|
Name |
Accession |
Description |
Interval |
E-value |
| GlmS |
COG0449 |
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ... |
1-608 |
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: 858.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 1 MCGIVGLTGSvgERIGLVLRRCLERLEYRGYDSAGVAVVNGGVITVRKGRGKISEVDARVNFTGLNGVSGIGHTRWATHG 80
Cdd:COG0449 1 MCGIVGYIGK--RDAAPILLEGLKRLEYRGYDSAGIAVLDDGGLEVRKAVGKLANLEEKLAEEPLSGTIGIGHTRWATHG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 81 KPSDENAHPHTDCSGTVAVVHNGIISNYRELREQLEARGHRFTSDTDTEVIAHLFEDYVKAGLTALEALREVVSRLRGTY 160
Cdd:COG0449 79 APSDENAHPHTSCSGRIAVVHNGIIENYAELREELEAKGHTFKSETDTEVIAHLIEEYLKGGGDLLEAVRKALKRLEGAY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 161 AIALLYVGEPDKVFFARNVSPLIIGLGNGFNFLASDIPAFLEYTNRVITLHDGEYGFITPGSVYVE-RGGEPVDVKarVR 239
Cdd:COG0449 159 ALAVISADEPDRIVAARKGSPLVIGLGEGENFLASDVPALLPYTRRVIYLEDGEIAVLTRDGVEIYdLDGEPVERE--VK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 240 VVNWSPELASKEGYPHFMLKEIHEQPRALRDTWAG-------LDTDQLSKLSDLLLKARRVFITGSGTSYHAGLVFDHLL 312
Cdd:COG0449 237 TVDWDAEAAEKGGYPHFMLKEIHEQPEAIRDTLRGrldedgrVVLDELNLAAEDLRNIDRIYIVACGTSYHAGLVGKYLI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 313 SGLMGLDTHAFNSSEYRRYVKLAGDGDVMVAVSQSGETIDTLMAVRVFRRLGVRVIAVSNVVDSTIPRESDYQLYTRAGP 392
Cdd:COG0449 317 EELARIPVEVEIASEFRYRDPVVDPGTLVIAISQSGETADTLAALREAKEKGAKVLAICNVVGSTIARESDAVLYTHAGP 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 393 EVGVAATKTFTAQLMVLNALAATAALGGGVLGKDEYGLIMGELEHLPDLVNlTITSVEAKARHIASRLASKASAYYLSRG 472
Cdd:COG0449 397 EIGVASTKAFTTQLAALYLLALYLARARGTLSAEEEAELLEELRKLPEKIE-EVLDLEEQIEELAEKYADARNALFLGRG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 473 LGLPIAMEGALKLKEVAYIHAEAYPAGESKHGPIALVEGGFPVLFIATDDEYVDALEGNVMEMNARGALTIGVIPAKHQp 552
Cdd:COG0449 476 INYPVALEGALKLKEISYIHAEGYAAGELKHGPIALIDEGMPVVAIAPQDELYEKTLSNIQEVKARGGKVIAIADEGDE- 554
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 974335136 553 RFGKLLSEVIQTPNVSPgALT-ILQSIPLQLLAYYTAVLRGHDPDKPRNLAKTVTVE 608
Cdd:COG0449 555 EVEELADDVIEVPEVDE-LLApILAVVPLQLLAYHVAVLRGTDVDQPRNLAKSVTVE 610
|
|
| PRK00331 |
PRK00331 |
isomerizing glutamine--fructose-6-phosphate transaminase; |
1-608 |
0e+00 |
|
isomerizing glutamine--fructose-6-phosphate transaminase;
Pssm-ID: 234729 [Multi-domain] Cd Length: 604 Bit Score: 844.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 1 MCGIVGLtgsVGER-IGLVLRRCLERLEYRGYDSAGVAVVNGGVITVRKGRGKISEVDARVNFTGLNGVSGIGHTRWATH 79
Cdd:PRK00331 1 MCGIVGY---VGQRnAAEILLEGLKRLEYRGYDSAGIAVLDDGGLEVRKAVGKVANLEAKLEEEPLPGTTGIGHTRWATH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 80 GKPSDENAHPHTDCSGTVAVVHNGIISNYRELREQLEARGHRFTSDTDTEVIAHLFEDYVKAGLTALEALREVVSRLRGT 159
Cdd:PRK00331 78 GKPTERNAHPHTDCSGRIAVVHNGIIENYAELKEELLAKGHVFKSETDTEVIAHLIEEELKEGGDLLEAVRKALKRLEGA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 160 YAIALLYVGEPDKVFFARNVSPLIIGLGNGFNFLASDIPAFLEYTNRVITLHDGEYGFITPGSVYVE-RGGEPVDvkARV 238
Cdd:PRK00331 158 YALAVIDKDEPDTIVAARNGSPLVIGLGEGENFLASDALALLPYTRRVIYLEDGEIAVLTRDGVEIFdFDGNPVE--REV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 239 RVVNWSPELASKEGYPHFMLKEIHEQPRALRDTWAG--LDTDQLSKLSDLLLKARRVFITGSGTSYHAGLVFDHLLSGLM 316
Cdd:PRK00331 236 YTVDWDASAAEKGGYRHFMLKEIYEQPEAIRDTLEGrlDELGEGELADEDLKKIDRIYIVACGTSYHAGLVAKYLIESLA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 317 GLDTHAFNSSEYRRYVKLAGDGDVMVAVSQSGETIDTLMAVRVFRRLGVRVIAVSNVVDSTIPRESDYQLYTRAGPEVGV 396
Cdd:PRK00331 316 GIPVEVEIASEFRYRDPVLSPKTLVIAISQSGETADTLAALRLAKELGAKTLAICNVPGSTIARESDAVLYTHAGPEIGV 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 397 AATKTFTAQLMVLNALAATAALGGGVLGKDEYGLIMGELEHLPDLVNLTITSVEaKARHIASRLASKASAYYLSRGLGLP 476
Cdd:PRK00331 396 ASTKAFTAQLAVLYLLALALAKARGTLSAEEEADLVHELRELPALIEQVLDLKE-QIEELAEDFADARNALFLGRGVDYP 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 477 IAMEGALKLKEVAYIHAEAYPAGESKHGPIALVEGGFPVLFIATDDEYVDALEGNVMEMNARGALTIGVIPAKHQprFGK 556
Cdd:PRK00331 475 VALEGALKLKEISYIHAEGYAAGELKHGPIALIDEGMPVVAIAPNDELYEKTKSNIQEVKARGARVIVIADEGDE--VAE 552
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 974335136 557 LLSEVIQTPNVSPGALTILQSIPLQLLAYYTAVLRGHDPDKPRNLAKTVTVE 608
Cdd:PRK00331 553 EADDVIEVPEVHELLAPLLYVVPLQLLAYHVALARGTDVDKPRNLAKSVTVE 604
|
|
| glmS |
TIGR01135 |
glucosamine--fructose-6-phosphate aminotransferase (isomerizing); The member from ... |
2-608 |
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: 742.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 2 CGIVGLtgsVGERIGL-VLRRCLERLEYRGYDSAGVAVVNGGVITVRKGRGKISEVDARVNFTGLNGVSGIGHTRWATHG 80
Cdd:TIGR01135 1 CGIVGY---IGQRDAVpILLEGLKRLEYRGYDSAGIAVVDEGKLFVRKAVGKVAELANKLGEKPLPGGVGIGHTRWATHG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 81 KPSDENAHPHTDCSGTVAVVHNGIISNYRELREQLEARGHRFTSDTDTEVIAHLFEDYVKAGLTALEALREVVSRLRGTY 160
Cdd:TIGR01135 78 KPTDENAHPHTDEGGRIAVVHNGIIENYAELREELEARGHVFSSDTDTEVIAHLIEEELREGGDLLEAVQKALKQLRGAY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 161 AIALLYVGEPDKVFFARNVSPLIIGLGNGFNFLASDIPAFLEYTNRVITLHDGEYGFITPGSVYVeRGGEPVDVKARVRV 240
Cdd:TIGR01135 158 ALAVLHADHPETLVAARSGSPLIVGLGDGENFVASDVTALLPYTRRVIYLEDGDIAILTKDGVEI-YNFEGAPVQREVRV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 241 VNWSPELASKEGYPHFMLKEIHEQPRALRDTWAG-LDTDQLSKLSDLLLK----ARRVFITGSGTSYHAGLVFDHLLSGL 315
Cdd:TIGR01135 237 IDWDLDAAEKGGYRHFMLKEIYEQPRALRDTLEGrIEENGGVFEELGAEEllknIDRIQIVACGTSYHAGLVAKYLIERL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 316 MGLDTHAFNSSEYRRYVKLAGDGDVMVAVSQSGETIDTLMAVRVFRRLGVRVIAVSNVVDSTIPRESDYQLYTRAGPEVG 395
Cdd:TIGR01135 317 AGIPVEVEIASEFRYRKPVVDKDTLVIAISQSGETADTLEALRLAKELGAKTLGICNVPGSTLVREADHTLYTRAGPEIG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 396 VAATKTFTAQLMVLNALAATAALGGGVLGKDEYGLIMGELEHLPDLVNlTITSVEAKARHIASRLASKASAYYLSRGLGL 475
Cdd:TIGR01135 397 VASTKAFTTQLTVLYLLALALAKARGTLSAEEEAELVDALRRLPDLVE-QVLLADESIAELAERYADKRNFLFLGRGLGY 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 476 PIAMEGALKLKEVAYIHAEAYPAGESKHGPIALVEGGFPVLFIATDDEYVDALEGNVMEMNARGALTIGVIPAKHQpRFG 555
Cdd:TIGR01135 476 PIALEGALKLKEISYIHAEGYPAGELKHGPIALIDEGLPVVAIAPKDSLLEKTKSNVEEVKARGARVIVFAPEDDE-TIA 554
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 974335136 556 KLLSEVIQTPNVSPGALTILQSIPLQLLAYYTAVLRGHDPDKPRNLAKTVTVE 608
Cdd:TIGR01135 555 SVADDVIKLPEVEELLAPIVYTIPLQLLAYHIALAKGTDVDKPRNLAKSVTVE 607
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
1-607 |
4.12e-156 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 462.57 E-value: 4.12e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 1 MCGIVGLTGSvgERIGLVLRRCLERLEYRGYDSAGVAVVN-GGVITVRKGRGKISEVDA------RVNFTGLNGVSGIGH 73
Cdd:PTZ00295 24 CCGIVGYLGN--EDASKILLEGIEILQNRGYDSCGISTISsGGELKTTKYASDGTTSDSieilkeKLLDSHKNSTIGIAH 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 74 TRWATHGKPSDENAHPHTDCSGTVAVVHNGIISNYRELREQLEARGHRFTSDTDTEVIAHLFEDYVKAGLTALEALREVV 153
Cdd:PTZ00295 102 TRWATHGGKTDENAHPHCDYKKRIALVHNGTIENYVELKSELIAKGIKFRSETDSEVIANLIGLELDQGEDFQEAVKSAI 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 154 SRLRGTYAIALLYVGEPDKVFFARNVSPLIIGLGNGFNFLASDIPAFLEYTNRVITLHDGEYGFITPGSVyverggepVD 233
Cdd:PTZ00295 182 SRLQGTWGLCIIHKDNPDSLIVARNGSPLLVGIGDDSIYVASEPSAFAKYTNEYISLKDGEIAELSLENV--------ND 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 234 VKARVRVVNWSPE--LASKEGYPHFMLKEIHEQPRAL------RDTWAGLDT-------DQLSKLSDLLlkaRRVFITGS 298
Cdd:PTZ00295 254 LYTQRRVEKIPEEviEKSPEPYPHWTLKEIFEQPIALsralnnGGRLSGYNNrvklgglDQYLEELLNI---KNLILVGC 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 299 GTSYHAGLVFDHLLSGLMGLDT-HAFNSSEYRRYVKLAGDGDvMVAVSQSGETIDTLMAVRVFRRLGVRVIAVSNVVDST 377
Cdd:PTZ00295 331 GTSYYAALFAASIMQKLKCFNTvQVIDASELTLYRLPDEDAG-VIFISQSGETLDVVRALNLADELNLPKISVVNTVGSL 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 378 IPRESDYQLYTRAGPEVGVAATKTFTAQLMVLNALAATAALGggvlgKDEYGL------IMGELEHLPDLVNLTITSVEA 451
Cdd:PTZ00295 410 IARSTDCGVYLNAGREVAVASTKAFTSQVTVLSLIALWFAQN-----KEYSCSnykcssLINSLHRLPTYIGMTLKSCEE 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 452 KARHIASRLASKASAYYLSRGLGLPIAMEGALKLKEVAYIHAEAYPAGESKHGPIALVEG--GFPVLFIATDDEYVDALE 529
Cdd:PTZ00295 485 QCKRIAEKLKNAKSMFILGKGLGYPIALEGALKIKEITYIHAEGFSGGALKHGPFALIDKekNTPVILIILDDEHKELMI 564
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 530 GNVMEMNARGALTIgVIP-----AKHqprfgkLLSEVIQTPNVspGALTILQS-IPLQLLAYYTAVLRGHDPDKPRNLAK 603
Cdd:PTZ00295 565 NAAEQVKARGAYII-VITddedlVKD------FADEIILIPSN--GPLTALLAvIPLQLLAYEIAILRGINPDKPRGLAK 635
|
....
gi 974335136 604 TVTV 607
Cdd:PTZ00295 636 TVTV 639
|
|
| PTZ00394 |
PTZ00394 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
1-608 |
8.33e-121 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 173585 [Multi-domain] Cd Length: 670 Bit Score: 372.67 E-value: 8.33e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 1 MCGIVGLTGS----VGERIGLVLRRCLERLEYRGYDSAGVAVVNGGVITVRKGR---------------GKISEVDARVn 61
Cdd:PTZ00394 1 MCGIFGYANHnvprTVEQILNVLLDGIQKVEYRGYDSAGLAIDANIGSEKEDGTaasaptprpcvvrsvGNISQLREKV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 62 FTGLNGVS------------GIGHTRWATHGKPSDENAHPHTDCSGTVAVVHNGIISNYRELREQLEARGHRFTSDTDTE 129
Cdd:PTZ00394 80 FSEAVAATlppmdattshhvGIAHTRWATHGGVCERNCHPQQSNNGEFTIVHNGIVTNYMTLKELLKEEGYHFSSDTDTE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 130 VIAHLFED-YVKAGLTAL-EALREVVSRLRGTYAIALLYVGEPDKVFFARNVSPLIIGLGNGFN---------------- 191
Cdd:PTZ00394 160 VISVLSEYlYTRKGIHNFaDLALEVSRMVEGSYALLVKSVYFPGQLAASRKGSPLMVGIRRTDDrgcvmklqtydltdls 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 192 -----FLASDIPAFLEYTNRVITLHDGEYGFITPGSV--YVERGGEPVDVKARVRVVNWSPELASKEGYPHFMLKEIHEQ 264
Cdd:PTZ00394 240 gplevFFSSDVNSFAEYTREVVFLEDGDIAHYCDGALrfYNAAERQRSIVKREVQHLDAKPEGLSKGNYPHFMLKEIYEQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 265 P----RALRD---------TWAGLDtdqlSKLSDLLLKARRVFITGSGTSYHAGLVFDHLLSGLMGLDTHAFNSSEYRRY 331
Cdd:PTZ00394 320 PesviSSMHGridfssgtvQLSGFT----QQSIRAILTSRRILFIACGTSLNSCLAVRPLFEELVPLPISVENASDFLDR 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 332 VKLAGDGDVMVAVSQSGETIDTLMAVRVFRRLGVRVIAVSNVVDSTIPRESDYQLYTRAGPEVGVAATKTFTAQLMVLNA 411
Cdd:PTZ00394 396 RPRIQRDDVCFFVSQSGETADTLMALQLCKEAGAMCVGITNVVGSSISRLTHYAIHLNAGVEVGVASTKAYTSQVVVLTL 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 412 LAATAALGGGVLGKDEYGLIMGeLEHLPDLVN--LTITSVEAKArhIASRLASKASAYYLSRGLGLPIAMEGALKLKEVA 489
Cdd:PTZ00394 476 VALLLSSDSVRLQERRNEIIRG-LAELPAAISecLKITHDPVKA--LAARLKESSSILVLGRGYDLATAMEAALKVKELS 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 490 YIHAEAYPAGESKHGPIALVEGGFPVLFIATDDEYVDALEGNVMEMNARGALTIgVIPAKHQPRFGKLLSEVIQTPNVSP 569
Cdd:PTZ00394 553 YVHTEGIHSGELKHGPLALIDETSPVLAMCTHDKHFGLSKSAVQQVKARGGAVV-VFATEVDAELKAAASEIVLVPKTVD 631
|
650 660 670
....*....|....*....|....*....|....*....
gi 974335136 570 GALTILQSIPLQLLAYYTAVLRGHDPDKPRNLAKTVTVE 608
Cdd:PTZ00394 632 CLQCVVNVIPFQLLAYYMALLRGNNVDCPRNLAKSVTVQ 670
|
|
| GFAT |
cd00714 |
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ... |
2-218 |
7.28e-117 |
|
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: 346.36 E-value: 7.28e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 2 CGIVGLTGSvgERIGLVLRRCLERLEYRGYDSAGVAVVNGGVITVRKGRGKISEVDARVNFTGLNGVSGIGHTRWATHGK 81
Cdd:cd00714 1 CGIVGYIGK--REAVDILLEGLKRLEYRGYDSAGIAVIGDGSLEVVKAVGKVANLEEKLAEKPLSGHVGIGHTRWATHGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 82 PSDENAHPHTDCSGTVAVVHNGIISNYRELREQLEARGHRFTSDTDTEVIAHLFEDYVKAGLTALEALREVVSRLRGTYA 161
Cdd:cd00714 79 PTDVNAHPHRSCDGEIAVVHNGIIENYAELKEELEAKGYKFESETDTEVIAHLIEYYYDGGLDLLEAVKKALKRLEGAYA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 974335136 162 IALLYVGEPDKVFFARNVSPLIIGLGNGFNFLASDIPAFLEYTNRVITLHDGEYGFI 218
Cdd:cd00714 159 LAVISKDEPDEIVAARNGSPLVIGIGDGENFVASDAPALLEHTRRVIYLEDGDIAVI 215
|
|
| PLN02981 |
PLN02981 |
glucosamine:fructose-6-phosphate aminotransferase |
1-608 |
7.42e-116 |
|
glucosamine:fructose-6-phosphate aminotransferase
Pssm-ID: 215531 [Multi-domain] Cd Length: 680 Bit Score: 360.22 E-value: 7.42e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 1 MCGIVG-LTGSVG-ER--IGLVLRRCLERLEYRGYDSAGVAVVNGGVIT-----VRKGRGKISE----VDARVNFTGLNG 67
Cdd:PLN02981 1 MCGIFAyLNYNVPrERrfILEVLFNGLRRLEYRGYDSAGIAIDNDPSLEsssplVFREEGKIESlvrsVYEEVAETDLNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 68 V------SGIGHTRWATHGKPSDENAHPHT-DCSGTVAVVHNGIISNYRELREQLEARGHRFTSDTDTEVIAHLFEdYV- 139
Cdd:PLN02981 81 DlvfenhAGIAHTRWATHGPPAPRNSHPQSsGPGNEFLVVHNGIITNYEVLKETLLRHGFTFESDTDTEVIPKLAK-FVf 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 140 ------KAGLTALEALREVVSRLRGTYAIALLYVGEPDKVFFARNVSPLIIG---LGNGFN------------------- 191
Cdd:PLN02981 160 dklneeEGDVTFSQVVMEVMRQLEGAYALIFKSPHYPNELVACKRGSPLLLGvkeLPEEKNssavftsegfltknrdkpk 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 192 --FLASDIPAFLEYTNRVITLHDGEYGFITPGSVYV-------ERGGEPVDVKARVR----VVNWSPELASKEGYPHFML 258
Cdd:PLN02981 240 efFLASDASAVVEHTKRVLVIEDNEVVHLKDGGVGIykfenekGRGGGGLSRPASVEralsTLEMEVEQIMKGNYDHYMQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 259 KEIHEQPRALRDTWAG-LDTDQLSKLSDLL-----------LKARRVFITGSGTSYHAGLVFDHLLSGLMGLD-THAFNS 325
Cdd:PLN02981 320 KEIHEQPESLTTTMRGrLIRGGSGKAKRVLlgglkdhlktiRRSRRIVFIGCGTSYNAALAARPILEELSGVPvTMELAS 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 326 SEYRRYVKLAGDgDVMVAVSQSGETIDTLMAVRVFRRLGVRVIAVSNVVDSTIPRESDYQLYTRAGPEVGVAATKTFTAQ 405
Cdd:PLN02981 400 DLLDRQGPIYRE-DTAVFVSQSGETADTLRALEYAKENGALCVGITNTVGSAISRGTHCGVHINAGAEIGVASTKAYTSQ 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 406 LMVLNALAATaalgggvLGKDEYGL------IMGELEHLPDLVNlTITSVEAKARHIASRLASKASAYYLSRGLGLPIAM 479
Cdd:PLN02981 479 IVAMTMLALA-------LGEDSISSrsrreaIIDGLFDLPNKVR-EVLKLDQEMKELAELLIDEQSLLVFGRGYNYATAL 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 480 EGALKLKEVAYIHAEAYPAGESKHGPIALVEGGFPVLFIATDDEYVDALEGNVMEMNARGALTIgVIPAKH--QPRFGKL 557
Cdd:PLN02981 551 EGALKVKEVALMHSEGILAGEMKHGPLALVDETLPIIVIATRDACFSKQQSVIQQLRARKGRLI-VICSKGdaSSVCPSG 629
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 974335136 558 LSEVIQTPNVSPGALTILQSIPLQLLAYYTAVLRGHDPDKPRNLAKTVTVE 608
Cdd:PLN02981 630 GCRVIEVPQVEDCLQPVINIVPLQLLAYHLTVLRGHNVDQPRNLAKSVTTQ 680
|
|
| AgaS |
COG2222 |
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ... |
258-608 |
3.46e-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: 3.46e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 258 LKEIHEQPRALRDTWAGLDTD-QLSKLSDLLLKARRVFITGSGTSYHAGLVFDHLLSGLMGLDTHAFNSSEYRRYVK-LA 335
Cdd:COG2222 1 AREIAQQPEAWRRALAALAAAiAALLARLRAKPPRRVVLVGAGSSDHAAQAAAYLLERLLGIPVAALAPSELVVYPAyLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 336 GDGDVMVAVSQSGETIDTLMAVRVFRRLGVRVIAVSNVVDSTIPRESDYQLYTRAGPEVGVAATKTFTAQLMVLNALAAT 415
Cdd:COG2222 81 LEGTLVVAISRSGNSPEVVAALELAKARGARTLAITNNPDSPLAEAADRVLPLPAGPEKSVAATKSFTTMLLALLALLAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 416 aalgggvLGKDEygLIMGELEHLPDLVNLTITSVEAKARHIAsrLASKASAYYLSRGLGLPIAMEGALKLKEVAYIHAEA 495
Cdd:COG2222 161 -------WGGDD--ALLAALDALPAALEAALAADWPAAALAA--LADAERVVFLGRGPLYGLAREAALKLKELSAGHAEA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 496 YPAGESKHGPIALVEGGFPVLFIATDDEYVDALEGNVMEMNARGALTIgVIPAKHQPRFgkllsEVIQTPNVSPGALTIL 575
Cdd:COG2222 230 YSAAEFRHGPKSLVDPGTLVVVLASEDPTRELDLDLAAELRALGARVV-AIGAEDDAAI-----TLPAIPDLHDALDPLL 303
|
330 340 350
....*....|....*....|....*....|...
gi 974335136 576 QSIPLQLLAYYTAVLRGHDPDKPRNLAKTVTVE 608
Cdd:COG2222 304 LLVVAQRLALALALARGLDPDTPRHLNKVVKTV 336
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
2-215 |
2.14e-67 |
|
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: 218.86 E-value: 2.14e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 2 CGIVGLTGSVGERIGLVLR--RCLERLEYRGYDSAGVAVVNGGVITVRKGRGKISEVDARVNFTGLNGVSGIGHTRWATH 79
Cdd:cd00352 1 CGIFGIVGADGAASLLLLLllRGLAALEHRGPDGAGIAVYDGDGLFVEKRAGPVSDVALDLLDEPLKSGVALGHVRLATN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 80 GKPSDENAHPHTDCSGTVAVVHNGIISNYRELREQLEARGHRFTSDTDTEVIAHLFEDYVKAGLTaLEALREVVSRLRGT 159
Cdd:cd00352 81 GLPSEANAQPFRSEDGRIALVHNGEIYNYRELREELEARGYRFEGESDSEVILHLLERLGREGGL-FEAVEDALKRLDGP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 974335136 160 YAIAlLYVGEPDKVFFARN---VSPLIIGLG-NGFNFLASDIPAFLEYT-NRVITLHDGEY 215
Cdd:cd00352 160 FAFA-LWDGKPDRLFAARDrfgIRPLYYGITkDGGLVFASEPKALLALPfKGVRRLPPGEL 219
|
|
| SIS_GlmS_GlmD_2 |
cd05009 |
SIS (Sugar ISomerase) domain repeat 2 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
452-606 |
1.30e-57 |
|
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: 190.55 E-value: 1.30e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 452 KARHIASRLASKASAYYLSRGLGLPIAMEGALKLKEVAYIHAEAYPAGESKHGPIALVEGGFPVLFIATDDEYVDALEGN 531
Cdd:cd05009 2 DIKELAEKLKEAKSFYVLGRGPNYGTALEGALKLKETSYIHAEAYSAGEFKHGPIALVDEGTPVIFLAPEDRLEEKLESL 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 974335136 532 VMEMNARGALTIGVIPAKHQPRFGkllSEVIQTPNVSPGALTILQSIPLQLLAYYTAVLRGHDPDKPRNLAKTVT 606
Cdd:cd05009 82 IKEVKARGAKVIVITDDGDAKDLA---DVVIRVPATVEELSPLLYIVPLQLLAYHLAVARGIDPDKPRNLAKSVT 153
|
|
| SIS_GlmS_GlmD_1 |
cd05008 |
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
292-408 |
2.72e-46 |
|
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: 159.20 E-value: 2.72e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 292 RVFITGSGTSYHAGLVFDHLLSGLMGLDTHAFNSSEYRRYVKLAGDGDVMVAVSQSGETIDTLMAVRVFRRLGVRVIAVS 371
Cdd:cd05008 1 RILIVGCGTSYHAALVAKYLLERLAGIPVEVEAASEFRYRRPLLDEDTLVIAISQSGETADTLAALRLAKEKGAKTVAIT 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 974335136 372 NVVDSTIPRESDYQLYTRAGPEVGVAATKTFTAQLMV 408
Cdd:cd05008 81 NVVGSTLAREADYVLYLRAGPEISVAATKAFTSQLLA 117
|
|
| PurF |
COG0034 |
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ... |
1-200 |
1.90e-40 |
|
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: 153.25 E-value: 1.90e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 1 MCGIVGLTGS--VGERI--GLVLrrclerLEYRGYDSAGVAVVNGGVITVRKGRGKISEVDARVNFTGLNGVSGIGHTRW 76
Cdd:COG0034 7 ECGVFGIYGHedVAQLTyyGLYA------LQHRGQESAGIATSDGGRFHLHKGMGLVSDVFDEEDLERLKGNIAIGHVRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 77 ATHGKPSDENAHPHT-DCS-GTVAVVHNGIISNYRELREQLEARGHRFTSDTDTEVIAHLFEDYVKAGlTALEALREVVS 154
Cdd:COG0034 81 STTGSSSLENAQPFYvNSPfGSIALAHNGNLTNAEELREELEEEGAIFQTTSDTEVILHLIARELTKE-DLEEAIKEALR 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 974335136 155 RLRGTYAIALLYvgePDKVFFARN---VSPLIIG-LGNGFnFLASDIPAF 200
Cdd:COG0034 160 RVKGAYSLVILT---GDGLIAARDpngIRPLVLGkLEDGY-VVASESCAL 205
|
|
| GPATase_N |
cd00715 |
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ... |
2-200 |
1.10e-37 |
|
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the N-terminus of glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase) . The glutaminase domain catalyzes amide nitrogen transfer from glutamine to the appropriate substrate. In this process, glutamine is hydrolyzed to glutamic acid and ammonia. GPATase catalyzes the first step in purine biosynthesis, an amide transfer from glutamine to PRPP, resulting in phosphoribosylamine, pyrophosphate and glutamate. GPATase crystalizes as a homotetramer, but can also exist as a homdimer.
Pssm-ID: 238367 [Multi-domain] Cd Length: 252 Bit Score: 140.29 E-value: 1.10e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 2 CGIVGLTGS--VGERI--GLVLrrclerLEYRGYDSAGVAVVNGGVITVRKGRGKISEVdarvnFTG-----LNGVSGIG 72
Cdd:cd00715 1 CGVFGIYGAedAARLTylGLYA------LQHRGQESAGIATSDGKRFHTHKGMGLVSDV-----FDEeklrrLPGNIAIG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 73 HTRWATHGKPSDENAHP---HTdCSGTVAVVHNGIISNYRELREQLEARGHRFTSDTDTEVIAHLFEDYVKAGlTALEAL 149
Cdd:cd00715 70 HVRYSTAGSSSLENAQPfvvNS-PLGGIALAHNGNLVNAKELREELEEEGRIFQTTSDSEVILHLIARSLAKD-DLFEAI 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 974335136 150 REVVSRLRGTYAIALLYvgePDKVFFARN---VSPLIIG-LGNGFNFLASDIPAF 200
Cdd:cd00715 148 IDALERVKGAYSLVIMT---ADGLIAVRDphgIRPLVLGkLEGDGYVVASESCAL 199
|
|
| purF |
TIGR01134 |
amidophosphoribosyltransferase; Alternate name: glutamine phosphoribosylpyrophosphate (PRPP) ... |
2-200 |
6.86e-34 |
|
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: 134.37 E-value: 6.86e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 2 CGIVGLTGSvGERIGLVLRRCLERLEYRGYDSAGVAVVNGGVITVRKGRGKISEVDARVNFTGLNGVSGIGHTRWATHGK 81
Cdd:TIGR01134 1 CGVVGIYGQ-EEVAASLTYYGLYALQHRGQESAGISVFDGNRFRLHKGNGLVSDVFNEEHLQRLKGNVGIGHVRYSTAGS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 82 PSDENAHPHT--DCSGTVAVVHNGIISNYRELREQLEARGHRFTSDTDTEVIAHLFEDYVKAGLTALEALREVVSRLRGT 159
Cdd:TIGR01134 80 SGLENAQPFVvnSPYGGLALAHNGNLVNADELRRELEEEGRHFNTTSDSEVLLHLLAHNDESKDDLFDAVARVLERVRGA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 974335136 160 YAialLYVGEPDKVFFARN---VSPLIIG-LGNGFnFLASDIPAF 200
Cdd:TIGR01134 160 YA---LVLMTEDGLVAVRDphgIRPLVLGrRGDGY-VVASESCAL 200
|
|
| PRK05793 |
PRK05793 |
amidophosphoribosyltransferase; Provisional |
23-200 |
3.20e-29 |
|
amidophosphoribosyltransferase; Provisional
Pssm-ID: 235611 [Multi-domain] Cd Length: 469 Bit Score: 121.29 E-value: 3.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 23 LERLEYRGYDSAGVAVVNGGVITVRKGRGKISEVDARVNFTGLNGVSGIGHTRWATHGKPSDENAHPHTDCS--GTVAVV 100
Cdd:PRK05793 36 LYALQHRGQESAGIAVSDGEKIKVHKGMGLVSEVFSKEKLKGLKGNSAIGHVRYSTTGASDLDNAQPLVANYklGSIAIA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 101 HNGIISNYRELREQLEARGHRFTSDTDTEVIAHLFEDYVKAGLTalEALREVVSRLRGTYAIALLYvgePDKVFFARN-- 178
Cdd:PRK05793 116 HNGNLVNADVIRELLEDGGRIFQTSIDSEVILNLIARSAKKGLE--KALVDAIQAIKGSYALVILT---EDKLIGVRDph 190
|
170 180
....*....|....*....|...
gi 974335136 179 -VSPLIIGLGNGFNFLASDIPAF 200
Cdd:PRK05793 191 gIRPLCLGKLGDDYILSSESCAL 213
|
|
| PLN02440 |
PLN02440 |
amidophosphoribosyltransferase |
1-221 |
6.11e-28 |
|
amidophosphoribosyltransferase
Pssm-ID: 215241 [Multi-domain] Cd Length: 479 Bit Score: 117.47 E-value: 6.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 1 MCGIVGLTGSvgeriGLVLRRC---LERLEYRGYDSAGVAVVNGGVITVRKGRGKISEVDARVNFTGLNGVSGIGHTRWA 77
Cdd:PLN02440 1 ECGVVGIFGD-----PEASRLCylgLHALQHRGQEGAGIVTVDGNRLQSITGNGLVSDVFDESKLDQLPGDIAIGHVRYS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 78 THGKPSDENAHPHTDCS--GTVAVVHNGIISNYRELREQLEARGHRFTSDTDTEVIAHLFEDYVKAglTALEALREVVSR 155
Cdd:PLN02440 76 TAGASSLKNVQPFVANYrfGSIGVAHNGNLVNYEELRAKLEENGSIFNTSSDTEVLLHLIAISKAR--PFFSRIVDACEK 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 974335136 156 LRGTYaiALLYVGEpDKVFFARN---VSPLIIGL-GNGFNFLASDIPAF--LEYTnRVITLHDGEYGFITPG 221
Cdd:PLN02440 154 LKGAY--SMVFLTE-DKLVAVRDphgFRPLVMGRrSNGAVVFASETCALdlIGAT-YEREVNPGEVIVVDKD 221
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
290-408 |
1.49e-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: 104.69 E-value: 1.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 290 ARRVFITGSGTSYHAGLVFDHLLSGLMGLDTHAFNSSEYR-RYVKLAGDGDVMVAVSQSGETIDTLMAVRVFRRLGVRVI 368
Cdd:pfam01380 5 AKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRhGVLALVDEDDLVIAISYSGETKDLLAAAELAKARGAKII 84
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 974335136 369 AVSNVVDSTIPRESDYQLYTRAGPEVGVAATKTFTAQLMV 408
Cdd:pfam01380 85 AITDSPGSPLAREADHVLYINAGPETGVASTKSITAQLAA 124
|
|
| AsnB |
cd00712 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ... |
2-202 |
2.85e-26 |
|
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: 106.87 E-value: 2.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 2 CGIVGLTGSVGERIGL-VLRRCLERLEYRGYDSAGVavvnggvitvrkgrgkisEVDARVnftglngvsGIGHTRWATHG 80
Cdd:cd00712 1 CGIAGIIGLDGASVDRaTLERMLDALAHRGPDGSGI------------------WIDEGV---------ALGHRRLSIID 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 81 kPSDEnAHPHTDCSGTVAVVHNGIISNYRELREQLEARGHRFTSDTDTEVIAHLFEDYvkaGLTALEalrevvsRLRGTY 160
Cdd:cd00712 54 -LSGG-AQPMVSEDGRLVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHLYEEW---GEDCLE-------RLNGMF 121
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 974335136 161 AIAlLYVGEPDKVFFARN---VSPLIIGLGNGFNFLASDIPAFLE 202
Cdd:cd00712 122 AFA-LWDKRKRRLFLARDrfgIKPLYYGRDGGGLAFASELKALLA 165
|
|
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
1-203 |
1.07e-25 |
|
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: 111.47 E-value: 1.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 1 MCGIVGLTGSVGERIGLVLRRCLERLEYRGYDSAGVavvnggvitvrkgrgkisEVDARVnftglngvsGIGHTRWAThg 80
Cdd:COG0367 1 MCGIAGIIDFDGGADREVLERMLDALAHRGPDGSGI------------------WVDGGV---------ALGHRRLSI-- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 81 KPSDENAH-PHTDCSGTVAVVHNGIISNYRELREQLEARGHRFTSDTDTEVIAHLFEDYvkaGLtalealrEVVSRLRGT 159
Cdd:COG0367 52 IDLSEGGHqPMVSEDGRYVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHAYEEW---GE-------DCLERLNGM 121
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 974335136 160 YAIAlLYVGEPDKVFFARN---VSPLIIGL-GNGFNFlASDIPAFLEY 203
Cdd:COG0367 122 FAFA-IWDRRERRLFLARDrfgIKPLYYAEdGGGLAF-ASELKALLAH 167
|
|
| GATase_7 |
pfam13537 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
73-201 |
3.58e-25 |
|
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: 100.67 E-value: 3.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 73 HTRWATHGkpSDENAHP-HTDCSGTVAVVHNGIISNYRELREQLEARGHRFTSDTDTEVIAHLFEDyvkagltalEALRE 151
Cdd:pfam13537 1 HRRLSIID--LEGGAQPmVSSEDGRYVIVFNGEIYNYRELRAELEAKGYRFRTHSDTEVILHLYEA---------EWGED 69
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 974335136 152 VVSRLRGTYAIAlLYVGEPDKVFFARN---VSPLIIGLGNGFNFL-ASDIPAFL 201
Cdd:pfam13537 70 CVDRLNGMFAFA-IWDRRRQRLFLARDrfgIKPLYYGRDDGGRLLfASELKALL 122
|
|
| GlxB |
cd01907 |
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ... |
2-215 |
5.01e-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: 104.27 E-value: 5.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 2 CGIVGLTGSVGERI-GLVLRRCLERLEYRG-YDSAGVAVVN---------GGVITVRKGRGKISEVDARVNFTGLNGVSG 70
Cdd:cd01907 1 CGIFGIMSKDGEPFvGALLVEMLDAMQERGpGDGAGFALYGdpdafvyssGKDMEVFKGVGYPEDIARRYDLEEYKGYHW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 71 IGHTRWATHGKPSDENAHPHtdCSGTVAVVHNGIISNYRELREQLEARGHRFTSDTDTEVIAHLFEDYVKAGLTALEA-- 148
Cdd:cd01907 81 IAHTRQPTNSAVWWYGAHPF--SIGDIAVVHNGEISNYGSNREYLERFGYKFETETDTEVIAYYLDLLLRKGGLPLEYyk 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 149 --------LREVVSRLRGTYAIALL------YVGEPDKVFFARNVS---PLIIGLGNGFNFLASDIPAFLEYTN----RV 207
Cdd:cd01907 159 hiirmpeeERELLLALRLTYRLADLdgpftiIVGTPDGFIVIRDRIklrPAVVAETDDYVAIASEECAIREIPDrdnaKV 238
|
....*...
gi 974335136 208 ITLHDGEY 215
Cdd:cd01907 239 WEPRPGEY 246
|
|
| GATase_6 |
pfam13522 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
70-196 |
6.90e-25 |
|
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: 100.07 E-value: 6.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 70 GIGHTRWATHGKPSDENaHPHTDCSGTVAVVHNGIISNYRELREQLEARGHRFTSDTDTEVIAHLFEDYVKagltaleal 149
Cdd:pfam13522 13 ALGHVRLAIVDLPDAGN-QPMLSRDGRLVLVHNGEIYNYGELREELADLGHAFRSRSDTEVLLALYEEWGE--------- 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 974335136 150 rEVVSRLRGTYAIAlLYVGEPDKVFFARN---VSPLIIGLGNGFNFLASD 196
Cdd:pfam13522 83 -DCLERLRGMFAFA-IWDRRRRTLFLARDrlgIKPLYYGILGGGFVFASE 130
|
|
| RpiR |
COG1737 |
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ... |
266-408 |
8.58e-20 |
|
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains [Transcription];
Pssm-ID: 441343 [Multi-domain] Cd Length: 286 Bit Score: 89.99 E-value: 8.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 266 RALRDTWAGLDTDQLSKLSDLLLKARRVFITGSGTSYHAGLVFDHLLSgLMGLDTHAFN--SSEYRRYVKLAGDGDVMVA 343
Cdd:COG1737 110 ANLEETLELLDEEALERAVDLLAKARRIYIFGVGASAPVAEDLAYKLL-RLGKNVVLLDgdGHLQAESAALLGPGDVVIA 188
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 974335136 344 VSQSGETIDTLMAVRVFRRLGVRVIAVSNVVDSTIPRESDYQLYTRA-GPEVGVAATKTFTAQLMV 408
Cdd:COG1737 189 ISFSGYTRETLEAARLAKERGAKVIAITDSPLSPLAKLADVVLYVPSeEPTLRSSAFSSRVAQLAL 254
|
|
| asn_synth_AEB |
TIGR01536 |
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing ... |
18-201 |
4.05e-18 |
|
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: 87.39 E-value: 4.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 18 VLRRCLERLEYRGYDSAGVAVVNGGVItvrkgrgkisevdarvnftglngvsgIGHTRWATHGkpSDENAHPHTDCSGTV 97
Cdd:TIGR01536 17 AIKRMSDTIAHRGPDASGIEYKDGNAI--------------------------LGHRRLAIID--LSGGAQPMSNEGKTY 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 98 AVVHNGIISNYRELREQLEARGHRFTSDTDTEVIAHLFEDYvkaGltalealREVVSRLRGTYAIALLYvGEPDKVFFAR 177
Cdd:TIGR01536 69 VIVFNGEIYNHEELREELEAKGYTFQTDSDTEVILHLYEEW---G-------EECVDRLDGMFAFALWD-SEKGELFLAR 137
|
170 180
....*....|....*....|....*..
gi 974335136 178 N---VSPLIIGLGNGFNFLASDIPAFL 201
Cdd:TIGR01536 138 DrfgIKPLYYAYDGGQLYFASEIKALL 164
|
|
| SIS_RpiR |
cd05013 |
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ... |
290-408 |
4.88e-17 |
|
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: 78.04 E-value: 4.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 290 ARRVFITGSGTSYHAGLVFDHLLSGLmGLDTHAFNSSEYRR-YVKLAGDGDVMVAVSQSGETIDTLMAVRVFRRLGVRVI 368
Cdd:cd05013 13 ARRIYIFGVGSSGLVAEYLAYKLLRL-GKPVVLLSDPHLQLmSAANLTPGDVVIAISFSGETKETVEAAEIAKERGAKVI 91
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 974335136 369 AVSNVVDSTIPRESDYQLYTRAGPE-VGVAATKTFTAQLMV 408
Cdd:cd05013 92 AITDSANSPLAKLADIVLLVSSEEGdFRSSAFSSRIAQLAL 132
|
|
| PTZ00077 |
PTZ00077 |
asparagine synthetase-like protein; Provisional |
1-226 |
1.04e-15 |
|
asparagine synthetase-like protein; Provisional
Pssm-ID: 185431 [Multi-domain] Cd Length: 586 Bit Score: 80.53 E-value: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 1 MCGIVGLTGSVGERIgLVLRRCLE---RLEYRGYDSAGVAVVNggvitvrkgrgkisevdarvNFTGLNGVsgIGHTRWA 77
Cdd:PTZ00077 1 MCGILAIFNSKGERH-ELRRKALElskRLRHRGPDWSGIIVLE--------------------NSPGTYNI--LAHERLA 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 78 THGkPSDeNAHPHTDCSGTVAVVHNGIISNYRELREQLEARGHRFTSDTDTEVIAHLFEDYVKagltalealREVVSRLR 157
Cdd:PTZ00077 58 IVD-LSD-GKQPLLDDDETVALMQNGEIYNHWEIRPELEKEGYKFSSNSDCEIIGHLYKEYGP---------KDFWNHLD 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 974335136 158 GTYAIaLLYVGEPDKVFFARN---VSPLIIGLG-NGFNFLASDIPAfleytnrvitLHDG--EYGFITPGSVYVE 226
Cdd:PTZ00077 127 GMFAT-VIYDMKTNTFFAARDhigIIPLYIGYAkDGSIWFSSELKA----------LHDQcvEVKQFPPGHYYDQ 190
|
|
| asnB |
PRK09431 |
asparagine synthetase B; Provisional |
1-232 |
8.83e-15 |
|
asparagine synthetase B; Provisional
Pssm-ID: 236513 [Multi-domain] Cd Length: 554 Bit Score: 77.26 E-value: 8.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 1 MCGIVGLTGSVGERIGLVLR--RCLERLEYRGYDSAGVAVVNGGVItvrkgrgkisevdarvnftglngvsgiGHTRWA- 77
Cdd:PRK09431 1 MCGIFGILDIKTDADELRKKalEMSRLMRHRGPDWSGIYASDNAIL---------------------------GHERLSi 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 78 ---THGkpsdenAHPHTDCSGTVAVVHNGIISNYRELREQLEARgHRFTSDTDTEVIAHLFEDYvkaGLtalealrEVVS 154
Cdd:PRK09431 54 vdvNGG------AQPLYNEDGTHVLAVNGEIYNHQELRAELGDK-YAFQTGSDCEVILALYQEK---GP-------DFLD 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 155 RLRGTYAIAlLYVGEPDKVFFARN---VSPLIIGLGNGFNFL-ASDIPAFLEYTNRVITLhdgeygfiTPGSVYVERGGE 230
Cdd:PRK09431 117 DLDGMFAFA-LYDSEKDAYLIARDpigIIPLYYGYDEHGNLYfASEMKALVPVCKTIKEF--------PPGHYYWSKDGE 187
|
..
gi 974335136 231 PV 232
Cdd:PRK09431 188 FV 189
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
460-591 |
6.27e-13 |
|
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: 66.17 E-value: 6.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 460 LASKASAYYLSRGLGLPIAMEGALKLKEVAYIHAEAYPAGESKHGPIALVEGGFPVLFIATDDEYVDALEGNVmEMNARG 539
Cdd:pfam01380 2 LAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGVLALVDEDDLVIAISYSGETKDLLAAAE-LAKARG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 974335136 540 ALTIGVIPAKHQPrFGKLLSEVIQTPNVSPGALTILQSIPLQLLAYYTAVLR 591
Cdd:pfam01380 81 AKIIAITDSPGSP-LAREADHVLYINAGPETGVASTKSITAQLAALDALAVA 131
|
|
| PLN02549 |
PLN02549 |
asparagine synthase (glutamine-hydrolyzing) |
1-230 |
8.83e-13 |
|
asparagine synthase (glutamine-hydrolyzing)
Pssm-ID: 178164 [Multi-domain] Cd Length: 578 Bit Score: 70.95 E-value: 8.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 1 MCGIVGLTGSVGERIGLvLRRCLE---RLEYRGYDSAGVAVvnggvitvrkgrgkisevdarvnftglNGVSGIGHTRWA 77
Cdd:PLN02549 1 MCGILAVLGCSDDSQAK-RSRVLElsrRLRHRGPDWSGLYG---------------------------NEDCYLAHERLA 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 78 THGKPSDEnaHPHTDCSGTVAVVHNGIISNYRELREQLEArgHRFTSDTDTEVIAHLFEDYVKagltalealrEVVSRLR 157
Cdd:PLN02549 53 IMDPESGD--QPLYNEDKTIVVTANGEIYNHKELREKLKL--HKFRTGSDCEVIAHLYEEHGE----------EFVDMLD 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 158 GTYAIALLyvGEPDKVFF-ARN---VSPLIIGLGN-GFNFLASDIPAfleytnrvitLHDGEYGFIT--PGSVYVERGGE 230
Cdd:PLN02549 119 GMFSFVLL--DTRDNSFIaARDhigITPLYIGWGLdGSVWFASEMKA----------LCDDCERFEEfpPGHYYSSKAGG 186
|
|
| frlB |
PRK11382 |
fructoselysine 6-phosphate deglycase; |
292-599 |
2.67e-12 |
|
fructoselysine 6-phosphate deglycase;
Pssm-ID: 183111 [Multi-domain] Cd Length: 340 Bit Score: 68.49 E-value: 2.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 292 RVFITGSGTSYHAGLVFDHLLSGLMGLDTHAFNSSEYRRYVKLAGDGD-VMVAVSQSGETIDTLMAVRVFRRLGVRVIAV 370
Cdd:PRK11382 46 RIYFVACGSPLNAAQTAKHLADRFSDLQVYAISGWEFCDNTPYRLDDRcAVIGVSDYGKTEEVIKALELGRACGALTAAF 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 371 SNVVDSTIPRESDYQLYTRAGP--EVGVAATKTFTAQLMVLNALAAtaalgggvlgkdEYGLIMGELEHLPDLVNLTITS 448
Cdd:PRK11382 126 TKRADSPITSAAEFSIDYQADCiwEIHLLLCYSVVLEMITRLAPNA------------EIGKIKNDLKQLPNALGHLVRT 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 449 VEAKARHIASRLASKASAYYLSRGLGLPIAM-EGALKLKEVAYIHAEAYPAGESKHGPIALVEGGFPVLFIATDDEYVDA 527
Cdd:PRK11382 194 WEEKGRQLGELASQWPMIYTVAAGPLRPLGYkEGIVTLMEFTWTHGCVIESGEFRHGPLEIVEPGVPFLFLLGNDESRHT 273
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 974335136 528 LEGNVMEMNARgalTIGVIPAKHqprfgkllSEVIQtpNVSPGALTILQSIPLQLLAYYTAVLRGHDPDKPR 599
Cdd:PRK11382 274 TERAINFVKQR---TDNVIVIDY--------AEISQ--GLHPWLAPFLMFVPMEWLCYYLSIYKDHNPDERR 332
|
|
| SIS_Kpsf |
cd05014 |
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ... |
291-408 |
1.82e-10 |
|
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: 58.71 E-value: 1.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 291 RRVFITGSGTSYHAGLVFDHLLSGLmGLDTHAFNSSEyrryvKLAGD------GDVMVAVSQSGETIDTLMAVRVFRRLG 364
Cdd:cd05014 1 GKVVVTGVGKSGHIARKIAATLSST-GTPAFFLHPTE-----ALHGDlgmvtpGDVVIAISNSGETDELLNLLPHLKRRG 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 974335136 365 VRVIAVSNVVDSTIPRESDYQLYTRAGPEV---GVAATKTFTAQLMV 408
Cdd:cd05014 75 APIIAITGNPNSTLAKLSDVVLDLPVEEEAcplGLAPTTSTTAMLAL 121
|
|
| YafJ |
COG0121 |
Predicted glutamine amidotransferase YafJ [General function prediction only]; |
71-157 |
3.23e-09 |
|
Predicted glutamine amidotransferase YafJ [General function prediction only];
Pssm-ID: 439891 [Multi-domain] Cd Length: 248 Bit Score: 57.67 E-value: 3.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 71 IGHTRWATHGKPSDENAHPHTDcsGTVAVVHNGIISNYRELREQLEAR---GHRFT--SDTDTEVIAHLFEDYVKA-GLT 144
Cdd:COG0121 80 IAHVRKATVGPVSLENTHPFRG--GRWLFAHNGQLDGFDRLRRRLAEElpdELYFQpvGTTDSELAFALLLSRLRDgGPD 157
|
90
....*....|...
gi 974335136 145 ALEALREVVSRLR 157
Cdd:COG0121 158 PAEALAEALRELA 170
|
|
| GutQ |
COG0794 |
D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall ... |
292-408 |
5.04e-09 |
|
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: 58.06 E-value: 5.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 292 RVFITGSGTSYHAGLVFDHLLS--GlmgldTHAFnsseyrrYVKLA----GD------GDVMVAVSQSGETIDTLMAVRV 359
Cdd:COG0794 46 RVVVTGMGKSGHIARKIAATLAstG-----TPAF-------FLHPAeashGDlgmitpGDVVIAISNSGETEELLALLPL 113
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 974335136 360 FRRLGVRVIAVSNVVDSTIPRESDYQLYTRAGPEV---GVAATKTFTAQLMV 408
Cdd:COG0794 114 LKRLGVPLIAITGNPDSTLARAADVVLDLPVEREAcplNLAPTTSTTATLAL 165
|
|
| YafJ |
cd01908 |
Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine ... |
71-170 |
8.06e-09 |
|
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: 56.63 E-value: 8.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 71 IGHTRWATHGKPSDENAHPHTDcsGTVAVVHNGIISNYRELREQLEARGHRFT-SDTDTEVIAHLF------------ED 137
Cdd:cd01908 84 LAHVRAATVGPVSLENCHPFTR--GRWLFAHNGQLDGFRLLRRRLLRLLPRLPvGTTDSELAFALLlsrllerdpldpAE 161
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 974335136 138 YVKAGLTALEALREVVSRLR-------GTYAIALLYVGEP 170
Cdd:cd01908 162 LLDAILQTLRELAALAPPGRlnlllsdGEYLIATRYASAP 201
|
|
| SIS |
cd04795 |
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
293-371 |
2.22e-08 |
|
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars.
Pssm-ID: 240112 [Multi-domain] Cd Length: 87 Bit Score: 51.61 E-value: 2.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 293 VFITGSGTSYHAGLVFDHLLSGLMGLDTHAFN--SSEYRRYVKLAGDGDVMVAVSQSGETIDTLMAVRVFRRLGVRVIAV 370
Cdd:cd04795 1 IFVIGIGGSGAIAAYFALELLELTGIEVVALIatELEHASLLSLLRKGDVVIALSYSGRTEELLAALEIAKELGIPVIAI 80
|
.
gi 974335136 371 S 371
Cdd:cd04795 81 T 81
|
|
| PRK11337 |
PRK11337 |
MurR/RpiR family transcriptional regulator; |
334-390 |
6.74e-08 |
|
MurR/RpiR family transcriptional regulator;
Pssm-ID: 183089 [Multi-domain] Cd Length: 292 Bit Score: 54.38 E-value: 6.74e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 974335136 334 LAGDGDVMVAVSQSGETIDTLMAVRVFRRLGVRVIAVSNVVDSTIPRESDYQLYTRA 390
Cdd:PRK11337 184 LLQEGDVVLVVSHSGRTSDVIEAVELAKKNGAKIICITNSYHSPIAKLADYVICSTA 240
|
|
| PRK15482 |
PRK15482 |
HTH-type transcriptional regulator MurR; |
263-405 |
6.27e-07 |
|
HTH-type transcriptional regulator MurR;
Pssm-ID: 185379 [Multi-domain] Cd Length: 285 Bit Score: 51.24 E-value: 6.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 263 EQPRALRDTWAGLDTDQLSKLSDLLLKARRVFITGSGTSyhaGLVFDHLLSGLMGL--------DTH--AFNSSEYRRyv 332
Cdd:PRK15482 108 EKELALEQTCALFDYARLQKIIEVISKAPFIQITGLGGS---ALVGRDLSFKLMKIgyrvaceaDTHvqATVSQALKK-- 182
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 974335136 333 klagdGDVMVAVSQSGETIDTLMAVRVFRRLGVRVIAVSNVVDSTIPRESDYQLYTRAG-PEVGVAATKTFTAQ 405
Cdd:PRK15482 183 -----GDVQIAISYSGSKKEIVLCAEAARKQGATVIAITSLADSPLRRLAHFTLDTVSGeTEWRSSSMSTRTAQ 251
|
|
| PRK11557 |
PRK11557 |
MurR/RpiR family transcriptional regulator; |
290-407 |
7.88e-07 |
|
MurR/RpiR family transcriptional regulator;
Pssm-ID: 183195 [Multi-domain] Cd Length: 278 Bit Score: 50.92 E-value: 7.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 290 ARRVFITGSGTSyhaGLVFDHLLSGLMGLDTHAFnsSEYRRYVKLA-----GDGDVMVAVSQSGETIDTLMAVRVFRRLG 364
Cdd:PRK11557 128 ARRIILTGIGAS---GLVAQNFAWKLMKIGINAV--AERDMHALLAtvqalSPDDLLLAISYSGERRELNLAADEALRVG 202
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 974335136 365 VRVIAVSNVVDSTIPRESDYQLYTRA-GPEVGVAATKTFTAQLM 407
Cdd:PRK11557 203 AKVLAITGFTPNALQQRASHCLYTIAeEQATRSAAISSTHAQGM 246
|
|
| SIS_1 |
cd05710 |
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ... |
292-406 |
9.84e-06 |
|
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: 44.87 E-value: 9.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 292 RVFITGSGTSYHAGLVFDHLLSGLMGLDTHAFNSSE--YRRYVKLaGDGDVMVAVSQSGETIDTLMAVRVFRRLGVRVIA 369
Cdd:cd05710 1 NVFFVGCGGSLADMYPAKYFLKKESKLPVFVYNAAEflHTGPKRL-TEKSVVILASHSGNTKETVAAAKFAKEKGATVIG 79
|
90 100 110
....*....|....*....|....*....|....*..
gi 974335136 370 VSNVVDSTIPRESDYQLYTRAgpevGVAATKTFTAQL 406
Cdd:cd05710 80 LTDDEDSPLAKLADYVIVYGF----EIDAVEEKYLLL 112
|
|
| SIS_PHI |
cd05005 |
Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) ... |
290-384 |
1.83e-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: 45.64 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 290 ARRVFITGSGTSyhaGLV-------FDHLlsglmGLDTH--------AFnsseyrryvklaGDGDVMVAVSQSGETIDTL 354
Cdd:cd05005 33 AKRIFVYGAGRS---GLVakafamrLMHL-----GLNVYvvgetttpAI------------GPGDLLIAISGSGETSSVV 92
|
90 100 110
....*....|....*....|....*....|
gi 974335136 355 MAVRVFRRLGVRVIAVSNVVDSTIPRESDY 384
Cdd:cd05005 93 NAAEKAKKAGAKVVLITSNPDSPLAKLADV 122
|
|
| SIS_Etherase |
cd05007 |
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ... |
336-408 |
2.53e-05 |
|
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ISomerase) domain. The SIS domain is found in many phosphosugar isomerases and phosphosugar binding proteins. The bacterial cell wall sugar N-acetylmuramic acid carries a unique D-lactyl ether substituent at the C3 position. The etherase catalyzes the cleavage of the lactyl ether bond of N-acetylmuramic acid 6-phosphate.
Pssm-ID: 240140 [Multi-domain] Cd Length: 257 Bit Score: 45.98 E-value: 2.53e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 974335136 336 GDGDVMVAVSQSGETIDTLMAVRVFRRLGVRVIAVSNVVDSTIPRESDYQLYTRAGPEV--GVAATKTFTAQLMV 408
Cdd:cd05007 117 TERDVVIGIAASGRTPYVLGALRYARARGALTIGIACNPGSPLLQLADIAIALITGPEVvaGSTRLKAGTAQKLA 191
|
|
| murQ |
PRK05441 |
N-acetylmuramic acid-6-phosphate etherase; Reviewed |
336-408 |
5.34e-05 |
|
N-acetylmuramic acid-6-phosphate etherase; Reviewed
Pssm-ID: 235467 [Multi-domain] Cd Length: 299 Bit Score: 45.54 E-value: 5.34e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 974335136 336 GDGDVMVAVSQSGETIDTLMAVRVFRRLGVRVIAVSNVVDSTIPRESDYQLYTRAGPEVGVAAT--KTFTAQLMV 408
Cdd:PRK05441 130 TAKDVVVGIAASGRTPYVIGALEYARERGALTIGISCNPGSPLSKEADIAIEVVVGPEVLTGSTrmKAGTAQKLV 204
|
|
| MurQ |
COG2103 |
N-acetylmuramic acid 6-phosphate (MurNAc-6-P) etherase [Cell wall/membrane/envelope biogenesis] ... |
336-408 |
7.93e-04 |
|
N-acetylmuramic acid 6-phosphate (MurNAc-6-P) etherase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441706 [Multi-domain] Cd Length: 301 Bit Score: 42.00 E-value: 7.93e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 974335136 336 GDGDVMVAVSQSGETIDTLMAVRVFRRLGVRVIAVSNVVDSTIPRESDYQLYTRAGPEVGVAAT--KTFTAQLMV 408
Cdd:COG2103 131 GPGDVVVGIAASGRTPYVIGALEYARARGALTVAIACNPGSPLSAAADIAIELVTGPEVITGSTrlKAGTAQKLV 205
|
|
| SIS_PGI_PMI_1 |
cd05017 |
The members of this protein family contain the SIS (Sugar ISomerase) domain and have both the ... |
292-371 |
7.97e-04 |
|
The members of this protein family contain the SIS (Sugar ISomerase) domain and have both the phosphoglucose isomerase (PGI) and the phosphomannose isomerase (PMI) functions. These functions catalyze the reversible reactions of glucose 6-phosphate to fructose 6-phosphate, and mannose 6-phosphate to fructose 6-phosphate, respectively at an equal rate. This protein contains two SIS domains. This alignment is based on the first SIS domain.
Pssm-ID: 240148 [Multi-domain] Cd Length: 119 Bit Score: 39.56 E-value: 7.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335136 292 RVFITGSGTSYHAGLVFDHLLSglmglDTHAFNSSEYRRYV--KLAGDGDVMVAVSQSGETIDTLMAVRVFRRLGVRVIA 369
Cdd:cd05017 1 NIVILGMGGSGIGGDLLESLLL-----DEAKIPVYVVKDYTlpAFVDRKTLVIAVSYSGNTEETLSAVEQAKERGAKIVA 75
|
..
gi 974335136 370 VS 371
Cdd:cd05017 76 IT 77
|
|
| PRK10892 |
PRK10892 |
arabinose-5-phosphate isomerase KdsD; |
338-406 |
4.77e-03 |
|
arabinose-5-phosphate isomerase KdsD;
Pssm-ID: 182814 [Multi-domain] Cd Length: 326 Bit Score: 39.32 E-value: 4.77e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 974335136 338 GDVMVAVSQSGETIDTLMAVRVFRRLGVRVIAVSNVVDSTIPRESDYQLYTRAGPE---VGVAATKTFTAQL 406
Cdd:PRK10892 95 QDVVIAISNSGESSEILALIPVLKRLHVPLICITGRPESSMARAADIHLCVKVPKEacpLGLAPTSSTTATL 166
|
|
| |
