|
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: 1054.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 1 MCGIVGAVAQRDVAEILLEGLRRLEYRGYDSAGLAVVDsEGNVARLRRLGKVQVLSQAAEEHELHGGTGIAHTRWATHGE 80
Cdd:COG0449 1 MCGIVGYIGKRDAAPILLEGLKRLEYRGYDSAGIAVLD-DGGLEVRKAVGKLANLEEKLAEEPLSGTIGIGHTRWATHGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 81 PSEENAHPHVS--EHITIVHNGIIENHEPLRELLIGRGYRFVSETDTEVVAHLVHFEQQQnGGTLVDVVKRVIPQLRGAY 158
Cdd:COG0449 80 PSDENAHPHTScsGRIAVVHNGIIENYAELREELEAKGHTFKSETDTEVIAHLIEEYLKG-GGDLLEAVRKALKRLEGAY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 159 GMVVLDNRDPSVLVAARSGSPLVIGRGVGENFIASDQLALLPVTRRFMFLEEGDIAEITRRDVRVFDKSGQLAAREEIES 238
Cdd:COG0449 159 ALAVISADEPDRIVAARKGSPLVIGLGEGENFLASDVPALLPYTRRVIYLEDGEIAVLTRDGVEIYDLDGEPVEREVKTV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 239 KVNYDAGDKGAYRHYMQKEIYEQPMAIKNTLEGRFS-HGEINLSELgPKADELLAKVEHVQIIACGTSYNSGMVSRYWFE 317
Cdd:COG0449 239 DWDAEAAEKGGYPHFMLKEIHEQPEAIRDTLRGRLDeDGRVVLDEL-NLAAEDLRNIDRIYIVACGTSYHAGLVGKYLIE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 318 SLAGIPCDVEIASEFRYRKPAVRKNSLMITLSQSGETADTLAALRLSKELGyLGSLAICNVAGSSLVRESDLALMTKAGV 397
Cdd:COG0449 318 ELARIPVEVEIASEFRYRDPVVDPGTLVIAISQSGETADTLAALREAKEKG-AKVLAICNVVGSTIARESDAVLYTHAGP 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 398 EIGVASTKAFTTQLTVLLMLVARVGRLRG-MDAQIEHDIVHGLQALPARIEQMLSQDKLIESLAEGFSDKHHALFLGRGD 476
Cdd:COG0449 397 EIGVASTKAFTTQLAALYLLALYLARARGtLSAEEEAELLEELRKLPEKIEEVLDLEEQIEELAEKYADARNALFLGRGI 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 477 QYPIAMEGALKLKEISYIHAEAYAAGELKHGPLALIDADMPVVVVAPNNELLEKLKSNIEEVRARGGELYVFADEDAGFT 556
Cdd:COG0449 477 NYPVALEGALKLKEISYIHAEGYAAGELKHGPIALIDEGMPVVAIAPQDELYEKTLSNIQEVKARGGKVIAIADEGDEEV 556
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 504730047 557 SSENMKIIPLPHIEEVIAPIFYTVPLQLLSYHVALIKGTDVDQPRNLAKSVTVE 610
Cdd:COG0449 557 EELADDVIEVPEVDELLAPILAVVPLQLLAYHVAVLRGTDVDQPRNLAKSVTVE 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: 1051.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 1 MCGIVGAVAQRDVAEILLEGLRRLEYRGYDSAGLAVVDsEGNVARLRRLGKVQVLSQAAEEHELHGGTGIAHTRWATHGE 80
Cdd:PRK00331 1 MCGIVGYVGQRNAAEILLEGLKRLEYRGYDSAGIAVLD-DGGLEVRKAVGKVANLEAKLEEEPLPGTTGIGHTRWATHGK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 81 PSEENAHPHVS--EHITIVHNGIIENHEPLRELLIGRGYRFVSETDTEVVAHLVHFEQQQnGGTLVDVVKRVIPQLRGAY 158
Cdd:PRK00331 80 PTERNAHPHTDcsGRIAVVHNGIIENYAELKEELLAKGHVFKSETDTEVIAHLIEEELKE-GGDLLEAVRKALKRLEGAY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 159 GMVVLDNRDPSVLVAARSGSPLVIGRGVGENFIASDQLALLPVTRRFMFLEEGDIAEITRRDVRVFDKSGQLAAREEIES 238
Cdd:PRK00331 159 ALAVIDKDEPDTIVAARNGSPLVIGLGEGENFLASDALALLPYTRRVIYLEDGEIAVLTRDGVEIFDFDGNPVEREVYTV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 239 KVNYDAGDKGAYRHYMQKEIYEQPMAIKNTLEGRfshgeINLSELGPKADELLAKVEHVQIIACGTSYNSGMVSRYWFES 318
Cdd:PRK00331 239 DWDASAAEKGGYRHFMLKEIYEQPEAIRDTLEGR-----LDELGEGELADEDLKKIDRIYIVACGTSYHAGLVAKYLIES 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 319 LAGIPCDVEIASEFRYRKPAVRKNSLMITLSQSGETADTLAALRLSKELGyLGSLAICNVAGSSLVRESDLALMTKAGVE 398
Cdd:PRK00331 314 LAGIPVEVEIASEFRYRDPVLSPKTLVIAISQSGETADTLAALRLAKELG-AKTLAICNVPGSTIARESDAVLYTHAGPE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 399 IGVASTKAFTTQLTVLLMLVARVGRLRG-MDAQIEHDIVHGLQALPARIEQMLSQDKLIESLAEGFSDKHHALFLGRGDQ 477
Cdd:PRK00331 393 IGVASTKAFTAQLAVLYLLALALAKARGtLSAEEEADLVHELRELPALIEQVLDLKEQIEELAEDFADARNALFLGRGVD 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 478 YPIAMEGALKLKEISYIHAEAYAAGELKHGPLALIDADMPVVVVAPNNELLEKLKSNIEEVRARGGELYVFADEDaGFTS 557
Cdd:PRK00331 473 YPVALEGALKLKEISYIHAEGYAAGELKHGPIALIDEGMPVVAIAPNDELYEKTKSNIQEVKARGARVIVIADEG-DEVA 551
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 504730047 558 SENMKIIPLPHIEEVIAPIFYTVPLQLLSYHVALIKGTDVDQPRNLAKSVTVE 610
Cdd:PRK00331 552 EEADDVIEVPEVHELLAPLLYVVPLQLLAYHVALARGTDVDKPRNLAKSVTVE 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: 960.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 2 CGIVGAVAQRDVAEILLEGLRRLEYRGYDSAGLAVVDsEGNVARLRRLGKVQVLSQAAEEHELHGGTGIAHTRWATHGEP 81
Cdd:TIGR01135 1 CGIVGYIGQRDAVPILLEGLKRLEYRGYDSAGIAVVD-EGKLFVRKAVGKVAELANKLGEKPLPGGVGIGHTRWATHGKP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 82 SEENAHPHVSEH--ITIVHNGIIENHEPLRELLIGRGYRFVSETDTEVVAHLVHFEQQqNGGTLVDVVKRVIPQLRGAYG 159
Cdd:TIGR01135 80 TDENAHPHTDEGgrIAVVHNGIIENYAELREELEARGHVFSSDTDTEVIAHLIEEELR-EGGDLLEAVQKALKQLRGAYA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 160 MVVLDNRDPSVLVAARSGSPLVIGRGVGENFIASDQLALLPVTRRFMFLEEGDIAEITRRDVRVFDKSGQLAAREEIESK 239
Cdd:TIGR01135 159 LAVLHADHPETLVAARSGSPLIVGLGDGENFVASDVTALLPYTRRVIYLEDGDIAILTKDGVEIYNFEGAPVQREVRVID 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 240 VNYDAGDKGAYRHYMQKEIYEQPMAIKNTLEGRFSHGEINLSELGpkADELLAKVEHVQIIACGTSYNSGMVSRYWFESL 319
Cdd:TIGR01135 239 WDLDAAEKGGYRHFMLKEIYEQPRALRDTLEGRIEENGGVFEELG--AEELLKNIDRIQIVACGTSYHAGLVAKYLIERL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 320 AGIPCDVEIASEFRYRKPAVRKNSLMITLSQSGETADTLAALRLSKELGyLGSLAICNVAGSSLVRESDLALMTKAGVEI 399
Cdd:TIGR01135 317 AGIPVEVEIASEFRYRKPVVDKDTLVIAISQSGETADTLEALRLAKELG-AKTLGICNVPGSTLVREADHTLYTRAGPEI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 400 GVASTKAFTTQLTVLLMLVARVGRLRG-MDAQIEHDIVHGLQALPARIEQMLSQDKLIESLAEGFSDKHHALFLGRGDQY 478
Cdd:TIGR01135 396 GVASTKAFTTQLTVLYLLALALAKARGtLSAEEEAELVDALRRLPDLVEQVLLADESIAELAERYADKRNFLFLGRGLGY 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 479 PIAMEGALKLKEISYIHAEAYAAGELKHGPLALIDADMPVVVVAPNNELLEKLKSNIEEVRARGGELYVFADEDAGFTSS 558
Cdd:TIGR01135 476 PIALEGALKLKEISYIHAEGYPAGELKHGPIALIDEGLPVVAIAPKDSLLEKTKSNVEEVKARGARVIVFAPEDDETIAS 555
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 504730047 559 ENMKIIPLPHIEEVIAPIFYTVPLQLLSYHVALIKGTDVDQPRNLAKSVTVE 610
Cdd:TIGR01135 556 VADDVIKLPEVEELLAPIVYTIPLQLLAYHIALAKGTDVDKPRNLAKSVTVE 607
|
|
| PLN02981 |
PLN02981 |
glucosamine:fructose-6-phosphate aminotransferase |
1-610 |
3.51e-165 |
|
glucosamine:fructose-6-phosphate aminotransferase
Pssm-ID: 215531 [Multi-domain] Cd Length: 680 Bit Score: 487.34 E-value: 3.51e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 1 MCGIVGAV------AQRDVAEILLEGLRRLEYRGYDSAGLAVvDSEGNVAR-----LRRLGKVQVL----SQAAEEHELH 65
Cdd:PLN02981 1 MCGIFAYLnynvprERRFILEVLFNGLRRLEYRGYDSAGIAI-DNDPSLESssplvFREEGKIESLvrsvYEEVAETDLN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 66 GG------TGIAHTRWATHGEPSEENAHPHVSE---HITIVHNGIIENHEPLRELLIGRGYRFVSETDTEVVAHLVHF-- 134
Cdd:PLN02981 80 LDlvfenhAGIAHTRWATHGPPAPRNSHPQSSGpgnEFLVVHNGIITNYEVLKETLLRHGFTFESDTDTEVIPKLAKFvf 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 135 ---EQQQNGGTLVDVVKRVIPQLRGAYGMVVLDNRDPSVLVAARSGSPLVIG------------------------RGVG 187
Cdd:PLN02981 160 dklNEEEGDVTFSQVVMEVMRQLEGAYALIFKSPHYPNELVACKRGSPLLLGvkelpeeknssavftsegfltknrDKPK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 188 ENFIASDQLALLPVTRRFMFLEEGDIAEITRRDVRVF-------DKSGQLAAREEIES-----KVNYDAGDKGAYRHYMQ 255
Cdd:PLN02981 240 EFFLASDASAVVEHTKRVLVIEDNEVVHLKDGGVGIYkfenekgRGGGGLSRPASVERalstlEMEVEQIMKGNYDHYMQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 256 KEIYEQPMAIKNTLEGRFSHGEINLSE---LGPKADEL--LAKVEHVQIIACGTSYNSGMVSRYWFESLAGIPCDVEIAS 330
Cdd:PLN02981 320 KEIHEQPESLTTTMRGRLIRGGSGKAKrvlLGGLKDHLktIRRSRRIVFIGCGTSYNAALAARPILEELSGVPVTMELAS 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 331 EFRYRK-PAVRKNSLMItLSQSGETADTLAALRLSKELGYLgSLAICNVAGSSLVRESDLALMTKAGVEIGVASTKAFTT 409
Cdd:PLN02981 400 DLLDRQgPIYREDTAVF-VSQSGETADTLRALEYAKENGAL-CVGITNTVGSAISRGTHCGVHINAGAEIGVASTKAYTS 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 410 QLTVLLMLVARVGRLRGMDAQIEHDIVHGLQALPARIEQMLSQDKLIESLAEGFSDKHHALFLGRGDQYPIAMEGALKLK 489
Cdd:PLN02981 478 QIVAMTMLALALGEDSISSRSRREAIIDGLFDLPNKVREVLKLDQEMKELAELLIDEQSLLVFGRGYNYATALEGALKVK 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 490 EISYIHAEAYAAGELKHGPLALIDADMPVVVVAPNNELLEKLKSNIEEVRARGGELYVFADE--DAGFTSSENMKIIPLP 567
Cdd:PLN02981 558 EVALMHSEGILAGEMKHGPLALVDETLPIIVIATRDACFSKQQSVIQQLRARKGRLIVICSKgdASSVCPSGGCRVIEVP 637
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 504730047 568 HIEEVIAPIFYTVPLQLLSYHVALIKGTDVDQPRNLAKSVTVE 610
Cdd:PLN02981 638 QVEDCLQPVINIVPLQLLAYHLTVLRGHNVDQPRNLAKSVTTQ 680
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
1-609 |
3.53e-161 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 475.67 E-value: 3.53e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 1 MCGIVGAVAQRDVAEILLEGLRRLEYRGYDSAGLAVVDSEGN--VARLRRLGK----VQVLSQAAEEHELHGGTGIAHTR 74
Cdd:PTZ00295 24 CCGIVGYLGNEDASKILLEGIEILQNRGYDSCGISTISSGGElkTTKYASDGTtsdsIEILKEKLLDSHKNSTIGIAHTR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 75 WATHGEPSEENAHPHV--SEHITIVHNGIIENHEPLRELLIGRGYRFVSETDTEVVAHLVHFEQQQnGGTLVDVVKRVIP 152
Cdd:PTZ00295 104 WATHGGKTDENAHPHCdyKKRIALVHNGTIENYVELKSELIAKGIKFRSETDSEVIANLIGLELDQ-GEDFQEAVKSAIS 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 153 QLRGAYGMVVLDNRDPSVLVAARSGSPLVIGRGVGENFIASDQLALLPVTRRFMFLEEGDIAEITRRDVRVFDKSGQL-- 230
Cdd:PTZ00295 183 RLQGTWGLCIIHKDNPDSLIVARNGSPLLVGIGDDSIYVASEPSAFAKYTNEYISLKDGEIAELSLENVNDLYTQRRVek 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 231 AAREEIESKvnydagdKGAYRHYMQKEIYEQPMAIKNTLE--GRFSHGEiNLSELG--PKADELLAKVEHVQIIACGTSY 306
Cdd:PTZ00295 263 IPEEVIEKS-------PEPYPHWTLKEIFEQPIALSRALNngGRLSGYN-NRVKLGglDQYLEELLNIKNLILVGCGTSY 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 307 NSGMVSRYWFESLAGI-PCDVEIASEF-RYRKPavRKNSLMITLSQSGETADTLAALRLSKELGYLgSLAICNVAGSSLV 384
Cdd:PTZ00295 335 YAALFAASIMQKLKCFnTVQVIDASELtLYRLP--DEDAGVIFISQSGETLDVVRALNLADELNLP-KISVVNTVGSLIA 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 385 RESDLALMTKAGVEIGVASTKAFTTQLTVLLMLVARVGRLRGMDAQIEH--DIVHGLQALPARIEQMLSQ-DKLIESLAE 461
Cdd:PTZ00295 412 RSTDCGVYLNAGREVAVASTKAFTSQVTVLSLIALWFAQNKEYSCSNYKcsSLINSLHRLPTYIGMTLKScEEQCKRIAE 491
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 462 GFSDKHHALFLGRGDQYPIAMEGALKLKEISYIHAEAYAAGELKHGPLALIDAD--MPVVVVAPNNELLEKLKSNIEEVR 539
Cdd:PTZ00295 492 KLKNAKSMFILGKGLGYPIALEGALKIKEITYIHAEGFSGGALKHGPFALIDKEknTPVILIILDDEHKELMINAAEQVK 571
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504730047 540 ARGGELYVfadedagFTSSENM------KIIPLPHIeEVIAPIFYTVPLQLLSYHVALIKGTDVDQPRNLAKSVTV 609
Cdd:PTZ00295 572 ARGAYIIV-------ITDDEDLvkdfadEIILIPSN-GPLTALLAVIPLQLLAYEIAILRGINPDKPRGLAKTVTV 639
|
|
| PTZ00394 |
PTZ00394 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
1-610 |
9.03e-158 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 173585 [Multi-domain] Cd Length: 670 Bit Score: 468.20 E-value: 9.03e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 1 MCGIVGAVAQ------RDVAEILLEGLRRLEYRGYDSAGLA-----------------------VVDSEGNVARLRRlgk 51
Cdd:PTZ00394 1 MCGIFGYANHnvprtvEQILNVLLDGIQKVEYRGYDSAGLAidanigsekedgtaasaptprpcVVRSVGNISQLRE--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 52 vQVLSQAAE------EHELHGGTGIAHTRWATHGEPSEENAHPHVSEH--ITIVHNGIIENHEPLRELLIGRGYRFVSET 123
Cdd:PTZ00394 78 -KVFSEAVAatlppmDATTSHHVGIAHTRWATHGGVCERNCHPQQSNNgeFTIVHNGIVTNYMTLKELLKEEGYHFSSDT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 124 DTEVVAHLVHFEQQQNGG-TLVDVVKRVIPQLRGAYGMVVLDNRDPSVLVAARSGSPLVIG------------------- 183
Cdd:PTZ00394 157 DTEVISVLSEYLYTRKGIhNFADLALEVSRMVEGSYALLVKSVYFPGQLAASRKGSPLMVGirrtddrgcvmklqtydlt 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 184 --RGVGENFIASDQLALLPVTRRFMFLEEGDIAEITRRDVRVFDKSGQ---LAAREEIESKVNYDAGDKGAYRHYMQKEI 258
Cdd:PTZ00394 237 dlSGPLEVFFSSDVNSFAEYTREVVFLEDGDIAHYCDGALRFYNAAERqrsIVKREVQHLDAKPEGLSKGNYPHFMLKEI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 259 YEQPMAIKNTLEGR--FSHGEINLSELGPKADELLAKVEHVQIIACGTSYNSGMVSRYWFESLAGIPCDVEIASEFRYRK 336
Cdd:PTZ00394 317 YEQPESVISSMHGRidFSSGTVQLSGFTQQSIRAILTSRRILFIACGTSLNSCLAVRPLFEELVPLPISVENASDFLDRR 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 337 PAVRKNSLMITLSQSGETADTLAALRLSKELGYLgSLAICNVAGSSLVRESDLALMTKAGVEIGVASTKAFTTQLtVLLM 416
Cdd:PTZ00394 397 PRIQRDDVCFFVSQSGETADTLMALQLCKEAGAM-CVGITNVVGSSISRLTHYAIHLNAGVEVGVASTKAYTSQV-VVLT 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 417 LVARVgrLRGMDAQIEH---DIVHGLQALPARIEQMLS-QDKLIESLAEGFSDKHHALFLGRGDQYPIAMEGALKLKEIS 492
Cdd:PTZ00394 475 LVALL--LSSDSVRLQErrnEIIRGLAELPAAISECLKiTHDPVKALAARLKESSSILVLGRGYDLATAMEAALKVKELS 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 493 YIHAEAYAAGELKHGPLALIDADMPVVVVAPNNELLEKLKSNIEEVRARGGELYVFADEDAGFTSSENMKIIPLPHIEEV 572
Cdd:PTZ00394 553 YVHTEGIHSGELKHGPLALIDETSPVLAMCTHDKHFGLSKSAVQQVKARGGAVVVFATEVDAELKAAASEIVLVPKTVDC 632
|
650 660 670
....*....|....*....|....*....|....*...
gi 504730047 573 IAPIFYTVPLQLLSYHVALIKGTDVDQPRNLAKSVTVE 610
Cdd:PTZ00394 633 LQCVVNVIPFQLLAYYMALLRGNNVDCPRNLAKSVTVQ 670
|
|
| GFAT |
cd00714 |
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ... |
2-216 |
6.49e-120 |
|
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: 354.06 E-value: 6.49e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 2 CGIVGAVAQRDVAEILLEGLRRLEYRGYDSAGLAVvDSEGNVARLRRLGKVQVLSQAAEEHELHGGTGIAHTRWATHGEP 81
Cdd:cd00714 1 CGIVGYIGKREAVDILLEGLKRLEYRGYDSAGIAV-IGDGSLEVVKAVGKVANLEEKLAEKPLSGHVGIGHTRWATHGEP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 82 SEENAHPHVSEH--ITIVHNGIIENHEPLRELLIGRGYRFVSETDTEVVAHLVHFEQQQnGGTLVDVVKRVIPQLRGAYG 159
Cdd:cd00714 80 TDVNAHPHRSCDgeIAVVHNGIIENYAELKEELEAKGYKFESETDTEVIAHLIEYYYDG-GLDLLEAVKKALKRLEGAYA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 504730047 160 MVVLDNRDPSVLVAARSGSPLVIGRGVGENFIASDQLALLPVTRRFMFLEEGDIAEI 216
Cdd:cd00714 159 LAVISKDEPDEIVAARNGSPLVIGIGDGENFVASDAPALLEHTRRVIYLEDGDIAVI 215
|
|
| AgaS |
COG2222 |
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ... |
256-610 |
9.43e-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: 242.11 E-value: 9.43e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 256 KEIYEQPMAIKNTLEgrfshgeINLSELGPKADELLAK-VEHVQIIACGTSYNSGMVSRYWFESLAGIPCDVEIASEF-R 333
Cdd:COG2222 2 REIAQQPEAWRRALA-------ALAAAIAALLARLRAKpPRRVVLVGAGSSDHAAQAAAYLLERLLGIPVAALAPSELvV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 334 YRKPAVRKNSLMITLSQSGETADTLAALRLSKELGYLgSLAICNVAGSSLVRESDLALMTKAGVEIGVASTKAFTTQLTV 413
Cdd:COG2222 75 YPAYLKLEGTLVVAISRSGNSPEVVAALELAKARGAR-TLAITNNPDSPLAEAADRVLPLPAGPEKSVAATKSFTTMLLA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 414 LLMLVARVGRlrgmdaqiEHDIVHGLQALPARIEQMLSQDKLIESLAEgFSDKHHALFLGRGDQYPIAMEGALKLKEISY 493
Cdd:COG2222 154 LLALLAAWGG--------DDALLAALDALPAALEAALAADWPAAALAA-LADAERVVFLGRGPLYGLAREAALKLKELSA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 494 IHAEAYAAGELKHGPLALIDADMPVVVVAPNNELLEKLKSNIEEVRARGGELYVFADEDAGFtssenmkiIPLPHIE--- 570
Cdd:COG2222 225 GHAEAYSAAEFRHGPKSLVDPGTLVVVLASEDPTRELDLDLAAELRALGARVVAIGAEDDAA--------ITLPAIPdlh 296
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 504730047 571 EVIAPIFYTVPLQLLSYHVALIKGTDVDQPRNLAKSVTVE 610
Cdd:COG2222 297 DALDPLLLLVVAQRLALALALARGLDPDTPRHLNKVVKTV 336
|
|
| SIS_GlmS_GlmD_2 |
cd05009 |
SIS (Sugar ISomerase) domain repeat 2 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
454-608 |
2.15e-67 |
|
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: 216.36 E-value: 2.15e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 454 KLIESLAEGFSDKHHALFLGRGDQYPIAMEGALKLKEISYIHAEAYAAGELKHGPLALIDADMPVVVVAPNNELLEKLKS 533
Cdd:cd05009 1 EDIKELAEKLKEAKSFYVLGRGPNYGTALEGALKLKETSYIHAEAYSAGEFKHGPIALVDEGTPVIFLAPEDRLEEKLES 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504730047 534 NIEEVRARGGELYVFADEDAgfTSSENMKIIPLPHIEEVIAPIFYTVPLQLLSYHVALIKGTDVDQPRNLAKSVT 608
Cdd:cd05009 81 LIKEVKARGAKVIVITDDGD--AKDLADVVIRVPATVEELSPLLYIVPLQLLAYHLAVARGIDPDKPRNLAKSVT 153
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
2-214 |
1.53e-61 |
|
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: 203.45 E-value: 1.53e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 2 CGIVGAVAQRDVAEILLE----GLRRLEYRGYDSAGLAVVDSEGNVaRLRRLGKVQVLSQAAEEHELHGGTGIAHTRWAT 77
Cdd:cd00352 1 CGIFGIVGADGAASLLLLlllrGLAALEHRGPDGAGIAVYDGDGLF-VEKRAGPVSDVALDLLDEPLKSGVALGHVRLAT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 78 HGEPSEENAHPHVSE--HITIVHNGIIENHEPLRELLIGRGYRFVSETDTEVVAHLvhFEQQQNGGTLVDVVKRVIPQLR 155
Cdd:cd00352 80 NGLPSEANAQPFRSEdgRIALVHNGEIYNYRELREELEARGYRFEGESDSEVILHL--LERLGREGGLFEAVEDALKRLD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504730047 156 GAYGMVVLDnRDPSVLVAARSG---SPLVIGRGV-GENFIASDQLALLPVT-RRFMFLEEGDIA 214
Cdd:cd00352 158 GPFAFALWD-GKPDRLFAARDRfgiRPLYYGITKdGGLVFASEPKALLALPfKGVRRLPPGELL 220
|
|
| SIS_GlmS_GlmD_1 |
cd05008 |
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
296-422 |
3.73e-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: 3.73e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 296 HVQIIACGTSYNSGMVSRYWFESLAGIPCDVEIASEFRYRKPAVRKNSLMITLSQSGETADTLAALRLSKELGYLgSLAI 375
Cdd:cd05008 1 RILIVGCGTSYHAALVAKYLLERLAGIPVEVEAASEFRYRRPLLDEDTLVIAISQSGETADTLAALRLAKEKGAK-TVAI 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 504730047 376 CNVAGSSLVRESDLALMTKAGVEIGVASTKAFTTQLTVLLMLVARVG 422
Cdd:cd05008 80 TNVVGSTLAREADYVLYLRAGPEISVAATKAFTSQLLALLLLALALA 126
|
|
| PurF |
COG0034 |
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ... |
1-198 |
1.80e-38 |
|
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: 147.86 E-value: 1.80e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 1 MCGIVGAVAQRDVAEILLEGLRRLEYRGYDSAGLAVVDseGNVARLRR-LGKV-QVLSqaaEEH--ELHGGTGIAHTRWA 76
Cdd:COG0034 7 ECGVFGIYGHEDVAQLTYYGLYALQHRGQESAGIATSD--GGRFHLHKgMGLVsDVFD---EEDleRLKGNIAIGHVRYS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 77 THGEPSEENAHPHVSEH----ITIVHNGIIENHEPLRELLIGRGYRFVSETDTEVVAHLvhFEQQQNGGTLVDVVKRVIP 152
Cdd:COG0034 82 TTGSSSLENAQPFYVNSpfgsIALAHNGNLTNAEELREELEEEGAIFQTTSDTEVILHL--IARELTKEDLEEAIKEALR 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 504730047 153 QLRGAYGMVVLDNRdpsVLVAAR--SG-SPLVIGRGVGENFIASDQLAL 198
Cdd:COG0034 160 RVKGAYSLVILTGD---GLIAARdpNGiRPLVLGKLEDGYVVASESCAL 205
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
290-420 |
3.46e-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: 126.26 E-value: 3.46e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 290 LLAKVEHVQIIACGTSYNSGMVSRYWFESLAGIPCDVEIASEFRYR-KPAVRKNSLMITLSQSGETADTLAALRLSKELG 368
Cdd:pfam01380 1 LLAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGvLALVDEDDLVIAISYSGETKDLLAAAELAKARG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 504730047 369 yLGSLAICNVAGSSLVRESDLALMTKAGVEIGVASTKAFTTQLTVLLMLVAR 420
Cdd:pfam01380 81 -AKIIAITDSPGSPLAREADHVLYINAGPETGVASTKSITAQLAALDALAVA 131
|
|
| GPATase_N |
cd00715 |
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ... |
2-198 |
1.32e-33 |
|
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: 128.73 E-value: 1.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 2 CGIVGAVAQRDVAEILLEGLRRLEYRGYDSAGLAVVDseGNVARLRR-LGKVqvlSQAAEEH---ELHGGTGIAHTRWAT 77
Cdd:cd00715 1 CGVFGIYGAEDAARLTYLGLYALQHRGQESAGIATSD--GKRFHTHKgMGLV---SDVFDEEklrRLPGNIAIGHVRYST 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 78 HGEPSEENAHPHVSEH----ITIVHNGIIENHEPLRELLIGRGYRFVSETDTEVVAHLVHFEQQQngGTLVDVVKRVIPQ 153
Cdd:cd00715 76 AGSSSLENAQPFVVNSplggIALAHNGNLVNAKELREELEEEGRIFQTTSDSEVILHLIARSLAK--DDLFEAIIDALER 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 504730047 154 LRGAYGMVVLDN------RDPsvlVAARsgsPLVIGRGVGENFI-ASDQLAL 198
Cdd:cd00715 154 VKGAYSLVIMTAdgliavRDP---HGIR---PLVLGKLEGDGYVvASESCAL 199
|
|
| purF |
TIGR01134 |
amidophosphoribosyltransferase; Alternate name: glutamine phosphoribosylpyrophosphate (PRPP) ... |
2-198 |
2.79e-30 |
|
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: 123.97 E-value: 2.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 2 CGIVGAVAQR-DVAEILLEGLRRLEYRGYDSAGLAVVDseGNVARLRR-LGKVQVLSQAAEEHELHGGTGIAHTRWATHG 79
Cdd:TIGR01134 1 CGVVGIYGQEeVAASLTYYGLYALQHRGQESAGISVFD--GNRFRLHKgNGLVSDVFNEEHLQRLKGNVGIGHVRYSTAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 80 EPSEENAHPHVSE----HITIVHNGIIENHEPLRELLIGRGYRFVSETDTEVVAHLVHFEQQQNgGTLVDVVKRVIPQLR 155
Cdd:TIGR01134 79 SSGLENAQPFVVNspygGLALAHNGNLVNADELRRELEEEGRHFNTTSDSEVLLHLLAHNDESK-DDLFDAVARVLERVR 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 504730047 156 GAYGMVVLDNRDpsvLVAARS--G-SPLVIGRgVGENF-IASDQLAL 198
Cdd:TIGR01134 158 GAYALVLMTEDG---LVAVRDphGiRPLVLGR-RGDGYvVASESCAL 200
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
463-593 |
6.61e-28 |
|
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: 108.54 E-value: 6.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 463 FSDKHHALFLGRGDQYPIAMEGALKLKEISYIHAEAYAAGELKHGPLALIDADMPVVVVAPNNELLEKLKsNIEEVRARG 542
Cdd:pfam01380 2 LAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGVLALVDEDDLVIAISYSGETKDLLA-AAELAKARG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 504730047 543 GELYVFADEDAGFTSSENMKIIPLPHIEEVIAPIFYTVPLQLLSYHVALIK 593
Cdd:pfam01380 81 AKIIAITDSPGSPLAREADHVLYINAGPETGVASTKSITAQLAALDALAVA 131
|
|
| PLN02440 |
PLN02440 |
amidophosphoribosyltransferase |
1-201 |
1.42e-24 |
|
amidophosphoribosyltransferase
Pssm-ID: 215241 [Multi-domain] Cd Length: 479 Bit Score: 107.46 E-value: 1.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 1 MCGIVGAVAQRDVAEILLEGLRRLEYRGYDSAGlaVVDSEGNVARLRR-LGKVQVLSQAAEEHELHGGTGIAHTRWATHG 79
Cdd:PLN02440 1 ECGVVGIFGDPEASRLCYLGLHALQHRGQEGAG--IVTVDGNRLQSITgNGLVSDVFDESKLDQLPGDIAIGHVRYSTAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 80 EPSEENAHPHVSEH----ITIVHNGIIENHEPLRELLIGRGYRFVSETDTEVVAHLVHFEQQQNggtLVDVVKRVIPQLR 155
Cdd:PLN02440 79 ASSLKNVQPFVANYrfgsIGVAHNGNLVNYEELRAKLEENGSIFNTSSDTEVLLHLIAISKARP---FFSRIVDACEKLK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 504730047 156 GAYGMVVLDNrdpSVLVAARSGS---PLVIG-RGVGENFIASDQLALLPV 201
Cdd:PLN02440 156 GAYSMVFLTE---DKLVAVRDPHgfrPLVMGrRSNGAVVFASETCALDLI 202
|
|
| PRK05793 |
PRK05793 |
amidophosphoribosyltransferase; Provisional |
2-198 |
5.69e-24 |
|
amidophosphoribosyltransferase; Provisional
Pssm-ID: 235611 [Multi-domain] Cd Length: 469 Bit Score: 105.50 E-value: 5.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 2 CGIVGAVA--QRDVAEILLEGLRRLEYRGYDSAGLAVVDSEgNVARLRRLGKVQVLSQAAEEHELHGGTGIAHTRWATHG 79
Cdd:PRK05793 15 CGVFGVFSknNIDVASLTYYGLYALQHRGQESAGIAVSDGE-KIKVHKGMGLVSEVFSKEKLKGLKGNSAIGHVRYSTTG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 80 EPSEENAHPHVSEH----ITIVHNGIIENHEPLRELLIGRGYRFVSETDTEVVAHLVhfeQQQNGGTLVDVVKRVIPQLR 155
Cdd:PRK05793 94 ASDLDNAQPLVANYklgsIAIAHNGNLVNADVIRELLEDGGRIFQTSIDSEVILNLI---ARSAKKGLEKALVDAIQAIK 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 504730047 156 GAYGMVVL-DNRdpsvLVAARSGS---PLVIGRGVGENFIASDQLAL 198
Cdd:PRK05793 171 GSYALVILtEDK----LIGVRDPHgirPLCLGKLGDDYILSSESCAL 213
|
|
| GlxB |
cd01907 |
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ... |
2-198 |
1.24e-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: 1.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 2 CGIVGAV---AQRDVAEILLEGLRRLEYRG-YDSAGLAVVDSEG--------NVARLRRLGKVQVLSQAAEEHELHGGTG 69
Cdd:cd01907 1 CGIFGIMskdGEPFVGALLVEMLDAMQERGpGDGAGFALYGDPDafvyssgkDMEVFKGVGYPEDIARRYDLEEYKGYHW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 70 IAHTRWATHGEPSEENAHPHVSEHITIVHNGIIENHEPLRELLIGRGYRFVSETDTEVVAHLVHFEQQQnGGTLVDVVKR 149
Cdd:cd01907 81 IAHTRQPTNSAVWWYGAHPFSIGDIAVVHNGEISNYGSNREYLERFGYKFETETDTEVIAYYLDLLLRK-GGLPLEYYKH 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 150 VI----------PQLRGAYGMVVLDNrdPSVLVAARSGS-----------PLVIGRGVGENFIASDQLAL 198
Cdd:cd01907 160 IIrmpeeerellLALRLTYRLADLDG--PFTIIVGTPDGfivirdriklrPAVVAETDDYVAIASEECAI 227
|
|
| GATase_6 |
pfam13522 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
59-175 |
4.89e-18 |
|
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: 80.43 E-value: 4.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 59 AEEHELHGGTGIAHTRWATHGEPSEENaHPHVSE--HITIVHNGIIENHEPLRELLIGRGYRFVSETDTEVVAHLVHfeq 136
Cdd:pfam13522 3 FSGIWVEGGVALGHVRLAIVDLPDAGN-QPMLSRdgRLVLVHNGEIYNYGELREELADLGHAFRSRSDTEVLLALYE--- 78
|
90 100 110
....*....|....*....|....*....|....*....
gi 504730047 137 qqNGGtlvdvvKRVIPQLRGAYGMVVLDnRDPSVLVAAR 175
Cdd:pfam13522 79 --EWG------EDCLERLRGMFAFAIWD-RRRRTLFLAR 108
|
|
| GATase_7 |
pfam13537 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
94-200 |
8.52e-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: 8.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 94 ITIVHNGIIENHEPLRELLIGRGYRFVSETDTEVVAHLVHFEqqqnGGTlvDVVKRvipqLRGAYGMVVLDNRDPSvLVA 173
Cdd:pfam13537 24 YVIVFNGEIYNYRELRAELEAKGYRFRTHSDTEVILHLYEAE----WGE--DCVDR----LNGMFAFAIWDRRRQR-LFL 92
|
90 100 110
....*....|....*....|....*....|.
gi 504730047 174 AR--SG-SPLVIGRGVGENFI-ASDQLALLP 200
Cdd:pfam13537 93 ARdrFGiKPLYYGRDDGGRLLfASELKALLA 123
|
|
| AsnB |
cd00712 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ... |
2-201 |
1.27e-14 |
|
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: 73.36 E-value: 1.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 2 CGIVGAV---AQRDVAEILLEGLRRLEYRGYDSAGLavvdsegnvarlrrlgkvqvlsqaaeehELHGGTGIAHTRWATH 78
Cdd:cd00712 1 CGIAGIIgldGASVDRATLERMLDALAHRGPDGSGI----------------------------WIDEGVALGHRRLSII 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 79 GEpseENAH-PHVSE--HITIVHNGIIENHEPLRELLIGRGYRFVSETDTEVVAHLvhFEQQqngGTlvDVVKRvipqLR 155
Cdd:cd00712 53 DL---SGGAqPMVSEdgRLVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHL--YEEW---GE--DCLER----LN 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 504730047 156 GAYGMVVLDNRDpSVLVAAR--SGS-PLVIGRGvGENFI-ASDQLALLPV 201
Cdd:cd00712 119 GMFAFALWDKRK-RRLFLARdrFGIkPLYYGRD-GGGLAfASELKALLAL 166
|
|
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
1-201 |
6.46e-14 |
|
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: 74.49 E-value: 6.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 1 MCGIVGAVAQRDVA--EILLEGLRRLEYRGYDSAGlavvdsegnvarlrrlgkvqvlsqaaeeHELHGGTGIAHTRWATH 78
Cdd:COG0367 1 MCGIAGIIDFDGGAdrEVLERMLDALAHRGPDGSG----------------------------IWVDGGVALGHRRLSII 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 79 GEpsEENAH-PHVSE--HITIVHNGIIENHEPLRELLIGRGYRFVSETDTEVVAHLVHfeqqQNGgtlVDVVKRvipqLR 155
Cdd:COG0367 53 DL--SEGGHqPMVSEdgRYVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHAYE----EWG---EDCLER----LN 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 504730047 156 GAYGMVVLDnRDPSVLVAAR--SGS-PLVIGRgVGENFI-ASDQLALLPV 201
Cdd:COG0367 120 GMFAFAIWD-RRERRLFLARdrFGIkPLYYAE-DGGGLAfASELKALLAH 167
|
|
| SIS_1 |
cd05710 |
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ... |
296-420 |
3.04e-13 |
|
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: 66.45 E-value: 3.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 296 HVQIIACGTSYNSGMVSRYWFESLAGIPCDVEIASEFRYRKPA-VRKNSLMITLSQSGETADTLAALRLSKELGYLgSLA 374
Cdd:cd05710 1 NVFFVGCGGSLADMYPAKYFLKKESKLPVFVYNAAEFLHTGPKrLTEKSVVILASHSGNTKETVAAAKFAKEKGAT-VIG 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 504730047 375 ICNVAGSSLVRESDLALMTKAGveigvasTKAFTTQLTVLLMLVAR 420
Cdd:cd05710 80 LTDDEDSPLAKLADYVIVYGFE-------IDAVEEKYLLLYMLALR 118
|
|
| YafJ |
COG0121 |
Predicted glutamine amidotransferase YafJ [General function prediction only]; |
3-178 |
4.16e-13 |
|
Predicted glutamine amidotransferase YafJ [General function prediction only];
Pssm-ID: 439891 [Multi-domain] Cd Length: 248 Bit Score: 69.61 E-value: 4.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 3 GIVGAVAqRDVAEILLEGLRRLEYRGYDSA--------GLAVVDSEGNVARLRRLGKV---QVLSQAAeeHELHGGTGIA 71
Cdd:COG0121 5 GYSGNVP-TDLEFLLLDPEHSLVRQSGATRegphadgwGIGWYEGDGEPRLYRDPLPAwsdPNLRLLA--RPIKSRLVIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 72 HTRWATHGEPSEENAHPHVSEHITIVHNGIIENHEPLRELL---IGRGYRF--VSETDTEVVAHLVHFEQQQNGGTLVDV 146
Cdd:COG0121 82 HVRKATVGPVSLENTHPFRGGRWLFAHNGQLDGFDRLRRRLaeeLPDELYFqpVGTTDSELAFALLLSRLRDGGPDPAEA 161
|
170 180 190
....*....|....*....|....*....|....*...
gi 504730047 147 VKRVIPQLR------GAYGMVVLDNRdpsVLVAARSGS 178
Cdd:COG0121 162 LAEALRELAelarapGRLNLLLSDGE---RLYATRYTS 196
|
|
| YafJ |
cd01908 |
Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine ... |
30-179 |
1.01e-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: 68.57 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 30 DSAGLAVVDSEGNVARLRRLGKVqVLSQAAEEHE---LHGGTGIAHTRWATHGEPSEENAHPHVSEHITIVHNGIIENHE 106
Cdd:cd01908 42 DGWGIGWYEGKGGRPFRYRSPLP-AWSDINLESLarpIKSPLVLAHVRAATVGPVSLENCHPFTRGRWLFAHNGQLDGFR 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 107 PLRELLI-GRGYRFVSETDTEVVAHL----VHFEQQQNGGTLVDVVKRVIPQLRGAYGMVVLdN---RDPSVLVAARSGS 178
Cdd:cd01908 121 LLRRRLLrLLPRLPVGTTDSELAFALllsrLLERDPLDPAELLDAILQTLRELAALAPPGRL-NlllSDGEYLIATRYAS 199
|
.
gi 504730047 179 P 179
Cdd:cd01908 200 A 200
|
|
| PLN02549 |
PLN02549 |
asparagine synthase (glutamine-hydrolyzing) |
1-206 |
9.72e-12 |
|
asparagine synthase (glutamine-hydrolyzing)
Pssm-ID: 178164 [Multi-domain] Cd Length: 578 Bit Score: 67.87 E-value: 9.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 1 MCGIVGAVAQRDVA----EILLEGLRRLEYRGYDSAGLAVvdsegnvarlrrlgkvqvlsqaaeehelHGGTGIAHTRWA 76
Cdd:PLN02549 1 MCGILAVLGCSDDSqakrSRVLELSRRLRHRGPDWSGLYG----------------------------NEDCYLAHERLA 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 77 THGEPSEEnaHPHVSEHITIV--HNGIIENHEPLRELLigRGYRFVSETDTEVVAHLVhfeqQQNGGTLVDvvkrvipQL 154
Cdd:PLN02549 53 IMDPESGD--QPLYNEDKTIVvtANGEIYNHKELREKL--KLHKFRTGSDCEVIAHLY----EEHGEEFVD-------ML 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 504730047 155 RGAYGMVVLDNRDPSVlVAARSG---SPLVIGRGV-GENFIASDQLALLPVTRRFM 206
Cdd:PLN02549 118 DGMFSFVLLDTRDNSF-IAARDHigiTPLYIGWGLdGSVWFASEMKALCDDCERFE 172
|
|
| SIS |
cd04795 |
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
297-376 |
1.18e-10 |
|
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: 58.15 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 297 VQIIACGTSYNSGMVSRYWFESLAGIPCDVEIASEFRYRKPAV--RKNSLMITLSQSGETADTLAALRLSKELGyLGSLA 374
Cdd:cd04795 1 IFVIGIGGSGAIAAYFALELLELTGIEVVALIATELEHASLLSllRKGDVVIALSYSGRTEELLAALEIAKELG-IPVIA 79
|
..
gi 504730047 375 IC 376
Cdd:cd04795 80 IT 81
|
|
| PTZ00077 |
PTZ00077 |
asparagine synthetase-like protein; Provisional |
1-198 |
6.02e-10 |
|
asparagine synthetase-like protein; Provisional
Pssm-ID: 185431 [Multi-domain] Cd Length: 586 Bit Score: 62.04 E-value: 6.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 1 MCGIVGAVAQRDVAEIL----LEGLRRLEYRGYDSAGLAVvdsegnvarlrrlgkvqvlsqaaEEHELHGGTGIAHTRWA 76
Cdd:PTZ00077 1 MCGILAIFNSKGERHELrrkaLELSKRLRHRGPDWSGIIV-----------------------LENSPGTYNILAHERLA 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 77 THGepSEENAHPHVS--EHITIVHNGIIENHEPLRELLIGRGYRFVSETDTEVVAHLvhFEQQQNGGTLvdvvkrviPQL 154
Cdd:PTZ00077 58 IVD--LSDGKQPLLDddETVALMQNGEIYNHWEIRPELEKEGYKFSSNSDCEIIGHL--YKEYGPKDFW--------NHL 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 504730047 155 RGAYGMVVLDNRDPSvLVAARSG---SPLVIGRGV-GENFIASDQLAL 198
Cdd:PTZ00077 126 DGMFATVIYDMKTNT-FFAARDHigiIPLYIGYAKdGSIWFSSELKAL 172
|
|
| asn_synth_AEB |
TIGR01536 |
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing ... |
4-175 |
1.03e-08 |
|
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing asparagine synthase. A poorly conserved C-terminal extension was removed from the model. Bacterial members of the family tend to have a long, poorly conserved insert lacking from archaeal and eukaryotic sequences. Multiple isozymes have been demonstrated, such as in Bacillus subtilis. Long-branch members of the phylogenetic tree (which typically were also second or third candidate members from their genomes) were removed from the seed alignment and score below trusted cutoff. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 273676 [Multi-domain] Cd Length: 466 Bit Score: 57.73 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 4 IVGAVAQRDVA----EILLEGLRRLEYRGYDSAGLAVVDsEGNVARLRRL------GKVQVLSQAAEEHelhggtgiaht 73
Cdd:TIGR01536 1 IAGFFDLDDKAveedEAIKRMSDTIAHRGPDASGIEYKD-GNAILGHRRLaiidlsGGAQPMSNEGKTY----------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 74 rwathgepseenahphvsehiTIVHNGIIENHEPLRELLIGRGYRFVSETDTEVVAHLVhfeqQQNGGTLVDvvkrvipQ 153
Cdd:TIGR01536 69 ---------------------VIVFNGEIYNHEELREELEAKGYTFQTDSDTEVILHLY----EEWGEECVD-------R 116
|
170 180
....*....|....*....|..
gi 504730047 154 LRGAYGMVVLDNRDpSVLVAAR 175
Cdd:TIGR01536 117 LDGMFAFALWDSEK-GELFLAR 137
|
|
| asnB |
PRK09431 |
asparagine synthetase B; Provisional |
1-236 |
1.18e-08 |
|
asparagine synthetase B; Provisional
Pssm-ID: 236513 [Multi-domain] Cd Length: 554 Bit Score: 58.00 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 1 MCGIVGAVAQRDVAEIL----LEGLRRLEYRGYDSAGLAVVDSegnvarlrrlgkvqvlsqaaeehelhggtGI-AHTRW 75
Cdd:PRK09431 1 MCGIFGILDIKTDADELrkkaLEMSRLMRHRGPDWSGIYASDN-----------------------------AIlGHERL 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 76 A----THGepseenAHPHVSEHIT--IVHNGIIENHEPLRELLIGRgYRFVSETDTEVVAHLVhfeqQQNGGTLVDvvkr 149
Cdd:PRK09431 52 SivdvNGG------AQPLYNEDGThvLAVNGEIYNHQELRAELGDK-YAFQTGSDCEVILALY----QEKGPDFLD---- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 150 vipQLRGAYGMVVLDNRDPSVLvAARS--G-SPLVIGR-GVGENFIASDQLALLPVTRRFM-FL-------EEGDIAEIT 217
Cdd:PRK09431 117 ---DLDGMFAFALYDSEKDAYL-IARDpiGiIPLYYGYdEHGNLYFASEMKALVPVCKTIKeFPpghyywsKDGEFVRYY 192
|
250 260
....*....|....*....|
gi 504730047 218 RRDVRVFDK-SGQLAAREEI 236
Cdd:PRK09431 193 QRDWFDYDAvKDNVTDKNEL 212
|
|
| SIS_RpiR |
cd05013 |
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ... |
289-419 |
2.61e-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: 53.00 E-value: 2.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 289 ELLAKVEHVQIIACGTSYNSGM-VSRYWFesLAGIPCDVEIAS-EFRYRKPAVRKNSLMITLSQSGETADTLAALRLSKE 366
Cdd:cd05013 8 DLLAKARRIYIFGVGSSGLVAEyLAYKLL--RLGKPVVLLSDPhLQLMSAANLTPGDVVIAISFSGETKETVEAAEIAKE 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 504730047 367 LGyLGSLAICNVAGSSLVRESDLALMTKA-GVEIGVASTKAFTTQLTVLLMLVA 419
Cdd:cd05013 86 RG-AKVIAITDSANSPLAKLADIVLLVSSeEGDFRSSAFSSRIAQLALIDALFL 138
|
|
| SIS |
cd04795 |
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
470-550 |
3.20e-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: 51.22 E-value: 3.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 470 LFLGRGDQYPIAMEGALKLKEISYIHAEAYAAGELKHGP-LALIDADMPVVVVAPNNElLEKLKSNIEEVRARGGELYVF 548
Cdd:cd04795 2 FVIGIGGSGAIAAYFALELLELTGIEVVALIATELEHASlLSLLRKGDVVIALSYSGR-TEELLAALEIAKELGIPVIAI 80
|
..
gi 504730047 549 AD 550
Cdd:cd04795 81 TD 82
|
|
| frlB |
PRK11382 |
fructoselysine 6-phosphate deglycase; |
288-601 |
1.13e-07 |
|
fructoselysine 6-phosphate deglycase;
Pssm-ID: 183111 [Multi-domain] Cd Length: 340 Bit Score: 54.24 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 288 DELLAK-VEHVQIIACGTSYNSGMVSRYWFESLAGIPCDVEIASEFRYRKP-AVRKNSLMITLSQSGETADTLAALRLSK 365
Cdd:PRK11382 37 EEMVKRdIDRIYFVACGSPLNAAQTAKHLADRFSDLQVYAISGWEFCDNTPyRLDDRCAVIGVSDYGKTEEVIKALELGR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 366 ELGYLgSLAICNVAGSSLVRESDLALMTKAGV--EIGVASTKAFTTQLTVLLMLVARVGRLRGMDAQIEHDIVHGLQALP 443
Cdd:PRK11382 117 ACGAL-TAAFTKRADSPITSAAEFSIDYQADCiwEIHLLLCYSVVLEMITRLAPNAEIGKIKNDLKQLPNALGHLVRTWE 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 444 ARIEQM---LSQDKLIESLAEGfsdkhhalflgrgDQYPIAM-EGALKLKEISYIHAEAYAAGELKHGPLALIDADMPVV 519
Cdd:PRK11382 196 EKGRQLgelASQWPMIYTVAAG-------------PLRPLGYkEGIVTLMEFTWTHGCVIESGEFRHGPLEIVEPGVPFL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 520 VVAPNNELLEKLKSNIEEVRARggelyvfadedagftsSENMKIIPLPHIEE----VIAPIFYTVPLQLLSYHVALIKGT 595
Cdd:PRK11382 263 FLLGNDESRHTTERAINFVKQR----------------TDNVIVIDYAEISQglhpWLAPFLMFVPMEWLCYYLSIYKDH 326
|
....*.
gi 504730047 596 DVDQPR 601
Cdd:PRK11382 327 NPDERR 332
|
|
| SIS_AgaS_like |
cd05010 |
AgaS-like protein. AgaS contains a SIS (Sugar ISomerase) domain which is found in many ... |
471-600 |
9.79e-05 |
|
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: 43.00 E-value: 9.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504730047 471 FLGRGDQYPIAMEGALKLKEIS--YIHAEAYAAGELKHGPLALIDADMPVVVVAPNNELLEKLKSN-IEEVRARGGELYV 547
Cdd:cd05010 3 YLGSGPLAGLAREAALKVLELTagKVATVYDSPLGFRHGPKSLVDDDTLVVVFVSNDPYTRQYDLDlLKELRRDGIAARV 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 504730047 548 FA---DEDAGFTSSENMKIIPLPHIEEV-IAPIfYTVPLQLLSYHVALIKGTDVDQP 600
Cdd:cd05010 83 IAispESDAGIEDNSHYYLPGSRDLDDVyLAFP-YILYAQLFALFNSIALGLTPDNP 138
|
|
| GATase_4 |
pfam13230 |
Glutamine amidotransferases class-II; This family captures members that are not found in ... |
70-126 |
3.10e-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: 43.09 E-value: 3.10e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504730047 70 IAHTRWATHGEPSEENAHPHVSE----HITIVHNGIIENHEPlreLLIGRgYRFVSETDTE 126
Cdd:pfam13230 75 IAHIRKATQGRVTLENTHPFMRElwgrYWIFAHNGDLKGYAP---KLSGR-FQPVGSTDSE 131
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