------------------EGVALGHRRLSII 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 79 gaPCERNAHPHFSAN-TLAVVHNGIIENHEALREQLKGLGYVFASDTDTEVIVHLLHHKLKDtadlavalkaAVKELHGA 157
Cdd:cd00712 53 --DLSGGAQPMVSEDgRLVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHLYEEWGED----------CLERLNGM 120
|
170
....*....|....*...
gi 1499951233 158 YGLAVINAAQpDRLLAAR 175
Cdd:cd00712 121 FAFALWDKRK-RRLFLAR 137
|
|
| YafJ |
cd01908 |
Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine ... |
30-179 |
7.69e-15 |
|
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: 74.73 E-value: 7.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 30 DSAGVAVFSNEGILERRRRSGKVSELEQALA--GEPLIGRLGIAHTRWATHGAPCERNAHPhFSANTLAVVHNGIIENHE 107
Cdd:cd01908 42 DGWGIGWYEGKGGRPFRYRSPLPAWSDINLEslARPIKSPLVLAHVRAATVGPVSLENCHP-FTRGRWLFAHNGQLDGFR 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 108 ALREQL-KGLGYVFASDTDTEVIVHLL-----HHKLKDTADLAVALKAAVKELHGAYGLAVINAA--QPDRLLAARSGSP 179
Cdd:cd01908 121 LLRRRLlRLLPRLPVGTTDSELAFALLlsrllERDPLDPAELLDAILQTLRELAALAPPGRLNLLlsDGEYLIATRYASA 200
|
|
| YafJ |
COG0121 |
Predicted glutamine amidotransferase YafJ [General function prediction only]; |
33-178 |
5.28e-13 |
|
Predicted glutamine amidotransferase YafJ [General function prediction only];
Pssm-ID: 439891 [Multi-domain] Cd Length: 248 Bit Score: 69.22 E-value: 5.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 33 GVAVFSNEGILERRRRSGKV--SELEQALAgEPLIGRLGIAHTRWATHGAPCERNAHPhFSANTLAVVHNGIIENHEALR 110
Cdd:COG0121 42 GIGWYEGDGEPRLYRDPLPAwsDPNLRLLA-RPIKSRLVIAHVRKATVGPVSLENTHP-FRGGRWLFAHNGQLDGFDRLR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 111 EQL-----KGLGYVFASDTDTEVIVHLLHHKLKDT-ADLAVALKAAVKEL------HGAYGLAVINaaqPDRLLAARSGS 178
Cdd:COG0121 120 RRLaeelpDELYFQPVGTTDSELAFALLLSRLRDGgPDPAEALAEALRELaelaraPGRLNLLLSD---GERLYATRYTS 196
|
|
| asnB |
PRK09431 |
asparagine synthetase B; Provisional |
1-206 |
4.44e-12 |
|
asparagine synthetase B; Provisional
Pssm-ID: 236513 [Multi-domain] Cd Length: 554 Bit Score: 68.78 E-value: 4.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 1 MCGIVGAVAERNITAIL----LEGLKRLEYRGYDSAGVAVfSNEGILerrrrsgkvseleqalagepligrlgiAHTRWA 76
Cdd:PRK09431 1 MCGIFGILDIKTDADELrkkaLEMSRLMRHRGPDWSGIYA-SDNAIL---------------------------GHERLS 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 77 ----THGApcernaHPHFSAN-TLAVVHNGIIENHEALREQLKGlGYVFASDTDTEVIVHLLHHKLKDtadlavalkaAV 151
Cdd:PRK09431 53 ivdvNGGA------QPLYNEDgTHVLAVNGEIYNHQELRAELGD-KYAFQTGSDCEVILALYQEKGPD----------FL 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1499951233 152 KELHGAYGLAVINAAQpDRLLAARsgSPLvvGI-----GLGEH---FLASDQLALRQVTDRFM 206
Cdd:PRK09431 116 DDLDGMFAFALYDSEK-DAYLIAR--DPI--GIiplyyGYDEHgnlYFASEMKALVPVCKTIK 173
|
|
| SIS_RpiR |
cd05013 |
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ... |
286-395 |
7.19e-11 |
|
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: 60.32 E-value: 7.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 286 QAAELFAKVRNVQIVACGTSYHAGMVARYWLeGLAGIPCQVEVAS-EFRYRKVVVQPDTLFVSISQSGETADTLAALRNA 364
Cdd:cd05013 5 KAVDLLAKARRIYIFGVGSSGLVAEYLAYKL-LRLGKPVVLLSDPhLQLMSAANLTPGDVVIAISFSGETKETVEAAEIA 83
|
90 100 110
....*....|....*....|....*....|.
gi 1499951233 365 KELGfLASLAICNVGISSLVRESDLTLLTQA 395
Cdd:cd05013 84 KERG-AKVIAITDSANSPLAKLADIVLLVSS 113
|
|
| SIS_1 |
cd05710 |
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ... |
296-368 |
6.31e-10 |
|
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars.
Pssm-ID: 240214 [Multi-domain] Cd Length: 120 Bit Score: 57.20 E-value: 6.31e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1499951233 296 NVQIVACGTSYHAGMVARYWLEGLAGIPCQVEVASEFRYRK-VVVQPDTLFVSISQSGETADTLAALRNAKELG 368
Cdd:cd05710 1 NVFFVGCGGSLADMYPAKYFLKKESKLPVFVYNAAEFLHTGpKRLTEKSVVILASHSGNTKETVAAAKFAKEKG 74
|
|
| RpiR |
COG1737 |
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ... |
286-395 |
1.75e-09 |
|
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains [Transcription];
Pssm-ID: 441343 [Multi-domain] Cd Length: 286 Bit Score: 59.17 E-value: 1.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 286 QAAELFAKVRNVQIVACGTSYHAGMVARYWLeGLAGIPCQV--EVASEFRYRKVVVQPDTLFVSISQSGETADTLAALRN 363
Cdd:COG1737 126 RAVDLLAKARRIYIFGVGASAPVAEDLAYKL-LRLGKNVVLldGDGHLQAESAALLGPGDVVIAISFSGYTRETLEAARL 204
|
90 100 110
....*....|....*....|....*....|..
gi 1499951233 364 AKELGfLASLAICNVGISSLVRESDLTLLTQA 395
Cdd:COG1737 205 AKERG-AKVIAITDSPLSPLAKLADVVLYVPS 235
|
|
| PTZ00077 |
PTZ00077 |
asparagine synthetase-like protein; Provisional |
1-254 |
1.02e-08 |
|
asparagine synthetase-like protein; Provisional
Pssm-ID: 185431 [Multi-domain] Cd Length: 586 Bit Score: 58.19 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 1 MCGIVgAVAERNITAILLEGL-----KRLEYRGYDSAGVAVFSNEgilerrrrsgkvSELEQALAGEpligRLGIAHTrw 75
Cdd:PTZ00077 1 MCGIL-AIFNSKGERHELRRKalelsKRLRHRGPDWSGIIVLENS------------PGTYNILAHE----RLAIVDL-- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 76 athgapcERNAHPHFSAN-TLAVVHNGIIENHEALREQLKGLGYVFASDTDTEVIVHLlhHKLKDTADLavalkaaVKEL 154
Cdd:PTZ00077 62 -------SDGKQPLLDDDeTVALMQNGEIYNHWEIRPELEKEGYKFSSNSDCEIIGHL--YKEYGPKDF-------WNHL 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 155 HGAYGLAVINAAQpDRLLAARSG---SPLVVGIGL-GEHFLASDQLAL-RQVTD--RF----MYLEEGDIAEIRRDSVQI 223
Cdd:PTZ00077 126 DGMFATVIYDMKT-NTFFAARDHigiIPLYIGYAKdGSIWFSSELKALhDQCVEvkQFppghYYDQTKEKGEFVRYYNPN 204
|
250 260 270
....*....|....*....|....*....|.
gi 1499951233 224 WNVDGVSVEREVVQYHEGAEAADKGEYRHFM 254
Cdd:PTZ00077 205 WHDFDHPIPTGEIDLEEIREALEAAVRKRLM 235
|
|
| PLN02549 |
PLN02549 |
asparagine synthase (glutamine-hydrolyzing) |
1-206 |
2.72e-08 |
|
asparagine synthase (glutamine-hydrolyzing)
Pssm-ID: 178164 [Multi-domain] Cd Length: 578 Bit Score: 56.70 E-value: 2.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 1 MCGIVGAV----AERNITAILLEGLKRLEYRGYDSAGVAVFsnegilerrrrsgkvseleqalagepliGRLGIAHTRWA 76
Cdd:PLN02549 1 MCGILAVLgcsdDSQAKRSRVLELSRRLRHRGPDWSGLYGN----------------------------EDCYLAHERLA 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 77 THgAPcERNAHPHFSAN-TLAVVHNGIIENHEALREQLKglGYVFASDTDTEVIVHLLHHKLKDTadlavalkaaVKELH 155
Cdd:PLN02549 53 IM-DP-ESGDQPLYNEDkTIVVTANGEIYNHKELREKLK--LHKFRTGSDCEVIAHLYEEHGEEF----------VDMLD 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1499951233 156 GAYGLaVINAAQPDRLLAARSG---SPLVVGIGL-GEHFLASDQLALRQVTDRFM 206
Cdd:PLN02549 119 GMFSF-VLLDTRDNSFIAARDHigiTPLYIGWGLdGSVWFASEMKALCDDCERFE 172
|
|
| asn_synth_AEB |
TIGR01536 |
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing ... |
94-175 |
6.42e-08 |
|
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing asparagine synthase. A poorly conserved C-terminal extension was removed from the model. Bacterial members of the family tend to have a long, poorly conserved insert lacking from archaeal and eukaryotic sequences. Multiple isozymes have been demonstrated, such as in Bacillus subtilis. Long-branch members of the phylogenetic tree (which typically were also second or third candidate members from their genomes) were removed from the seed alignment and score below trusted cutoff. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 273676 [Multi-domain] Cd Length: 466 Bit Score: 55.42 E-value: 6.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 94 TLAVVHNGIIENHEALREQLKGLGYVFASDTDTEVIVHLLHHKLKDTADLavalkaavkeLHGAYGLAVINAAQpDRLLA 173
Cdd:TIGR01536 67 TYVIVFNGEIYNHEELREELEAKGYTFQTDSDTEVILHLYEEWGEECVDR----------LDGMFAFALWDSEK-GELFL 135
|
..
gi 1499951233 174 AR 175
Cdd:TIGR01536 136 AR 137
|
|
| frlB |
PRK11382 |
fructoselysine 6-phosphate deglycase; |
434-602 |
1.98e-07 |
|
fructoselysine 6-phosphate deglycase;
Pssm-ID: 183111 [Multi-domain] Cd Length: 340 Bit Score: 53.47 E-value: 1.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 434 AQLVEELRRLPTRLGEAL-AMDGTVEKVAELFAEKHHTLFLGRGAQFPVAM-EGALKLKEISYIHAEAYPAGELKHGPLA 511
Cdd:PRK11382 174 GKIKNDLKQLPNALGHLVrTWEEKGRQLGELASQWPMIYTVAAGPLRPLGYkEGIVTLMEFTWTHGCVIESGEFRHGPLE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 512 LVDADMPVVTVAPNNELLEKLKSNLQEVRARGGELIVFADEQAgmknGEGTHviamphiiDSLAPILYTIPLQLLSYYVA 591
Cdd:PRK11382 254 IVEPGVPFLFLLGNDESRHTTERAINFVKQRTDNVIVIDYAEI----SQGLH--------PWLAPFLMFVPMEWLCYYLS 321
|
170
....*....|.
gi 1499951233 592 VLKGTDVDQPR 602
Cdd:PRK11382 322 IYKDHNPDERR 332
|
|
| SIS |
cd04795 |
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
297-368 |
2.89e-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: 48.52 E-value: 2.89e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1499951233 297 VQIVACGTSYHAGMVARYWLEGLAGIPCQVEVASEFRY--RKVVVQPDTLFVSISQSGETADTLAALRNAKELG 368
Cdd:cd04795 1 IFVIGIGGSGAIAAYFALELLELTGIEVVALIATELEHasLLSLLRKGDVVIALSYSGRTEELLAALEIAKELG 74
|
|
| SIS |
cd04795 |
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
471-551 |
7.45e-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: 47.37 E-value: 7.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 471 LFLGRGAQFPVAMEGALKLKEISYIHAEAYPAGELKHGP-LALVDADMPVVTVAPNNElLEKLKSNLQEVRARGGELIVF 549
Cdd:cd04795 2 FVIGIGGSGAIAAYFALELLELTGIEVVALIATELEHASlLSLLRKGDVVIALSYSGR-TEELLAALEIAKELGIPVIAI 80
|
..
gi 1499951233 550 AD 551
Cdd:cd04795 81 TD 82
|
|
| SIS_AgaS_like |
cd05010 |
AgaS-like protein. AgaS contains a SIS (Sugar ISomerase) domain which is found in many ... |
472-601 |
6.66e-06 |
|
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: 46.47 E-value: 6.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951233 472 FLGRGAQFPVAMEGALKLKEIS--YIHAEAYPAGELKHGPLALVDADMPVVTVAPNNE--------LLEKLKSNLQevra 541
Cdd:cd05010 3 YLGSGPLAGLAREAALKVLELTagKVATVYDSPLGFRHGPKSLVDDDTLVVVFVSNDPytrqydldLLKELRRDGI---- 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1499951233 542 rGGELIVFADEQAGMKNGEGTHVI-AMPHIIDS-LAPIlYTIPLQLLSYYVAVLKGTDVDQP 601
Cdd:cd05010 79 -AARVIAISPESDAGIEDNSHYYLpGSRDLDDVyLAFP-YILYAQLFALFNSIALGLTPDNP 138
|
|
| SIS_PGI_PMI_1 |
cd05017 |
The members of this protein family contain the SIS (Sugar ISomerase) domain and have both the ... |
298-368 |
6.55e-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: 39.94 E-value: 6.55e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1499951233 298 QIVACGT--SYHAGMVARYWLEGLAGIPCQVeVASEFRYRKVvvQPDTLFVSISQSGETADTLAALRNAKELG 368
Cdd:cd05017 1 NIVILGMggSGIGGDLLESLLLDEAKIPVYV-VKDYTLPAFV--DRKTLVIAVSYSGNTEETLSAVEQAKERG 70
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