|
Name |
Accession |
Description |
Interval |
E-value |
| GlmS |
COG0449 |
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ... |
1-609 |
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: 1071.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 1 MCGIVGAVAQRDIAEILLEGLRRLEYRGYDSAGLAVVDsEGHMTRVRRLGKVQMLAQAVEEQPLHGGTGIAHTRWATHGE 80
Cdd:COG0449 1 MCGIVGYIGKRDAAPILLEGLKRLEYRGYDSAGIAVLD-DGGLEVRKAVGKLANLEEKLAEEPLSGTIGIGHTRWATHGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 81 PSESNAHPHVS--EHIVVVHNGIIENHEPLRALLQSRGYVFVTETDTEVIAHLVHWELEQGGTLREAVLRAIPQLRGAYG 158
Cdd:COG0449 80 PSDENAHPHTScsGRIAVVHNGIIENYAELREELEAKGHTFKSETDTEVIAHLIEEYLKGGGDLLEAVRKALKRLEGAYA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 159 TVIMDTRDPGTLLAARSGSPLVIGLGMGENFIASDQLALLPVTRRFIFLEEGDIAEVTRRSVVIFDKSGAEVKRQEIESN 238
Cdd:COG0449 160 LAVISADEPDRIVAARKGSPLVIGLGEGENFLASDVPALLPYTRRVIYLEDGEIAVLTRDGVEIYDLDGEPVEREVKTVD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 239 LQYDAGDKGIYRHYMQKEIFEQPNAIKNTLTGRIS-HGEVDLSELgPNANEMLAQVEHIQIVACGTSYNSGMVSRYWFEA 317
Cdd:COG0449 240 WDAEAAEKGGYPHFMLKEIHEQPEAIRDTLRGRLDeDGRVVLDEL-NLAAEDLRNIDRIYIVACGTSYHAGLVGKYLIEE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 318 LAGVPCDVEIASEFRYRKSAVRRNSLMITLSQSGETADTLAALRLSKELGyLGSLAICNVPGSSLVRESDLALMTKAGTE 397
Cdd:COG0449 319 LARIPVEVEIASEFRYRDPVVDPGTLVIAISQSGETADTLAALREAKEKG-AKVLAICNVVGSTIARESDAVLYTHAGPE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 398 IGVASTKAFTTQLTVLLMLVAKLARLKGQ-DASIEHDIVHGLQALPNRIEQMLSQDKRIEQLAERFSDKHHALFLGRGDQ 476
Cdd:COG0449 398 IGVASTKAFTTQLAALYLLALYLARARGTlSAEEEAELLEELRKLPEKIEEVLDLEEQIEELAEKYADARNALFLGRGIN 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 477 YPIAMEGALKLKEISYIHAEAYAAGELKHGPLALIDAEMPVIVVAPNNELLEKLKSNIEEVRARGGELYVFADGEAGFNG 556
Cdd:COG0449 478 YPVALEGALKLKEISYIHAEGYAAGELKHGPIALIDEGMPVVAIAPQDELYEKTLSNIQEVKARGGKVIAIADEGDEEVE 557
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 1440323431 557 SDNMHIIEMPHVEETIAPIFYTVPLQLLAYHVALIKGTDVDQPRNLAKSVTVE 609
Cdd:COG0449 558 ELADDVIEVPEVDELLAPILAVVPLQLLAYHVAVLRGTDVDQPRNLAKSVTVE 610
|
|
| PRK00331 |
PRK00331 |
isomerizing glutamine--fructose-6-phosphate transaminase; |
1-609 |
0e+00 |
|
isomerizing glutamine--fructose-6-phosphate transaminase;
Pssm-ID: 234729 [Multi-domain] Cd Length: 604 Bit Score: 1069.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 1 MCGIVGAVAQRDIAEILLEGLRRLEYRGYDSAGLAVVDsEGHMTRVRRLGKVQMLAQAVEEQPLHGGTGIAHTRWATHGE 80
Cdd:PRK00331 1 MCGIVGYVGQRNAAEILLEGLKRLEYRGYDSAGIAVLD-DGGLEVRKAVGKVANLEAKLEEEPLPGTTGIGHTRWATHGK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 81 PSESNAHPHVS--EHIVVVHNGIIENHEPLRALLQSRGYVFVTETDTEVIAHLVHWELEQGGTLREAVLRAIPQLRGAYG 158
Cdd:PRK00331 80 PTERNAHPHTDcsGRIAVVHNGIIENYAELKEELLAKGHVFKSETDTEVIAHLIEEELKEGGDLLEAVRKALKRLEGAYA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 159 TVIMDTRDPGTLLAARSGSPLVIGLGMGENFIASDQLALLPVTRRFIFLEEGDIAEVTRRSVVIFDKSGAEVKRQEIESN 238
Cdd:PRK00331 160 LAVIDKDEPDTIVAARNGSPLVIGLGEGENFLASDALALLPYTRRVIYLEDGEIAVLTRDGVEIFDFDGNPVEREVYTVD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 239 LQYDAGDKGIYRHYMQKEIFEQPNAIKNTLTGRIshgevDLSELGPNANEMLAQVEHIQIVACGTSYNSGMVSRYWFEAL 318
Cdd:PRK00331 240 WDASAAEKGGYRHFMLKEIYEQPEAIRDTLEGRL-----DELGEGELADEDLKKIDRIYIVACGTSYHAGLVAKYLIESL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 319 AGVPCDVEIASEFRYRKSAVRRNSLMITLSQSGETADTLAALRLSKELGyLGSLAICNVPGSSLVRESDLALMTKAGTEI 398
Cdd:PRK00331 315 AGIPVEVEIASEFRYRDPVLSPKTLVIAISQSGETADTLAALRLAKELG-AKTLAICNVPGSTIARESDAVLYTHAGPEI 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 399 GVASTKAFTTQLTVLLMLVAKLARLKG-QDASIEHDIVHGLQALPNRIEQMLSQDKRIEQLAERFSDKHHALFLGRGDQY 477
Cdd:PRK00331 394 GVASTKAFTAQLAVLYLLALALAKARGtLSAEEEADLVHELRELPALIEQVLDLKEQIEELAEDFADARNALFLGRGVDY 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 478 PIAMEGALKLKEISYIHAEAYAAGELKHGPLALIDAEMPVIVVAPNNELLEKLKSNIEEVRARGGELYVFADgEAGFNGS 557
Cdd:PRK00331 474 PVALEGALKLKEISYIHAEGYAAGELKHGPIALIDEGMPVVAIAPNDELYEKTKSNIQEVKARGARVIVIAD-EGDEVAE 552
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 1440323431 558 DNMHIIEMPHVEETIAPIFYTVPLQLLAYHVALIKGTDVDQPRNLAKSVTVE 609
Cdd:PRK00331 553 EADDVIEVPEVHELLAPLLYVVPLQLLAYHVALARGTDVDKPRNLAKSVTVE 604
|
|
| glmS |
TIGR01135 |
glucosamine--fructose-6-phosphate aminotransferase (isomerizing); The member from ... |
2-609 |
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: 991.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 2 CGIVGAVAQRDIAEILLEGLRRLEYRGYDSAGLAVVDsEGHMTRVRRLGKVQMLAQAVEEQPLHGGTGIAHTRWATHGEP 81
Cdd:TIGR01135 1 CGIVGYIGQRDAVPILLEGLKRLEYRGYDSAGIAVVD-EGKLFVRKAVGKVAELANKLGEKPLPGGVGIGHTRWATHGKP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 82 SESNAHPHVSEH--IVVVHNGIIENHEPLRALLQSRGYVFVTETDTEVIAHLVHWELEQGGTLREAVLRAIPQLRGAYGT 159
Cdd:TIGR01135 80 TDENAHPHTDEGgrIAVVHNGIIENYAELREELEARGHVFSSDTDTEVIAHLIEEELREGGDLLEAVQKALKQLRGAYAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 160 VIMDTRDPGTLLAARSGSPLVIGLGMGENFIASDQLALLPVTRRFIFLEEGDIAEVTRRSVVIFDKSGAEVKRQEIESNL 239
Cdd:TIGR01135 160 AVLHADHPETLVAARSGSPLIVGLGDGENFVASDVTALLPYTRRVIYLEDGDIAILTKDGVEIYNFEGAPVQREVRVIDW 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 240 QYDAGDKGIYRHYMQKEIFEQPNAIKNTLTGRISHGEVDLSELGpnANEMLAQVEHIQIVACGTSYNSGMVSRYWFEALA 319
Cdd:TIGR01135 240 DLDAAEKGGYRHFMLKEIYEQPRALRDTLEGRIEENGGVFEELG--AEELLKNIDRIQIVACGTSYHAGLVAKYLIERLA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 320 GVPCDVEIASEFRYRKSAVRRNSLMITLSQSGETADTLAALRLSKELGyLGSLAICNVPGSSLVRESDLALMTKAGTEIG 399
Cdd:TIGR01135 318 GIPVEVEIASEFRYRKPVVDKDTLVIAISQSGETADTLEALRLAKELG-AKTLGICNVPGSTLVREADHTLYTRAGPEIG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 400 VASTKAFTTQLTVLLMLVAKLARLKGQ-DASIEHDIVHGLQALPNRIEQMLSQDKRIEQLAERFSDKHHALFLGRGDQYP 478
Cdd:TIGR01135 397 VASTKAFTTQLTVLYLLALALAKARGTlSAEEEAELVDALRRLPDLVEQVLLADESIAELAERYADKRNFLFLGRGLGYP 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 479 IAMEGALKLKEISYIHAEAYAAGELKHGPLALIDAEMPVIVVAPNNELLEKLKSNIEEVRARGGELYVFADGEAGFNGSD 558
Cdd:TIGR01135 477 IALEGALKLKEISYIHAEGYPAGELKHGPIALIDEGLPVVAIAPKDSLLEKTKSNVEEVKARGARVIVFAPEDDETIASV 556
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 1440323431 559 NMHIIEMPHVEETIAPIFYTVPLQLLAYHVALIKGTDVDQPRNLAKSVTVE 609
Cdd:TIGR01135 557 ADDVIKLPEVEELLAPIVYTIPLQLLAYHIALAKGTDVDKPRNLAKSVTVE 607
|
|
| PLN02981 |
PLN02981 |
glucosamine:fructose-6-phosphate aminotransferase |
1-609 |
9.82e-172 |
|
glucosamine:fructose-6-phosphate aminotransferase
Pssm-ID: 215531 [Multi-domain] Cd Length: 680 Bit Score: 503.90 E-value: 9.82e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 1 MCGIVGAV------AQRDIAEILLEGLRRLEYRGYDSAGLAVVDSEGHMTR----VRRLGKVQMLAQAVEEQ----PLHG 66
Cdd:PLN02981 1 MCGIFAYLnynvprERRFILEVLFNGLRRLEYRGYDSAGIAIDNDPSLESSsplvFREEGKIESLVRSVYEEvaetDLNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 67 G------TGIAHTRWATHGEPSESNAHPHVSE---HIVVVHNGIIENHEPLRALLQSRGYVFVTETDTEVIAHLVHW--- 134
Cdd:PLN02981 81 DlvfenhAGIAHTRWATHGPPAPRNSHPQSSGpgnEFLVVHNGIITNYEVLKETLLRHGFTFESDTDTEVIPKLAKFvfd 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 135 ---ELEQGGTLREAVLRAIPQLRGAYGTVIMDTRDPGTLLAARSGSPLVIG---LGMGEN-------------------- 188
Cdd:PLN02981 161 klnEEEGDVTFSQVVMEVMRQLEGAYALIFKSPHYPNELVACKRGSPLLLGvkeLPEEKNssavftsegfltknrdkpke 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 189 -FIASDQLALLPVTRRFIFLEEGDIAEVTRRSVVIF-------DKSGAEVKRQEIE---SNLQYDAGD--KGIYRHYMQK 255
Cdd:PLN02981 241 fFLASDASAVVEHTKRVLVIEDNEVVHLKDGGVGIYkfenekgRGGGGLSRPASVEralSTLEMEVEQimKGNYDHYMQK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 256 EIFEQPNAIKNTLTGRISHGEVDLSE---LGPNANEM--LAQVEHIQIVACGTSYNSGMVSRYWFEALAGVPCDVEIASE 330
Cdd:PLN02981 321 EIHEQPESLTTTMRGRLIRGGSGKAKrvlLGGLKDHLktIRRSRRIVFIGCGTSYNAALAARPILEELSGVPVTMELASD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 331 FRYRKSAVRRNSLMITLSQSGETADTLAALRLSKELGYLgSLAICNVPGSSLVRESDLALMTKAGTEIGVASTKAFTTQL 410
Cdd:PLN02981 401 LLDRQGPIYREDTAVFVSQSGETADTLRALEYAKENGAL-CVGITNTVGSAISRGTHCGVHINAGAEIGVASTKAYTSQI 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 411 TVLLMLVAKLARLKGQDASIEHDIVHGLQALPNRIEQMLSQDKRIEQLAERFSDKHHALFLGRGDQYPIAMEGALKLKEI 490
Cdd:PLN02981 480 VAMTMLALALGEDSISSRSRREAIIDGLFDLPNKVREVLKLDQEMKELAELLIDEQSLLVFGRGYNYATALEGALKVKEV 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 491 SYIHAEAYAAGELKHGPLALIDAEMPVIVVAPNNELLEKLKSNIEEVRARGGELYVFA---DGEAGFNGSDNMhIIEMPH 567
Cdd:PLN02981 560 ALMHSEGILAGEMKHGPLALVDETLPIIVIATRDACFSKQQSVIQQLRARKGRLIVICskgDASSVCPSGGCR-VIEVPQ 638
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1440323431 568 VEETIAPIFYTVPLQLLAYHVALIKGTDVDQPRNLAKSVTVE 609
Cdd:PLN02981 639 VEDCLQPVINIVPLQLLAYHLTVLRGHNVDQPRNLAKSVTTQ 680
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
1-608 |
2.13e-164 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 483.75 E-value: 2.13e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 1 MCGIVGAVAQRDIAEILLEGLRRLEYRGYDSAGLAVVDSEGHMTrVRRLGKVQMLAQAVEE-----QPLHGGT--GIAHT 73
Cdd:PTZ00295 24 CCGIVGYLGNEDASKILLEGIEILQNRGYDSCGISTISSGGELK-TTKYASDGTTSDSIEIlkeklLDSHKNStiGIAHT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 74 RWATHGEPSESNAHPHV--SEHIVVVHNGIIENHEPLRALLQSRGYVFVTETDTEVIAHLVHWELEQGGTLREAVLRAIP 151
Cdd:PTZ00295 103 RWATHGGKTDENAHPHCdyKKRIALVHNGTIENYVELKSELIAKGIKFRSETDSEVIANLIGLELDQGEDFQEAVKSAIS 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 152 QLRGAYGTVIMDTRDPGTLLAARSGSPLVIGLGMGENFIASDQLALLPVTRRFIFLEEGDIAEVTrRSVVIFDKSGAEVK 231
Cdd:PTZ00295 183 RLQGTWGLCIIHKDNPDSLIVARNGSPLLVGIGDDSIYVASEPSAFAKYTNEYISLKDGEIAELS-LENVNDLYTQRRVE 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 232 R---QEIESNlqydagdKGIYRHYMQKEIFEQPNAIKNTLT--GRISHGE--VDLSELGPNANEmLAQVEHIQIVACGTS 304
Cdd:PTZ00295 262 KipeEVIEKS-------PEPYPHWTLKEIFEQPIALSRALNngGRLSGYNnrVKLGGLDQYLEE-LLNIKNLILVGCGTS 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 305 YNSGMVSRYWFEALAGV-PCDVEIASEF-RYRKSavRRNSLMITLSQSGETADTLAALRLSKELGYLgSLAICNVPGSSL 382
Cdd:PTZ00295 334 YYAALFAASIMQKLKCFnTVQVIDASELtLYRLP--DEDAGVIFISQSGETLDVVRALNLADELNLP-KISVVNTVGSLI 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 383 VRESDLALMTKAGTEIGVASTKAFTTQLTVLLMLVAKLARLKGQDASIEH--DIVHGLQALPNRIEQMLSQDKRI-EQLA 459
Cdd:PTZ00295 411 ARSTDCGVYLNAGREVAVASTKAFTSQVTVLSLIALWFAQNKEYSCSNYKcsSLINSLHRLPTYIGMTLKSCEEQcKRIA 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 460 ERFSDKHHALFLGRGDQYPIAMEGALKLKEISYIHAEAYAAGELKHGPLALIDAE--MPVIVVAPNNELLEKLKSNIEEV 537
Cdd:PTZ00295 491 EKLKNAKSMFILGKGLGYPIALEGALKIKEITYIHAEGFSGGALKHGPFALIDKEknTPVILIILDDEHKELMINAAEQV 570
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1440323431 538 RARGGELYVFADGEA-GFNGSDnmHIIEMPHVeETIAPIFYTVPLQLLAYHVALIKGTDVDQPRNLAKSVTV 608
Cdd:PTZ00295 571 KARGAYIIVITDDEDlVKDFAD--EIILIPSN-GPLTALLAVIPLQLLAYEIAILRGINPDKPRGLAKTVTV 639
|
|
| PTZ00394 |
PTZ00394 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
1-609 |
5.45e-154 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 173585 [Multi-domain] Cd Length: 670 Bit Score: 458.19 E-value: 5.45e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 1 MCGIVGAVAQ------RDIAEILLEGLRRLEYRGYDSAGLAVVDSEGHMTR--------------VRRLGKVQML----- 55
Cdd:PTZ00394 1 MCGIFGYANHnvprtvEQILNVLLDGIQKVEYRGYDSAGLAIDANIGSEKEdgtaasaptprpcvVRSVGNISQLrekvf 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 56 --AQAVEEQPLHGGT----GIAHTRWATHGEPSESNAHPHVSEH--IVVVHNGIIENHEPLRALLQSRGYVFVTETDTEV 127
Cdd:PTZ00394 81 seAVAATLPPMDATTshhvGIAHTRWATHGGVCERNCHPQQSNNgeFTIVHNGIVTNYMTLKELLKEEGYHFSSDTDTEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 128 IAHLVHWELEQGG--TLREAVLRAIPQLRGAYGTVIMDTRDPGTLLAARSGSPLVIGL---------------------G 184
Cdd:PTZ00394 161 ISVLSEYLYTRKGihNFADLALEVSRMVEGSYALLVKSVYFPGQLAASRKGSPLMVGIrrtddrgcvmklqtydltdlsG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 185 MGENFIASDQLALLPVTRRFIFLEEGDIAEVTRRSVVIFDKSGAE---VKRQEIESNLQYDAGDKGIYRHYMQKEIFEQP 261
Cdd:PTZ00394 241 PLEVFFSSDVNSFAEYTREVVFLEDGDIAHYCDGALRFYNAAERQrsiVKREVQHLDAKPEGLSKGNYPHFMLKEIYEQP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 262 NAIKNTLTGRI--SHGEVDLSELGPNANEMLAQVEHIQIVACGTSYNSGMVSRYWFEALAGVPCDVEIASEFRYRKSAVR 339
Cdd:PTZ00394 321 ESVISSMHGRIdfSSGTVQLSGFTQQSIRAILTSRRILFIACGTSLNSCLAVRPLFEELVPLPISVENASDFLDRRPRIQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 340 RNSLMITLSQSGETADTLAALRLSKELGYLgSLAICNVPGSSLVRESDLALMTKAGTEIGVASTKAFTTQLtVLLMLVAK 419
Cdd:PTZ00394 401 RDDVCFFVSQSGETADTLMALQLCKEAGAM-CVGITNVVGSSISRLTHYAIHLNAGVEVGVASTKAYTSQV-VVLTLVAL 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 420 LarLKGQDASIEH---DIVHGLQALPNRIEQMLS-QDKRIEQLAERFSDKHHALFLGRGDQYPIAMEGALKLKEISYIHA 495
Cdd:PTZ00394 479 L--LSSDSVRLQErrnEIIRGLAELPAAISECLKiTHDPVKALAARLKESSSILVLGRGYDLATAMEAALKVKELSYVHT 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 496 EAYAAGELKHGPLALIDAEMPVIVVAPNNELLEKLKSNIEEVRARGGELYVFADGEAGFNGSDNMHIIEMPHVEETIAPI 575
Cdd:PTZ00394 557 EGIHSGELKHGPLALIDETSPVLAMCTHDKHFGLSKSAVQQVKARGGAVVVFATEVDAELKAAASEIVLVPKTVDCLQCV 636
|
650 660 670
....*....|....*....|....*....|....
gi 1440323431 576 FYTVPLQLLAYHVALIKGTDVDQPRNLAKSVTVE 609
Cdd:PTZ00394 637 VNVIPFQLLAYYMALLRGNNVDCPRNLAKSVTVQ 670
|
|
| GFAT |
cd00714 |
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ... |
2-215 |
1.17e-124 |
|
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: 366.39 E-value: 1.17e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 2 CGIVGAVAQRDIAEILLEGLRRLEYRGYDSAGLAVvDSEGHMTRVRRLGKVQMLAQAVEEQPLHGGTGIAHTRWATHGEP 81
Cdd:cd00714 1 CGIVGYIGKREAVDILLEGLKRLEYRGYDSAGIAV-IGDGSLEVVKAVGKVANLEEKLAEKPLSGHVGIGHTRWATHGEP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 82 SESNAHPHVSEH--IVVVHNGIIENHEPLRALLQSRGYVFVTETDTEVIAHLVHWELEQGGTLREAVLRAIPQLRGAYGT 159
Cdd:cd00714 80 TDVNAHPHRSCDgeIAVVHNGIIENYAELKEELEAKGYKFESETDTEVIAHLIEYYYDGGLDLLEAVKKALKRLEGAYAL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1440323431 160 VIMDTRDPGTLLAARSGSPLVIGLGMGENFIASDQLALLPVTRRFIFLEEGDIAEV 215
Cdd:cd00714 160 AVISKDEPDEIVAARNGSPLVIGIGDGENFVASDAPALLEHTRRVIYLEDGDIAVI 215
|
|
| AgaS |
COG2222 |
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ... |
255-609 |
1.54e-75 |
|
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: 244.04 E-value: 1.54e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 255 KEIFEQPNAIKNTLTGRISHGEVDLSELGPNANEMLAqvehiqIVACGTSYNSGMVSRYWFEALAGVPCDVEIASEF-RY 333
Cdd:COG2222 2 REIAQQPEAWRRALAALAAAIAALLARLRAKPPRRVV------LVGAGSSDHAAQAAAYLLERLLGIPVAALAPSELvVY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 334 RKSAVRRNSLMITLSQSGETADTLAALRLSKELGYLgSLAICNVPGSSLVRESDLALMTKAGTEIGVASTKAFTTQLTVL 413
Cdd:COG2222 76 PAYLKLEGTLVVAISRSGNSPEVVAALELAKARGAR-TLAITNNPDSPLAEAADRVLPLPAGPEKSVAATKSFTTMLLAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 414 LMLVAKLarlkGQDASIEHDivhgLQALPNRIEQMLSQDKRIEQLAErFSDKHHALFLGRGDQYPIAMEGALKLKEISYI 493
Cdd:COG2222 155 LALLAAW----GGDDALLAA----LDALPAALEAALAADWPAAALAA-LADAERVVFLGRGPLYGLAREAALKLKELSAG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 494 HAEAYAAGELKHGPLALIDAEMPVIVVAPNNELLEKLKSNIEEVRARGGELYVFADGeagfnGSDNMHIIEMPHVEETIA 573
Cdd:COG2222 226 HAEAYSAAEFRHGPKSLVDPGTLVVVLASEDPTRELDLDLAAELRALGARVVAIGAE-----DDAAITLPAIPDLHDALD 300
|
330 340 350
....*....|....*....|....*....|....*.
gi 1440323431 574 PIFYTVPLQLLAYHVALIKGTDVDQPRNLAKSVTVE 609
Cdd:COG2222 301 PLLLLVVAQRLALALALARGLDPDTPRHLNKVVKTV 336
|
|
| SIS_GlmS_GlmD_2 |
cd05009 |
SIS (Sugar ISomerase) domain repeat 2 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
453-607 |
5.82e-70 |
|
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: 222.91 E-value: 5.82e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 453 KRIEQLAERFSDKHHALFLGRGDQYPIAMEGALKLKEISYIHAEAYAAGELKHGPLALIDAEMPVIVVAPNNELLEKLKS 532
Cdd:cd05009 1 EDIKELAEKLKEAKSFYVLGRGPNYGTALEGALKLKETSYIHAEAYSAGEFKHGPIALVDEGTPVIFLAPEDRLEEKLES 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1440323431 533 NIEEVRARGGELYVFADGEAGFNGSDnmHIIEMPHVEETIAPIFYTVPLQLLAYHVALIKGTDVDQPRNLAKSVT 607
Cdd:cd05009 81 LIKEVKARGAKVIVITDDGDAKDLAD--VVIRVPATVEELSPLLYIVPLQLLAYHLAVARGIDPDKPRNLAKSVT 153
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
2-213 |
4.67e-64 |
|
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: 210.00 E-value: 4.67e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 2 CGIVGAVAQRDIAEILLE----GLRRLEYRGYDSAGLAVVDSEGHMtRVRRLGKVQMLAQAVEEQPLHGGTGIAHTRWAT 77
Cdd:cd00352 1 CGIFGIVGADGAASLLLLlllrGLAALEHRGPDGAGIAVYDGDGLF-VEKRAGPVSDVALDLLDEPLKSGVALGHVRLAT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 78 HGEPSESNAHPHVSE--HIVVVHNGIIENHEPLRALLQSRGYVFVTETDTEVIAHLVHWELEQGGtLREAVLRAIPQLRG 155
Cdd:cd00352 80 NGLPSEANAQPFRSEdgRIALVHNGEIYNYRELREELEARGYRFEGESDSEVILHLLERLGREGG-LFEAVEDALKRLDG 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1440323431 156 AYGTVIMDtRDPGTLLAARSG---SPLVIGLGM-GENFIASDQLALLPVT-RRFIFLEEGDIA 213
Cdd:cd00352 159 PFAFALWD-GKPDRLFAARDRfgiRPLYYGITKdGGLVFASEPKALLALPfKGVRRLPPGELL 220
|
|
| SIS_GlmS_GlmD_1 |
cd05008 |
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
295-421 |
3.82e-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: 193.48 E-value: 3.82e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 295 HIQIVACGTSYNSGMVSRYWFEALAGVPCDVEIASEFRYRKSAVRRNSLMITLSQSGETADTLAALRLSKELGYLgSLAI 374
Cdd:cd05008 1 RILIVGCGTSYHAALVAKYLLERLAGIPVEVEAASEFRYRRPLLDEDTLVIAISQSGETADTLAALRLAKEKGAK-TVAI 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1440323431 375 CNVPGSSLVRESDLALMTKAGTEIGVASTKAFTTQLTVLLMLVAKLA 421
Cdd:cd05008 80 TNVVGSTLAREADYVLYLRAGPEISVAATKAFTSQLLALLLLALALA 126
|
|
| PurF |
COG0034 |
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ... |
1-182 |
8.16e-37 |
|
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: 143.24 E-value: 8.16e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 1 MCGIVGAVAQRDIAEILLEGLRRLEYRGYDSAGLAVVDsEGHMTRVRRLGKVqmlAQAVEE---QPLHGGTGIAHTRWAT 77
Cdd:COG0034 7 ECGVFGIYGHEDVAQLTYYGLYALQHRGQESAGIATSD-GGRFHLHKGMGLV---SDVFDEedlERLKGNIAIGHVRYST 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 78 HGEPSESNAHPHVSEH----IVVVHNGIIENHEPLRALLQSRGYVFVTETDTEVIAHLVHWELEqGGTLREAVLRAIPQL 153
Cdd:COG0034 83 TGSSSLENAQPFYVNSpfgsIALAHNGNLTNAEELREELEEEGAIFQTTSDTEVILHLIARELT-KEDLEEAIKEALRRV 161
|
170 180 190
....*....|....*....|....*....|..
gi 1440323431 154 RGAYGTVIMdtrDPGTLLAAR--SG-SPLVIG 182
Cdd:COG0034 162 KGAYSLVIL---TGDGLIAARdpNGiRPLVLG 190
|
|
| GPATase_N |
cd00715 |
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ... |
2-225 |
7.13e-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: 132.20 E-value: 7.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 2 CGIVGAVAQRDIAEILLEGLRRLEYRGYDSAGLAVVDSEgHMTRVRRLGkvqMLAQAVEE---QPLHGGTGIAHTRWATH 78
Cdd:cd00715 1 CGVFGIYGAEDAARLTYLGLYALQHRGQESAGIATSDGK-RFHTHKGMG---LVSDVFDEeklRRLPGNIAIGHVRYSTA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 79 GEPSESNAHPHVSEH----IVVVHNGIIENHEPLRALLQSRGYVFVTETDTEVIAHLVHWELEQgGTLREAVLRAIPQLR 154
Cdd:cd00715 77 GSSSLENAQPFVVNSplggIALAHNGNLVNAKELREELEEEGRIFQTTSDSEVILHLIARSLAK-DDLFEAIIDALERVK 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1440323431 155 GAYGTVIMdTRDpgTLLAAR--SG-SPLVIG-LGMGENFIASDQLALLPVTRRFIF-LEEGDIAEVTR---RSVVIFDK 225
Cdd:cd00715 156 GAYSLVIM-TAD--GLIAVRdpHGiRPLVLGkLEGDGYVVASESCALDIIGAEFVRdVEPGEIVVIDDdglESSQRAPK 231
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
289-419 |
2.76e-33 |
|
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars. Presumably the SIS domains bind to the end-product of the pathway.
Pssm-ID: 426230 [Multi-domain] Cd Length: 131 Bit Score: 123.95 E-value: 2.76e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 289 MLAQVEHIQIVACGTSYNSGMVSRYWFEALAGVPCDVEIASEFRYR-KSAVRRNSLMITLSQSGETADTLAALRLSKELG 367
Cdd:pfam01380 1 LLAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGvLALVDEDDLVIAISYSGETKDLLAAAELAKARG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1440323431 368 yLGSLAICNVPGSSLVRESDLALMTKAGTEIGVASTKAFTTQLTVLLMLVAK 419
Cdd:pfam01380 81 -AKIIAITDSPGSPLAREADHVLYINAGPETGVASTKSITAQLAALDALAVA 131
|
|
| purF |
TIGR01134 |
amidophosphoribosyltransferase; Alternate name: glutamine phosphoribosylpyrophosphate (PRPP) ... |
2-197 |
1.53e-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: 130.52 E-value: 1.53e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 2 CGIVGAVAQR-DIAEILLEGLRRLEYRGYDSAGLAVVDseGHMTRVRR-LGKVQMLAQAVEEQPLHGGTGIAHTRWATHG 79
Cdd:TIGR01134 1 CGVVGIYGQEeVAASLTYYGLYALQHRGQESAGISVFD--GNRFRLHKgNGLVSDVFNEEHLQRLKGNVGIGHVRYSTAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 80 EPSESNAHPHVSE----HIVVVHNGIIENHEPLRALLQSRGYVFVTETDTEVIAHLVHWELEQGGTLREAVLRAIPQLRG 155
Cdd:TIGR01134 79 SSGLENAQPFVVNspygGLALAHNGNLVNADELRRELEEEGRHFNTTSDSEVLLHLLAHNDESKDDLFDAVARVLERVRG 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1440323431 156 AYGTVIMdtrDPGTLLAARS--G-SPLVIGlGMGENF-IASDQLAL 197
Cdd:TIGR01134 159 AYALVLM---TEDGLVAVRDphGiRPLVLG-RRGDGYvVASESCAL 200
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
462-592 |
4.51e-29 |
|
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: 112.01 E-value: 4.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 462 FSDKHHALFLGRGDQYPIAMEGALKLKEISYIHAEAYAAGELKHGPLALIDAEMPVIVVAPNNELLEKLKsNIEEVRARG 541
Cdd:pfam01380 2 LAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGVLALVDEDDLVIAISYSGETKDLLA-AAELAKARG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1440323431 542 GELYVFADGEAGFNGSDNMHIIEMPHVEETIAPIFYTVPLQLLAYHVALIK 592
Cdd:pfam01380 81 AKIIAITDSPGSPLAREADHVLYINAGPETGVASTKSITAQLAALDALAVA 131
|
|
| PRK05793 |
PRK05793 |
amidophosphoribosyltransferase; Provisional |
2-227 |
3.00e-28 |
|
amidophosphoribosyltransferase; Provisional
Pssm-ID: 235611 [Multi-domain] Cd Length: 469 Bit Score: 118.21 E-value: 3.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 2 CGIVGAVA--QRDIAEILLEGLRRLEYRGYDSAGLAVVDSEgHMTRVRRLGKVQMLAQAVEEQPLHGGTGIAHTRWATHG 79
Cdd:PRK05793 15 CGVFGVFSknNIDVASLTYYGLYALQHRGQESAGIAVSDGE-KIKVHKGMGLVSEVFSKEKLKGLKGNSAIGHVRYSTTG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 80 EPSESNAHPHVSEH----IVVVHNGIIENHEPLRALLQSRGYVFVTETDTEVIAHLVHWELEQGgtLREAVLRAIPQLRG 155
Cdd:PRK05793 94 ASDLDNAQPLVANYklgsIAIAHNGNLVNADVIRELLEDGGRIFQTSIDSEVILNLIARSAKKG--LEKALVDAIQAIKG 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1440323431 156 AYGTVIMdTRDpgTLLAARSGS---PLVIGLGMGENFIASDQLALLPVTRRFIF-LEEGDIaevtrrsvVIFDKSG 227
Cdd:PRK05793 172 SYALVIL-TED--KLIGVRDPHgirPLCLGKLGDDYILSSESCALDTIGAEFIRdVEPGEI--------VIIDEDG 236
|
|
| PLN02440 |
PLN02440 |
amidophosphoribosyltransferase |
1-266 |
1.57e-23 |
|
amidophosphoribosyltransferase
Pssm-ID: 215241 [Multi-domain] Cd Length: 479 Bit Score: 103.99 E-value: 1.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 1 MCGIVGAVAQRDIAEILLEGLRRLEYRGYDSAGLAVVDsEGHMTRVRRLGKVQMLAQAVEEQPLHGGTGIAHTRWATHGE 80
Cdd:PLN02440 1 ECGVVGIFGDPEASRLCYLGLHALQHRGQEGAGIVTVD-GNRLQSITGNGLVSDVFDESKLDQLPGDIAIGHVRYSTAGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 81 PSESNAHPHVSEH----IVVVHNGIIENHEPLRALLQSRGYVFVTETDTEVIAHLVHWELEQggTLREAVLRAIPQLRGA 156
Cdd:PLN02440 80 SSLKNVQPFVANYrfgsIGVAHNGNLVNYEELRAKLEENGSIFNTSSDTEVLLHLIAISKAR--PFFSRIVDACEKLKGA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 157 YGTVIMDTrdpGTLLAARSGS---PLVIGL-GMGENFIASDQLALLPvtrrfifLEEGDIAEVTRRSVVIFDKsGAEVKR 232
Cdd:PLN02440 158 YSMVFLTE---DKLVAVRDPHgfrPLVMGRrSNGAVVFASETCALDL-------IGATYEREVNPGEVIVVDK-DKGVSS 226
|
250 260 270
....*....|....*....|....*....|....*
gi 1440323431 233 QEIESNLQYDAgdkGIYRH-YmqkeiFEQPNAIKN 266
Cdd:PLN02440 227 QCLMPHPEPKP---CIFEHiY-----FARPNSIVF 253
|
|
| GlxB |
cd01907 |
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ... |
2-197 |
5.57e-23 |
|
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: 98.49 E-value: 5.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 2 CGIVGAV---AQRDIAEILLEGLRRLEYRG-YDSAGLAVVD-------SEGH-MTRVRRLGKVQMLAQA--VEEqpLHGG 67
Cdd:cd01907 1 CGIFGIMskdGEPFVGALLVEMLDAMQERGpGDGAGFALYGdpdafvySSGKdMEVFKGVGYPEDIARRydLEE--YKGY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 68 TGIAHTRWATHGEPSESNAHPHVSEHIVVVHNGIIENHEPLRALLQSRGYVFVTETDTEVIAHLVHWELEQGGTLREAVL 147
Cdd:cd01907 79 HWIAHTRQPTNSAVWWYGAHPFSIGDIAVVHNGEISNYGSNREYLERFGYKFETETDTEVIAYYLDLLLRKGGLPLEYYK 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1440323431 148 RAI----------PQLRGAYGTVIMDtrDPGTLLAARSGS-----------PLVIGLGMGENFIASDQLAL 197
Cdd:cd01907 159 HIIrmpeeerellLALRLTYRLADLD--GPFTIIVGTPDGfivirdriklrPAVVAETDDYVAIASEECAI 227
|
|
| GATase_6 |
pfam13522 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
65-174 |
1.08e-19 |
|
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain found in a variety of enzymes, such as asparagine synthetase and glutamine--fructose-6-phosphate transaminase.
Pssm-ID: 433279 [Multi-domain] Cd Length: 130 Bit Score: 85.44 E-value: 1.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 65 HGGTGIAHTRWATHGEPSESNaHPHVSE--HIVVVHNGIIENHEPLRALLQSRGYVFVTETDTEVIAHLvhweLEQGGTl 142
Cdd:pfam13522 9 EGGVALGHVRLAIVDLPDAGN-QPMLSRdgRLVLVHNGEIYNYGELREELADLGHAFRSRSDTEVLLAL----YEEWGE- 82
|
90 100 110
....*....|....*....|....*....|..
gi 1440323431 143 reavlRAIPQLRGAYGTVIMDtRDPGTLLAAR 174
Cdd:pfam13522 83 -----DCLERLRGMFAFAIWD-RRRRTLFLAR 108
|
|
| AsnB |
cd00712 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ... |
2-200 |
6.29e-17 |
|
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine synthetase B catalyses the ATP-dependent conversion of aspartate to asparagine. This enzyme is a homodimer, with each monomer composed of a glutaminase domain and a synthetase domain. The N-terminal glutaminase domain hydrolyzes glutamine to glutamic acid and ammonia.
Pssm-ID: 238364 [Multi-domain] Cd Length: 220 Bit Score: 79.91 E-value: 6.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 2 CGIVGAVAQRDIA---EILLEGLRRLEYRGYDSAGLAVvdseghmtrvrrlgkvqmlaqaveeqplHGGTGIAHTRWATH 78
Cdd:cd00712 1 CGIAGIIGLDGASvdrATLERMLDALAHRGPDGSGIWI----------------------------DEGVALGHRRLSII 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 79 GEpseSNAH-PHVSE--HIVVVHNGIIENHEPLRALLQSRGYVFVTETDTEVIAHLvhweLEQGGTlreavlRAIPQLRG 155
Cdd:cd00712 53 DL---SGGAqPMVSEdgRLVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHL----YEEWGE------DCLERLNG 119
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1440323431 156 AYGTVIMDTRDpGTLLAAR--SGS-PLVIGLGmGENFI-ASDQLALLPV 200
Cdd:cd00712 120 MFAFALWDKRK-RRLFLARdrFGIkPLYYGRD-GGGLAfASELKALLAL 166
|
|
| GATase_7 |
pfam13537 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
72-199 |
7.01e-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: 433289 [Multi-domain] Cd Length: 123 Bit Score: 74.09 E-value: 7.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 72 HTRWATHGepSESNAHPHVSEH---IVVVHNGIIENHEPLRALLQSRGYVFVTETDTEVIAHLVHwelEQGGTlrEAVLR 148
Cdd:pfam13537 1 HRRLSIID--LEGGAQPMVSSEdgrYVIVFNGEIYNYRELRAELEAKGYRFRTHSDTEVILHLYE---AEWGE--DCVDR 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1440323431 149 aipqLRGAYGTVIMDTRDpGTLLAAR--SG-SPLVIGLGMGENFI-ASDQLALLP 199
Cdd:pfam13537 74 ----LNGMFAFAIWDRRR-QRLFLARdrFGiKPLYYGRDDGGRLLfASELKALLA 123
|
|
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
1-174 |
4.96e-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: 78.34 E-value: 4.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 1 MCGIVGAVA--QRDIAEILLEGLRRLEYRGYDSAGLAVvdseghmtrvrrlgkvqmlaqaveeqplHGGTGIAHTRWATH 78
Cdd:COG0367 1 MCGIAGIIDfdGGADREVLERMLDALAHRGPDGSGIWV----------------------------DGGVALGHRRLSII 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 79 GePSESNAHPHVSE--HIVVVHNGIIENHEPLRALLQSRGYVFVTETDTEVIAHLvhweLEQGGTlreavlRAIPQLRGA 156
Cdd:COG0367 53 D-LSEGGHQPMVSEdgRYVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHA----YEEWGE------DCLERLNGM 121
|
170
....*....|....*...
gi 1440323431 157 YGTVIMDTRDpGTLLAAR 174
Cdd:COG0367 122 FAFAIWDRRE-RRLFLAR 138
|
|
| PLN02549 |
PLN02549 |
asparagine synthase (glutamine-hydrolyzing) |
1-197 |
2.10e-13 |
|
asparagine synthase (glutamine-hydrolyzing)
Pssm-ID: 178164 [Multi-domain] Cd Length: 578 Bit Score: 72.88 E-value: 2.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 1 MCGIVGAVAQRDIA----EILLEGLRRLEYRGYDSAGLAVvdseghmtrvrrlgkvqmlaqaveeqplHGGTGIAHTRWA 76
Cdd:PLN02549 1 MCGILAVLGCSDDSqakrSRVLELSRRLRHRGPDWSGLYG----------------------------NEDCYLAHERLA 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 77 THgEPsESNAHPHVSEH--IVVVHNGIIENHEPLRALLQSrgYVFVTETDTEVIAHLVhwelEQGGtlrEAVLRaipQLR 154
Cdd:PLN02549 53 IM-DP-ESGDQPLYNEDktIVVTANGEIYNHKELREKLKL--HKFRTGSDCEVIAHLY----EEHG---EEFVD---MLD 118
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1440323431 155 GAYGTVIMDTRDpGTLLAARSG---SPLVIGLGM-GENFIASDQLAL 197
Cdd:PLN02549 119 GMFSFVLLDTRD-NSFIAARDHigiTPLYIGWGLdGSVWFASEMKAL 164
|
|
| YafJ |
COG0121 |
Predicted glutamine amidotransferase YafJ [General function prediction only]; |
62-177 |
1.16e-12 |
|
Predicted glutamine amidotransferase YafJ [General function prediction only];
Pssm-ID: 439891 [Multi-domain] Cd Length: 248 Bit Score: 68.07 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 62 QPLHGGTGIAHTRWATHGEPSESNAHPHVSEHIVVVHNGIIENHEPLRALLQSRGYVF-----VTETDTEVIAHLVHWEL 136
Cdd:COG0121 72 RPIKSRLVIAHVRKATVGPVSLENTHPFRGGRWLFAHNGQLDGFDRLRRRLAEELPDElyfqpVGTTDSELAFALLLSRL 151
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1440323431 137 EQGG-TLREAVLRAIPQLR------GAYGTVIMdtrDPGTLLAARSGS 177
Cdd:COG0121 152 RDGGpDPAEALAEALRELAelarapGRLNLLLS---DGERLYATRYTS 196
|
|
| YafJ |
cd01908 |
Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine ... |
63-178 |
6.06e-12 |
|
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: 66.26 E-value: 6.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 63 PLHGGTGIAHTRWATHGEPSESNAHPHVSEHIVVVHNGIIENHEPLRA-LLQSRGYVFVTETDTEVIAHLVhweLEQGGT 141
Cdd:cd01908 77 PIKSPLVLAHVRAATVGPVSLENCHPFTRGRWLFAHNGQLDGFRLLRRrLLRLLPRLPVGTTDSELAFALL---LSRLLE 153
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1440323431 142 --------LREAVLRAIPQLR-----GAYGTVIMDTRdpgTLLAARSGSP 178
Cdd:cd01908 154 rdpldpaeLLDAILQTLRELAalappGRLNLLLSDGE---YLIATRYASA 200
|
|
| PTZ00077 |
PTZ00077 |
asparagine synthetase-like protein; Provisional |
1-197 |
7.96e-12 |
|
asparagine synthetase-like protein; Provisional
Pssm-ID: 185431 [Multi-domain] Cd Length: 586 Bit Score: 68.20 E-value: 7.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 1 MCGIVGAVAQRDIAEIL----LEGLRRLEYRGYDSAGLAVVDSEGHMTRVrrlgkvqmlaqaveeqplhggtgIAHTRWA 76
Cdd:PTZ00077 1 MCGILAIFNSKGERHELrrkaLELSKRLRHRGPDWSGIIVLENSPGTYNI-----------------------LAHERLA 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 77 THGepSESNAHPHVS--EHIVVVHNGIIENHEPLRALLQSRGYVFVTETDTEVIAHLvhweLEQGGTlreavlRAIP-QL 153
Cdd:PTZ00077 58 IVD--LSDGKQPLLDddETVALMQNGEIYNHWEIRPELEKEGYKFSSNSDCEIIGHL----YKEYGP------KDFWnHL 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1440323431 154 RGAYGTVIMDTRDpGTLLAARSG---SPLVIGLGM-GENFIASDQLAL 197
Cdd:PTZ00077 126 DGMFATVIYDMKT-NTFFAARDHigiIPLYIGYAKdGSIWFSSELKAL 172
|
|
| SIS_1 |
cd05710 |
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ... |
295-420 |
3.78e-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: 60.67 E-value: 3.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 295 HIQIVACGTSYNSGMVSRYWFEALAGVPCDVEIASEFRYRKSA-VRRNSLMITLSQSGETADTLAALRLSKELGYLgSLA 373
Cdd:cd05710 1 NVFFVGCGGSLADMYPAKYFLKKESKLPVFVYNAAEFLHTGPKrLTEKSVVILASHSGNTKETVAAAKFAKEKGAT-VIG 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1440323431 374 ICNVPGSSLVRESDLALMTKAGteigvasTKAFTTQLTVLLMLVAKL 420
Cdd:cd05710 80 LTDDEDSPLAKLADYVIVYGFE-------IDAVEEKYLLLYMLALRL 119
|
|
| asnB |
PRK09431 |
asparagine synthetase B; Provisional |
1-202 |
5.76e-11 |
|
asparagine synthetase B; Provisional
Pssm-ID: 236513 [Multi-domain] Cd Length: 554 Bit Score: 65.31 E-value: 5.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 1 MCGIVGAVAQRDIAEIL----LEGLRRLEYRGYDSAGLAVVDSeghmtrvrrlgkvqmlaqaveeqplhggtGI-AHTRW 75
Cdd:PRK09431 1 MCGIFGILDIKTDADELrkkaLEMSRLMRHRGPDWSGIYASDN-----------------------------AIlGHERL 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 76 ATHGepSESNAHPHVSEH--IVVVHNGIIENHEPLRALLQSRgYVFVTETDTEVIAHLvhweleqggtLREAVLRAIPQL 153
Cdd:PRK09431 52 SIVD--VNGGAQPLYNEDgtHVLAVNGEIYNHQELRAELGDK-YAFQTGSDCEVILAL----------YQEKGPDFLDDL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1440323431 154 RGAYGTVIMDTrDPGTLLAARsgSPL-VIGLGMGEN-----FIASDQLALLPVTR 202
Cdd:PRK09431 119 DGMFAFALYDS-EKDAYLIAR--DPIgIIPLYYGYDehgnlYFASEMKALVPVCK 170
|
|
| asn_synth_AEB |
TIGR01536 |
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing ... |
4-174 |
3.16e-10 |
|
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: 62.74 E-value: 3.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 4 IVGAVAQRDIA----EILLEGLRRLEYRGYDSAGLAVVDSE---GHmtrvRRLGKVQMLAQAveeQPLHGgtgiahtrwa 76
Cdd:TIGR01536 1 IAGFFDLDDKAveedEAIKRMSDTIAHRGPDASGIEYKDGNailGH----RRLAIIDLSGGA---QPMSN---------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 77 thgepsESNAHphvsehiVVVHNGIIENHEPLRALLQSRGYVFVTETDTEVIAHLvhweLEQGGtlREAVLRaipqLRGA 156
Cdd:TIGR01536 64 ------EGKTY-------VIVFNGEIYNHEELREELEAKGYTFQTDSDTEVILHL----YEEWG--EECVDR----LDGM 120
|
170
....*....|....*...
gi 1440323431 157 YGTVIMDTRDpGTLLAAR 174
Cdd:TIGR01536 121 FAFALWDSEK-GELFLAR 137
|
|
| frlB |
PRK11382 |
fructoselysine 6-phosphate deglycase; |
287-600 |
3.74e-10 |
|
fructoselysine 6-phosphate deglycase;
Pssm-ID: 183111 [Multi-domain] Cd Length: 340 Bit Score: 61.94 E-value: 3.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 287 NEMLAQ-VEHIQIVACGTSYNSGMVSRYWFEALAGVPCDVEIASEF----RYRKSAvrrNSLMITLSQSGETADTLAALR 361
Cdd:PRK11382 37 EEMVKRdIDRIYFVACGSPLNAAQTAKHLADRFSDLQVYAISGWEFcdntPYRLDD---RCAVIGVSDYGKTEEVIKALE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 362 LSKELGYLgSLAICNVPGSSLVRESDLALMTKAGTEIGVASTKAFTtqltVLLMLVAKLARlKGQDASIEHDivhgLQAL 441
Cdd:PRK11382 114 LGRACGAL-TAAFTKRADSPITSAAEFSIDYQADCIWEIHLLLCYS----VVLEMITRLAP-NAEIGKIKND----LKQL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 442 PNRIEQML-SQDKRIEQLAERFSDKHHALFLGRGDQYPIAM-EGALKLKEISYIHAEAYAAGELKHGPLALIDAEMPVIV 519
Cdd:PRK11382 184 PNALGHLVrTWEEKGRQLGELASQWPMIYTVAAGPLRPLGYkEGIVTLMEFTWTHGCVIESGEFRHGPLEIVEPGVPFLF 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 520 VAPNNELLEKLKSNIEEVRARggelyvfadgeagfngSDNMHIIEMPHVEET----IAPIFYTVPLQLLAYHVALIKGTD 595
Cdd:PRK11382 264 LLGNDESRHTTERAINFVKQR----------------TDNVIVIDYAEISQGlhpwLAPFLMFVPMEWLCYYLSIYKDHN 327
|
....*
gi 1440323431 596 VDQPR 600
Cdd:PRK11382 328 PDERR 332
|
|
| SIS |
cd04795 |
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
296-375 |
1.12e-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: 55.46 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 296 IQIVACGTSYNSGMVSRYWFEALAGVPCDVEIASEFRY--RKSAVRRNSLMITLSQSGETADTLAALRLSKELGyLGSLA 373
Cdd:cd04795 1 IFVIGIGGSGAIAAYFALELLELTGIEVVALIATELEHasLLSLLRKGDVVIALSYSGRTEELLAALEIAKELG-IPVIA 79
|
..
gi 1440323431 374 IC 375
Cdd:cd04795 80 IT 81
|
|
| SIS_RpiR |
cd05013 |
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ... |
285-419 |
9.10e-09 |
|
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: 54.16 E-value: 9.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 285 NANEMLAQVEHIQIVACGTSYNSGM-VSRYWFeaLAGVPCDVEIAS-EFRYRKSAVRRNSLMITLSQSGETADTLAALRL 362
Cdd:cd05013 5 KAVDLLAKARRIYIFGVGSSGLVAEyLAYKLL--RLGKPVVLLSDPhLQLMSAANLTPGDVVIAISFSGETKETVEAAEI 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1440323431 363 SKELGyLGSLAICNVPGSSLVRESDLALMTKA-GTEIGVASTKAFTTQLTVLLMLVAK 419
Cdd:cd05013 83 AKERG-AKVIAITDSANSPLAKLADIVLLVSSeEGDFRSSAFSSRIAQLALIDALFLA 139
|
|
| SIS |
cd04795 |
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
469-549 |
4.81e-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: 50.84 E-value: 4.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 469 LFLGRGDQYPIAMEGALKLKEISYIHAEAYAAGELKHGP-LALIDAEMPVIVVAPNNElLEKLKSNIEEVRARGGELYVF 547
Cdd:cd04795 2 FVIGIGGSGAIAAYFALELLELTGIEVVALIATELEHASlLSLLRKGDVVIALSYSGR-TEELLAALEIAKELGIPVIAI 80
|
..
gi 1440323431 548 AD 549
Cdd:cd04795 81 TD 82
|
|
| GATase_4 |
pfam13230 |
Glutamine amidotransferases class-II; This family captures members that are not found in ... |
55-159 |
2.17e-05 |
|
Glutamine amidotransferases class-II; This family captures members that are not found in pfam00310.
Pssm-ID: 433047 [Multi-domain] Cd Length: 272 Bit Score: 46.55 E-value: 2.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 55 LAQAVEEQPLHGGTGIAHTRWATHGEPSESNAHPHVSE----HIVVVHNGIIENHEPLRALLqsrgYVFVTETDTEVI-A 129
Cdd:pfam13230 60 IAELVRRYPIRSRNVIAHIRKATQGRVTLENTHPFMRElwgrYWIFAHNGDLKGYAPKLSGR----FQPVGSTDSELAfC 135
|
90 100 110
....*....|....*....|....*....|....*.
gi 1440323431 130 HLVHWELEQGGTLRE------AVLRAIPQLRGAYGT 159
Cdd:pfam13230 136 WLLDRLASRFPYARPsagelfRALRELAREIAAHGT 171
|
|
| SIS_Etherase |
cd05007 |
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ... |
324-416 |
1.59e-04 |
|
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: 43.67 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 324 DVEIASEFRYRKSAVRRNSLMITLSQSGETADTLAALRLSKELGYLgSLAICNVPGSSLVRESDLALMTKAGTEIGVAST 403
Cdd:cd05007 102 DDEEAGAADLQAINLTERDVVIGIAASGRTPYVLGALRYARARGAL-TIGIACNPGSPLLQLADIAIALITGPEVVAGST 180
|
90
....*....|....*
gi 1440323431 404 --KAFTTQLTVLLML 416
Cdd:cd05007 181 rlKAGTAQKLALNML 195
|
|
| SIS_AgaS_like |
cd05010 |
AgaS-like protein. AgaS contains a SIS (Sugar ISomerase) domain which is found in many ... |
470-599 |
3.30e-04 |
|
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: 41.46 E-value: 3.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 470 FLGRGDQYPIAMEGALKLKEIS--YIHAEAYAAGELKHGPLALIDAEMPVIVVAPNNELLEKLKSN-IEEVRARGGELYV 546
Cdd:cd05010 3 YLGSGPLAGLAREAALKVLELTagKVATVYDSPLGFRHGPKSLVDDDTLVVVFVSNDPYTRQYDLDlLKELRRDGIAARV 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1440323431 547 FA---DGEAGFNGSDNMHIIEMPHVEET-IAPIfYTVPLQLLAYHVALIKGTDVDQP 599
Cdd:cd05010 83 IAispESDAGIEDNSHYYLPGSRDLDDVyLAFP-YILYAQLFALFNSIALGLTPDNP 138
|
|
| murQ |
PRK05441 |
N-acetylmuramic acid-6-phosphate etherase; Reviewed |
338-416 |
4.35e-03 |
|
N-acetylmuramic acid-6-phosphate etherase; Reviewed
Pssm-ID: 235467 [Multi-domain] Cd Length: 299 Bit Score: 39.38 E-value: 4.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323431 338 VRRNSLMITLSQSGETADTLAALRLSKELGYLgSLAICNVPGSSLVRESDLALMTKAGTEIGVAST--KAFTTQLTVLLM 415
Cdd:PRK05441 129 LTAKDVVVGIAASGRTPYVIGALEYARERGAL-TIGISCNPGSPLSKEADIAIEVVVGPEVLTGSTrmKAGTAQKLVLNM 207
|
.
gi 1440323431 416 L 416
Cdd:PRK05441 208 I 208
|
|
| |
