|
Name |
Accession |
Description |
Interval |
E-value |
| GlmS |
COG0449 |
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ... |
1-610 |
0e+00 |
|
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase domains [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440218 [Multi-domain] Cd Length: 610 Bit Score: 1065.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 1 MCGIVGAVAQRDVAEILVEGLRRLEYRGYDSAGVAVFSALHpLQRVRRLGKVAELAKALEEQSVHGGTGIAHTRWATHGE 80
Cdd:COG0449 1 MCGIVGYIGKRDAAPILLEGLKRLEYRGYDSAGIAVLDDGG-LEVRKAVGKLANLEEKLAEEPLSGTIGIGHTRWATHGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 81 PSERNAHPHVS--EHIVVVHNGIIENHEPLRDRLKELGYVFTSDTDTEVIAHLVHHELKEAPNLITAMQKAVKQLRGAYG 158
Cdd:COG0449 80 PSDENAHPHTScsGRIAVVHNGIIENYAELREELEAKGHTFKSETDTEVIAHLIEEYLKGGGDLLEAVRKALKRLEGAYA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 159 TVVMDTRDDSRLVVARSGSPLVIGRGIGENFIASDQLALLPVTRRFIFLEEGDVAEVTRRDVQVFDIDGKPVVREEKESD 238
Cdd:COG0449 160 LAVISADEPDRIVAARKGSPLVIGLGEGENFLASDVPALLPYTRRVIYLEDGEIAVLTRDGVEIYDLDGEPVEREVKTVD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 239 ISHDAGDKGEYRHYMLKEIHEQPAAINQTLDGRLGIDHVVVESFGNGARAIFDKVDHIQIVACGTSYHSGMVARYWFESI 318
Cdd:COG0449 240 WDAEAAEKGGYPHFMLKEIHEQPEAIRDTLRGRLDEDGRVVLDELNLAAEDLRNIDRIYIVACGTSYHAGLVGKYLIEEL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 319 AGVSCDVEIASEFRYRKSVVRPNSLLITLSQSGETADTLAALRLAKASGyMSSLAICNVPGSSLVRESDLAFMTRAGAEI 398
Cdd:COG0449 320 ARIPVEVEIASEFRYRDPVVDPGTLVIAISQSGETADTLAALREAKEKG-AKVLAICNVVGSTIARESDAVLYTHAGPEI 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 399 GVASTKAFTTQLAGLLMLVAAIGRCRGNLDAAAEAALVKSLQALPQRIKESLSLAKQIETLAEEFADKHHSLFLGRGDQY 478
Cdd:COG0449 399 GVASTKAFTTQLAALYLLALYLARARGTLSAEEEAELLEELRKLPEKIEEVLDLEEQIEELAEKYADARNALFLGRGINY 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 479 PIAMEGALKLKEISYIHAEAYAAGELKHGPLALIDAEMPIIVVAPNNDLLEKLKSNVEEVRARGGILYVFADAETGFKSD 558
Cdd:COG0449 479 PVALEGALKLKEISYIHAEGYAAGELKHGPIALIDEGMPVVAIAPQDELYEKTLSNIQEVKARGGKVIAIADEGDEEVEE 558
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 2059193400 559 ETMRVMNLNHMEEVIAPIVYTVPLQLLSYYVALIKGTDVDQPRNLAKSVTVE 610
Cdd:COG0449 559 LADDVIEVPEVDELLAPILAVVPLQLLAYHVAVLRGTDVDQPRNLAKSVTVE 610
|
|
| PRK00331 |
PRK00331 |
isomerizing glutamine--fructose-6-phosphate transaminase; |
1-610 |
0e+00 |
|
isomerizing glutamine--fructose-6-phosphate transaminase;
Pssm-ID: 234729 [Multi-domain] Cd Length: 604 Bit Score: 1047.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 1 MCGIVGAVAQRDVAEILVEGLRRLEYRGYDSAGVAVFSALHpLQRVRRLGKVAELAKALEEQSVHGGTGIAHTRWATHGE 80
Cdd:PRK00331 1 MCGIVGYVGQRNAAEILLEGLKRLEYRGYDSAGIAVLDDGG-LEVRKAVGKVANLEAKLEEEPLPGTTGIGHTRWATHGK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 81 PSERNAHPHVS--EHIVVVHNGIIENHEPLRDRLKELGYVFTSDTDTEVIAHLVHHELKEAPNLITAMQKAVKQLRGAYG 158
Cdd:PRK00331 80 PTERNAHPHTDcsGRIAVVHNGIIENYAELKEELLAKGHVFKSETDTEVIAHLIEEELKEGGDLLEAVRKALKRLEGAYA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 159 TVVMDTRDDSRLVVARSGSPLVIGRGIGENFIASDQLALLPVTRRFIFLEEGDVAEVTRRDVQVFDIDGKPVVREEKESD 238
Cdd:PRK00331 160 LAVIDKDEPDTIVAARNGSPLVIGLGEGENFLASDALALLPYTRRVIYLEDGEIAVLTRDGVEIFDFDGNPVEREVYTVD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 239 ISHDAGDKGEYRHYMLKEIHEQPAAINQTLDGRLGIDhvvveSFGNGARAIFDKVDHIQIVACGTSYHSGMVARYWFESI 318
Cdd:PRK00331 240 WDASAAEKGGYRHFMLKEIYEQPEAIRDTLEGRLDEL-----GEGELADEDLKKIDRIYIVACGTSYHAGLVAKYLIESL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 319 AGVSCDVEIASEFRYRKSVVRPNSLLITLSQSGETADTLAALRLAKASGyMSSLAICNVPGSSLVRESDLAFMTRAGAEI 398
Cdd:PRK00331 315 AGIPVEVEIASEFRYRDPVLSPKTLVIAISQSGETADTLAALRLAKELG-AKTLAICNVPGSTIARESDAVLYTHAGPEI 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 399 GVASTKAFTTQLAGLLMLVAAIGRCRGNLDAAAEAALVKSLQALPQRIKESLSLAKQIETLAEEFADKHHSLFLGRGDQY 478
Cdd:PRK00331 394 GVASTKAFTAQLAVLYLLALALAKARGTLSAEEEADLVHELRELPALIEQVLDLKEQIEELAEDFADARNALFLGRGVDY 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 479 PIAMEGALKLKEISYIHAEAYAAGELKHGPLALIDAEMPIIVVAPNNDLLEKLKSNVEEVRARGGILYVFADAEtGFKSD 558
Cdd:PRK00331 474 PVALEGALKLKEISYIHAEGYAAGELKHGPIALIDEGMPVVAIAPNDELYEKTKSNIQEVKARGARVIVIADEG-DEVAE 552
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 2059193400 559 ETMRVMNLNHMEEVIAPIVYTVPLQLLSYYVALIKGTDVDQPRNLAKSVTVE 610
Cdd:PRK00331 553 EADDVIEVPEVHELLAPLLYVVPLQLLAYHVALARGTDVDKPRNLAKSVTVE 604
|
|
| glmS |
TIGR01135 |
glucosamine--fructose-6-phosphate aminotransferase (isomerizing); The member from ... |
2-610 |
0e+00 |
|
glucosamine--fructose-6-phosphate aminotransferase (isomerizing); The member from Methanococcus jannaschii contains an intein. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan, Central intermediary metabolism, Amino sugars]
Pssm-ID: 273462 [Multi-domain] Cd Length: 607 Bit Score: 925.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 2 CGIVGAVAQRDVAEILVEGLRRLEYRGYDSAGVAVFSALHpLQRVRRLGKVAELAKALEEQSVHGGTGIAHTRWATHGEP 81
Cdd:TIGR01135 1 CGIVGYIGQRDAVPILLEGLKRLEYRGYDSAGIAVVDEGK-LFVRKAVGKVAELANKLGEKPLPGGVGIGHTRWATHGKP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 82 SERNAHPHVSEH--IVVVHNGIIENHEPLRDRLKELGYVFTSDTDTEVIAHLVHHELKEAPNLITAMQKAVKQLRGAYGT 159
Cdd:TIGR01135 80 TDENAHPHTDEGgrIAVVHNGIIENYAELREELEARGHVFSSDTDTEVIAHLIEEELREGGDLLEAVQKALKQLRGAYAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 160 VVMDTRDDSRLVVARSGSPLVIGRGIGENFIASDQLALLPVTRRFIFLEEGDVAEVTRRDVQVFDIDGKPVVREEKESDI 239
Cdd:TIGR01135 160 AVLHADHPETLVAARSGSPLIVGLGDGENFVASDVTALLPYTRRVIYLEDGDIAILTKDGVEIYNFEGAPVQREVRVIDW 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 240 SHDAGDKGEYRHYMLKEIHEQPAAINQTLDGRLGIDHVVVESFGNGAraIFDKVDHIQIVACGTSYHSGMVARYWFESIA 319
Cdd:TIGR01135 240 DLDAAEKGGYRHFMLKEIYEQPRALRDTLEGRIEENGGVFEELGAEE--LLKNIDRIQIVACGTSYHAGLVAKYLIERLA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 320 GVSCDVEIASEFRYRKSVVRPNSLLITLSQSGETADTLAALRLAKASGyMSSLAICNVPGSSLVRESDLAFMTRAGAEIG 399
Cdd:TIGR01135 318 GIPVEVEIASEFRYRKPVVDKDTLVIAISQSGETADTLEALRLAKELG-AKTLGICNVPGSTLVREADHTLYTRAGPEIG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 400 VASTKAFTTQLAGLLMLVAAIGRCRGNLDAAAEAALVKSLQALPQRIKESLSLAKQIETLAEEFADKHHSLFLGRGDQYP 479
Cdd:TIGR01135 397 VASTKAFTTQLTVLYLLALALAKARGTLSAEEEAELVDALRRLPDLVEQVLLADESIAELAERYADKRNFLFLGRGLGYP 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 480 IAMEGALKLKEISYIHAEAYAAGELKHGPLALIDAEMPIIVVAPNNDLLEKLKSNVEEVRARGGILYVFADAETGFKSDE 559
Cdd:TIGR01135 477 IALEGALKLKEISYIHAEGYPAGELKHGPIALIDEGLPVVAIAPKDSLLEKTKSNVEEVKARGARVIVFAPEDDETIASV 556
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 2059193400 560 TMRVMNLNHMEEVIAPIVYTVPLQLLSYYVALIKGTDVDQPRNLAKSVTVE 610
Cdd:TIGR01135 557 ADDVIKLPEVEELLAPIVYTIPLQLLAYHIALAKGTDVDKPRNLAKSVTVE 607
|
|
| PLN02981 |
PLN02981 |
glucosamine:fructose-6-phosphate aminotransferase |
1-610 |
2.54e-162 |
|
glucosamine:fructose-6-phosphate aminotransferase
Pssm-ID: 215531 [Multi-domain] Cd Length: 680 Bit Score: 480.02 E-value: 2.54e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 1 MCGIVGAV------AQRDVAEILVEGLRRLEYRGYDSAGVAV-----FSALHPLQrVRRLGKVAELAKALEEQ------- 62
Cdd:PLN02981 1 MCGIFAYLnynvprERRFILEVLFNGLRRLEYRGYDSAGIAIdndpsLESSSPLV-FREEGKIESLVRSVYEEvaetdln 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 63 -----SVHggTGIAHTRWATHGEPSERNAHPHVSE---HIVVVHNGIIENHEPLRDRLKELGYVFTSDTDTEVIAHL--- 131
Cdd:PLN02981 80 ldlvfENH--AGIAHTRWATHGPPAPRNSHPQSSGpgnEFLVVHNGIITNYEVLKETLLRHGFTFESDTDTEVIPKLakf 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 132 VHHELKEAPNLITAMQ---KAVKQLRGAYGTVVMDTRDDSRLVVARSGSPLVIG------------------------RG 184
Cdd:PLN02981 158 VFDKLNEEEGDVTFSQvvmEVMRQLEGAYALIFKSPHYPNELVACKRGSPLLLGvkelpeeknssavftsegfltknrDK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 185 IGENFIASDQLALLPVTRRFIFLEEGDVAEVTRRDVQVFDIDGKpvvREEKESDISHDAG---------------DKGEY 249
Cdd:PLN02981 238 PKEFFLASDASAVVEHTKRVLVIEDNEVVHLKDGGVGIYKFENE---KGRGGGGLSRPASveralstlemeveqiMKGNY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 250 RHYMLKEIHEQPAAINQTLDGRLgidhvVVESFGNGARAIFDK-VDH---------IQIVACGTSYHSGMVARYWFESIA 319
Cdd:PLN02981 315 DHYMQKEIHEQPESLTTTMRGRL-----IRGGSGKAKRVLLGGlKDHlktirrsrrIVFIGCGTSYNAALAARPILEELS 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 320 GVSCDVEIASEFRYRKSVVRPNSLLITLSQSGETADTLAALRLAKASGYMSsLAICNVPGSSLVRESDLAFMTRAGAEIG 399
Cdd:PLN02981 390 GVPVTMELASDLLDRQGPIYREDTAVFVSQSGETADTLRALEYAKENGALC-VGITNTVGSAISRGTHCGVHINAGAEIG 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 400 VASTKAFTTQLAGLLMLVAAIGRcrgnlDAAAEA----ALVKSLQALPQRIKESLSLAKQIETLAEEFADKHHSLFLGRG 475
Cdd:PLN02981 469 VASTKAYTSQIVAMTMLALALGE-----DSISSRsrreAIIDGLFDLPNKVREVLKLDQEMKELAELLIDEQSLLVFGRG 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 476 DQYPIAMEGALKLKEISYIHAEAYAAGELKHGPLALIDAEMPIIVVAPNNDLLEKLKSNVEEVRARGGILYVFA---DAE 552
Cdd:PLN02981 544 YNYATALEGALKVKEVALMHSEGILAGEMKHGPLALVDETLPIIVIATRDACFSKQQSVIQQLRARKGRLIVICskgDAS 623
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 2059193400 553 TGFKSDETmRVMNLNHMEEVIAPIVYTVPLQLLSYYVALIKGTDVDQPRNLAKSVTVE 610
Cdd:PLN02981 624 SVCPSGGC-RVIEVPQVEDCLQPVINIVPLQLLAYHLTVLRGHNVDQPRNLAKSVTTQ 680
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
1-609 |
2.86e-158 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 468.35 E-value: 2.86e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 1 MCGIVGAVAQRDVAEILVEGLRRLEYRGYDSAGVAVFSALHPLqRVRRLGKVAELAKALEE-----QSVHGGT--GIAHT 73
Cdd:PTZ00295 24 CCGIVGYLGNEDASKILLEGIEILQNRGYDSCGISTISSGGEL-KTTKYASDGTTSDSIEIlkeklLDSHKNStiGIAHT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 74 RWATHGEPSERNAHPHV--SEHIVVVHNGIIENHEPLRDRLKELGYVFTSDTDTEVIAHLVHHELKEAPNLITAMQKAVK 151
Cdd:PTZ00295 103 RWATHGGKTDENAHPHCdyKKRIALVHNGTIENYVELKSELIAKGIKFRSETDSEVIANLIGLELDQGEDFQEAVKSAIS 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 152 QLRGAYGTVVMDTRDDSRLVVARSGSPLVIGRGIGENFIASDQLALLPVTRRFIFLEEGDVAEVTRRDVQVFdIDGKPVV 231
Cdd:PTZ00295 183 RLQGTWGLCIIHKDNPDSLIVARNGSPLLVGIGDDSIYVASEPSAFAKYTNEYISLKDGEIAELSLENVNDL-YTQRRVE 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 232 REEKESDIShdagDKGEYRHYMLKEIHEQPAAINQTLD--GRL-GIDH-VVVESFGNGARAIFDKVDHIqIVACGTSYHS 307
Cdd:PTZ00295 262 KIPEEVIEK----SPEPYPHWTLKEIFEQPIALSRALNngGRLsGYNNrVKLGGLDQYLEELLNIKNLI-LVGCGTSYYA 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 308 GMVARYWFESIAGV-SCDVEIASEF-RYRksVVRPNSLLITLSQSGETADTLAALRLAKASGyMSSLAICNVPGSSLVRE 385
Cdd:PTZ00295 337 ALFAASIMQKLKCFnTVQVIDASELtLYR--LPDEDAGVIFISQSGETLDVVRALNLADELN-LPKISVVNTVGSLIARS 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 386 SDLAFMTRAGAEIGVASTKAFTTQLAGLLMLVAAIGRCRGNLDAAAE-AALVKSLQALPQRIKESLSLAK-QIETLAEEF 463
Cdd:PTZ00295 414 TDCGVYLNAGREVAVASTKAFTSQVTVLSLIALWFAQNKEYSCSNYKcSSLINSLHRLPTYIGMTLKSCEeQCKRIAEKL 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 464 ADKHHSLFLGRGDQYPIAMEGALKLKEISYIHAEAYAAGELKHGPLALIDAE--MPIIVVAPNNDLLEKLKSNVEEVRAR 541
Cdd:PTZ00295 494 KNAKSMFILGKGLGYPIALEGALKIKEITYIHAEGFSGGALKHGPFALIDKEknTPVILIILDDEHKELMINAAEQVKAR 573
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 542 GGILYVFADAETGFK--SDETMRVMNlnhmEEVIAPIVYTVPLQLLSYYVALIKGTDVDQPRNLAKSVTV 609
Cdd:PTZ00295 574 GAYIIVITDDEDLVKdfADEIILIPS----NGPLTALLAVIPLQLLAYEIAILRGINPDKPRGLAKTVTV 639
|
|
| PTZ00394 |
PTZ00394 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
1-610 |
3.85e-142 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 173585 [Multi-domain] Cd Length: 670 Bit Score: 427.76 E-value: 3.85e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 1 MCGIVGAVAQ------RDVAEILVEGLRRLEYRGYDSAGVAV-----------FSALHPLQR---VRRLGKVAELAKAL- 59
Cdd:PTZ00394 1 MCGIFGYANHnvprtvEQILNVLLDGIQKVEYRGYDSAGLAIdanigsekedgTAASAPTPRpcvVRSVGNISQLREKVf 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 60 ------------EEQSVHggTGIAHTRWATHGEPSERNAHPHVSEH--IVVVHNGIIENHEPLRDRLKELGYVFTSDTDT 125
Cdd:PTZ00394 81 seavaatlppmdATTSHH--VGIAHTRWATHGGVCERNCHPQQSNNgeFTIVHNGIVTNYMTLKELLKEEGYHFSSDTDT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 126 EVIAHLVHHELKEAP--NLITAMQKAVKQLRGAYGTVVMDTRDDSRLVVARSGSPLVIG--------------------- 182
Cdd:PTZ00394 159 EVISVLSEYLYTRKGihNFADLALEVSRMVEGSYALLVKSVYFPGQLAASRKGSPLMVGirrtddrgcvmklqtydltdl 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 183 RGIGENFIASDQLALLPVTRRFIFLEEGDVAEVTRRDVQVFDIDGKP---VVREEKESDISHDAGDKGEYRHYMLKEIHE 259
Cdd:PTZ00394 239 SGPLEVFFSSDVNSFAEYTREVVFLEDGDIAHYCDGALRFYNAAERQrsiVKREVQHLDAKPEGLSKGNYPHFMLKEIYE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 260 QPAAINQTLDGRLGIDH--VVVESFGNGARAIFDKVDHIQIVACGTSYHSGMVARYWFESIAGVSCDVEIASEFRYRKSV 337
Cdd:PTZ00394 319 QPESVISSMHGRIDFSSgtVQLSGFTQQSIRAILTSRRILFIACGTSLNSCLAVRPLFEELVPLPISVENASDFLDRRPR 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 338 VRPNSLLITLSQSGETADTLAALRLAKASGYMSsLAICNVPGSSLVRESDLAFMTRAGAEIGVASTKAFTTQLAgLLMLV 417
Cdd:PTZ00394 399 IQRDDVCFFVSQSGETADTLMALQLCKEAGAMC-VGITNVVGSSISRLTHYAIHLNAGVEVGVASTKAYTSQVV-VLTLV 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 418 AAIGRCRGNLDAAAEAALVKSLQALPQRIKESLSLAKQ-IETLAEEFADKHHSLFLGRGDQYPIAMEGALKLKEISYIHA 496
Cdd:PTZ00394 477 ALLLSSDSVRLQERRNEIIRGLAELPAAISECLKITHDpVKALAARLKESSSILVLGRGYDLATAMEAALKVKELSYVHT 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 497 EAYAAGELKHGPLALIDAEMPIIVVAPNNDLLEKLKSNVEEVRARGGILYVFA---DAETGFKSDETMRVMNLnhmEEVI 573
Cdd:PTZ00394 557 EGIHSGELKHGPLALIDETSPVLAMCTHDKHFGLSKSAVQQVKARGGAVVVFAtevDAELKAAASEIVLVPKT---VDCL 633
|
650 660 670
....*....|....*....|....*....|....*..
gi 2059193400 574 APIVYTVPLQLLSYYVALIKGTDVDQPRNLAKSVTVE 610
Cdd:PTZ00394 634 QCVVNVIPFQLLAYYMALLRGNNVDCPRNLAKSVTVQ 670
|
|
| GFAT |
cd00714 |
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ... |
2-215 |
7.65e-122 |
|
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: 359.07 E-value: 7.65e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 2 CGIVGAVAQRDVAEILVEGLRRLEYRGYDSAGVAVFSALHpLQRVRRLGKVAELAKALEEQSVHGGTGIAHTRWATHGEP 81
Cdd:cd00714 1 CGIVGYIGKREAVDILLEGLKRLEYRGYDSAGIAVIGDGS-LEVVKAVGKVANLEEKLAEKPLSGHVGIGHTRWATHGEP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 82 SERNAHPHVSEH--IVVVHNGIIENHEPLRDRLKELGYVFTSDTDTEVIAHLVHHELKEAPNLITAMQKAVKQLRGAYGT 159
Cdd:cd00714 80 TDVNAHPHRSCDgeIAVVHNGIIENYAELKEELEAKGYKFESETDTEVIAHLIEYYYDGGLDLLEAVKKALKRLEGAYAL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2059193400 160 VVMDTRDDSRLVVARSGSPLVIGRGIGENFIASDQLALLPVTRRFIFLEEGDVAEV 215
Cdd:cd00714 160 AVISKDEPDEIVAARNGSPLVIGIGDGENFVASDAPALLEHTRRVIYLEDGDIAVI 215
|
|
| AgaS |
COG2222 |
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ... |
254-610 |
1.78e-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: 241.34 E-value: 1.78e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 254 LKEIHEQPAAINQTLDgrlgIDHVVVESFGNGARAifDKVDHIQIVACGTSYHSGMVARYWFESIAGVSCDVEIASEF-R 332
Cdd:COG2222 1 AREIAQQPEAWRRALA----ALAAAIAALLARLRA--KPPRRVVLVGAGSSDHAAQAAAYLLERLLGIPVAALAPSELvV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 333 YRKSVVRPNSLLITLSQSGETADTLAALRLAKASGyMSSLAICNVPGSSLVRESDLAFMTRAGAEIGVASTKAFTTQLAG 412
Cdd:COG2222 75 YPAYLKLEGTLVVAISRSGNSPEVVAALELAKARG-ARTLAITNNPDSPLAEAADRVLPLPAGPEKSVAATKSFTTMLLA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 413 LLMLVAAIGrcrgnldaaAEAALVKSLQALPQRIKESLSLAKQIETLAEeFADKHHSLFLGRGDQYPIAMEGALKLKEIS 492
Cdd:COG2222 154 LLALLAAWG---------GDDALLAALDALPAALEAALAADWPAAALAA-LADAERVVFLGRGPLYGLAREAALKLKELS 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 493 YIHAEAYAAGELKHGPLALIDAEMPIIVVAPNNDLLEKLKSNVEEVRARGGILYVFADAEtgfksDETMRVMNLNHMEEV 572
Cdd:COG2222 224 AGHAEAYSAAEFRHGPKSLVDPGTLVVVLASEDPTRELDLDLAAELRALGARVVAIGAED-----DAAITLPAIPDLHDA 298
|
330 340 350
....*....|....*....|....*....|....*...
gi 2059193400 573 IAPIVYTVPLQLLSYYVALIKGTDVDQPRNLAKSVTVE 610
Cdd:COG2222 299 LDPLLLLVVAQRLALALALARGLDPDTPRHLNKVVKTV 336
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
2-213 |
3.52e-63 |
|
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: 207.69 E-value: 3.52e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 2 CGIVGAVAQRDVAEILVE----GLRRLEYRGYDSAGVAVFSAlHPLQRVRRLGKVAELAKALEEQSVHGGTGIAHTRWAT 77
Cdd:cd00352 1 CGIFGIVGADGAASLLLLlllrGLAALEHRGPDGAGIAVYDG-DGLFVEKRAGPVSDVALDLLDEPLKSGVALGHVRLAT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 78 HGEPSERNAHPHVSE--HIVVVHNGIIENHEPLRDRLKELGYVFTSDTDTEVIAHLVHHELKEAPnLITAMQKAVKQLRG 155
Cdd:cd00352 80 NGLPSEANAQPFRSEdgRIALVHNGEIYNYRELREELEARGYRFEGESDSEVILHLLERLGREGG-LFEAVEDALKRLDG 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2059193400 156 AYGTVVMDTRDDsRLVVARSG---SPLVIGRGI-GENFIASDQLALLPVT-RRFIFLEEGDVA 213
Cdd:cd00352 159 PFAFALWDGKPD-RLFAARDRfgiRPLYYGITKdGGLVFASEPKALLALPfKGVRRLPPGELL 220
|
|
| SIS_GlmS_GlmD_2 |
cd05009 |
SIS (Sugar ISomerase) domain repeat 2 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
454-608 |
1.16e-62 |
|
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: 203.65 E-value: 1.16e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 454 KQIETLAEEFADKHHSLFLGRGDQYPIAMEGALKLKEISYIHAEAYAAGELKHGPLALIDAEMPIIVVAPNNDLLEKLKS 533
Cdd:cd05009 1 EDIKELAEKLKEAKSFYVLGRGPNYGTALEGALKLKETSYIHAEAYSAGEFKHGPIALVDEGTPVIFLAPEDRLEEKLES 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2059193400 534 NVEEVRARGGILYVFADAETGfkSDETMRVMNLNHMEEVIAPIVYTVPLQLLSYYVALIKGTDVDQPRNLAKSVT 608
Cdd:cd05009 81 LIKEVKARGAKVIVITDDGDA--KDLADVVIRVPATVEELSPLLYIVPLQLLAYHLAVARGIDPDKPRNLAKSVT 153
|
|
| SIS_GlmS_GlmD_1 |
cd05008 |
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
295-421 |
9.29e-59 |
|
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: 192.33 E-value: 9.29e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 295 HIQIVACGTSYHSGMVARYWFESIAGVSCDVEIASEFRYRKSVVRPNSLLITLSQSGETADTLAALRLAKASGYMsSLAI 374
Cdd:cd05008 1 RILIVGCGTSYHAALVAKYLLERLAGIPVEVEAASEFRYRRPLLDEDTLVIAISQSGETADTLAALRLAKEKGAK-TVAI 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2059193400 375 CNVPGSSLVRESDLAFMTRAGAEIGVASTKAFTTQLAGLLMLVAAIG 421
Cdd:cd05008 80 TNVVGSTLAREADYVLYLRAGPEISVAATKAFTSQLLALLLLALALA 126
|
|
| PurF |
COG0034 |
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ... |
1-197 |
7.39e-39 |
|
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; Glutamine phosphoribosylpyrophosphate amidotransferase is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439804 [Multi-domain] Cd Length: 464 Bit Score: 149.02 E-value: 7.39e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 1 MCGIVGAVAQRDVAEILVEGLRRLEYRGYDSAGVAVFSALHpLQRVRRLGKVAELAKALEEQSVHGGTGIAHTRWATHGE 80
Cdd:COG0034 7 ECGVFGIYGHEDVAQLTYYGLYALQHRGQESAGIATSDGGR-FHLHKGMGLVSDVFDEEDLERLKGNIAIGHVRYSTTGS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 81 PSERNAHPHVSEH----IVVVHNGIIENHEPLRDRLKELGYVFTSDTDTEVIAHLVHHELKEaPNLITAMQKAVKQLRGA 156
Cdd:COG0034 86 SSLENAQPFYVNSpfgsIALAHNGNLTNAEELREELEEEGAIFQTTSDTEVILHLIARELTK-EDLEEAIKEALRRVKGA 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2059193400 157 YGTVVMdtrDDSRLVVAR--SG-SPLVIGRGIGENFIASDQLAL 197
Cdd:COG0034 165 YSLVIL---TGDGLIAARdpNGiRPLVLGKLEDGYVVASESCAL 205
|
|
| GPATase_N |
cd00715 |
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ... |
2-232 |
1.29e-35 |
|
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the N-terminus of glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase) . The glutaminase domain catalyzes amide nitrogen transfer from glutamine to the appropriate substrate. In this process, glutamine is hydrolyzed to glutamic acid and ammonia. GPATase catalyzes the first step in purine biosynthesis, an amide transfer from glutamine to PRPP, resulting in phosphoribosylamine, pyrophosphate and glutamate. GPATase crystalizes as a homotetramer, but can also exist as a homdimer.
Pssm-ID: 238367 [Multi-domain] Cd Length: 252 Bit Score: 134.51 E-value: 1.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 2 CGIVGAVAQRDVAEILVEGLRRLEYRGYDSAGVAVFSALHpLQRVRRLGKVAELAKALEEQSVHGGTGIAHTRWATHGEP 81
Cdd:cd00715 1 CGVFGIYGAEDAARLTYLGLYALQHRGQESAGIATSDGKR-FHTHKGMGLVSDVFDEEKLRRLPGNIAIGHVRYSTAGSS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 82 SERNAHPHVSEH----IVVVHNGIIENHEPLRDRLKELGYVFTSDTDTEVIAHLVHHELKEaPNLITAMQKAVKQLRGAY 157
Cdd:cd00715 80 SLENAQPFVVNSplggIALAHNGNLVNAKELREELEEEGRIFQTTSDSEVILHLIARSLAK-DDLFEAIIDALERVKGAY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 158 GTVVMdTRDdsRLVVARSGS---PLVIGRGIGENFI-ASDQLALLPVTRRFIF-LEEGDVAEVTRRDVQVFDIDGKPVVR 232
Cdd:cd00715 159 SLVIM-TAD--GLIAVRDPHgirPLVLGKLEGDGYVvASESCALDIIGAEFVRdVEPGEIVVIDDDGLESSQRAPKPKPA 235
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
292-419 |
3.01e-34 |
|
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: 126.64 E-value: 3.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 292 KVDHIQIVACGTSYHSGMVARYWFESIAGVSCDVEIASEFRYR-KSVVRPNSLLITLSQSGETADTLAALRLAKASGyMS 370
Cdd:pfam01380 4 KAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGvLALVDEDDLVIAISYSGETKDLLAAAELAKARG-AK 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2059193400 371 SLAICNVPGSSLVRESDLAFMTRAGAEIGVASTKAFTTQLAGLLMLVAA 419
Cdd:pfam01380 83 IIAITDSPGSPLAREADHVLYINAGPETGVASTKSITAQLAALDALAVA 131
|
|
| purF |
TIGR01134 |
amidophosphoribosyltransferase; Alternate name: glutamine phosphoribosylpyrophosphate (PRPP) ... |
2-197 |
5.08e-32 |
|
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: 128.98 E-value: 5.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 2 CGIVGAVAQR-DVAEILVEGLRRLEYRGYDSAGVAVFSALHPLQRvRRLGKVAELAKALEEQSVHGGTGIAHTRWATHGE 80
Cdd:TIGR01134 1 CGVVGIYGQEeVAASLTYYGLYALQHRGQESAGISVFDGNRFRLH-KGNGLVSDVFNEEHLQRLKGNVGIGHVRYSTAGS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 81 PSERNAHPHVSE----HIVVVHNGIIENHEPLRDRLKELGYVFTSDTDTEVIAHLVHHELKEAPNLITAMQKAVKQLRGA 156
Cdd:TIGR01134 80 SGLENAQPFVVNspygGLALAHNGNLVNADELRRELEEEGRHFNTTSDSEVLLHLLAHNDESKDDLFDAVARVLERVRGA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2059193400 157 YGTVVMdtrDDSRLVVARS--G-SPLVIGRGIGENFIASDQLAL 197
Cdd:TIGR01134 160 YALVLM---TEDGLVAVRDphGiRPLVLGRRGDGYVVASESCAL 200
|
|
| PLN02440 |
PLN02440 |
amidophosphoribosyltransferase |
1-200 |
1.60e-27 |
|
amidophosphoribosyltransferase
Pssm-ID: 215241 [Multi-domain] Cd Length: 479 Bit Score: 116.32 E-value: 1.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 1 MCGIVGAVAQRDVAEILVEGLRRLEYRGYDSAGVAVFSAlHPLQRVRRLGKVAELAKALEEQSVHGGTGIAHTRWATHGE 80
Cdd:PLN02440 1 ECGVVGIFGDPEASRLCYLGLHALQHRGQEGAGIVTVDG-NRLQSITGNGLVSDVFDESKLDQLPGDIAIGHVRYSTAGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 81 PSERNAHPHVSEH----IVVVHNGIIENHEPLRDRLKELGYVFTSDTDTEVIAHLVHHELkeAPNLITAMQKAVKQLRGA 156
Cdd:PLN02440 80 SSLKNVQPFVANYrfgsIGVAHNGNLVNYEELRAKLEENGSIFNTSSDTEVLLHLIAISK--ARPFFSRIVDACEKLKGA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2059193400 157 YGTVVMdTRDdsRLVVARSGS---PLVIG-RGIGENFIASDQLALLPV 200
Cdd:PLN02440 158 YSMVFL-TED--KLVAVRDPHgfrPLVMGrRSNGAVVFASETCALDLI 202
|
|
| PRK05793 |
PRK05793 |
amidophosphoribosyltransferase; Provisional |
2-205 |
1.40e-26 |
|
amidophosphoribosyltransferase; Provisional
Pssm-ID: 235611 [Multi-domain] Cd Length: 469 Bit Score: 113.21 E-value: 1.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 2 CGIVGAVA--QRDVAEILVEGLRRLEYRGYDSAGVAVfSALHPLQRVRRLGKVAELAKALEEQSVHGGTGIAHTRWATHG 79
Cdd:PRK05793 15 CGVFGVFSknNIDVASLTYYGLYALQHRGQESAGIAV-SDGEKIKVHKGMGLVSEVFSKEKLKGLKGNSAIGHVRYSTTG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 80 EPSERNAHPHVSEH----IVVVHNGIIENHEPLRDRLKELGYVFTSDTDTEVIAHLVHHELKEapNLITAMQKAVKQLRG 155
Cdd:PRK05793 94 ASDLDNAQPLVANYklgsIAIAHNGNLVNADVIRELLEDGGRIFQTSIDSEVILNLIARSAKK--GLEKALVDAIQAIKG 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2059193400 156 AYGTVVMdTRDdsRLVVARSGS---PLVIGRGIGENFIASDQLALLPVTRRFI 205
Cdd:PRK05793 172 SYALVIL-TED--KLIGVRDPHgirPLCLGKLGDDYILSSESCALDTIGAEFI 221
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
462-593 |
9.25e-26 |
|
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars. Presumably the SIS domains bind to the end-product of the pathway.
Pssm-ID: 426230 [Multi-domain] Cd Length: 131 Bit Score: 102.76 E-value: 9.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 462 EFADKHHSLFLGRGDQYPIAMEGALKLKEISYIHAEAYAAGELKHGPLALIDAEMPIIVVAPNNDLLEKLKsNVEEVRAR 541
Cdd:pfam01380 1 LLAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGVLALVDEDDLVIAISYSGETKDLLA-AAELAKAR 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2059193400 542 GGILYVFADAETGFKSDETMRVMNLNHMEEVIAPIVYTVPLQLLSYYVALIK 593
Cdd:pfam01380 80 GAKIIAITDSPGSPLAREADHVLYINAGPETGVASTKSITAQLAALDALAVA 131
|
|
| GlxB |
cd01907 |
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ... |
2-197 |
1.35e-22 |
|
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine amidotransferase-like protein of unknown function found in bacteria and archaea. GlxB has a structural fold similar to that of other class II glutamine amidotransferases including glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), beta lactam synthetase (beta-LS) and glutamate synthase (GltS). The GlxB fold is also somewhat similar to the Ntn (N-terminal nucleophile) hydrolase fold of the proteasomal alpha and beta subunits.
Pssm-ID: 238888 [Multi-domain] Cd Length: 249 Bit Score: 97.34 E-value: 1.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 2 CGIVGAV---AQRDVAEILVEGLRRLEYRG-YDSAGVA--------VFSALHPLQRVRRLGKVAELAKALEEQSVHGGTG 69
Cdd:cd01907 1 CGIFGIMskdGEPFVGALLVEMLDAMQERGpGDGAGFAlygdpdafVYSSGKDMEVFKGVGYPEDIARRYDLEEYKGYHW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 70 IAHTRWATHGEPSERNAHPHVSEHIVVVHNGIIENHEPLRDRLKELGYVFTSDTDTEVIAHLVHHELKE----------A 139
Cdd:cd01907 81 IAHTRQPTNSAVWWYGAHPFSIGDIAVVHNGEISNYGSNREYLERFGYKFETETDTEVIAYYLDLLLRKgglpleyykhI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2059193400 140 PNLITAMQKAVKQLRGAYGTVVMD-------TRDDSRLVVA-RSG-SPLVIGRGIGENFIASDQLAL 197
Cdd:cd01907 161 IRMPEEERELLLALRLTYRLADLDgpftiivGTPDGFIVIRdRIKlRPAVVAETDDYVAIASEECAI 227
|
|
| GATase_6 |
pfam13522 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
64-174 |
7.69e-20 |
|
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain found in a variety of enzymes, such as asparagine synthetase and glutamine--fructose-6-phosphate transaminase.
Pssm-ID: 433279 [Multi-domain] Cd Length: 130 Bit Score: 85.82 E-value: 7.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 64 VHGGTGIAHTRWATHGEPSERNaHPHVSE--HIVVVHNGIIENHEPLRDRLKELGYVFTSDTDTEVIAHLvHHELKEapn 141
Cdd:pfam13522 8 VEGGVALGHVRLAIVDLPDAGN-QPMLSRdgRLVLVHNGEIYNYGELREELADLGHAFRSRSDTEVLLAL-YEEWGE--- 82
|
90 100 110
....*....|....*....|....*....|...
gi 2059193400 142 litamqKAVKQLRGAYGTVVMDtRDDSRLVVAR 174
Cdd:pfam13522 83 ------DCLERLRGMFAFAIWD-RRRRTLFLAR 108
|
|
| AsnB |
cd00712 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ... |
2-200 |
1.02e-17 |
|
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine synthetase B catalyses the ATP-dependent conversion of aspartate to asparagine. This enzyme is a homodimer, with each monomer composed of a glutaminase domain and a synthetase domain. The N-terminal glutaminase domain hydrolyzes glutamine to glutamic acid and ammonia.
Pssm-ID: 238364 [Multi-domain] Cd Length: 220 Bit Score: 82.22 E-value: 1.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 2 CGIVGAV---AQRDVAEILVEGLRRLEYRGYDSAGVAVfsalhplqrvrrlgkvaelakaleeqsvHGGTGIAHTRWATH 78
Cdd:cd00712 1 CGIAGIIgldGASVDRATLERMLDALAHRGPDGSGIWI----------------------------DEGVALGHRRLSII 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 79 GEpsERNAHPHVSE--HIVVVHNGIIENHEPLRDRLKELGYVFTSDTDTEVIAHLvHHELKEApnlitamqkAVKQLRGA 156
Cdd:cd00712 53 DL--SGGAQPMVSEdgRLVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHL-YEEWGED---------CLERLNGM 120
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2059193400 157 YGTVVMDTRDDsRLVVAR--SGS-PLVIGRGiGENFI-ASDQLALLPV 200
Cdd:cd00712 121 FAFALWDKRKR-RLFLARdrFGIkPLYYGRD-GGGLAfASELKALLAL 166
|
|
| GATase_7 |
pfam13537 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
94-199 |
2.47e-17 |
|
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain found in a variety of enzymes such as asparagine synthetase and glutamine-fructose-6-phosphate transaminase.
Pssm-ID: 433289 [Multi-domain] Cd Length: 123 Bit Score: 78.33 E-value: 2.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 94 IVVVHNGIIENHEPLRDRLKELGYVFTSDTDTEVIAHLVHHELKEApnlitamqkAVKQLRGAYGTVVMDTRDDsRLVVA 173
Cdd:pfam13537 24 YVIVFNGEIYNYRELRAELEAKGYRFRTHSDTEVILHLYEAEWGED---------CVDRLNGMFAFAIWDRRRQ-RLFLA 93
|
90 100 110
....*....|....*....|....*....|
gi 2059193400 174 R--SG-SPLVIGRGIGENFI-ASDQLALLP 199
Cdd:pfam13537 94 RdrFGiKPLYYGRDDGGRLLfASELKALLA 123
|
|
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
1-174 |
2.38e-15 |
|
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: 79.11 E-value: 2.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 1 MCGIVGAVAQRDVA--EILVEGLRRLEYRGYDSAGVAVfsalhplqrvrrlgkvaelakaleeqsvHGGTGIAHTRWATH 78
Cdd:COG0367 1 MCGIAGIIDFDGGAdrEVLERMLDALAHRGPDGSGIWV----------------------------DGGVALGHRRLSII 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 79 GePSERNAHPHVSE--HIVVVHNGIIENHEPLRDRLKELGYVFTSDTDTEVIAHLVhHELKEApnlitamqkAVKQLRGA 156
Cdd:COG0367 53 D-LSEGGHQPMVSEdgRYVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHAY-EEWGED---------CLERLNGM 121
|
170
....*....|....*...
gi 2059193400 157 YGTVVMDTRDDsRLVVAR 174
Cdd:COG0367 122 FAFAIWDRRER-RLFLAR 138
|
|
| YafJ |
COG0121 |
Predicted glutamine amidotransferase YafJ [General function prediction only]; |
3-177 |
5.59e-14 |
|
Predicted glutamine amidotransferase YafJ [General function prediction only];
Pssm-ID: 439891 [Multi-domain] Cd Length: 248 Bit Score: 71.92 E-value: 5.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 3 GIVGAVAqRDVAEILVEGLRRLEYRGYDSA--------GVAVFSALHPLQRVRRLGKVAE--LAKALEEQsVHGGTGIAH 72
Cdd:COG0121 5 GYSGNVP-TDLEFLLLDPEHSLVRQSGATRegphadgwGIGWYEGDGEPRLYRDPLPAWSdpNLRLLARP-IKSRLVIAH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 73 TRWATHGEPSERNAHPHVSEHIVVVHNGIIENHEPLRDRLKEL---GYVFT--SDTDTEVIAHLVHHELKEA-PNLITAM 146
Cdd:COG0121 83 VRKATVGPVSLENTHPFRGGRWLFAHNGQLDGFDRLRRRLAEElpdELYFQpvGTTDSELAFALLLSRLRDGgPDPAEAL 162
|
170 180 190
....*....|....*....|....*....|....*..
gi 2059193400 147 QKAVKQLR------GAYGTVVMdtrDDSRLVVARSGS 177
Cdd:COG0121 163 AEALRELAelarapGRLNLLLS---DGERLYATRYTS 196
|
|
| YafJ |
cd01908 |
Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine ... |
30-178 |
9.37e-14 |
|
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: 71.65 E-value: 9.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 30 DSAGVAVFSALHPLQRVRRLGKVAELAKALEEQ--SVHGGTGIAHTRWATHGEPSERNAHPHVSEHIVVVHNGIIENHEP 107
Cdd:cd01908 42 DGWGIGWYEGKGGRPFRYRSPLPAWSDINLESLarPIKSPLVLAHVRAATVGPVSLENCHPFTRGRWLFAHNGQLDGFRL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 108 LR-DRLKELGYVFTSDTDTEVIAHLVHHELKEAP-----NLITAMQKAVKQLR-----GAYGTVVMDTRddsRLVVARSG 176
Cdd:cd01908 122 LRrRLLRLLPRLPVGTTDSELAFALLLSRLLERDpldpaELLDAILQTLRELAalappGRLNLLLSDGE---YLIATRYA 198
|
..
gi 2059193400 177 SP 178
Cdd:cd01908 199 SA 200
|
|
| PLN02549 |
PLN02549 |
asparagine synthase (glutamine-hydrolyzing) |
1-197 |
2.02e-13 |
|
asparagine synthase (glutamine-hydrolyzing)
Pssm-ID: 178164 [Multi-domain] Cd Length: 578 Bit Score: 73.26 E-value: 2.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 1 MCGIVGAVAQRDVA---EILVEGL-RRLEYRGYDSAGvavfsaLHplqrvrrlgkvaelakaleeqsVHGGTGIAHTRWA 76
Cdd:PLN02549 1 MCGILAVLGCSDDSqakRSRVLELsRRLRHRGPDWSG------LY----------------------GNEDCYLAHERLA 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 77 THGEPSerNAHPHVSEH--IVVVHNGIIENHEPLRDRLKElgYVFTSDTDTEVIAHLVHHELKEapnlitamqkAVKQLR 154
Cdd:PLN02549 53 IMDPES--GDQPLYNEDktIVVTANGEIYNHKELREKLKL--HKFRTGSDCEVIAHLYEEHGEE----------FVDMLD 118
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2059193400 155 GAYGTVVMDTRDDSrLVVARSG---SPLVIGRGI-GENFIASDQLAL 197
Cdd:PLN02549 119 GMFSFVLLDTRDNS-FIAARDHigiTPLYIGWGLdGSVWFASEMKAL 164
|
|
| SIS_1 |
cd05710 |
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ... |
295-399 |
1.33e-11 |
|
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: 61.82 E-value: 1.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 295 HIQIVACGTSYHSGMVARYWFESIAGVSCDVEIASEFRYRKSV-VRPNSLLITLSQSGETADTLAALRLAKASGyMSSLA 373
Cdd:cd05710 1 NVFFVGCGGSLADMYPAKYFLKKESKLPVFVYNAAEFLHTGPKrLTEKSVVILASHSGNTKETVAAAKFAKEKG-ATVIG 79
|
90 100
....*....|....*....|....*.
gi 2059193400 374 ICNVPGSSLVRESDLAFMTRAGAEIG 399
Cdd:cd05710 80 LTDDEDSPLAKLADYVIVYGFEIDAV 105
|
|
| PTZ00077 |
PTZ00077 |
asparagine synthetase-like protein; Provisional |
1-197 |
2.86e-10 |
|
asparagine synthetase-like protein; Provisional
Pssm-ID: 185431 [Multi-domain] Cd Length: 586 Bit Score: 63.19 E-value: 2.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 1 MCGIVGAVAQRDVAEIL----VEGLRRLEYRGYDSAGVAVfsalhplqrvrrlgkvaelakalEEQSVHGGTGIAHTRWA 76
Cdd:PTZ00077 1 MCGILAIFNSKGERHELrrkaLELSKRLRHRGPDWSGIIV-----------------------LENSPGTYNILAHERLA 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 77 THGEPSERNAHPHVSEHIVVVHNGIIENHEPLRDRLKELGYVFTSDTDTEVIAHLvhheLKEAPNlitamQKAVKQLRGA 156
Cdd:PTZ00077 58 IVDLSDGKQPLLDDDETVALMQNGEIYNHWEIRPELEKEGYKFSSNSDCEIIGHL----YKEYGP-----KDFWNHLDGM 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2059193400 157 YGTVVMDTRDDSrLVVARSG---SPLVIGRGI-GENFIASDQLAL 197
Cdd:PTZ00077 129 FATVIYDMKTNT-FFAARDHigiIPLYIGYAKdGSIWFSSELKAL 172
|
|
| SIS |
cd04795 |
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
296-367 |
1.43e-09 |
|
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars.
Pssm-ID: 240112 [Multi-domain] Cd Length: 87 Bit Score: 55.07 E-value: 1.43e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2059193400 296 IQIVACGTSYHSGMVARYWFESIAGVSCDVEIASEFRY--RKSVVRPNSLLITLSQSGETADTLAALRLAKASG 367
Cdd:cd04795 1 IFVIGIGGSGAIAAYFALELLELTGIEVVALIATELEHasLLSLLRKGDVVIALSYSGRTEELLAALEIAKELG 74
|
|
| frlB |
PRK11382 |
fructoselysine 6-phosphate deglycase; |
293-601 |
1.68e-09 |
|
fructoselysine 6-phosphate deglycase;
Pssm-ID: 183111 [Multi-domain] Cd Length: 340 Bit Score: 59.63 E-value: 1.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 293 VDHIQIVACGTSYHSGMVARYWFESIAGVSCDVEIASEF----RYRksvVRPNSLLITLSQSGETADTLAALRLAKASGY 368
Cdd:PRK11382 44 IDRIYFVACGSPLNAAQTAKHLADRFSDLQVYAISGWEFcdntPYR---LDDRCAVIGVSDYGKTEEVIKALELGRACGA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 369 MSSlAICNVPGSSLVRESDLAFMTRAGA--EIGVASTKAFTTQLAGLLMLVAAIGRCRGNLDAAAEAA--LVKSLQALPQ 444
Cdd:PRK11382 121 LTA-AFTKRADSPITSAAEFSIDYQADCiwEIHLLLCYSVVLEMITRLAPNAEIGKIKNDLKQLPNALghLVRTWEEKGR 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 445 RIKESLSLAKQIETLAEefadkhhslflgrGDQYPIAM-EGALKLKEISYIHAEAYAAGELKHGPLALIDAEMPIIVVAP 523
Cdd:PRK11382 200 QLGELASQWPMIYTVAA-------------GPLRPLGYkEGIVTLMEFTWTHGCVIESGEFRHGPLEIVEPGVPFLFLLG 266
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2059193400 524 NNDLLEKLKSNVEEVRARGGILYVFADAETGfksdetmrvmnlNHMEEVIAPIVYTVPLQLLSYYVALIKGTDVDQPR 601
Cdd:PRK11382 267 NDESRHTTERAINFVKQRTDNVIVIDYAEIS------------QGLHPWLAPFLMFVPMEWLCYYLSIYKDHNPDERR 332
|
|
| asn_synth_AEB |
TIGR01536 |
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing ... |
95-174 |
8.92e-09 |
|
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: 58.11 E-value: 8.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 95 VVVHNGIIENHEPLRDRLKELGYVFTSDTDTEVIAHLvHHELKEApnlitamqkAVKQLRGAYGTVVMDTRDDsRLVVAR 174
Cdd:TIGR01536 69 VIVFNGEIYNHEELREELEAKGYTFQTDSDTEVILHL-YEEWGEE---------CVDRLDGMFAFALWDSEKG-ELFLAR 137
|
|
| asnB |
PRK09431 |
asparagine synthetase B; Provisional |
1-202 |
1.16e-08 |
|
asparagine synthetase B; Provisional
Pssm-ID: 236513 [Multi-domain] Cd Length: 554 Bit Score: 58.00 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 1 MCGIVGAVAQRDVAEIL----VEGLRRLEYRGYDSAGVavfsalhplqrvrrlgkvaelakaleeqsVHGGTGI-AHTRW 75
Cdd:PRK09431 1 MCGIFGILDIKTDADELrkkaLEMSRLMRHRGPDWSGI-----------------------------YASDNAIlGHERL 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 76 A----THGepsernAHPHVSEH--IVVVHNGIIENHEPLRDRLKElGYVFTSDTDTEVIAHLvhheLKEAPnliTAMqka 149
Cdd:PRK09431 52 SivdvNGG------AQPLYNEDgtHVLAVNGEIYNHQELRAELGD-KYAFQTGSDCEVILAL----YQEKG---PDF--- 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2059193400 150 VKQLRGAYGTVVMDTRDDSRLvVARS--G-SPLVIGR-GIGENFIASDQLALLPVTR 202
Cdd:PRK09431 115 LDDLDGMFAFALYDSEKDAYL-IARDpiGiIPLYYGYdEHGNLYFASEMKALVPVCK 170
|
|
| SIS |
cd04795 |
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
470-551 |
1.75e-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: 51.99 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 470 LFLGRGDQYPIAMEGALKLKEISYIHAEAYAAGELKHGP-LALIDAEMPIIVVAPNNDlLEKLKSNVEEVRARGGILYVF 548
Cdd:cd04795 2 FVIGIGGSGAIAAYFALELLELTGIEVVALIATELEHASlLSLLRKGDVVIALSYSGR-TEELLAALEIAKELGIPVIAI 80
|
...
gi 2059193400 549 ADA 551
Cdd:cd04795 81 TDA 83
|
|
| SIS_RpiR |
cd05013 |
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ... |
286-416 |
2.11e-08 |
|
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many phosphosugar isomerases and phosphosugar binding proteins. In E. coli, rpiR negatively regulates the expression of rpiB gene. Both rpiB and rpiA are ribose phosphate isomerases that catalyze the reversible reactions of ribose 5-phosphate into ribulose 5-phosphate.
Pssm-ID: 240144 [Multi-domain] Cd Length: 139 Bit Score: 53.39 E-value: 2.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 286 ARAIFDKVDHIQIVACGtsyHSGMVARYwFE---SIAGVSCDVEIAS-EFRYRKSVVRPNSLLITLSQSGETADTLAALR 361
Cdd:cd05013 6 AVDLLAKARRIYIFGVG---SSGLVAEY-LAyklLRLGKPVVLLSDPhLQLMSAANLTPGDVVIAISFSGETKETVEAAE 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2059193400 362 LAKASGyMSSLAICNVPGSSLVRESDLAFMTraGAEIGVASTKAFTTQLAGLLML 416
Cdd:cd05013 82 IAKERG-AKVIAITDSANSPLAKLADIVLLV--SSEEGDFRSSAFSSRIAQLALI 133
|
|
| RpiR |
COG1737 |
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ... |
230-445 |
6.41e-08 |
|
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains [Transcription];
Pssm-ID: 441343 [Multi-domain] Cd Length: 286 Bit Score: 54.55 E-value: 6.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 230 VVREEKESDISHDAGDKGEYRHYMLKEIHEQPAAINQTLDGrlgIDHVVVESFgngARAIFDKvDHIQIVACGTSYHSGM 309
Cdd:COG1737 78 LAEGLSSYERLRRLSPDDSLEDILAKVLEAEIANLEETLEL---LDEEALERA---VDLLAKA-RRIYIFGVGASAPVAE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 310 VARYWFESIaGVSCDV--EIASEFRYRKSVVRPNSLLITLSQSGETADTLAALRLAKASGyMSSLAICNVPGSSLVRESD 387
Cdd:COG1737 151 DLAYKLLRL-GKNVVLldGDGHLQAESAALLGPGDVVIAISFSGYTRETLEAARLAKERG-AKVIAITDSPLSPLAKLAD 228
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2059193400 388 LAFMTRAGAEIGVAStkAFTTQLAGLLM---LVAAIGRCRGnldAAAEAALVKSLQALPQR 445
Cdd:COG1737 229 VVLYVPSEEPTLRSS--AFSSRVAQLALidaLAAAVAQRDG---DKARERLERTEALLSEL 284
|
|
| SIS_AgaS_like |
cd05010 |
AgaS-like protein. AgaS contains a SIS (Sugar ISomerase) domain which is found in many ... |
471-600 |
2.18e-07 |
|
AgaS-like protein. AgaS contains a SIS (Sugar ISomerase) domain which is found in many phosphosugar isomerases and phosphosugar binding proteins. AgaS is a putative isomerase in Escherichia coli. It is similar to the glucosamine-6-phosphate synthases (GlmS) which catalyzes the first step in hexosamine metabolism, converting fructose 6-phosphate into glucosamine 6-phosphate using glutamine as nitrogen source.
Pssm-ID: 240143 [Multi-domain] Cd Length: 151 Bit Score: 50.70 E-value: 2.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 471 FLGRGDQYPIAMEGALKLKEIS--YIHAEAYAAGELKHGPLALIDAEMPIIVVAPNN--------DLLEKLKSNveevRA 540
Cdd:cd05010 3 YLGSGPLAGLAREAALKVLELTagKVATVYDSPLGFRHGPKSLVDDDTLVVVFVSNDpytrqydlDLLKELRRD----GI 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2059193400 541 RGGILYVFADAETGFKSDETMRVMNLNHMEEV-IAPiVYTVPLQLLSYYVALIKGTDVDQP 600
Cdd:cd05010 79 AARVIAISPESDAGIEDNSHYYLPGSRDLDDVyLAF-PYILYAQLFALFNSIALGLTPDNP 138
|
|
| SIS_Etherase |
cd05007 |
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ... |
324-427 |
9.02e-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: 44.44 E-value: 9.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 324 DVEIASEFRYRKSVVRPNSLLITLSQSGETADTLAALRLAKASGYMSsLAICNVPGSSLVRESDLAFMTRAGAEIGVAST 403
Cdd:cd05007 102 DDEEAGAADLQAINLTERDVVIGIAASGRTPYVLGALRYARARGALT-IGIACNPGSPLLQLADIAIALITGPEVVAGST 180
|
90 100 110
....*....|....*....|....*....|
gi 2059193400 404 --KAFTTQLAGLLMLVAAI----GRCRGNL 427
Cdd:cd05007 181 rlKAGTAQKLALNMLSTAVmirlGKVYGNL 210
|
|
| GATase_4 |
pfam13230 |
Glutamine amidotransferases class-II; This family captures members that are not found in ... |
29-128 |
3.58e-04 |
|
Glutamine amidotransferases class-II; This family captures members that are not found in pfam00310.
Pssm-ID: 433047 [Multi-domain] Cd Length: 272 Bit Score: 42.70 E-value: 3.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 29 YDSAGVAVFSALHPLQRVRrlgkVAELAKALEEQSVhggTGIAHTRWATHGEPSERNAHPHVSE----HIVVVHNGIIEN 104
Cdd:pfam13230 41 YEGRGARVFKDPQPSADSP----IAELVRRYPIRSR---NVIAHIRKATQGRVTLENTHPFMRElwgrYWIFAHNGDLKG 113
|
90 100
....*....|....*....|....
gi 2059193400 105 HEPLRDRLkelgYVFTSDTDTEVI 128
Cdd:pfam13230 114 YAPKLSGR----FQPVGSTDSELA 133
|
|
| murQ |
PRK05441 |
N-acetylmuramic acid-6-phosphate etherase; Reviewed |
338-427 |
5.75e-04 |
|
N-acetylmuramic acid-6-phosphate etherase; Reviewed
Pssm-ID: 235467 [Multi-domain] Cd Length: 299 Bit Score: 42.08 E-value: 5.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059193400 338 VRPNSLLITLSQSGETADTLAALRLAKASGyMSSLAICNVPGSSLVRESDLAFMTRAGAEIGVAST--KAFTTQLAGLLM 415
Cdd:PRK05441 129 LTAKDVVVGIAASGRTPYVIGALEYARERG-ALTIGISCNPGSPLSKEADIAIEVVVGPEVLTGSTrmKAGTAQKLVLNM 207
|
90
....*....|....*.
gi 2059193400 416 LVAA----IGRCRGNL 427
Cdd:PRK05441 208 ISTGvmirLGKVYGNL 223
|
|
| |
