|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02981 |
PLN02981 |
glucosamine:fructose-6-phosphate aminotransferase |
2-675 |
0e+00 |
|
glucosamine:fructose-6-phosphate aminotransferase
Pssm-ID: 215531 [Multi-domain] Cd Length: 680 Bit Score: 929.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 2 NYRVPKTRKEIFETLIRGLQRLEYRGYDSAGVAIDgNNHEVKERHIHLVKKRGKVKALDEELYK---QDSMDLKVEFETH 78
Cdd:PLN02981 9 NYNVPRERRFILEVLFNGLRRLEYRGYDSAGIAID-NDPSLESSSPLVFREEGKIESLVRSVYEevaETDLNLDLVFENH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 79 FGIAHTRWATHGVPNAVNSHPQRSDKDNEFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIAKLIKYVFD--NRETE 156
Cdd:PLN02981 88 AGIAHTRWATHGPPAPRNSHPQSSGPGNEFLVVHNGIITNYEVLKETLLRHGFTFESDTDTEVIPKLAKFVFDklNEEEG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 157 DITFSTLVERVIQQLEGAFALVFKSIHYPGEAVATRRGSPLLIGVrskyKLSTEQipvlyptcnienvknicKTRMKRLD 236
Cdd:PLN02981 168 DVTFSQVVMEVMRQLEGAYALIFKSPHYPNELVACKRGSPLLLGV----KELPEE-----------------KNSSAVFT 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 237 SSTCLHAVGDKAVEFFFASDASAIIEHTNRVIFLEDDDIAAVADGKLSIHRVKRSATDDPS---------RAIQTLQMEL 307
Cdd:PLN02981 227 SEGFLTKNRDKPKEFFLASDASAVVEHTKRVLVIEDNEVVHLKDGGVGIYKFENEKGRGGGglsrpasveRALSTLEMEV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 308 QQIMKGNFSAFMQKEIFEQPESVFNTMRGRV----NFETNTVLLGGLKDHLKEIRRCRRLIVIGCGTSYHAAVATRQVLE 383
Cdd:PLN02981 307 EQIMKGNYDHYMQKEIHEQPESLTTTMRGRLirggSGKAKRVLLGGLKDHLKTIRRSRRIVFIGCGTSYNAALAARPILE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 384 ELTELPVMVELASDFLDRNTPVFRDDVCFFISQSGETADTLLALRYCKDRGALTVGITNTVGSSISRETDCGVHINAGPE 463
Cdd:PLN02981 387 ELSGVPVTMELASDLLDRQGPIYREDTAVFVSQSGETADTLRALEYAKENGALCVGITNTVGSAISRGTHCGVHINAGAE 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 464 IGVASTKAYTSQFISLVMFGLMMSEDRISLQNRRQEIIRGLRSLPELIKEVLSLDEKIHDLALELYTQRSLLVMGRGYNY 543
Cdd:PLN02981 467 IGVASTKAYTSQIVAMTMLALALGEDSISSRSRREAIIDGLFDLPNKVREVLKLDQEMKELAELLIDEQSLLVFGRGYNY 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 544 ATCLEGALKIKEITYMHSEGILAGELKHGPLALVDKQMPVIMVIMKDPCFAKCQNALQQVTARQGRPIILCSKDDtESSK 623
Cdd:PLN02981 547 ATALEGALKVKEVALMHSEGILAGEMKHGPLALVDETLPIIVIATRDACFSKQQSVIQQLRARKGRLIVICSKGD-ASSV 625
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 1907080035 624 FAYKT---IELPHTVDCLQGILSVIPLQLLSFHLAVLRGYDVDFPRNLAKSVTVE 675
Cdd:PLN02981 626 CPSGGcrvIEVPQVEDCLQPVINIVPLQLLAYHLTVLRGHNVDQPRNLAKSVTTQ 680
|
|
| GlmS |
COG0449 |
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ... |
9-675 |
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: 772.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 9 RKEIFETLIRGLQRLEYRGYDSAGVAIdgnnheVKERHIHLVKKRGKVKALDEELYKQDsmdlkveFETHFGIAHTRWAT 88
Cdd:COG0449 10 KRDAAPILLEGLKRLEYRGYDSAGIAV------LDDGGLEVRKAVGKLANLEEKLAEEP-------LSGTIGIGHTRWAT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 89 HGVPNAVNSHPQRSDkDNEFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIAKLIKYVFDnretEDITFSTLVERVI 168
Cdd:COG0449 77 HGAPSDENAHPHTSC-SGRIAVVHNGIIENYAELREELEAKGHTFKSETDTEVIAHLIEEYLK----GGGDLLEAVRKAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 169 QQLEGAFALVFKSIHYPGEAVATRRGSPLLIGVrskyklsteqipvlyptcnienvknicktrmkrldsstclhavGDKa 248
Cdd:COG0449 152 KRLEGAYALAVISADEPDRIVAARKGSPLVIGL-------------------------------------------GEG- 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 249 vEFFFASDASAIIEHTNRVIFLEDDDIAAVADGKLSIHRVKRSATDdpsRAIQTLQMELQQIMKGNFSAFMQKEIFEQPE 328
Cdd:COG0449 188 -ENFLASDVPALLPYTRRVIYLEDGEIAVLTRDGVEIYDLDGEPVE---REVKTVDWDAEAAEKGGYPHFMLKEIHEQPE 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 329 SVFNTMRGRVNfETNTVLLGGLKDHLKEIRRCRRLIVIGCGTSYHAAVATRQVLEELTELPVMVELASDFLDRNTPVFRD 408
Cdd:COG0449 264 AIRDTLRGRLD-EDGRVVLDELNLAAEDLRNIDRIYIVACGTSYHAGLVGKYLIEELARIPVEVEIASEFRYRDPVVDPG 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 409 DVCFFISQSGETADTLLALRYCKDRGALTVGITNTVGSSISRETDCGVHINAGPEIGVASTKAYTSQFISLVMFGLMMSE 488
Cdd:COG0449 343 TLVIAISQSGETADTLAALREAKEKGAKVLAICNVVGSTIARESDAVLYTHAGPEIGVASTKAFTTQLAALYLLALYLAR 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 489 DRISL-QNRRQEIIRGLRSLPELIKEVLSLDEKIHDLALELYTQRSLLVMGRGYNYATCLEGALKIKEITYMHSEGILAG 567
Cdd:COG0449 423 ARGTLsAEEEAELLEELRKLPEKIEEVLDLEEQIEELAEKYADARNALFLGRGINYPVALEGALKLKEISYIHAEGYAAG 502
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 568 ELKHGPLALVDKQMPVIMVIMKDPCFAKCQNALQQVTARQGRPIILCSKDDTESSKFAYKTIELPHTVDCLQGILSVIPL 647
Cdd:COG0449 503 ELKHGPIALIDEGMPVVAIAPQDELYEKTLSNIQEVKARGGKVIAIADEGDEEVEELADDVIEVPEVDELLAPILAVVPL 582
|
650 660
....*....|....*....|....*...
gi 1907080035 648 QLLSFHLAVLRGYDVDFPRNLAKSVTVE 675
Cdd:COG0449 583 QLLAYHVAVLRGTDVDQPRNLAKSVTVE 610
|
|
| PRK00331 |
PRK00331 |
isomerizing glutamine--fructose-6-phosphate transaminase; |
9-675 |
0e+00 |
|
isomerizing glutamine--fructose-6-phosphate transaminase;
Pssm-ID: 234729 [Multi-domain] Cd Length: 604 Bit Score: 720.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 9 RKEIFETLIRGLQRLEYRGYDSAGVAIdgnnheVKERHIHLVKKRGKVKALDEELyKQDSMdlkvefETHFGIAHTRWAT 88
Cdd:PRK00331 10 QRNAAEILLEGLKRLEYRGYDSAGIAV------LDDGGLEVRKAVGKVANLEAKL-EEEPL------PGTTGIGHTRWAT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 89 HGVPNAVNSHPQRsDKDNEFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIAKLIKYVFDNretediTFSTL--VER 166
Cdd:PRK00331 77 HGKPTERNAHPHT-DCSGRIAVVHNGIIENYAELKEELLAKGHVFKSETDTEVIAHLIEEELKE------GGDLLeaVRK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 167 VIQQLEGAFALVFKSIHYPGEAVATRRGSPLLIGVrskyklsteqipvlyptcnienvknicktrmkrldsstclhavGD 246
Cdd:PRK00331 150 ALKRLEGAYALAVIDKDEPDTIVAARNGSPLVIGL-------------------------------------------GE 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 247 KavEFFFASDASAIIEHTNRVIFLEDDDIAAVADGKLSIHrvkrSATDDP-SRAIQTLQMELQQIMKGNFSAFMQKEIFE 325
Cdd:PRK00331 187 G--ENFLASDALALLPYTRRVIYLEDGEIAVLTRDGVEIF----DFDGNPvEREVYTVDWDASAAEKGGYRHFMLKEIYE 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 326 QPESVFNTMRGRVNFetntvlLGGLKDHLKEIRRCRRLIVIGCGTSYHAAVATRQVLEELTELPVMVELASDFLDRNTPV 405
Cdd:PRK00331 261 QPEAIRDTLEGRLDE------LGEGELADEDLKKIDRIYIVACGTSYHAGLVAKYLIESLAGIPVEVEIASEFRYRDPVL 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 406 FRDDVCFFISQSGETADTLLALRYCKDRGALTVGITNTVGSSISRETDCGVHINAGPEIGVASTKAYTSQFISLVMFGLM 485
Cdd:PRK00331 335 SPKTLVIAISQSGETADTLAALRLAKELGAKTLAICNVPGSTIARESDAVLYTHAGPEIGVASTKAFTAQLAVLYLLALA 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 486 MSEDRISLQNRR-QEIIRGLRSLPELIKEVLSLDEKIHDLALELYTQRSLLVMGRGYNYATCLEGALKIKEITYMHSEGI 564
Cdd:PRK00331 415 LAKARGTLSAEEeADLVHELRELPALIEQVLDLKEQIEELAEDFADARNALFLGRGVDYPVALEGALKLKEISYIHAEGY 494
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 565 LAGELKHGPLALVDKQMPVIMVIMKDPCFAKCQNALQQVTARQGRPIILCSKDDTESSKFAYkTIELPHTVDCLQGILSV 644
Cdd:PRK00331 495 AAGELKHGPIALIDEGMPVVAIAPNDELYEKTKSNIQEVKARGARVIVIADEGDEVAEEADD-VIEVPEVHELLAPLLYV 573
|
650 660 670
....*....|....*....|....*....|.
gi 1907080035 645 IPLQLLSFHLAVLRGYDVDFPRNLAKSVTVE 675
Cdd:PRK00331 574 VPLQLLAYHVALARGTDVDKPRNLAKSVTVE 604
|
|
| PTZ00394 |
PTZ00394 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
2-675 |
0e+00 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 173585 [Multi-domain] Cd Length: 670 Bit Score: 683.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 2 NYRVPKTRKEIFETLIRGLQRLEYRGYDSAGVAIDGNNHEVKE----------RHIhLVKKRGKVKALDEELYKQDS--- 68
Cdd:PTZ00394 9 NHNVPRTVEQILNVLLDGIQKVEYRGYDSAGLAIDANIGSEKEdgtaasaptpRPC-VVRSVGNISQLREKVFSEAVaat 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 69 -MDLKVEFETHFGIAHTRWATHGVPNAVNSHPQRSDkDNEFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIAKLIK 147
Cdd:PTZ00394 88 lPPMDATTSHHVGIAHTRWATHGGVCERNCHPQQSN-NGEFTIVHNGIVTNYMTLKELLKEEGYHFSSDTDTEVISVLSE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 148 YVFDNRETedITFSTLVERVIQQLEGAFALVFKSIHYPGEAVATRRGSPLLIGVRskyklsteqipvlyptcnienvkni 227
Cdd:PTZ00394 167 YLYTRKGI--HNFADLALEVSRMVEGSYALLVKSVYFPGQLAASRKGSPLMVGIR------------------------- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 228 cktrmkRLDSSTCL-----HAVGD--KAVEFFFASDASAIIEHTNRVIFLEDDDIAAVADGKLSIHRVKRSATDDPSRAI 300
Cdd:PTZ00394 220 ------RTDDRGCVmklqtYDLTDlsGPLEVFFSSDVNSFAEYTREVVFLEDGDIAHYCDGALRFYNAAERQRSIVKREV 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 301 QTLQMELQQIMKGNFSAFMQKEIFEQPESVFNTMRGRVNFETNTVLLGGLKDH-LKEIRRCRRLIVIGCGTSYHAAVATR 379
Cdd:PTZ00394 294 QHLDAKPEGLSKGNYPHFMLKEIYEQPESVISSMHGRIDFSSGTVQLSGFTQQsIRAILTSRRILFIACGTSLNSCLAVR 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 380 QVLEELTELPVMVELASDFLDRNTPVFRDDVCFFISQSGETADTLLALRYCKDRGALTVGITNTVGSSISRETDCGVHIN 459
Cdd:PTZ00394 374 PLFEELVPLPISVENASDFLDRRPRIQRDDVCFFVSQSGETADTLMALQLCKEAGAMCVGITNVVGSSISRLTHYAIHLN 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 460 AGPEIGVASTKAYTSQFISLVMFGLMMSEDRISLQNRRQEIIRGLRSLPELIKEVLSL-DEKIHDLALELYTQRSLLVMG 538
Cdd:PTZ00394 454 AGVEVGVASTKAYTSQVVVLTLVALLLSSDSVRLQERRNEIIRGLAELPAAISECLKItHDPVKALAARLKESSSILVLG 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 539 RGYNYATCLEGALKIKEITYMHSEGILAGELKHGPLALVDKQMPVIMVIMKDPCFAKCQNALQQVTARQGRPIILCSKDD 618
Cdd:PTZ00394 534 RGYDLATAMEAALKVKELSYVHTEGIHSGELKHGPLALIDETSPVLAMCTHDKHFGLSKSAVQQVKARGGAVVVFATEVD 613
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907080035 619 TESSKFAYKTIELPHTVDCLQGILSVIPLQLLSFHLAVLRGYDVDFPRNLAKSVTVE 675
Cdd:PTZ00394 614 AELKAAASEIVLVPKTVDCLQCVVNVIPFQLLAYYMALLRGNNVDCPRNLAKSVTVQ 670
|
|
| glmS |
TIGR01135 |
glucosamine--fructose-6-phosphate aminotransferase (isomerizing); The member from ... |
16-675 |
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: 640.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 16 LIRGLQRLEYRGYDSAGVAIdgnnheVKERHIHLVKKRGKVKALDEELYKQdsmdlkvEFETHFGIAHTRWATHGVPNAV 95
Cdd:TIGR01135 16 LLEGLKRLEYRGYDSAGIAV------VDEGKLFVRKAVGKVAELANKLGEK-------PLPGGVGIGHTRWATHGKPTDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 96 NSHPQRsDKDNEFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIAKLIKYVFdnRETEDITFStlVERVIQQLEGAF 175
Cdd:TIGR01135 83 NAHPHT-DEGGRIAVVHNGIIENYAELREELEARGHVFSSDTDTEVIAHLIEEEL--REGGDLLEA--VQKALKQLRGAY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 176 ALVFKSIHYPGEAVATRRGSPLLIGVrskyklsteqipvlyptcnienvknicktrmkrldsstclhavGDKavEFFFAS 255
Cdd:TIGR01135 158 ALAVLHADHPETLVAARSGSPLIVGL-------------------------------------------GDG--ENFVAS 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 256 DASAIIEHTNRVIFLEDDDIAAVADGKLSIHrvkrSATDDP-SRAIQTLQMELQQIMKGNFSAFMQKEIFEQPESVFNTM 334
Cdd:TIGR01135 193 DVTALLPYTRRVIYLEDGDIAILTKDGVEIY----NFEGAPvQREVRVIDWDLDAAEKGGYRHFMLKEIYEQPRALRDTL 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 335 RGRVNFETNTVLLGGLKDHLKEIRRcrrLIVIGCGTSYHAAVATRQVLEELTELPVMVELASDFLDRNTPVFRDDVCFFI 414
Cdd:TIGR01135 269 EGRIEENGGVFEELGAEELLKNIDR---IQIVACGTSYHAGLVAKYLIERLAGIPVEVEIASEFRYRKPVVDKDTLVIAI 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 415 SQSGETADTLLALRYCKDRGALTVGITNTVGSSISRETDCGVHINAGPEIGVASTKAYTSQFISLVMFGLMMSEDR-ISL 493
Cdd:TIGR01135 346 SQSGETADTLEALRLAKELGAKTLGICNVPGSTLVREADHTLYTRAGPEIGVASTKAFTTQLTVLYLLALALAKARgTLS 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 494 QNRRQEIIRGLRSLPELIKEVLSLDEKIHDLALELYTQRSLLVMGRGYNYATCLEGALKIKEITYMHSEGILAGELKHGP 573
Cdd:TIGR01135 426 AEEEAELVDALRRLPDLVEQVLLADESIAELAERYADKRNFLFLGRGLGYPIALEGALKLKEISYIHAEGYPAGELKHGP 505
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 574 LALVDKQMPVIMVIMKDPCFAKCQNALQQVTARQGRPIILCSKDDTESSKFAYKTIELPHTVDCLQGILSVIPLQLLSFH 653
Cdd:TIGR01135 506 IALIDEGLPVVAIAPKDSLLEKTKSNVEEVKARGARVIVFAPEDDETIASVADDVIKLPEVEELLAPIVYTIPLQLLAYH 585
|
650 660
....*....|....*....|..
gi 1907080035 654 LAVLRGYDVDFPRNLAKSVTVE 675
Cdd:TIGR01135 586 IALAKGTDVDKPRNLAKSVTVE 607
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
14-674 |
5.56e-154 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 459.49 E-value: 5.56e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 14 ETLIRGLQRLEYRGYDSAGVA-IDGNNHEVKERHIHLVKKRGKVKALDEELykqdsmdLKVEFETHFGIAHTRWATHGVP 92
Cdd:PTZ00295 38 KILLEGIEILQNRGYDSCGIStISSGGELKTTKYASDGTTSDSIEILKEKL-------LDSHKNSTIGIAHTRWATHGGK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 93 NAVNSHPQrSDKDNEFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIAKLIKYVFDNRETeditFSTLVERVIQQLE 172
Cdd:PTZ00295 111 TDENAHPH-CDYKKRIALVHNGTIENYVELKSELIAKGIKFRSETDSEVIANLIGLELDQGED----FQEAVKSAISRLQ 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 173 GAFALVFKSIHYPGEAVATRRGSPLLIGVRSKyklsteqipvlyptcnienvknicktrmkrldsstclhavgdkavEFF 252
Cdd:PTZ00295 186 GTWGLCIIHKDNPDSLIVARNGSPLLVGIGDD---------------------------------------------SIY 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 253 FASDASAIIEHTNRVIFLEDDDIAavadgklSIHRVKRSATDDPSRAIQtLQMELQQIMKGNFSAFMQKEIFEQPESVFN 332
Cdd:PTZ00295 221 VASEPSAFAKYTNEYISLKDGEIA-------ELSLENVNDLYTQRRVEK-IPEEVIEKSPEPYPHWTLKEIFEQPIALSR 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 333 TM--RGRVNFETNTVLLGGLKDHLKEIRRCRRLIVIGCGTSYHAAVATRQVLEELTEL-PVMVELASDF-LDRNTpvfRD 408
Cdd:PTZ00295 293 ALnnGGRLSGYNNRVKLGGLDQYLEELLNIKNLILVGCGTSYYAALFAASIMQKLKCFnTVQVIDASELtLYRLP---DE 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 409 DVCF-FISQSGETADTLLALRYCKDRGALTVGITNTVGSSISRETDCGVHINAGPEIGVASTKAYTSQFISLVMFGLMMS 487
Cdd:PTZ00295 370 DAGViFISQSGETLDVVRALNLADELNLPKISVVNTVGSLIARSTDCGVYLNAGREVAVASTKAFTSQVTVLSLIALWFA 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 488 E--DRISLQNRRQEIIRGLRSLPELIKEVL-SLDEKIHDLALELYTQRSLLVMGRGYNYATCLEGALKIKEITYMHSEGI 564
Cdd:PTZ00295 450 QnkEYSCSNYKCSSLINSLHRLPTYIGMTLkSCEEQCKRIAEKLKNAKSMFILGKGLGYPIALEGALKIKEITYIHAEGF 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 565 LAGELKHGPLALVD--KQMPVIMVIMKDPCFAKCQNALQQVTARQGRPIILCSkDDTESSKFAYKTIELPhTVDCLQGIL 642
Cdd:PTZ00295 530 SGGALKHGPFALIDkeKNTPVILIILDDEHKELMINAAEQVKARGAYIIVITD-DEDLVKDFADEIILIP-SNGPLTALL 607
|
650 660 670
....*....|....*....|....*....|..
gi 1907080035 643 SVIPLQLLSFHLAVLRGYDVDFPRNLAKSVTV 674
Cdd:PTZ00295 608 AVIPLQLLAYEIAILRGINPDKPRGLAKTVTV 639
|
|
| GFAT |
cd00714 |
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ... |
9-278 |
7.43e-106 |
|
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: 320.16 E-value: 7.43e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 9 RKEIFETLIRGLQRLEYRGYDSAGVAIDGNNHevkerhIHLVKKRGKVKALDEELYKQDSmdlkvefETHFGIAHTRWAT 88
Cdd:cd00714 9 KREAVDILLEGLKRLEYRGYDSAGIAVIGDGS------LEVVKAVGKVANLEEKLAEKPL-------SGHVGIGHTRWAT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 89 HGVPNAVNSHPQRSDkDNEFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIAKLIKYVFDnretEDITFSTLVERVI 168
Cdd:cd00714 76 HGEPTDVNAHPHRSC-DGEIAVVHNGIIENYAELKEELEAKGYKFESETDTEVIAHLIEYYYD----GGLDLLEAVKKAL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 169 QQLEGAFALVFKSIHYPGEAVATRRGSPLLIGVrskyklsteqipvlyptcnienvknicktrmkrldsstclhavgdKA 248
Cdd:cd00714 151 KRLEGAYALAVISKDEPDEIVAARNGSPLVIGI---------------------------------------------GD 185
|
250 260 270
....*....|....*....|....*....|
gi 1907080035 249 VEFFFASDASAIIEHTNRVIFLEDDDIAAV 278
Cdd:cd00714 186 GENFVASDAPALLEHTRRVIYLEDGDIAVI 215
|
|
| AgaS |
COG2222 |
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ... |
321-675 |
1.30e-71 |
|
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: 235.56 E-value: 1.30e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 321 KEIFEQPESVfntmrgRVNFETNTVLLGGLKDHLKEIRRcRRLIVIGCGTSYHAAVATRQVLEELTELPVMVELASDFLD 400
Cdd:COG2222 2 REIAQQPEAW------RRALAALAAAIAALLARLRAKPP-RRVVLVGAGSSDHAAQAAAYLLERLLGIPVAALAPSELVV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 401 RNTPVFRD-DVCFFISQSGETADTLLALRYCKDRGALTVGITNTVGSSISRETDCGVHINAGPEIGVASTKAYTSQFISL 479
Cdd:COG2222 75 YPAYLKLEgTLVVAISRSGNSPEVVAALELAKARGARTLAITNNPDSPLAEAADRVLPLPAGPEKSVAATKSFTTMLLAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 480 VMFGLMMSEDrislqnrrQEIIRGLRSLPELIKEVLSLDEKIHDLAlELYTQRSLLVMGRGYNYATCLEGALKIKEITYM 559
Cdd:COG2222 155 LALLAAWGGD--------DALLAALDALPAALEAALAADWPAAALA-ALADAERVVFLGRGPLYGLAREAALKLKELSAG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 560 HSEGILAGELKHGPLALVDKQMPVIMVIMKDPCFAKCQNALQQVTARQGRPIILCSKDDTEsskfayktIELPHTVDC-- 637
Cdd:COG2222 226 HAEAYSAAEFRHGPKSLVDPGTLVVVLASEDPTRELDLDLAAELRALGARVVAIGAEDDAA--------ITLPAIPDLhd 297
|
330 340 350
....*....|....*....|....*....|....*....
gi 1907080035 638 -LQGILSVIPLQLLSFHLAVLRGYDVDFPRNLAKSVTVE 675
Cdd:COG2222 298 aLDPLLLLVVAQRLALALALARGLDPDTPRHLNKVVKTV 336
|
|
| SIS_GlmS_GlmD_2 |
cd05009 |
SIS (Sugar ISomerase) domain repeat 2 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
519-673 |
4.68e-66 |
|
SIS (Sugar ISomerase) domain repeat 2 found in Glucosamine 6-phosphate synthase (GlmS) and Glucosamine-6-phosphate deaminase (GlmD). The SIS domain is found in many phosphosugar isomerases and phosphosugar binding proteins. GlmS contains a N-terminal glutaminase domain and two C-terminal SIS domains and catalyzes the first step in hexosamine metabolism, converting fructose 6-phosphate into glucosamine 6-phosphate using glutamine as nitrogen source. The glutaminase domain hydrolyzes glutamine to glutamate and ammonia. Ammonia is transferred through a channel to the isomerase domain for glucosamine 6-phosphate synthesis. The end product of the pathway is N-acetylglucosamine, which plays multiple roles in eukaryotic cells including being a building block of bacterial and fungal cell walls. In the absence of glutamine, GlmS catalyzes the isomerization of fructose 6-phosphate into glucose 6- phosphate (PGI-like activity). Glucosamine-6-phosphate deaminase (GlmD) contains two SIS domains and catalyzes the deamination and isomerization of glucosamine-6-phosphate into fructose-6-phosphate with the release of ammonia; in presence of high ammonia concentration, GlmD can catalyze the reverse reaction.
Pssm-ID: 240142 [Multi-domain] Cd Length: 153 Bit Score: 214.05 E-value: 4.68e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 519 EKIHDLALELYTQRSLLVMGRGYNYATCLEGALKIKEITYMHSEGILAGELKHGPLALVDKQMPVIMVIMKDPCFAKCQN 598
Cdd:cd05009 1 EDIKELAEKLKEAKSFYVLGRGPNYGTALEGALKLKETSYIHAEAYSAGEFKHGPIALVDEGTPVIFLAPEDRLEEKLES 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907080035 599 ALQQVTARQGRPIILCSKDDTEssKFAYKTIELPHTVDCLQGILSVIPLQLLSFHLAVLRGYDVDFPRNLAKSVT 673
Cdd:cd05009 81 LIKEVKARGAKVIVITDDGDAK--DLADVVIRVPATVEELSPLLYIVPLQLLAYHLAVARGIDPDKPRNLAKSVT 153
|
|
| SIS_GlmS_GlmD_1 |
cd05008 |
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
362-487 |
5.87e-62 |
|
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: 202.34 E-value: 5.87e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 362 RLIVIGCGTSYHAAVATRQVLEELTELPVMVELASDFLDRNTPVFRDDVCFFISQSGETADTLLALRYCKDRGALTVGIT 441
Cdd:cd05008 1 RILIVGCGTSYHAALVAKYLLERLAGIPVEVEAASEFRYRRPLLDEDTLVIAISQSGETADTLAALRLAKEKGAKTVAIT 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1907080035 442 NTVGSSISRETDCGVHINAGPEIGVASTKAYTSQFISLVMFGLMMS 487
Cdd:cd05008 81 NVVGSTLAREADYVLYLRAGPEISVAATKAFTSQLLALLLLALALA 126
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
3-276 |
3.71e-48 |
|
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: 168.78 E-value: 3.71e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 3 YRVPKTRKEIFETLIRGLQRLEYRGYDSAGVAIDGNnhevkeRHIHLVKKRGKVKALDEELykqdsmdLKVEFETHFGIA 82
Cdd:cd00352 7 VGADGAASLLLLLLLRGLAALEHRGPDGAGIAVYDG------DGLFVEKRAGPVSDVALDL-------LDEPLKSGVALG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 83 HTRWATHGVPNAVNSHPQRSDkDNEFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIAKLIKYVFDNRETEDitfst 162
Cdd:cd00352 74 HVRLATNGLPSEANAQPFRSE-DGRIALVHNGEIYNYRELREELEARGYRFEGESDSEVILHLLERLGREGGLFE----- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 163 LVERVIQQLEGAFALVFKSIHyPGEAVATRRG---SPLLIGVRskyklsteqipvlyptcnienvknicktrmkrldsst 239
Cdd:cd00352 148 AVEDALKRLDGPFAFALWDGK-PDRLFAARDRfgiRPLYYGIT------------------------------------- 189
|
250 260 270
....*....|....*....|....*....|....*...
gi 1907080035 240 clhavgdKAVEFFFASDASAIIEHT-NRVIFLEDDDIA 276
Cdd:cd00352 190 -------KDGGLVFASEPKALLALPfKGVRRLPPGELL 220
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
356-485 |
1.20e-40 |
|
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: 144.75 E-value: 1.20e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 356 EIRRCRRLIVIGCGTSYHAAVATRQVLEELTELPVMVELASDFLDR-NTPVFRDDVCFFISQSGETADTLLALRYCKDRG 434
Cdd:pfam01380 1 LLAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGvLALVDEDDLVIAISYSGETKDLLAAAELAKARG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1907080035 435 ALTVGITNTVGSSISRETDCGVHINAGPEIGVASTKAYTSQFISLVMFGLM 485
Cdd:pfam01380 81 AKIIAITDSPGSPLAREADHVLYINAGPETGVASTKSITAQLAALDALAVA 131
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
527-658 |
9.36e-27 |
|
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars. Presumably the SIS domains bind to the end-product of the pathway.
Pssm-ID: 426230 [Multi-domain] Cd Length: 131 Bit Score: 105.46 E-value: 9.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 527 ELYTQRSLLVMGRGYNYATCLEGALKIKEITYMHSEGILAGELKHGPLALVDKQMPVIMVIMKDPCFAKCQnALQQVTAR 606
Cdd:pfam01380 1 LLAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGVLALVDEDDLVIAISYSGETKDLLA-AAELAKAR 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1907080035 607 QGRPIILCSKDDTESSKFAYKTIELPHTVDCLQGILSVIPLQLLSFHLAVLR 658
Cdd:pfam01380 80 GAKIIAITDSPGSPLAREADHVLYINAGPETGVASTKSITAQLAALDALAVA 131
|
|
| GPATase_N |
cd00715 |
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ... |
19-179 |
1.15e-21 |
|
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: 94.83 E-value: 1.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 19 GLQRLEYRGYDSAGVAIDGNNHevkerhIHLVKKRGKVkaldEELYKQDSMDlkvEFETHFGIAHTRWATHGVPNAVNSH 98
Cdd:cd00715 19 GLYALQHRGQESAGIATSDGKR------FHTHKGMGLV----SDVFDEEKLR---RLPGNIAIGHVRYSTAGSSSLENAQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 99 PQRSD-KDNEFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIAKLIKyvfdnRETEDITFSTLVERVIQQLEGAFAL 177
Cdd:cd00715 86 PFVVNsPLGGIALAHNGNLVNAKELREELEEEGRIFQTTSDSEVILHLIA-----RSLAKDDLFEAIIDALERVKGAYSL 160
|
..
gi 1907080035 178 VF 179
Cdd:cd00715 161 VI 162
|
|
| PurF |
COG0034 |
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ... |
16-179 |
1.08e-20 |
|
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: 95.47 E-value: 1.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 16 LIRGLQRLEYRGYDSAG-VAIDGNnhevkerHIHLVKKRGKVKaldeELYKQDSMDlkvEFETHFGIAHTRWATHGVPNA 94
Cdd:COG0034 23 TYYGLYALQHRGQESAGiATSDGG-------RFHLHKGMGLVS----DVFDEEDLE---RLKGNIAIGHVRYSTTGSSSL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 95 VNSHP-QRSDKDNEFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIAKLIKyvfdnRETEDITFSTLVERVIQQLEG 173
Cdd:COG0034 89 ENAQPfYVNSPFGSIALAHNGNLTNAEELREELEEEGAIFQTTSDTEVILHLIA-----RELTKEDLEEAIKEALRRVKG 163
|
....*.
gi 1907080035 174 AFALVF 179
Cdd:COG0034 164 AYSLVI 169
|
|
| purF |
TIGR01134 |
amidophosphoribosyltransferase; Alternate name: glutamine phosphoribosylpyrophosphate (PRPP) ... |
19-210 |
2.96e-17 |
|
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: 84.68 E-value: 2.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 19 GLQRLEYRGYDSAGVAIDGNNHevkerhIHLVKKRGKVKaldeELYKQDSMDlkvEFETHFGIAHTRWATHGVPNAVNSH 98
Cdd:TIGR01134 20 GLYALQHRGQESAGISVFDGNR------FRLHKGNGLVS----DVFNEEHLQ---RLKGNVGIGHVRYSTAGSSGLENAQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 99 PQRSDKDNEFVVI-HNGIITNYKDLRKFLESKGYEFESETDTETIAKLIKyvfdNRETEDITFSTLVERVIQQLEGAFAL 177
Cdd:TIGR01134 87 PFVVNSPYGGLALaHNGNLVNADELRRELEEEGRHFNTTSDSEVLLHLLA----HNDESKDDLFDAVARVLERVRGAYAL 162
|
170 180 190
....*....|....*....|....*....|....*..
gi 1907080035 178 VFKSIHypgEAVATR--RG-SPLLIGVR-SKYKLSTE 210
Cdd:TIGR01134 163 VLMTED---GLVAVRdpHGiRPLVLGRRgDGYVVASE 196
|
|
| PLN02440 |
PLN02440 |
amidophosphoribosyltransferase |
19-203 |
4.13e-16 |
|
amidophosphoribosyltransferase
Pssm-ID: 215241 [Multi-domain] Cd Length: 479 Bit Score: 81.65 E-value: 4.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 19 GLQRLEYRGYDSAG-VAIDGNNhevkerhIHLVKKRGKVKaldeELYKQDSMDlkvEFETHFGIAHTRWATHGVPNAVNS 97
Cdd:PLN02440 20 GLHALQHRGQEGAGiVTVDGNR-------LQSITGNGLVS----DVFDESKLD---QLPGDIAIGHVRYSTAGASSLKNV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 98 HPqrsdkdneFV---------VIHNGIITNYKDLRKFLESKGYEFESETDTETIAKLIkyvfdnreTEDI--TFSTLVER 166
Cdd:PLN02440 86 QP--------FVanyrfgsigVAHNGNLVNYEELRAKLEENGSIFNTSSDTEVLLHLI--------AISKarPFFSRIVD 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1907080035 167 VIQQLEGAFALVFKSihyPGEAVATR-----RgsPLLIGVRS 203
Cdd:PLN02440 150 ACEKLKGAYSMVFLT---EDKLVAVRdphgfR--PLVMGRRS 186
|
|
| GATase_6 |
pfam13522 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
75-179 |
8.63e-16 |
|
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: 74.26 E-value: 8.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 75 FETHFGIAHTRWATHGVPNAVNsHPQRSdKDNEFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIAKLIKYvfdnre 154
Cdd:pfam13522 8 VEGGVALGHVRLAIVDLPDAGN-QPMLS-RDGRLVLVHNGEIYNYGELREELADLGHAFRSRSDTEVLLALYEE------ 79
|
90 100
....*....|....*....|....*
gi 1907080035 155 teditfstLVERVIQQLEGAFALVF 179
Cdd:pfam13522 80 --------WGEDCLERLRGMFAFAI 96
|
|
| SIS_1 |
cd05710 |
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ... |
362-485 |
9.77e-15 |
|
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: 71.07 E-value: 9.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 362 RLIVIGCGTSYHAAVATRQVLEELTELPVMVELASDFLDRNTPVFRDD-VCFFISQSGETADTLLALRYCKDRGALTVGI 440
Cdd:cd05710 1 NVFFVGCGGSLADMYPAKYFLKKESKLPVFVYNAAEFLHTGPKRLTEKsVVILASHSGNTKETVAAAKFAKEKGATVIGL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1907080035 441 TNTVGSSISRETDcgVHINAGPEIGVASTKAYtsqFISLVMFGLM 485
Cdd:cd05710 81 TDDEDSPLAKLAD--YVIVYGFEIDAVEEKYL---LLYMLALRLL 120
|
|
| PRK05793 |
PRK05793 |
amidophosphoribosyltransferase; Provisional |
19-178 |
1.62e-14 |
|
amidophosphoribosyltransferase; Provisional
Pssm-ID: 235611 [Multi-domain] Cd Length: 469 Bit Score: 76.61 E-value: 1.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 19 GLQRLEYRGYDSAGVAI-DGnnhevkeRHIHLVKKRGKV-KALDEELYKqdsmdlkvEFETHFGIAHTRWATHGVPNAVN 96
Cdd:PRK05793 35 GLYALQHRGQESAGIAVsDG-------EKIKVHKGMGLVsEVFSKEKLK--------GLKGNSAIGHVRYSTTGASDLDN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 97 SHPQRSDKDNEFVVI-HNGIITNYKDLRKFLESKGYEFESETDTETIAKLI----KYVFDNreteditfsTLVErVIQQL 171
Cdd:PRK05793 100 AQPLVANYKLGSIAIaHNGNLVNADVIRELLEDGGRIFQTSIDSEVILNLIarsaKKGLEK---------ALVD-AIQAI 169
|
....*..
gi 1907080035 172 EGAFALV 178
Cdd:PRK05793 170 KGSYALV 176
|
|
| GATase_7 |
pfam13537 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
83-178 |
6.68e-14 |
|
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: 68.70 E-value: 6.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 83 HTRWATHGVPNAvnSHPQRSDKDNEFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIAKLIKYVFdnreteditfst 162
Cdd:pfam13537 1 HRRLSIIDLEGG--AQPMVSSEDGRYVIVFNGEIYNYRELRAELEAKGYRFRTHSDTEVILHLYEAEW------------ 66
|
90
....*....|....*.
gi 1907080035 163 lVERVIQQLEGAFALV 178
Cdd:pfam13537 67 -GEDCVDRLNGMFAFA 81
|
|
| GlxB |
cd01907 |
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ... |
14-148 |
5.23e-12 |
|
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: 66.52 E-value: 5.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 14 ETLIRGLQRLEYRG-YDSAGVAIDGNNHEvkerhihLVKKRGKvkalDEELYKQ--------DSMDLKvEFETHFGIAHT 84
Cdd:cd01907 17 ALLVEMLDAMQERGpGDGAGFALYGDPDA-------FVYSSGK----DMEVFKGvgypediaRRYDLE-EYKGYHWIAHT 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907080035 85 RWATHGVPNAVNSHPqrsdkdneF-----VVIHNGIITNYKDLRKFLESKGYEFESETDTETIAKLIKY 148
Cdd:cd01907 85 RQPTNSAVWWYGAHP--------FsigdiAVVHNGEISNYGSNREYLERFGYKFETETDTEVIAYYLDL 145
|
|
| SIS |
cd04795 |
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
363-441 |
3.10e-11 |
|
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: 60.08 E-value: 3.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 363 LIVIGCGTSYHAAVATRQVLEELTELPVMVELASDFLDRNTPVF--RDDVCFFISQSGETADTLLALRYCKDRGALTVGI 440
Cdd:cd04795 1 IFVIGIGGSGAIAAYFALELLELTGIEVVALIATELEHASLLSLlrKGDVVIALSYSGRTEELLAALEIAKELGIPVIAI 80
|
.
gi 1907080035 441 T 441
Cdd:cd04795 81 T 81
|
|
| murQ |
PRK05441 |
N-acetylmuramic acid-6-phosphate etherase; Reviewed |
414-485 |
9.90e-11 |
|
N-acetylmuramic acid-6-phosphate etherase; Reviewed
Pssm-ID: 235467 [Multi-domain] Cd Length: 299 Bit Score: 63.26 E-value: 9.90e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907080035 414 ISQSGETADTLLALRYCKDRGALTVGITNTVGSSISRETDCGVHINAGPEIGVAST--KAYTSQFISLVMF--GLM 485
Cdd:PRK05441 138 IAASGRTPYVIGALEYARERGALTIGISCNPGSPLSKEADIAIEVVVGPEVLTGSTrmKAGTAQKLVLNMIstGVM 213
|
|
| SIS_Etherase |
cd05007 |
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ... |
395-502 |
1.15e-10 |
|
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: 62.54 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 395 ASDFLDRNTPvfRDDVCFFISQSGETADTLLALRYCKDRGALTVGITNTVGSSISRETDCGVHINAGPEIGVAST--KAY 472
Cdd:cd05007 108 AADLQAINLT--ERDVVIGIAASGRTPYVLGALRYARARGALTIGIACNPGSPLLQLADIAIALITGPEVVAGSTrlKAG 185
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1907080035 473 TSQFISLVMF-------------GLM--MSEDRISLQNRRQEIIR 502
Cdd:cd05007 186 TAQKLALNMLstavmirlgkvygNLMvdVRATNEKLRERAIRIVM 230
|
|
| SIS_RpiR |
cd05013 |
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ... |
357-481 |
2.91e-10 |
|
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: 58.78 E-value: 2.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 357 IRRCRRLIVIGCGTSYHAA--VATRqvleeLTELPVMVELASD---FLDRNTPVFRDDVCFFISQSGETADTLLALRYCK 431
Cdd:cd05013 10 LAKARRIYIFGVGSSGLVAeyLAYK-----LLRLGKPVVLLSDphlQLMSAANLTPGDVVIAISFSGETKETVEAAEIAK 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1907080035 432 DRGALTVGITNTVGSSISRETDcgVHINAGPEIGVASTKAYTSQFISLVM 481
Cdd:cd05013 85 ERGAKVIAITDSANSPLAKLAD--IVLLVSSEEGDFRSSAFSSRIAQLAL 132
|
|
| RpiR |
COG1737 |
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ... |
357-507 |
9.17e-10 |
|
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains [Transcription];
Pssm-ID: 441343 [Multi-domain] Cd Length: 286 Bit Score: 60.33 E-value: 9.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 357 IRRCRRLIVIGCGTSYHAAVATRQVLEEL----TELPVMVELASDFLDRNTPvfrDDVCFFISQSGETADTLLALRYCKD 432
Cdd:COG1737 131 LAKARRIYIFGVGASAPVAEDLAYKLLRLgknvVLLDGDGHLQAESAALLGP---GDVVIAISFSGYTRETLEAARLAKE 207
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907080035 433 RGALTVGITNTVGSSISRETDcgVHINAGPEIGVASTKAYTSQFISLVM----FGLMMSEDRISLQNRRQEIIRGLRSL 507
Cdd:COG1737 208 RGAKVIAITDSPLSPLAKLAD--VVLYVPSEEPTLRSSAFSSRVAQLALidalAAAVAQRDGDKARERLERTEALLSEL 284
|
|
| frlB |
PRK11382 |
fructoselysine 6-phosphate deglycase; |
358-663 |
1.30e-09 |
|
fructoselysine 6-phosphate deglycase;
Pssm-ID: 183111 [Multi-domain] Cd Length: 340 Bit Score: 60.40 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 358 RRCRRLIVIGCGTSYHAAVATRQVLEELTELPVMVELASDFLDrNTPVFRDDVCFFI--SQSGETADTLLALRYCKDRGA 435
Cdd:PRK11382 42 RDIDRIYFVACGSPLNAAQTAKHLADRFSDLQVYAISGWEFCD-NTPYRLDDRCAVIgvSDYGKTEEVIKALELGRACGA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 436 LTVGITNTVGSSISRETDCGVHINAGP--EIGVASTKAYTSQFISlvmfglmmsedRISLQNRRQEIIRGLRSLPELIKE 513
Cdd:PRK11382 121 LTAAFTKRADSPITSAAEFSIDYQADCiwEIHLLLCYSVVLEMIT-----------RLAPNAEIGKIKNDLKQLPNALGH 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 514 -VLSLDEKIHDLALE------LYTQRSLLVMGRGYNyatclEGALKIKEITYMHSEGILAGELKHGPLALVDKQMPVIMV 586
Cdd:PRK11382 190 lVRTWEEKGRQLGELasqwpmIYTVAAGPLRPLGYK-----EGIVTLMEFTWTHGCVIESGEFRHGPLEIVEPGVPFLFL 264
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907080035 587 IMKDPCFAKCQNALQQVTARQGRPIILcskDDTESSKFAYKtielphtvdCLQGILSVIPLQLLSFHLAVLRGYDVD 663
Cdd:PRK11382 265 LGNDESRHTTERAINFVKQRTDNVIVI---DYAEISQGLHP---------WLAPFLMFVPMEWLCYYLSIYKDHNPD 329
|
|
| SIS_Kpsf |
cd05014 |
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ... |
361-482 |
1.34e-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: 56.40 E-value: 1.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 361 RRLIVIGCGTSYHAA---VATRQVleelTELPvmvelaSDFLDrntP----------VFRDDVCFFISQSGETADTLLAL 427
Cdd:cd05014 1 GKVVVTGVGKSGHIArkiAATLSS----TGTP------AFFLH---PtealhgdlgmVTPGDVVIAISNSGETDELLNLL 67
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907080035 428 RYCKDRGALTVGITNTVGSSISRETD----CGVHINAGPeIGVASTkayTSQFISLVMF 482
Cdd:cd05014 68 PHLKRRGAPIIAITGNPNSTLAKLSDvvldLPVEEEACP-LGLAPT---TSTTAMLALG 122
|
|
| AsnB |
cd00712 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ... |
14-145 |
1.94e-09 |
|
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: 58.34 E-value: 1.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 14 ETLIRGLQRLEYRGYDSAGVAIDGNnhevkerhihlvkkrgkvkaldeelykqdsmdlkvefethFGIAHTRWATHGVpn 93
Cdd:cd00712 17 ATLERMLDALAHRGPDGSGIWIDEG----------------------------------------VALGHRRLSIIDL-- 54
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1907080035 94 avnSH---PQRSDkDNEFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIAKL 145
Cdd:cd00712 55 ---SGgaqPMVSE-DGRLVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHL 105
|
|
| MurQ |
COG2103 |
N-acetylmuramic acid 6-phosphate (MurNAc-6-P) etherase [Cell wall/membrane/envelope biogenesis] ... |
395-485 |
2.94e-09 |
|
N-acetylmuramic acid 6-phosphate (MurNAc-6-P) etherase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441706 [Multi-domain] Cd Length: 301 Bit Score: 58.95 E-value: 2.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 395 ASDFLDRN-TPvfrDDVCFFISQSGETADTLLALRYCKDRGALTVGITNTVGSSISRETDCGVHINAGPEIgVA-ST--K 470
Cdd:COG2103 122 AADLKALGlGP---GDVVVGIAASGRTPYVIGALEYARARGALTVAIACNPGSPLSAAADIAIELVTGPEV-ITgSTrlK 197
|
90
....*....|....*..
gi 1907080035 471 AYTSQFISLVMF--GLM 485
Cdd:COG2103 198 AGTAQKLVLNMLstAAM 214
|
|
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
14-145 |
2.08e-08 |
|
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: 57.15 E-value: 2.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 14 ETLIRGLQRLEYRGYDSAGVAIDGnnhevkerhihlvkkrgkvkaldeelykqdsmdlkvefetHFGIAHTRWAThgVPN 93
Cdd:COG0367 17 EVLERMLDALAHRGPDGSGIWVDG----------------------------------------GVALGHRRLSI--IDL 54
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1907080035 94 AVNSHpQ-RSDKDNEFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIAKL 145
Cdd:COG0367 55 SEGGH-QpMVSEDGRYVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHA 106
|
|
| asn_synth_AEB |
TIGR01536 |
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing ... |
76-179 |
3.40e-08 |
|
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing asparagine synthase. A poorly conserved C-terminal extension was removed from the model. Bacterial members of the family tend to have a long, poorly conserved insert lacking from archaeal and eukaryotic sequences. Multiple isozymes have been demonstrated, such as in Bacillus subtilis. Long-branch members of the phylogenetic tree (which typically were also second or third candidate members from their genomes) were removed from the seed alignment and score below trusted cutoff. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 273676 [Multi-domain] Cd Length: 466 Bit Score: 56.57 E-value: 3.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 76 ETHFGIAHTRWATHGVPNAVnsHPQRSDKDnEFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIAKLIkyvfdnRET 155
Cdd:TIGR01536 39 DGNAILGHRRLAIIDLSGGA--QPMSNEGK-TYVIVFNGEIYNHEELREELEAKGYTFQTDSDTEVILHLY------EEW 109
|
90 100
....*....|....*....|....
gi 1907080035 156 EditfstlvERVIQQLEGAFALVF 179
Cdd:TIGR01536 110 G--------EECVDRLDGMFAFAL 125
|
|
| GutQ |
COG0794 |
D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall ... |
357-463 |
1.03e-06 |
|
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: 51.13 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 357 IRRCR-RLIVIGCGTSYHAA---VATrqvleeltelpvmveLASdfldRNTPVF----------------RDDVCFFISQ 416
Cdd:COG0794 40 ILNCKgRVVVTGMGKSGHIArkiAAT---------------LAS----TGTPAFflhpaeashgdlgmitPGDVVIAISN 100
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1907080035 417 SGETADTLLALRYCKDRGALTVGITNTVGSSISRETDcgVHINAGPE 463
Cdd:COG0794 101 SGETEELLALLPLLKRLGVPLIAITGNPDSTLARAAD--VVLDLPVE 145
|
|
| YafJ |
COG0121 |
Predicted glutamine amidotransferase YafJ [General function prediction only]; |
76-146 |
2.42e-06 |
|
Predicted glutamine amidotransferase YafJ [General function prediction only];
Pssm-ID: 439891 [Multi-domain] Cd Length: 248 Bit Score: 49.19 E-value: 2.42e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907080035 76 ETHFGIAHTRWATHGVPNAVNSHPQRSDkdnEFVVIHNGIITNYKDLRKFLESK-----GYEFESETDTETIAKLI 146
Cdd:COG0121 75 KSRLVIAHVRKATVGPVSLENTHPFRGG---RWLFAHNGQLDGFDRLRRRLAEElpdelYFQPVGTTDSELAFALL 147
|
|
| PTZ00077 |
PTZ00077 |
asparagine synthetase-like protein; Provisional |
81-147 |
3.22e-06 |
|
asparagine synthetase-like protein; Provisional
Pssm-ID: 185431 [Multi-domain] Cd Length: 586 Bit Score: 50.48 E-value: 3.22e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907080035 81 IAHTRWATHGVpnaVNSHPQRSDKDNEFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIAKLIK 147
Cdd:PTZ00077 51 LAHERLAIVDL---SDGKQPLLDDDETVALMQNGEIYNHWEIRPELEKEGYKFSSNSDCEIIGHLYK 114
|
|
| YafJ |
cd01908 |
Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine ... |
81-171 |
1.20e-05 |
|
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: 47.38 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 81 IAHTRWATHGVPNAVNSHPQRSDkdnEFVVIHNGIITNYKDLR-KFLESKGYEFESETDTETIAKLIkyvFDNRETEDIT 159
Cdd:cd01908 84 LAHVRAATVGPVSLENCHPFTRG---RWLFAHNGQLDGFRLLRrRLLRLLPRLPVGTTDSELAFALL---LSRLLERDPL 157
|
90
....*....|..
gi 1907080035 160 FSTLVERVIQQL 171
Cdd:cd01908 158 DPAELLDAILQT 169
|
|
| PRK12570 |
PRK12570 |
N-acetylmuramic acid-6-phosphate etherase; Reviewed |
408-482 |
4.02e-05 |
|
N-acetylmuramic acid-6-phosphate etherase; Reviewed
Pssm-ID: 237142 [Multi-domain] Cd Length: 296 Bit Score: 46.22 E-value: 4.02e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907080035 408 DDVCFFISQSGETADTLLALRYCKDRGALTVGITNTVGSSISRETDCGVHINAGPEIGVAST--KAYTSQFISLVMF 482
Cdd:PRK12570 128 DDVVVGIAASGRTPYVIGALEYAKQIGATTIALSCNPDSPIAKIADIAISPVVGPEVLTGSTrlKSGTAQKMVLNML 204
|
|
| asnB |
PRK09431 |
asparagine synthetase B; Provisional |
105-178 |
2.86e-04 |
|
asparagine synthetase B; Provisional
Pssm-ID: 236513 [Multi-domain] Cd Length: 554 Bit Score: 44.13 E-value: 2.86e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907080035 105 DNEFVVIHNGIITNYKDLRKFLESKgYEFESETDTETIAKLikYvfdnrETEDITFstlvervIQQLEGAFALV 178
Cdd:PRK09431 67 DGTHVLAVNGEIYNHQELRAELGDK-YAFQTGSDCEVILAL--Y-----QEKGPDF-------LDDLDGMFAFA 125
|
|
| SIS |
cd04795 |
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
534-587 |
1.62e-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: 38.12 E-value: 1.62e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1907080035 534 LLVMGRGYNYATCLEGALKIKEITYMHSEGILAGELKHGP-LALVDKQMPVIMVI 587
Cdd:cd04795 1 IFVIGIGGSGAIAAYFALELLELTGIEVVALIATELEHASlLSLLRKGDVVIALS 55
|
|
| SIS_PHI |
cd05005 |
Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) ... |
402-492 |
3.00e-03 |
|
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: 39.10 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 402 NTPVF-RDDVCFFISQSGETADTLLALRYCKDRGALTVGITNTVGSSISRETDCGVHINA----GPEIGVASTKAYTSQF 476
Cdd:cd05005 69 TTPAIgPGDLLIAISGSGETSSVVNAAEKAKKAGAKVVLITSNPDSPLAKLADVVVVIPAatkdDHGGEHKSIQPLGTLF 148
|
90 100
....*....|....*....|..
gi 1907080035 477 -ISLVMFG-----LMMSEDRIS 492
Cdd:cd05005 149 eQSALVFLdaviaKLMEELGVS 170
|
|
| PRK11337 |
PRK11337 |
MurR/RpiR family transcriptional regulator; |
408-453 |
3.47e-03 |
|
MurR/RpiR family transcriptional regulator;
Pssm-ID: 183089 [Multi-domain] Cd Length: 292 Bit Score: 40.13 E-value: 3.47e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1907080035 408 DDVCFFISQSGETADTLLALRYCKDRGALTVGITNTVGSSISRETD 453
Cdd:PRK11337 188 GDVVLVVSHSGRTSDVIEAVELAKKNGAKIICITNSYHSPIAKLAD 233
|
|
| GATase_4 |
pfam13230 |
Glutamine amidotransferases class-II; This family captures members that are not found in ... |
74-142 |
4.16e-03 |
|
Glutamine amidotransferases class-II; This family captures members that are not found in pfam00310.
Pssm-ID: 433047 [Multi-domain] Cd Length: 272 Bit Score: 39.62 E-value: 4.16e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 74 EFETHFGIAHTRWATHGVPNAVNSHP-QRSDKDNEFVVIHNGIITNYKDLRkfleSKGYEFESETDTETI 142
Cdd:pfam13230 68 PIRSRNVIAHIRKATQGRVTLENTHPfMRELWGRYWIFAHNGDLKGYAPKL----SGRFQPVGSTDSELA 133
|
|
| PLN02549 |
PLN02549 |
asparagine synthase (glutamine-hydrolyzing) |
79-178 |
6.12e-03 |
|
asparagine synthase (glutamine-hydrolyzing)
Pssm-ID: 178164 [Multi-domain] Cd Length: 578 Bit Score: 39.75 E-value: 6.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080035 79 FGIAHTRWAThgVPNAVNSHPQRSDkDNEFVVIHNGIITNYKDLRKFLESkgYEFESETDTETIAKLIKYVFdnretedi 158
Cdd:PLN02549 44 CYLAHERLAI--MDPESGDQPLYNE-DKTIVVTANGEIYNHKELREKLKL--HKFRTGSDCEVIAHLYEEHG-------- 110
|
90 100
....*....|....*....|
gi 1907080035 159 tfstlvERVIQQLEGAFALV 178
Cdd:PLN02549 111 ------EEFVDMLDGMFSFV 124
|
|
| |
