|
Name |
Accession |
Description |
Interval |
E-value |
| GlmS |
COG0449 |
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ... |
1-637 |
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: 963.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 1 MCGIIAYMGAREAAPILVAGLRRLEYRGYDSAGIAVLDErrpGGIQRVRAAGKIAALADKLGVEEPTGRAGIGHTRWATH 80
Cdd:COG0449 1 MCGIVGYIGKRDAAPILLEGLKRLEYRGYDSAGIAVLDD---GGLEVRKAVGKLANLEEKLAEEPLSGTIGIGHTRWATH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 81 GRPCERNAHPHRG--GSVCVVHNGIIENHAELRARLEEEeGRRLTSDTDTEVIAHLVDSHYGRlraaalaqaggeGARLV 158
Cdd:COG0449 78 GAPSDENAHPHTScsGRIAVVHNGIIENYAELREELEAK-GHTFKSETDTEVIAHLIEEYLKG------------GGDLL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 159 AAVQASLAELRGAYALALIHDDHPGTIVGARSASPLIVGVGEGgeaaELFLASDVAAILEHTRTVLDLEDGDVVHLDADa 238
Cdd:COG0449 145 EAVRKALKRLEGAYALAVISADEPDRIVAARKGSPLVIGLGEG----ENFLASDVPALLPYTRRVIYLEDGEIAVLTRD- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 239 GLAIHDLAGQIVERPRRRVEWSPVAVEKQGFSHFMAKEIFEQPQAIRATTSGRLPRAGEDDLGrgepSFPELAELdvpaL 318
Cdd:COG0449 220 GVEIYDLDGEPVEREVKTVDWDAEAAEKGGYPHFMLKEIHEQPEAIRDTLRGRLDEDGRVVLD----ELNLAAED----L 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 319 AARAKVTMLACGTSWHAALAGKYLFEQLARVPVEVDLASEFRYRQPIVRPGDLAVAISQSGETADTRAALMEARRLGATG 398
Cdd:COG0449 292 RNIDRIYIVACGTSYHAGLVGKYLIEELARIPVEVEIASEFRYRDPVVDPGTLVIAISQSGETADTLAALREAKEKGAKV 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 399 LAICNVVDSSIAREADRVLYTHAGPEISVASTKAFTTQLAMLTLLAVHLGRRTGALTLERAAGLLDGLRELPVALDAVLG 478
Cdd:COG0449 372 LAICNVVGSTIARESDAVLYTHAGPEIGVASTKAFTTQLAALYLLALYLARARGTLSAEEEAELLEELRKLPEKIEEVLD 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 479 QAAAIEIIARRWRSARDWLYLGRGLAFPVALEGALKLKEISYVHAEGYACGEIKHGPIALVDERVPVVVLALEGPGYHKT 558
Cdd:COG0449 452 LEEQIEELAEKYADARNALFLGRGINYPVALEGALKLKEISYIHAEGYAAGELKHGPIALIDEGMPVVAIAPQDELYEKT 531
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 770218757 559 LASLEEVRARGGKIIALASAGDRRIGDLADDVILVPQVDPYLQPILASVPLQLLAYHLARLEGRDVDQPRNLAKSVTVE 637
Cdd:COG0449 532 LSNIQEVKARGGKVIAIADEGDEEVEELADDVIEVPEVDELLAPILAVVPLQLLAYHVAVLRGTDVDQPRNLAKSVTVE 610
|
|
| PRK00331 |
PRK00331 |
isomerizing glutamine--fructose-6-phosphate transaminase; |
1-637 |
0e+00 |
|
isomerizing glutamine--fructose-6-phosphate transaminase;
Pssm-ID: 234729 [Multi-domain] Cd Length: 604 Bit Score: 907.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 1 MCGIIAYMGAREAAPILVAGLRRLEYRGYDSAGIAVLDErrpGGIQRVRAAGKIAALADKLGVEEPTGRAGIGHTRWATH 80
Cdd:PRK00331 1 MCGIVGYVGQRNAAEILLEGLKRLEYRGYDSAGIAVLDD---GGLEVRKAVGKVANLEAKLEEEPLPGTTGIGHTRWATH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 81 GRPCERNAHPHR--GGSVCVVHNGIIENHAELRARLEEEeGRRLTSDTDTEVIAHLVDSHYGRlraaalaqaggeGARLV 158
Cdd:PRK00331 78 GKPTERNAHPHTdcSGRIAVVHNGIIENYAELKEELLAK-GHVFKSETDTEVIAHLIEEELKE------------GGDLL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 159 AAVQASLAELRGAYALALIHDDHPGTIVGARSASPLIVGVGEGgeaaELFLASDVAAILEHTRTVLDLEDGDVVHLDADa 238
Cdd:PRK00331 145 EAVRKALKRLEGAYALAVIDKDEPDTIVAARNGSPLVIGLGEG----ENFLASDALALLPYTRRVIYLEDGEIAVLTRD- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 239 GLAIHDLAGQIVERPRRRVEWSPVAVEKQGFSHFMAKEIFEQPQAIRATTSGRLPRAGEDDLGRGEpsfpeLAELDvpal 318
Cdd:PRK00331 220 GVEIFDFDGNPVEREVYTVDWDASAAEKGGYRHFMLKEIYEQPEAIRDTLEGRLDELGEGELADED-----LKKID---- 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 319 aaraKVTMLACGTSWHAALAGKYLFEQLARVPVEVDLASEFRYRQPIVRPGDLAVAISQSGETADTRAALMEARRLGATG 398
Cdd:PRK00331 291 ----RIYIVACGTSYHAGLVAKYLIESLAGIPVEVEIASEFRYRDPVLSPKTLVIAISQSGETADTLAALRLAKELGAKT 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 399 LAICNVVDSSIAREADRVLYTHAGPEISVASTKAFTTQLAMLTLLAVHLGRRTGALTLERAAGLLDGLRELPVALDAVLG 478
Cdd:PRK00331 367 LAICNVPGSTIARESDAVLYTHAGPEIGVASTKAFTAQLAVLYLLALALAKARGTLSAEEEADLVHELRELPALIEQVLD 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 479 QAAAIEIIARRWRSARDWLYLGRGLAFPVALEGALKLKEISYVHAEGYACGEIKHGPIALVDERVPVVVLALEGPGYHKT 558
Cdd:PRK00331 447 LKEQIEELAEDFADARNALFLGRGVDYPVALEGALKLKEISYIHAEGYAAGELKHGPIALIDEGMPVVAIAPNDELYEKT 526
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 770218757 559 LASLEEVRARGGKIIALASAGDrRIGDLADDVILVPQVDPYLQPILASVPLQLLAYHLARLEGRDVDQPRNLAKSVTVE 637
Cdd:PRK00331 527 KSNIQEVKARGARVIVIADEGD-EVAEEADDVIEVPEVHELLAPLLYVVPLQLLAYHVALARGTDVDKPRNLAKSVTVE 604
|
|
| glmS |
TIGR01135 |
glucosamine--fructose-6-phosphate aminotransferase (isomerizing); The member from ... |
2-637 |
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: 811.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 2 CGIIAYMGAREAAPILVAGLRRLEYRGYDSAGIAVLDErrpGGIQRVRAAGKIAALADKLGVEEPTGRAGIGHTRWATHG 81
Cdd:TIGR01135 1 CGIVGYIGQRDAVPILLEGLKRLEYRGYDSAGIAVVDE---GKLFVRKAVGKVAELANKLGEKPLPGGVGIGHTRWATHG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 82 RPCERNAHPHR--GGSVCVVHNGIIENHAELRARLEEEeGRRLTSDTDTEVIAHLVDSHYGRlraaalaqaggeGARLVA 159
Cdd:TIGR01135 78 KPTDENAHPHTdeGGRIAVVHNGIIENYAELREELEAR-GHVFSSDTDTEVIAHLIEEELRE------------GGDLLE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 160 AVQASLAELRGAYALALIHDDHPGTIVGARSASPLIVGVGEGgeaaELFLASDVAAILEHTRTVLDLEDGDVVHLDADaG 239
Cdd:TIGR01135 145 AVQKALKQLRGAYALAVLHADHPETLVAARSGSPLIVGLGDG----ENFVASDVTALLPYTRRVIYLEDGDIAILTKD-G 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 240 LAIHDLAGQIVERPRRRVEWSPVAVEKQGFSHFMAKEIFEQPQAIRATTSGRLprageddlgRGEPSFPElaELDVPALA 319
Cdd:TIGR01135 220 VEIYNFEGAPVQREVRVIDWDLDAAEKGGYRHFMLKEIYEQPRALRDTLEGRI---------EENGGVFE--ELGAEELL 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 320 ARAK-VTMLACGTSWHAALAGKYLFEQLARVPVEVDLASEFRYRQPIVRPGDLAVAISQSGETADTRAALMEARRLGATG 398
Cdd:TIGR01135 289 KNIDrIQIVACGTSYHAGLVAKYLIERLAGIPVEVEIASEFRYRKPVVDKDTLVIAISQSGETADTLEALRLAKELGAKT 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 399 LAICNVVDSSIAREADRVLYTHAGPEISVASTKAFTTQLAMLTLLAVHLGRRTGALTLERAAGLLDGLRELPVALDAVLG 478
Cdd:TIGR01135 369 LGICNVPGSTLVREADHTLYTRAGPEIGVASTKAFTTQLTVLYLLALALAKARGTLSAEEEAELVDALRRLPDLVEQVLL 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 479 QAAAIEIIARRWRSARDWLYLGRGLAFPVALEGALKLKEISYVHAEGYACGEIKHGPIALVDERVPVVVLALEGPGYHKT 558
Cdd:TIGR01135 449 ADESIAELAERYADKRNFLFLGRGLGYPIALEGALKLKEISYIHAEGYPAGELKHGPIALIDEGLPVVAIAPKDSLLEKT 528
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 770218757 559 LASLEEVRARGGKIIALASAGDRRIGDLADDVILVPQVDPYLQPILASVPLQLLAYHLARLEGRDVDQPRNLAKSVTVE 637
Cdd:TIGR01135 529 KSNVEEVKARGARVIVFAPEDDETIASVADDVIKLPEVEELLAPIVYTIPLQLLAYHIALAKGTDVDKPRNLAKSVTVE 607
|
|
| PLN02981 |
PLN02981 |
glucosamine:fructose-6-phosphate aminotransferase |
1-637 |
1.09e-163 |
|
glucosamine:fructose-6-phosphate aminotransferase
Pssm-ID: 215531 [Multi-domain] Cd Length: 680 Bit Score: 484.64 E-value: 1.09e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 1 MCGIIAYMG------AREAAPILVAGLRRLEYRGYDSAGIAVLDERRPGGIQRV--RAAGKIAAL---------ADKLGV 63
Cdd:PLN02981 1 MCGIFAYLNynvpreRRFILEVLFNGLRRLEYRGYDSAGIAIDNDPSLESSSPLvfREEGKIESLvrsvyeevaETDLNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 64 EEP-TGRAGIGHTRWATHGRPCERNAHPH---RGGSVCVVHNGIIENHAELRARLEEEeGRRLTSDTDTEVIAHLVDSHY 139
Cdd:PLN02981 81 DLVfENHAGIAHTRWATHGPPAPRNSHPQssgPGNEFLVVHNGIITNYEVLKETLLRH-GFTFESDTDTEVIPKLAKFVF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 140 GRLraaALAQAGGEGARLVAAVqasLAELRGAYALALIHDDHPGTIVGARSASPLIVGVGEGGEA--------------- 204
Cdd:PLN02981 160 DKL---NEEEGDVTFSQVVMEV---MRQLEGAYALIFKSPHYPNELVACKRGSPLLLGVKELPEEknssavftsegfltk 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 205 -----AELFLASDVAAILEHTRTVLDLEDGDVVHLdADAGLAIHDLAGqivERPRRRVEWS-PVAVE------------- 265
Cdd:PLN02981 234 nrdkpKEFFLASDASAVVEHTKRVLVIEDNEVVHL-KDGGVGIYKFEN---EKGRGGGGLSrPASVEralstlemeveqi 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 266 -KQGFSHFMAKEIFEQPQAIRATTSGRLPRAGEddlGRGEPSFpeLAEL-DVPALAARAK-VTMLACGTSWHAALAGKYL 342
Cdd:PLN02981 310 mKGNYDHYMQKEIHEQPESLTTTMRGRLIRGGS---GKAKRVL--LGGLkDHLKTIRRSRrIVFIGCGTSYNAALAARPI 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 343 FEQLARVPVEVDLASEFRYRQ-PIVRPgDLAVAISQSGETADTRAALMEARRLGATGLAICNVVDSSIAREADRVLYTHA 421
Cdd:PLN02981 385 LEELSGVPVTMELASDLLDRQgPIYRE-DTAVFVSQSGETADTLRALEYAKENGALCVGITNTVGSAISRGTHCGVHINA 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 422 GPEISVASTKAFTTQLAMLTLLAVHLGRRTGALTLERAAgLLDGLRELPVALDAVLGQAAAIEIIARRWRSARDWLYLGR 501
Cdd:PLN02981 464 GAEIGVASTKAYTSQIVAMTMLALALGEDSISSRSRREA-IIDGLFDLPNKVREVLKLDQEMKELAELLIDEQSLLVFGR 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 502 GLAFPVALEGALKLKEISYVHAEGYACGEIKHGPIALVDERVPVVVLALEGPGYHKTLASLEEVRARGGKIIALASAGDR 581
Cdd:PLN02981 543 GYNYATALEGALKVKEVALMHSEGILAGEMKHGPLALVDETLPIIVIATRDACFSKQQSVIQQLRARKGRLIVICSKGDA 622
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 770218757 582 RIGDLADD--VILVPQVDPYLQPILASVPLQLLAYHLARLEGRDVDQPRNLAKSVTVE 637
Cdd:PLN02981 623 SSVCPSGGcrVIEVPQVEDCLQPVINIVPLQLLAYHLTVLRGHNVDQPRNLAKSVTTQ 680
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
1-636 |
3.72e-155 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 461.03 E-value: 3.72e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 1 MCGIIAYMGAREAAPILVAGLRRLEYRGYDSAGIAVLDerRPGGIQRVRAAGK------IAALADKLGVEEPTGRAGIGH 74
Cdd:PTZ00295 24 CCGIVGYLGNEDASKILLEGIEILQNRGYDSCGISTIS--SGGELKTTKYASDgttsdsIEILKEKLLDSHKNSTIGIAH 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 75 TRWATHGRPCERNAHPH--RGGSVCVVHNGIIENHAELRARLEEEeGRRLTSDTDTEVIAHLVDSHYgrlraaalaqagG 152
Cdd:PTZ00295 102 TRWATHGGKTDENAHPHcdYKKRIALVHNGTIENYVELKSELIAK-GIKFRSETDSEVIANLIGLEL------------D 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 153 EGARLVAAVQASLAELRGAYALALIHDDHPGTIVGARSASPLIVGVGEGGeaaeLFLASDVAAILEHTRTVLDLEDGDVV 232
Cdd:PTZ00295 169 QGEDFQEAVKSAISRLQGTWGLCIIHKDNPDSLIVARNGSPLLVGIGDDS----IYVASEPSAFAKYTNEYISLKDGEIA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 233 HLDADAglaIHDLAGQI-VER-PRRRVEWSPvavekQGFSHFMAKEIFEQPQAIRATTS--GRLprAGEDD---LGRGEP 305
Cdd:PTZ00295 245 ELSLEN---VNDLYTQRrVEKiPEEVIEKSP-----EPYPHWTLKEIFEQPIALSRALNngGRL--SGYNNrvkLGGLDQ 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 306 SFPELAELDvpalaaraKVTMLACGTSWHAALAGKYLFEQLARV-PVEVDLASEF-RYRQPivRPGDLAVAISQSGETAD 383
Cdd:PTZ00295 315 YLEELLNIK--------NLILVGCGTSYYAALFAASIMQKLKCFnTVQVIDASELtLYRLP--DEDAGVIFISQSGETLD 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 384 TRAALMEARRLGATGLAICNVVDSSIAREADRVLYTHAGPEISVASTKAFTTQLAMLTLLAVHLGRRTGALTLE-RAAGL 462
Cdd:PTZ00295 385 VVRALNLADELNLPKISVVNTVGSLIARSTDCGVYLNAGREVAVASTKAFTSQVTVLSLIALWFAQNKEYSCSNyKCSSL 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 463 LDGLRELPVALDAVLGQAAAI-EIIARRWRSARDWLYLGRGLAFPVALEGALKLKEISYVHAEGYACGEIKHGPIALVDE 541
Cdd:PTZ00295 465 INSLHRLPTYIGMTLKSCEEQcKRIAEKLKNAKSMFILGKGLGYPIALEGALKIKEITYIHAEGFSGGALKHGPFALIDK 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 542 R--VPVVVLALEGPGYHKTLASLEEVRARGGKIIALASAGDrRIGDLADDVILVPQVDPyLQPILASVPLQLLAYHLARL 619
Cdd:PTZ00295 545 EknTPVILIILDDEHKELMINAAEQVKARGAYIIVITDDED-LVKDFADEIILIPSNGP-LTALLAVIPLQLLAYEIAIL 622
|
650
....*....|....*..
gi 770218757 620 EGRDVDQPRNLAKSVTV 636
Cdd:PTZ00295 623 RGINPDKPRGLAKTVTV 639
|
|
| PTZ00394 |
PTZ00394 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
1-637 |
2.23e-150 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 173585 [Multi-domain] Cd Length: 670 Bit Score: 450.10 E-value: 2.23e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 1 MCGIIAYMG------AREAAPILVAGLRRLEYRGYDSAGIAV---LDERRPGGIQR---------VRAAGKIAALADKLG 62
Cdd:PTZ00394 1 MCGIFGYANhnvprtVEQILNVLLDGIQKVEYRGYDSAGLAIdanIGSEKEDGTAAsaptprpcvVRSVGNISQLREKVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 63 VEEPTG-----------RAGIGHTRWATHGRPCERNAHPHRG--GSVCVVHNGIIENHAELRARLEEEeGRRLTSDTDTE 129
Cdd:PTZ00394 81 SEAVAAtlppmdattshHVGIAHTRWATHGGVCERNCHPQQSnnGEFTIVHNGIVTNYMTLKELLKEE-GYHFSSDTDTE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 130 VIAHLVDSHYGRlraaalaqagGEGARLVAAVQASLAELRGAYALALIHDDHPGTIVGARSASPLIVGVGEGGE------ 203
Cdd:PTZ00394 160 VISVLSEYLYTR----------KGIHNFADLALEVSRMVEGSYALLVKSVYFPGQLAASRKGSPLMVGIRRTDDrgcvmk 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 204 -----------AAELFLASDVAAILEHTRTVLDLEDGDVVHLdADAGLAIHDLAGQ---IVERPRRRVEWSPVAVEKQGF 269
Cdd:PTZ00394 230 lqtydltdlsgPLEVFFSSDVNSFAEYTREVVFLEDGDIAHY-CDGALRFYNAAERqrsIVKREVQHLDAKPEGLSKGNY 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 270 SHFMAKEIFEQPQAIRATTSGRLpragedDLGRGEPSFPELAELDVPALAARAKVTMLACGTSWHAALAGKYLFEQLARV 349
Cdd:PTZ00394 309 PHFMLKEIYEQPESVISSMHGRI------DFSSGTVQLSGFTQQSIRAILTSRRILFIACGTSLNSCLAVRPLFEELVPL 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 350 PVEVDLASEFRYRQPIVRPGDLAVAISQSGETADTRAALMEARRLGATGLAICNVVDSSIAREADRVLYTHAGPEISVAS 429
Cdd:PTZ00394 383 PISVENASDFLDRRPRIQRDDVCFFVSQSGETADTLMALQLCKEAGAMCVGITNVVGSSISRLTHYAIHLNAGVEVGVAS 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 430 TKAFTTQLAMLTLLAVHLGRRTGALTlERAAGLLDGLRELPVALDAVLG-QAAAIEIIARRWRSARDWLYLGRGLAFPVA 508
Cdd:PTZ00394 463 TKAYTSQVVVLTLVALLLSSDSVRLQ-ERRNEIIRGLAELPAAISECLKiTHDPVKALAARLKESSSILVLGRGYDLATA 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 509 LEGALKLKEISYVHAEGYACGEIKHGPIALVDERVPVVVLALEGPGYHKTLASLEEVRARGGKIIALASAGDRRIGDLAD 588
Cdd:PTZ00394 542 MEAALKVKELSYVHTEGIHSGELKHGPLALIDETSPVLAMCTHDKHFGLSKSAVQQVKARGGAVVVFATEVDAELKAAAS 621
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 770218757 589 DVILVPQVDPYLQPILASVPLQLLAYHLARLEGRDVDQPRNLAKSVTVE 637
Cdd:PTZ00394 622 EIVLVPKTVDCLQCVVNVIPFQLLAYYMALLRGNNVDCPRNLAKSVTVQ 670
|
|
| GFAT |
cd00714 |
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ... |
2-234 |
2.67e-103 |
|
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: 312.46 E-value: 2.67e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 2 CGIIAYMGAREAAPILVAGLRRLEYRGYDSAGIAVLDerrPGGIQRVRAAGKIAALADKLGVEEPTGRAGIGHTRWATHG 81
Cdd:cd00714 1 CGIVGYIGKREAVDILLEGLKRLEYRGYDSAGIAVIG---DGSLEVVKAVGKVANLEEKLAEKPLSGHVGIGHTRWATHG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 82 RPCERNAHPHR--GGSVCVVHNGIIENHaELRARLEEEEGRRLTSDTDTEVIAHLVDSHYgrlraaalaqagGEGARLVA 159
Cdd:cd00714 78 EPTDVNAHPHRscDGEIAVVHNGIIENY-AELKEELEAKGYKFESETDTEVIAHLIEYYY------------DGGLDLLE 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 770218757 160 AVQASLAELRGAYALALIHDDHPGTIVGARSASPLIVGVGEGgeaaELFLASDVAAILEHTRTVLDLEDGDVVHL 234
Cdd:cd00714 145 AVKKALKRLEGAYALAVISKDEPDEIVAARNGSPLVIGIGDG----ENFVASDAPALLEHTRRVIYLEDGDIAVI 215
|
|
| AgaS |
COG2222 |
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ... |
274-637 |
4.73e-77 |
|
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: 248.66 E-value: 4.73e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 274 AKEIFEQPQAIRATtsgrlprageddLGRGEPSFPELaeLDVPALAARAKVTMLACGTSWHAALAGKYLFEQLARVPVEV 353
Cdd:COG2222 1 AREIAQQPEAWRRA------------LAALAAAIAAL--LARLRAKPPRRVVLVGAGSSDHAAQAAAYLLERLLGIPVAA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 354 DLASEF-RYRQPIVRPGDLAVAISQSGETADTRAALMEARRLGATGLAICNVVDSSIAREADRVLYTHAGPEISVASTKA 432
Cdd:COG2222 67 LAPSELvVYPAYLKLEGTLVVAISRSGNSPEVVAALELAKARGARTLAITNNPDSPLAEAADRVLPLPAGPEKSVAATKS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 433 FTTQLAMLTLLAVHLGrrtgaltleRAAGLLDGLRELPVALDAVLGQAAAiEIIARRWRSARDWLYLGRGLAFPVALEGA 512
Cdd:COG2222 147 FTTMLLALLALLAAWG---------GDDALLAALDALPAALEAALAADWP-AAALAALADAERVVFLGRGPLYGLAREAA 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 513 LKLKEISYVHAEGYACGEIKHGPIALVDERVPVVVLALEGPGYHKTLASLEEVRARGGKIIALASAGDRRIgdladDVIL 592
Cdd:COG2222 217 LKLKELSAGHAEAYSAAEFRHGPKSLVDPGTLVVVLASEDPTRELDLDLAAELRALGARVVAIGAEDDAAI-----TLPA 291
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 770218757 593 VPQVDPYLQPILASVPLQLLAYHLARLEGRDVDQPRNLAKSVTVE 637
Cdd:COG2222 292 IPDLHDALDPLLLLVVAQRLALALALARGLDPDTPRHLNKVVKTV 336
|
|
| SIS_GlmS_GlmD_1 |
cd05008 |
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
323-448 |
1.51e-61 |
|
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: 200.42 E-value: 1.51e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 323 KVTMLACGTSWHAALAGKYLFEQLARVPVEVDLASEFRYRQPIVRPGDLAVAISQSGETADTRAALMEARRLGATGLAIC 402
Cdd:cd05008 1 RILIVGCGTSYHAALVAKYLLERLAGIPVEVEAASEFRYRRPLLDEDTLVIAISQSGETADTLAALRLAKEKGAKTVAIT 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 770218757 403 NVVDSSIAREADRVLYTHAGPEISVASTKAFTTQLAMLTLLAVHLG 448
Cdd:cd05008 81 NVVGSTLAREADYVLYLRAGPEISVAATKAFTSQLLALLLLALALA 126
|
|
| SIS_GlmS_GlmD_2 |
cd05009 |
SIS (Sugar ISomerase) domain repeat 2 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
482-635 |
1.34e-60 |
|
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: 199.03 E-value: 1.34e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 482 AIEIIARRWRSARDWLYLGRGLAFPVALEGALKLKEISYVHAEGYACGEIKHGPIALVDERVPVVVLALEGPGYHKTLAS 561
Cdd:cd05009 2 DIKELAEKLKEAKSFYVLGRGPNYGTALEGALKLKETSYIHAEAYSAGEFKHGPIALVDEGTPVIFLAPEDRLEEKLESL 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 770218757 562 LEEVRARGGKIIALASAGDRRigDLADDVILVPQVDPYLQPILASVPLQLLAYHLARLEGRDVDQPRNLAKSVT 635
Cdd:cd05009 82 IKEVKARGAKVIVITDDGDAK--DLADVVIRVPATVEELSPLLYIVPLQLLAYHLAVARGIDPDKPRNLAKSVT 153
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
2-232 |
7.98e-52 |
|
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: 178.03 E-value: 7.98e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 2 CGIIAYMGAREAAPILV----AGLRRLEYRGYDSAGIAVLDerrPGGIQRVRAAGKIAALADKLGVEEPTGRAGIGHTRW 77
Cdd:cd00352 1 CGIFGIVGADGAASLLLllllRGLAALEHRGPDGAGIAVYD---GDGLFVEKRAGPVSDVALDLLDEPLKSGVALGHVRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 78 ATHGRPCERNAHPHR--GGSVCVVHNGIIENHaELRARLEEEEGRRLTSDTDTEVIAHLVDSHYGRlraaalaqaggegA 155
Cdd:cd00352 78 ATNGLPSEANAQPFRseDGRIALVHNGEIYNY-RELREELEARGYRFEGESDSEVILHLLERLGRE-------------G 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 156 RLVAAVQASLAELRGAYALALIhDDHPGTIVGARSA---SPLIVGVGEGGeaaELFLASDVAAILEHT-RTVLDLEDGDV 231
Cdd:cd00352 144 GLFEAVEDALKRLDGPFAFALW-DGKPDRLFAARDRfgiRPLYYGITKDG---GLVFASEPKALLALPfKGVRRLPPGEL 219
|
.
gi 770218757 232 V 232
Cdd:cd00352 220 L 220
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
323-445 |
4.10e-33 |
|
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars. Presumably the SIS domains bind to the end-product of the pathway.
Pssm-ID: 426230 [Multi-domain] Cd Length: 131 Bit Score: 123.56 E-value: 4.10e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 323 KVTMLACGTSWHAALAGKYLFEQLARVPVEVDLASEFRYRQ-PIVRPGDLAVAISQSGETADTRAALMEARRLGATGLAI 401
Cdd:pfam01380 7 RIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGVlALVDEDDLVIAISYSGETKDLLAAAELAKARGAKIIAI 86
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 770218757 402 CNVVDSSIAREADRVLYTHAGPEISVASTKAFTTQLAMLTLLAV 445
Cdd:pfam01380 87 TDSPGSPLAREADHVLYINAGPETGVASTKSITAQLAALDALAV 130
|
|
| PurF |
COG0034 |
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ... |
1-256 |
1.34e-26 |
|
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: 113.19 E-value: 1.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 1 MCGIIAYMGAREAAPILVAGLRRLEYRGYDSAGIAVLDERRpggIQRVRAAGKIAALADKLGVEEPTGRAGIGHTRWATH 80
Cdd:COG0034 7 ECGVFGIYGHEDVAQLTYYGLYALQHRGQESAGIATSDGGR---FHLHKGMGLVSDVFDEEDLERLKGNIAIGHVRYSTT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 81 GRPCERNAHP----HRGGSVCVVHNGIIENHaELRARLEEEEGRRLTSDTDTEVIAHLVdSHYGRlraaalaqaggeGAR 156
Cdd:COG0034 84 GSSSLENAQPfyvnSPFGSIALAHNGNLTNA-EELREELEEEGAIFQTTSDTEVILHLI-ARELT------------KED 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 157 LVAAVQASLAELRGAYALALIHDDhpgTIVGARSAS---PLIVGVGEGGeaaeLFLASDVAA--ILEHTRtVLDLEDGDV 231
Cdd:COG0034 150 LEEAIKEALRRVKGAYSLVILTGD---GLIAARDPNgirPLVLGKLEDG----YVVASESCAldILGAEF-VRDVEPGEI 221
|
250 260
....*....|....*....|....*
gi 770218757 232 VHLDADaGLAIHdlagQIVERPRRR 256
Cdd:COG0034 222 VVIDED-GLRSR----QFAEKPRPA 241
|
|
| GPATase_N |
cd00715 |
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ... |
2-256 |
5.28e-23 |
|
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: 98.69 E-value: 5.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 2 CGIIAYMGAREAAPILVAGLRRLEYRGYDSAGIAVLDERRpggIQRVRAAGKIAALADKLGVEEPTGRAGIGHTRWATHG 81
Cdd:cd00715 1 CGVFGIYGAEDAARLTYLGLYALQHRGQESAGIATSDGKR---FHTHKGMGLVSDVFDEEKLRRLPGNIAIGHVRYSTAG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 82 RPCERNAHP----HRGGSVCVVHNGIIENhAELRARLEEEEGRRLTSDTDTEVIAHLVDSHYGRlraaalaqaggegARL 157
Cdd:cd00715 78 SSSLENAQPfvvnSPLGGIALAHNGNLVN-AKELREELEEEGRIFQTTSDSEVILHLIARSLAK-------------DDL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 158 VAAVQASLAELRGAYALALIHDDhpgTIVGARSAS---PLIVGVGEGGeaaELFLASDVAAIL----EHTRtvlDLEDGD 230
Cdd:cd00715 144 FEAIIDALERVKGAYSLVIMTAD---GLIAVRDPHgirPLVLGKLEGD---GYVVASESCALDiigaEFVR---DVEPGE 214
|
250 260
....*....|....*....|....*.
gi 770218757 231 VVHLDADAGLAIhdlagQIVERPRRR 256
Cdd:cd00715 215 IVVIDDDGLESS-----QRAPKPKPA 235
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
491-617 |
8.64e-21 |
|
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: 88.51 E-value: 8.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 491 RSARDWLYLGRGLAFPVALEGALKLKEISYVHAEGYACGEIKHGPIALVDERVPVVVLALegPGY-HKTLASLEEVRARG 569
Cdd:pfam01380 3 AKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGVLALVDEDDLVIAISY--SGEtKDLLAAAELAKARG 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 770218757 570 GKIIALASAGDRRIGDLADDVILVPQVDPYLQPILASVPLQLLAYHLA 617
Cdd:pfam01380 81 AKIIAITDSPGSPLAREADHVLYINAGPETGVASTKSITAQLAALDAL 128
|
|
| PLN02440 |
PLN02440 |
amidophosphoribosyltransferase |
1-253 |
1.89e-18 |
|
amidophosphoribosyltransferase
Pssm-ID: 215241 [Multi-domain] Cd Length: 479 Bit Score: 88.58 E-value: 1.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 1 MCGIIAYMGAREAAPILVAGLRRLEYRGYDSAGIAVLDERRpggIQRVRAAGKIAALADKLGVEEPTGRAGIGHTRWATH 80
Cdd:PLN02440 1 ECGVVGIFGDPEASRLCYLGLHALQHRGQEGAGIVTVDGNR---LQSITGNGLVSDVFDESKLDQLPGDIAIGHVRYSTA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 81 GRPCERNAHP----HRGGSVCVVHNGIIENHaELRARLEEEEGRRLTSDTDTEVIAHLVDSHYGRLraaalaqaggegar 156
Cdd:PLN02440 78 GASSLKNVQPfvanYRFGSIGVAHNGNLVNY-EELRAKLEENGSIFNTSSDTEVLLHLIAISKARP-------------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 157 LVAAVQASLAELRGAYA-LALIHDdhpgTIVGARSAS---PLIVGVGEGGEAAelfLASDVAAI--LEHTRtVLDLEDGD 230
Cdd:PLN02440 143 FFSRIVDACEKLKGAYSmVFLTED----KLVAVRDPHgfrPLVMGRRSNGAVV---FASETCALdlIGATY-EREVNPGE 214
|
250 260
....*....|....*....|...
gi 770218757 231 VVHLDADAGLAIHDLAGQIVERP 253
Cdd:PLN02440 215 VIVVDKDKGVSSQCLMPHPEPKP 237
|
|
| GlxB |
cd01907 |
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ... |
2-216 |
6.99e-17 |
|
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: 80.78 E-value: 6.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 2 CGIIAYM---GAREAAPILVAGLRRLEYRG-YDSAGIAVLderrpgGIQRVRA------------AGKIAALADKLGVEE 65
Cdd:cd01907 1 CGIFGIMskdGEPFVGALLVEMLDAMQERGpGDGAGFALY------GDPDAFVyssgkdmevfkgVGYPEDIARRYDLEE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 66 PTGRAGIGHTRWATHGRPCERNAHPHRGGSVCVVHNGIIENHaELRARLEEEEGRRLTSDTDTEVIAHLVDSHYGRLraA 145
Cdd:cd01907 75 YKGYHWIAHTRQPTNSAVWWYGAHPFSIGDIAVVHNGEISNY-GSNREYLERFGYKFETETDTEVIAYYLDLLLRKG--G 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 146 ALAQAGGEGARLVAAVQASLAELRGAYALALIhdDHPGTIVGARSAS-----------PLIVGVGEGgeaaELFLASDVA 214
Cdd:cd01907 152 LPLEYYKHIIRMPEEERELLLALRLTYRLADL--DGPFTIIVGTPDGfivirdriklrPAVVAETDD----YVAIASEEC 225
|
..
gi 770218757 215 AI 216
Cdd:cd01907 226 AI 227
|
|
| PRK05793 |
PRK05793 |
amidophosphoribosyltransferase; Provisional |
2-237 |
1.10e-16 |
|
amidophosphoribosyltransferase; Provisional
Pssm-ID: 235611 [Multi-domain] Cd Length: 469 Bit Score: 83.16 E-value: 1.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 2 CGI--IAYMGAREAAPILVAGLRRLEYRGYDSAGIAVLDERRpggIQRVRAAGKIAALADKLGVEEPTGRAGIGHTRWAT 79
Cdd:PRK05793 15 CGVfgVFSKNNIDVASLTYYGLYALQHRGQESAGIAVSDGEK---IKVHKGMGLVSEVFSKEKLKGLKGNSAIGHVRYST 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 80 HGRPCERNAHP----HRGGSVCVVHNGIIENhAELRARLEEEEGRRLTSDTDTEVIAHLV--DSHYGrlraaalaqagge 153
Cdd:PRK05793 92 TGASDLDNAQPlvanYKLGSIAIAHNGNLVN-ADVIRELLEDGGRIFQTSIDSEVILNLIarSAKKG------------- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 154 garLVAAVQASLAELRGAYALALIHDDhpgTIVGAR---SASPLIVGVGEGGeaaeLFLASDVAAI----LEHTRtvlDL 226
Cdd:PRK05793 158 ---LEKALVDAIQAIKGSYALVILTED---KLIGVRdphGIRPLCLGKLGDD----YILSSESCALdtigAEFIR---DV 224
|
250
....*....|.
gi 770218757 227 EDGDVVHLDAD 237
Cdd:PRK05793 225 EPGEIVIIDED 235
|
|
| SIS_RpiR |
cd05013 |
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ... |
328-443 |
1.73e-14 |
|
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: 70.72 E-value: 1.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 328 ACGTSWHAALAGKYLFEQLARVPVEVDLASEFRYRQPIVRPGDLAVAISQSGETADTRAALMEARRLGATGLAICNVVDS 407
Cdd:cd05013 20 GVGSSGLVAEYLAYKLLRLGKPVVLLSDPHLQLMSAANLTPGDVVIAISFSGETKETVEAAEIAKERGAKVIAITDSANS 99
|
90 100 110
....*....|....*....|....*....|....*.
gi 770218757 408 SIAREADRVLYTHAGPEISVAStkAFTTQLAMLTLL 443
Cdd:cd05013 100 PLAKLADIVLLVSSEEGDFRSS--AFSSRIAQLALI 133
|
|
| RpiR |
COG1737 |
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ... |
317-468 |
1.42e-13 |
|
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains [Transcription];
Pssm-ID: 441343 [Multi-domain] Cd Length: 286 Bit Score: 71.50 E-value: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 317 ALAARAKVTMLACGTSWHAALAGKYLFEQLaRVPVEV--DLASEFRYRQPIVRPGDLAVAISQSGETADTRAALMEARRL 394
Cdd:COG1737 130 LLAKARRIYIFGVGASAPVAEDLAYKLLRL-GKNVVLldGDGHLQAESAALLGPGDVVIAISFSGYTRETLEAARLAKER 208
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 770218757 395 GATGLAICNVVDSSIAREADRVLYTHA-GPEISVASTKAFTTQLAMLTLLAVHLGRRTGALT---LERAAGLLDGLRE 468
Cdd:COG1737 209 GAKVIAITDSPLSPLAKLADVVLYVPSeEPTLRSSAFSSRVAQLALIDALAAAVAQRDGDKArerLERTEALLSELRE 286
|
|
| GATase_6 |
pfam13522 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
67-202 |
1.68e-11 |
|
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: 61.94 E-value: 1.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 67 TGRAGIGHTRWATHGRPCERNaHP--HRGGSVCVVHNGIIENHaELRARLEEEEGRRLTSDTDTEVIAHLvDSHYGrlra 144
Cdd:pfam13522 9 EGGVALGHVRLAIVDLPDAGN-QPmlSRDGRLVLVHNGEIYNY-GELREELADLGHAFRSRSDTEVLLAL-YEEWG---- 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 770218757 145 aalaqaggegarlvaavQASLAELRGAYALAlIHDDHPGTIVGARSA---SPLIVGVGEGG 202
Cdd:pfam13522 82 -----------------EDCLERLRGMFAFA-IWDRRRRTLFLARDRlgiKPLYYGILGGG 124
|
|
| frlB |
PRK11382 |
fructoselysine 6-phosphate deglycase; |
323-628 |
3.00e-11 |
|
fructoselysine 6-phosphate deglycase;
Pssm-ID: 183111 [Multi-domain] Cd Length: 340 Bit Score: 65.41 E-value: 3.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 323 KVTMLACGTSWHAALAGKYLFEQLARVPVEVDLASEFRYRQPIVRPGDLAV-AISQSGETADTRAALMEARRLGATGLAI 401
Cdd:PRK11382 46 RIYFVACGSPLNAAQTAKHLADRFSDLQVYAISGWEFCDNTPYRLDDRCAViGVSDYGKTEEVIKALELGRACGALTAAF 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 402 CNVVDSSIAREADRVLYTHAGPEISVASTKAFTTQLAMLTLLAVHlgrrtgaltlERAAGLLDGLRELPVALDAVLgqaa 481
Cdd:PRK11382 126 TKRADSPITSAAEFSIDYQADCIWEIHLLLCYSVVLEMITRLAPN----------AEIGKIKNDLKQLPNALGHLV---- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 482 aieiiaRRWRS--------ARDWLYLGRGLAFPVA----LEGALKLKEISYVHAEGYACGEIKHGPIALVDERVPVVVLA 549
Cdd:PRK11382 192 ------RTWEEkgrqlgelASQWPMIYTVAAGPLRplgyKEGIVTLMEFTWTHGCVIESGEFRHGPLEIVEPGVPFLFLL 265
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 770218757 550 LEGPGYHKTLASLEEVRARGGKIIALasagdrrigDLADdviLVPQVDPYLQPILASVPLQLLAYHLARLEGRDVDQPR 628
Cdd:PRK11382 266 GNDESRHTTERAINFVKQRTDNVIVI---------DYAE---ISQGLHPWLAPFLMFVPMEWLCYYLSIYKDHNPDERR 332
|
|
| SIS_1 |
cd05710 |
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ... |
324-447 |
1.08e-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: 59.13 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 324 VTMLACGTSWHAALAGKYLFEQLARVPVEVDLASEFRYRQPiVRPGDLAVAI--SQSGETADTRAALMEARRLGATGLAI 401
Cdd:cd05710 2 VFFVGCGGSLADMYPAKYFLKKESKLPVFVYNAAEFLHTGP-KRLTEKSVVIlaSHSGNTKETVAAAKFAKEKGATVIGL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 770218757 402 CNVVDSSIAREADRVLYTHAGpeisvasTKAFTTQLAMLTLLAVHL 447
Cdd:cd05710 81 TDDEDSPLAKLADYVIVYGFE-------IDAVEEKYLLLYMLALRL 119
|
|
| murQ |
PRK05441 |
N-acetylmuramic acid-6-phosphate etherase; Reviewed |
366-449 |
7.12e-09 |
|
N-acetylmuramic acid-6-phosphate etherase; Reviewed
Pssm-ID: 235467 [Multi-domain] Cd Length: 299 Bit Score: 57.49 E-value: 7.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 366 VRPGDLAVAISQSGETADTRAALMEARRLGATGLAICNVVDSSIAREADRVLYTHAGPEISVAST--KAFTTQ---LAML 440
Cdd:PRK05441 129 LTAKDVVVGIAASGRTPYVIGALEYARERGALTIGISCNPGSPLSKEADIAIEVVVGPEVLTGSTrmKAGTAQklvLNMI 208
|
90
....*....|
gi 770218757 441 -TLLAVHLGR 449
Cdd:PRK05441 209 sTGVMIRLGK 218
|
|
| SIS_Kpsf |
cd05014 |
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ... |
365-445 |
8.43e-09 |
|
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ISomerase) domains. SIS domains are found in many phosphosugar isomerases and phosphosugar binding proteins. KpsF catalyzes the reversible reaction of ribulose 5-phosphate to arabinose 5-phosphate. This is the second step in the CMP-Kdo biosynthesis pathway.
Pssm-ID: 240145 [Multi-domain] Cd Length: 128 Bit Score: 54.09 E-value: 8.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 365 IVRPGDLAVAISQSGETADTRAALMEARRLGATGLAICNVVDSSIAREADRVLYTHAGPE---ISVASTKAFTTQLAMLT 441
Cdd:cd05014 44 MVTPGDVVIAISNSGETDELLNLLPHLKRRGAPIIAITGNPNSTLAKLSDVVLDLPVEEEacpLGLAPTTSTTAMLALGD 123
|
....
gi 770218757 442 LLAV 445
Cdd:cd05014 124 ALAV 127
|
|
| AsnB |
cd00712 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ... |
2-254 |
1.31e-08 |
|
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: 55.64 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 2 CGIIAYMGAREAAPILVAGLRRLEYRGYDSAGIAVLderrpggiqrvraagkiaaladklgveeptGRAGIGHTRWAThg 81
Cdd:cd00712 4 AGIIGLDGASVDRATLERMLDALAHRGPDGSGIWID------------------------------EGVALGHRRLSI-- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 82 RPCERNAHPHRG--GSVCVVHNGIIENHAELRaRLEEEEGRRLTSDTDTEVIAHLVDsHYGRlraaalaqaggegarlva 159
Cdd:cd00712 52 IDLSGGAQPMVSedGRLVLVFNGEIYNYRELR-AELEALGHRFRTHSDTEVILHLYE-EWGE------------------ 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 160 avqASLAELRGAYALAlIHDDHPGTIVGARSAS---PLIVGVGEGGeaaeLFLASDVAAILEHtrtvldledgDVVHLDA 236
Cdd:cd00712 112 ---DCLERLNGMFAFA-LWDKRKRRLFLARDRFgikPLYYGRDGGG----LAFASELKALLAL----------PGVPREL 173
|
250
....*....|....*...
gi 770218757 237 DAGLAIHDLAGQIVERPR 254
Cdd:cd00712 174 DEAALAEYLAFQYVPAPR 191
|
|
| SIS_Etherase |
cd05007 |
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ... |
368-449 |
2.02e-08 |
|
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ISomerase) domain. The SIS domain is found in many phosphosugar isomerases and phosphosugar binding proteins. The bacterial cell wall sugar N-acetylmuramic acid carries a unique D-lactyl ether substituent at the C3 position. The etherase catalyzes the cleavage of the lactyl ether bond of N-acetylmuramic acid 6-phosphate.
Pssm-ID: 240140 [Multi-domain] Cd Length: 257 Bit Score: 55.61 E-value: 2.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 368 PGDLAVAISQSGETADTRAALMEARRLGATGLAICNVVDSSIAREADRVLYTHAGPEISVAST--KAFTTQ---LAML-T 441
Cdd:cd05007 118 ERDVVIGIAASGRTPYVLGALRYARARGALTIGIACNPGSPLLQLADIAIALITGPEVVAGSTrlKAGTAQklaLNMLsT 197
|
....*...
gi 770218757 442 LLAVHLGR 449
Cdd:cd05007 198 AVMIRLGK 205
|
|
| GutQ |
COG0794 |
D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall ... |
365-452 |
6.79e-08 |
|
D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440557 [Multi-domain] Cd Length: 317 Bit Score: 54.60 E-value: 6.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 365 IVRPGDLAVAISQSGETADTRAALMEARRLGATGLAICNVVDSSIAREADRVLYTHAGPE---ISVASTKAFTTQLAMLT 441
Cdd:COG0794 88 MITPGDVVIAISNSGETEELLALLPLLKRLGVPLIAITGNPDSTLARAADVVLDLPVEREacpLNLAPTTSTTATLALGD 167
|
90
....*....|.
gi 770218757 442 LLAVHLGRRTG 452
Cdd:COG0794 168 ALAVALLEARG 178
|
|
| GATase_7 |
pfam13537 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
93-217 |
2.40e-07 |
|
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: 49.82 E-value: 2.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 93 GGSVCVVHNGIIENHaELRARLEEEEGRRLTSDTDTEVIAHLVDSHYGRlraaalaqaggegarlvaavqASLAELRGAY 172
Cdd:pfam13537 21 DGRYVIVFNGEIYNY-RELRAELEAKGYRFRTHSDTEVILHLYEAEWGE---------------------DCVDRLNGMF 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 770218757 173 ALAlIHDDHPGTIVGARSAS---PLIVGVGEGGeaaELFLASDVAAIL 217
Cdd:pfam13537 79 AFA-IWDRRRQRLFLARDRFgikPLYYGRDDGG---RLLFASELKALL 122
|
|
| YafJ |
cd01908 |
Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine ... |
1-237 |
4.58e-07 |
|
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: 51.62 E-value: 4.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 1 MCGIIAYMGA---------REAAPILVAGLRRLEYRGY---DSAGIAVLDERRPG-GIQR-VRAAGKIAALADKlgVEEP 66
Cdd:cd01908 1 MCRLLGYSGApipleplliRPSHSLLVQSGGPREMKGTvhaDGWGIGWYEGKGGRpFRYRsPLPAWSDINLESL--ARPI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 67 TGRAGIGHTRWATHGRPCERNAHPHRGGSVCVVHNGIIENHAELRARLEEEEGRRLTSDTDTEVIAHLVdSHYGRLRaaa 146
Cdd:cd01908 79 KSPLVLAHVRAATVGPVSLENCHPFTRGRWLFAHNGQLDGFRLLRRRLLRLLPRLPVGTTDSELAFALL-LSRLLER--- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 147 LAQAGGEGARLVAAVQASLAELRGAYALALIHDDhPGTIVGARSASPL----IVGVGEGGEAAELFL-----ASDVAAI- 216
Cdd:cd01908 155 DPLDPAELLDAILQTLRELAALAPPGRLNLLLSD-GEYLIATRYASAPslyyLTRRAPFGCARLLFRsvttpNDDGVVVa 233
|
250 260
....*....|....*....|....
gi 770218757 217 ---LEHTRTVLDLEDGDVVHLDAD 237
Cdd:cd01908 234 sepLTDDEGWTEVPPGELVVVSEG 257
|
|
| SIS |
cd04795 |
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
324-402 |
5.32e-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: 47.75 E-value: 5.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 324 VTMLACGTSWHAALAGKYLFEQLARVPVEVDLASEFRYRQPIV--RPGDLAVAISQSGETADTRAALMEARRLGATGLAI 401
Cdd:cd04795 1 IFVIGIGGSGAIAAYFALELLELTGIEVVALIATELEHASLLSllRKGDVVIALSYSGRTEELLAALEIAKELGIPVIAI 80
|
.
gi 770218757 402 C 402
Cdd:cd04795 81 T 81
|
|
| PRK11337 |
PRK11337 |
MurR/RpiR family transcriptional regulator; |
368-421 |
2.26e-06 |
|
MurR/RpiR family transcriptional regulator;
Pssm-ID: 183089 [Multi-domain] Cd Length: 292 Bit Score: 49.76 E-value: 2.26e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 770218757 368 PGDLAVAISQSGETADTRAALMEARRLGATGLAICNVVDSSIAREADRVLYTHA 421
Cdd:PRK11337 187 EGDVVLVVSHSGRTSDVIEAVELAKKNGAKIICITNSYHSPIAKLADYVICSTA 240
|
|
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
1-219 |
2.94e-06 |
|
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: 50.22 E-value: 2.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 1 MCGIIAYMGAREAA--PILVAGLRRLEYRGYDSAGIAVlderrpggiqrvraagkiaaladklgveepTGRAGIGHTR-- 76
Cdd:COG0367 1 MCGIAGIIDFDGGAdrEVLERMLDALAHRGPDGSGIWV------------------------------DGGVALGHRRls 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 77 ---WATHGR-PCERNahphrGGSVCVVHNGIIENHAELRaRLEEEEGRRLTSDTDTEVIAHLVDsHYGRlraaalaqagg 152
Cdd:COG0367 51 iidLSEGGHqPMVSE-----DGRYVLVFNGEIYNYRELR-AELEALGHRFRTHSDTEVILHAYE-EWGE----------- 112
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 153 egarlvaavqASLAELRGAYALAlIHDDHPGTIVGAR---SASPLIVGVGEGGeaaeLFLASDVAAILEH 219
Cdd:COG0367 113 ----------DCLERLNGMFAFA-IWDRRERRLFLARdrfGIKPLYYAEDGGG----LAFASELKALLAH 167
|
|
| YafJ |
COG0121 |
Predicted glutamine amidotransferase YafJ [General function prediction only]; |
2-169 |
3.39e-06 |
|
Predicted glutamine amidotransferase YafJ [General function prediction only];
Pssm-ID: 439891 [Multi-domain] Cd Length: 248 Bit Score: 48.81 E-value: 3.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 2 CGIIAYMGARE--AAPILVAGLRRLEYRGYDSA--------GIAVLDERrpGGIQRVRAAGKIA--ALADKLgVEEPTGR 69
Cdd:COG0121 1 CRLLGYSGNVPtdLEFLLLDPEHSLVRQSGATRegphadgwGIGWYEGD--GEPRLYRDPLPAWsdPNLRLL-ARPIKSR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 70 AGIGHTRWATHGRPCERNAHPHRGGSVCVVHNGIIENHAELRARLEEEEG----RRLTSDTDTEVIAHLVdshYGRLRaa 145
Cdd:COG0121 78 LVIAHVRKATVGPVSLENTHPFRGGRWLFAHNGQLDGFDRLRRRLAEELPdelyFQPVGTTDSELAFALL---LSRLR-- 152
|
170 180
....*....|....*....|....
gi 770218757 146 alaqagGEGARLVAAVQASLAELR 169
Cdd:COG0121 153 ------DGGPDPAEALAEALRELA 170
|
|
| PRK15482 |
PRK15482 |
HTH-type transcriptional regulator MurR; |
335-447 |
4.96e-06 |
|
HTH-type transcriptional regulator MurR;
Pssm-ID: 185379 [Multi-domain] Cd Length: 285 Bit Score: 48.54 E-value: 4.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 335 AALAGKYLFEQLA----RVPVEVDLASEFRYRQPIvRPGDLAVAISQSGETADTRAALMEARRLGATGLAICNVVDSSIA 410
Cdd:PRK15482 146 SALVGRDLSFKLMkigyRVACEADTHVQATVSQAL-KKGDVQIAISYSGSKKEIVLCAEAARKQGATVIAITSLADSPLR 224
|
90 100 110
....*....|....*....|....*....|....*...
gi 770218757 411 READRVLYTHAG-PEISVASTKAFTTQLAMLTLLAVHL 447
Cdd:PRK15482 225 RLAHFTLDTVSGeTEWRSSSMSTRTAQNSVTDLLFVGL 262
|
|
| PRK11557 |
PRK11557 |
MurR/RpiR family transcriptional regulator; |
368-443 |
2.37e-05 |
|
MurR/RpiR family transcriptional regulator;
Pssm-ID: 183195 [Multi-domain] Cd Length: 278 Bit Score: 46.68 E-value: 2.37e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 770218757 368 PGDLAVAISQSGETADTRAALMEARRLGATGLAICNVVDSSIAREADRVLYTHA-GPEISVASTKAFTTQLAMLTLL 443
Cdd:PRK11557 175 PDDLLLAISYSGERRELNLAADEALRVGAKVLAITGFTPNALQQRASHCLYTIAeEQATRSAAISSTHAQGMLTDLL 251
|
|
| SIS_PHI |
cd05005 |
Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) ... |
364-445 |
7.65e-05 |
|
Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) superfamily. In the ribulose monophosphate pathway of formaldehyde fixation, hexulose-6-phosphate synthase catalyzes the condensation of ribulose-5-phosphate with formadelhyde to become hexulose-6-phosphate, which is then isomerized to fructose-6-phosphate by PHI.
Pssm-ID: 240138 [Multi-domain] Cd Length: 179 Bit Score: 43.72 E-value: 7.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 364 PIVRPGDLAVAISQSGETADTRAALMEARRLGATGLAICNVVDSSIAREADRVLYTHAGPEISVASTKAFTT-------Q 436
Cdd:cd05005 71 PAIGPGDLLIAISGSGETSSVVNAAEKAKKAGAKVVLITSNPDSPLAKLADVVVVIPAATKDDHGGEHKSIQplgtlfeQ 150
|
....*....
gi 770218757 437 LAMLTLLAV 445
Cdd:cd05005 151 SALVFLDAV 159
|
|
| PRK12570 |
PRK12570 |
N-acetylmuramic acid-6-phosphate etherase; Reviewed |
370-449 |
9.84e-05 |
|
N-acetylmuramic acid-6-phosphate etherase; Reviewed
Pssm-ID: 237142 [Multi-domain] Cd Length: 296 Bit Score: 44.68 E-value: 9.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 370 DLAVAISQSGETADTRAALMEARRLGATGLAI-CNvVDSSIAREADRVLYTHAGPEISVAST--KAFTTQ---LAMLTLL 443
Cdd:PRK12570 129 DVVVGIAASGRTPYVIGALEYAKQIGATTIALsCN-PDSPIAKIADIAISPVVGPEVLTGSTrlKSGTAQkmvLNMLSTA 207
|
....*..
gi 770218757 444 A-VHLGR 449
Cdd:PRK12570 208 SmIRLGK 214
|
|
| RpiR |
COG1737 |
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ... |
480-626 |
3.31e-03 |
|
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains [Transcription];
Pssm-ID: 441343 [Multi-domain] Cd Length: 286 Bit Score: 39.91 E-value: 3.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 480 AAAIEIIARrwrsARD-WLYlGRGLAFPVALEGALKL----KEISYVHAEGYACGEIkhgpIALVDERVpvVVLALEGPG 554
Cdd:COG1737 125 ERAVDLLAK----ARRiYIF-GVGASAPVAEDLAYKLlrlgKNVVLLDGDGHLQAES----AALLGPGD--VVIAISFSG 193
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 770218757 555 YHK-TLASLEEVRARGGKIIALASAGDRRIGDLADDVILVPQVDPYLQ--PILASVP----LQLLAYHLARLEGRDVDQ 626
Cdd:COG1737 194 YTReTLEAARLAKERGAKVIAITDSPLSPLAKLADVVLYVPSEEPTLRssAFSSRVAqlalIDALAAAVAQRDGDKARE 272
|
|
| SIS |
cd04795 |
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
497-576 |
7.21e-03 |
|
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: 36.20 E-value: 7.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 497 LYLGRGLAFPVALEGALKLKEISYVHAEGYACGEIKHGPIALVDERVPVVVLALEGPGYHKTLASLEEVRARGGKIIALA 576
Cdd:cd04795 2 FVIGIGGSGAIAAYFALELLELTGIEVVALIATELEHASLLSLLRKGDVVIALSYSGRTEELLAALEIAKELGIPVIAIT 81
|
|
| PTZ00077 |
PTZ00077 |
asparagine synthetase-like protein; Provisional |
1-216 |
7.52e-03 |
|
asparagine synthetase-like protein; Provisional
Pssm-ID: 185431 [Multi-domain] Cd Length: 586 Bit Score: 39.31 E-value: 7.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 1 MCGIIAYMGAREAAPILVAGL----RRLEYRGYDSAGIAVLDErrpggiqrvraagkiaaladklgveEPTGRAGIGHTR 76
Cdd:PTZ00077 1 MCGILAIFNSKGERHELRRKAlelsKRLRHRGPDWSGIIVLEN-------------------------SPGTYNILAHER 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770218757 77 WA----THGR-PCERNAHPhrggsVCVVHNGIIENHaELRARLEEEEGRRLTSDTDTEVIAHLVDSHYGRlraaalaqag 151
Cdd:PTZ00077 56 LAivdlSDGKqPLLDDDET-----VALMQNGEIYNH-WEIRPELEKEGYKFSSNSDCEIIGHLYKEYGPK---------- 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 770218757 152 gegarlvaavqASLAELRGAYAlALIHDDHPGTIVGARS---ASPLIVGVGEGGeaaELFLASDVAAI 216
Cdd:PTZ00077 120 -----------DFWNHLDGMFA-TVIYDMKTNTFFAARDhigIIPLYIGYAKDG---SIWFSSELKAL 172
|
|
| |
