|
Name |
Accession |
Description |
Interval |
E-value |
| GlmS |
COG0449 |
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ... |
1-608 |
0e+00 |
|
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase domains [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440218 [Multi-domain] Cd Length: 610 Bit Score: 1073.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 1 MCGIVGYIGKNQAAPILLEGLSKLEYRGYDSAGIAVYNNNELEVAKSKGKLAVLSEKIDGgKKLSGNMGIGHTRWATHGE 80
Cdd:COG0449 1 MCGIVGYIGKRDAAPILLEGLKRLEYRGYDSAGIAVLDDGGLEVRKAVGKLANLEEKLAE-EPLSGTIGIGHTRWATHGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 81 PSDVNAHPHLSQSGRFAVVHNGIIENYISLKKKLESKGFEFISETDTEVIAHLFEYYYKG--DIMDTMIKVINRVEGSYA 158
Cdd:COG0449 80 PSDENAHPHTSCSGRIAVVHNGIIENYAELREELEAKGHTFKSETDTEVIAHLIEEYLKGggDLLEAVRKALKRLEGAYA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 159 LGVLCVDYPDQFIAVRKASPMIVGLGDEENFIASDVTAILKHTRDIYYLEDNEIVVLKKDSVKVYNADKEEVKKEKFTVD 238
Cdd:COG0449 160 LAVISADEPDRIVAARKGSPLVIGLGEGENFLASDVPALLPYTRRVIYLEDGEIAVLTRDGVEIYDLDGEPVEREVKTVD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 239 WDVSAAEKGGYEHFMMKEIEEQPKAIRDTISPRIK-DGKIVLDDISLTEEDIKNINKIYIVACGSAYHVGVVGKYVIEKM 317
Cdd:COG0449 240 WDAEAAEKGGYPHFMLKEIHEQPEAIRDTLRGRLDeDGRVVLDELNLAAEDLRNIDRIYIVACGTSYHAGLVGKYLIEEL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 318 CRIPVEVQVASEFRYCDPIVGKDDLVIVISQSGETADTKAALEEAKARGARVLSIVNVVGSAIAKASDDVIYTWAGPEIA 397
Cdd:COG0449 320 ARIPVEVEIASEFRYRDPVVDPGTLVIAISQSGETADTLAALREAKEKGAKVLAICNVVGSTIARESDAVLYTHAGPEIG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 398 VATTKAYSTQLTVIYLIAAYMADKLGKISKEEYADFIKEIESLPDKVAEILKSKEDVQYLASKFYNCHSIFFIGRNLDYA 477
Cdd:COG0449 400 VASTKAFTTQLAALYLLALYLARARGTLSAEEEAELLEELRKLPEKIEEVLDLEEQIEELAEKYADARNALFLGRGINYP 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 478 VSLEGSLKLKEISYIHSEAYAAGELKHGTISLIEDGTLVVALATGKNLFDKTVSNVKEVKARGAVVMGVTTEEHEHMDDV 557
Cdd:COG0449 480 VALEGALKLKEISYIHAEGYAAGELKHGPIALIDEGMPVVAIAPQDELYEKTLSNIQEVKARGGKVIAIADEGDEEVEEL 559
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 1052836952 558 ADYTVKIPATHEMLLPSLTVIPLQLFGYYVASLKGCDIDKPRNLAKSVTVE 608
Cdd:COG0449 560 ADDVIEVPEVDELLAPILAVVPLQLLAYHVAVLRGTDVDQPRNLAKSVTVE 610
|
|
| PRK00331 |
PRK00331 |
isomerizing glutamine--fructose-6-phosphate transaminase; |
1-608 |
0e+00 |
|
isomerizing glutamine--fructose-6-phosphate transaminase;
Pssm-ID: 234729 [Multi-domain] Cd Length: 604 Bit Score: 997.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 1 MCGIVGYIGKNQAAPILLEGLSKLEYRGYDSAGIAVYNNNELEVAKSKGKLAVLSEKIDGgKKLSGNMGIGHTRWATHGE 80
Cdd:PRK00331 1 MCGIVGYVGQRNAAEILLEGLKRLEYRGYDSAGIAVLDDGGLEVRKAVGKVANLEAKLEE-EPLPGTTGIGHTRWATHGK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 81 PSDVNAHPHLSQSGRFAVVHNGIIENYISLKKKLESKGFEFISETDTEVIAHLFEYYYK--GDIMDTMIKVINRVEGSYA 158
Cdd:PRK00331 80 PTERNAHPHTDCSGRIAVVHNGIIENYAELKEELLAKGHVFKSETDTEVIAHLIEEELKegGDLLEAVRKALKRLEGAYA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 159 LGVLCVDYPDQFIAVRKASPMIVGLGDEENFIASDVTAILKHTRDIYYLEDNEIVVLKKDSVKVYNADKEEVKKEKFTVD 238
Cdd:PRK00331 160 LAVIDKDEPDTIVAARNGSPLVIGLGEGENFLASDALALLPYTRRVIYLEDGEIAVLTRDGVEIFDFDGNPVEREVYTVD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 239 WDVSAAEKGGYEHFMMKEIEEQPKAIRDTISPRIKDgkivLDDISLTEEDIKNINKIYIVACGSAYHVGVVGKYVIEKMC 318
Cdd:PRK00331 240 WDASAAEKGGYRHFMLKEIYEQPEAIRDTLEGRLDE----LGEGELADEDLKKIDRIYIVACGTSYHAGLVAKYLIESLA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 319 RIPVEVQVASEFRYCDPIVGKDDLVIVISQSGETADTKAALEEAKARGARVLSIVNVVGSAIAKASDDVIYTWAGPEIAV 398
Cdd:PRK00331 316 GIPVEVEIASEFRYRDPVLSPKTLVIAISQSGETADTLAALRLAKELGAKTLAICNVPGSTIARESDAVLYTHAGPEIGV 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 399 ATTKAYSTQLTVIYLIAAYMADKLGKISKEEYADFIKEIESLPDKVAEILKSKEDVQYLASKFYNCHSIFFIGRNLDYAV 478
Cdd:PRK00331 396 ASTKAFTAQLAVLYLLALALAKARGTLSAEEEADLVHELRELPALIEQVLDLKEQIEELAEDFADARNALFLGRGVDYPV 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 479 SLEGSLKLKEISYIHSEAYAAGELKHGTISLIEDGTLVVALATGKNLFDKTVSNVKEVKARGAVVMGVTTEEHEHMDDvA 558
Cdd:PRK00331 476 ALEGALKLKEISYIHAEGYAAGELKHGPIALIDEGMPVVAIAPNDELYEKTKSNIQEVKARGARVIVIADEGDEVAEE-A 554
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 1052836952 559 DYTVKIPATHEMLLPSLTVIPLQLFGYYVASLKGCDIDKPRNLAKSVTVE 608
Cdd:PRK00331 555 DDVIEVPEVHELLAPLLYVVPLQLLAYHVALARGTDVDKPRNLAKSVTVE 604
|
|
| glmS |
TIGR01135 |
glucosamine--fructose-6-phosphate aminotransferase (isomerizing); The member from ... |
2-608 |
0e+00 |
|
glucosamine--fructose-6-phosphate aminotransferase (isomerizing); The member from Methanococcus jannaschii contains an intein. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan, Central intermediary metabolism, Amino sugars]
Pssm-ID: 273462 [Multi-domain] Cd Length: 607 Bit Score: 864.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 2 CGIVGYIGKNQAAPILLEGLSKLEYRGYDSAGIAVYNNNELEVAKSKGKLAVLSEKIDGgKKLSGNMGIGHTRWATHGEP 81
Cdd:TIGR01135 1 CGIVGYIGQRDAVPILLEGLKRLEYRGYDSAGIAVVDEGKLFVRKAVGKVAELANKLGE-KPLPGGVGIGHTRWATHGKP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 82 SDVNAHPHLSQSGRFAVVHNGIIENYISLKKKLESKGFEFISETDTEVIAHLFEYYYK--GDIMDTMIKVINRVEGSYAL 159
Cdd:TIGR01135 80 TDENAHPHTDEGGRIAVVHNGIIENYAELREELEARGHVFSSDTDTEVIAHLIEEELRegGDLLEAVQKALKQLRGAYAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 160 GVLCVDYPDQFIAVRKASPMIVGLGDEENFIASDVTAILKHTRDIYYLEDNEIVVLKKDSVKVYNADKEEVKKEKFTVDW 239
Cdd:TIGR01135 160 AVLHADHPETLVAARSGSPLIVGLGDGENFVASDVTALLPYTRRVIYLEDGDIAILTKDGVEIYNFEGAPVQREVRVIDW 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 240 DVSAAEKGGYEHFMMKEIEEQPKAIRDTISPRIKDGKIVLDDIsLTEEDIKNINKIYIVACGSAYHVGVVGKYVIEKMCR 319
Cdd:TIGR01135 240 DLDAAEKGGYRHFMLKEIYEQPRALRDTLEGRIEENGGVFEEL-GAEELLKNIDRIQIVACGTSYHAGLVAKYLIERLAG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 320 IPVEVQVASEFRYCDPIVGKDDLVIVISQSGETADTKAALEEAKARGARVLSIVNVVGSAIAKASDDVIYTWAGPEIAVA 399
Cdd:TIGR01135 319 IPVEVEIASEFRYRKPVVDKDTLVIAISQSGETADTLEALRLAKELGAKTLGICNVPGSTLVREADHTLYTRAGPEIGVA 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 400 TTKAYSTQLTVIYLIAAYMADKLGKISKEEYADFIKEIESLPDKVAEILKSKEDVQYLASKFYNCHSIFFIGRNLDYAVS 479
Cdd:TIGR01135 399 STKAFTTQLTVLYLLALALAKARGTLSAEEEAELVDALRRLPDLVEQVLLADESIAELAERYADKRNFLFLGRGLGYPIA 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 480 LEGSLKLKEISYIHSEAYAAGELKHGTISLIEDGTLVVALATGKNLFDKTVSNVKEVKARGAVVMGVTTEEHEHMDDVAD 559
Cdd:TIGR01135 479 LEGALKLKEISYIHAEGYPAGELKHGPIALIDEGLPVVAIAPKDSLLEKTKSNVEEVKARGARVIVFAPEDDETIASVAD 558
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 1052836952 560 YTVKIPATHEMLLPSLTVIPLQLFGYYVASLKGCDIDKPRNLAKSVTVE 608
Cdd:TIGR01135 559 DVIKLPEVEELLAPIVYTIPLQLLAYHIALAKGTDVDKPRNLAKSVTVE 607
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
1-607 |
3.23e-173 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 506.48 E-value: 3.23e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 1 MCGIVGYIGKNQAAPILLEGLSKLEYRGYDSAGIA-VYNNNELEVAKskgkLAVLSEKIDGGKKLSGN---------MGI 70
Cdd:PTZ00295 24 CCGIVGYLGNEDASKILLEGIEILQNRGYDSCGIStISSGGELKTTK----YASDGTTSDSIEILKEKlldshknstIGI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 71 GHTRWATHGEPSDVNAHPHLSQSGRFAVVHNGIIENYISLKKKLESKGFEFISETDTEVIAHLFEYYY--KGDIMDTMIK 148
Cdd:PTZ00295 100 AHTRWATHGGKTDENAHPHCDYKKRIALVHNGTIENYVELKSELIAKGIKFRSETDSEVIANLIGLELdqGEDFQEAVKS 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 149 VINRVEGSYALGVLCVDYPDQFIAVRKASPMIVGLGDEENFIASDVTAILKHTRDIYYLEDNEIVVLKKDSVKVYNADKE 228
Cdd:PTZ00295 180 AISRLQGTWGLCIIHKDNPDSLIVARNGSPLLVGIGDDSIYVASEPSAFAKYTNEYISLKDGEIAELSLENVNDLYTQRR 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 229 EVKKEKftvdwDVSAAEKGGYEHFMMKEIEEQPKAIRDTISPRIK----DGKIVLDDISLTEEDIKNINKIYIVACGSAY 304
Cdd:PTZ00295 260 VEKIPE-----EVIEKSPEPYPHWTLKEIFEQPIALSRALNNGGRlsgyNNRVKLGGLDQYLEELLNIKNLILVGCGTSY 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 305 HVGVVGKYVIEKM-CRIPVEVQVASEF---RYCDPIVGkddlVIVISQSGETADTKAALEEAKARGARVLSIVNVVGSAI 380
Cdd:PTZ00295 335 YAALFAASIMQKLkCFNTVQVIDASELtlyRLPDEDAG----VIFISQSGETLDVVRALNLADELNLPKISVVNTVGSLI 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 381 AKASDDVIYTWAGPEIAVATTKAYSTQLTVIYLIAAYMADKlGKISKEEY--ADFIKEIESLPDKVAEILKS-KEDVQYL 457
Cdd:PTZ00295 411 ARSTDCGVYLNAGREVAVASTKAFTSQVTVLSLIALWFAQN-KEYSCSNYkcSSLINSLHRLPTYIGMTLKScEEQCKRI 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 458 ASKFYNCHSIFFIGRNLDYAVSLEGSLKLKEISYIHSEAYAAGELKHGTISLI--EDGTLVVALATGKNLFDKTVSNVKE 535
Cdd:PTZ00295 490 AEKLKNAKSMFILGKGLGYPIALEGALKIKEITYIHAEGFSGGALKHGPFALIdkEKNTPVILIILDDEHKELMINAAEQ 569
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1052836952 536 VKARGAVVMGVTTEEHEhMDDVADYTVKIPaTHEMLLPSLTVIPLQLFGYYVASLKGCDIDKPRNLAKSVTV 607
Cdd:PTZ00295 570 VKARGAYIIVITDDEDL-VKDFADEIILIP-SNGPLTALLAVIPLQLLAYEIAILRGINPDKPRGLAKTVTV 639
|
|
| PLN02981 |
PLN02981 |
glucosamine:fructose-6-phosphate aminotransferase |
1-608 |
1.14e-160 |
|
glucosamine:fructose-6-phosphate aminotransferase
Pssm-ID: 215531 [Multi-domain] Cd Length: 680 Bit Score: 475.78 E-value: 1.14e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 1 MCGIVGYIGKNQAAP------ILLEGLSKLEYRGYDSAGIAVYNNNELE-----VAKSKGKLAVL---------SEKIDG 60
Cdd:PLN02981 1 MCGIFAYLNYNVPRErrfileVLFNGLRRLEYRGYDSAGIAIDNDPSLEsssplVFREEGKIESLvrsvyeevaETDLNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 61 GKKLSGNMGIGHTRWATHGEPSDVNAHPHLSQSG-RFAVVHNGIIENYISLKKKLESKGFEFISETDTEVIAHLFEYYY- 138
Cdd:PLN02981 81 DLVFENHAGIAHTRWATHGPPAPRNSHPQSSGPGnEFLVVHNGIITNYEVLKETLLRHGFTFESDTDTEVIPKLAKFVFd 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 139 -----KGDIM--DTMIKVINRVEGSYALGVLCVDYPDQFIAVRKASPMIVGLGDE------------------------E 187
Cdd:PLN02981 161 klneeEGDVTfsQVVMEVMRQLEGAYALIFKSPHYPNELVACKRGSPLLLGVKELpeeknssavftsegfltknrdkpkE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 188 NFIASDVTAILKHTRDIYYLEDNEIVVLKKDSVKVYNADKE------------EVKKEKFTVDWDVSAAEKGGYEHFMMK 255
Cdd:PLN02981 241 FFLASDASAVVEHTKRVLVIEDNEVVHLKDGGVGIYKFENEkgrgggglsrpaSVERALSTLEMEVEQIMKGNYDHYMQK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 256 EIEEQPKAIRDTISPRIKDG------KIVLDDISLTEEDIKNINKIYIVACGSAYHVGVVGKYVIEKMCRIPVEVQVASE 329
Cdd:PLN02981 321 EIHEQPESLTTTMRGRLIRGgsgkakRVLLGGLKDHLKTIRRSRRIVFIGCGTSYNAALAARPILEELSGVPVTMELASD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 330 F--RYCdPIVgKDDLVIVISQSGETADTKAALEEAKARGARVLSIVNVVGSAIAKASDDVIYTWAGPEIAVATTKAYSTQ 407
Cdd:PLN02981 401 LldRQG-PIY-REDTAVFVSQSGETADTLRALEYAKENGALCVGITNTVGSAISRGTHCGVHINAGAEIGVASTKAYTSQ 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 408 LTVIYLIA-AYMADKLGKISKEEyaDFIKEIESLPDKVAEILKSKEDVQYLASKFYNCHSIFFIGRNLDYAVSLEGSLKL 486
Cdd:PLN02981 479 IVAMTMLAlALGEDSISSRSRRE--AIIDGLFDLPNKVREVLKLDQEMKELAELLIDEQSLLVFGRGYNYATALEGALKV 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 487 KEISYIHSEAYAAGELKHGTISLIEDGTLVVALATGKNLFDKTVSNVKEVKARGAVVMGVTTEEhehmDDVADYT----- 561
Cdd:PLN02981 557 KEVALMHSEGILAGEMKHGPLALVDETLPIIVIATRDACFSKQQSVIQQLRARKGRLIVICSKG----DASSVCPsggcr 632
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1052836952 562 -VKIPATHEMLLPSLTVIPLQLFGYYVASLKGCDIDKPRNLAKSVTVE 608
Cdd:PLN02981 633 vIEVPQVEDCLQPVINIVPLQLLAYHLTVLRGHNVDQPRNLAKSVTTQ 680
|
|
| PTZ00394 |
PTZ00394 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
1-608 |
4.13e-156 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 173585 [Multi-domain] Cd Length: 670 Bit Score: 463.58 E-value: 4.13e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 1 MCGIVGYIGKN------QAAPILLEGLSKLEYRGYDSAGIAVYNNNELE---------------VAKSKGKLAVLSEKI- 58
Cdd:PTZ00394 1 MCGIFGYANHNvprtveQILNVLLDGIQKVEYRGYDSAGLAIDANIGSEkedgtaasaptprpcVVRSVGNISQLREKVf 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 59 ---------DGGKKLSGNMGIGHTRWATHGEPSDVNAHPHLSQSGRFAVVHNGIIENYISLKKKLESKGFEFISETDTEV 129
Cdd:PTZ00394 81 seavaatlpPMDATTSHHVGIAHTRWATHGGVCERNCHPQQSNNGEFTIVHNGIVTNYMTLKELLKEEGYHFSSDTDTEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 130 IAHLFEYYYKGD----IMDTMIKVINRVEGSYALGVLCVDYPDQFIAVRKASPMIVGL---------------------G 184
Cdd:PTZ00394 161 ISVLSEYLYTRKgihnFADLALEVSRMVEGSYALLVKSVYFPGQLAASRKGSPLMVGIrrtddrgcvmklqtydltdlsG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 185 DEENFIASDVTAILKHTRDIYYLEDNEIVVLKKDSVKVYNADKEE---VKKEKFTVDWDVSAAEKGGYEHFMMKEIEEQP 261
Cdd:PTZ00394 241 PLEVFFSSDVNSFAEYTREVVFLEDGDIAHYCDGALRFYNAAERQrsiVKREVQHLDAKPEGLSKGNYPHFMLKEIYEQP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 262 KAIRDTISPRIK--DGKIVLDDISLTE-EDIKNINKIYIVACGSAYHVGVVGKYVIEKMCRIPVEVQVASEFRYCDPIVG 338
Cdd:PTZ00394 321 ESVISSMHGRIDfsSGTVQLSGFTQQSiRAILTSRRILFIACGTSLNSCLAVRPLFEELVPLPISVENASDFLDRRPRIQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 339 KDDLVIVISQSGETADTKAALEEAKARGARVLSIVNVVGSAIAKASDDVIYTWAGPEIAVATTKAYSTQLTVIYLIAAYM 418
Cdd:PTZ00394 401 RDDVCFFVSQSGETADTLMALQLCKEAGAMCVGITNVVGSSISRLTHYAIHLNAGVEVGVASTKAYTSQVVVLTLVALLL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 419 ADKLGKISKEEyADFIKEIESLPDKVAEILKSKED-VQYLASKFYNCHSIFFIGRNLDYAVSLEGSLKLKEISYIHSEAY 497
Cdd:PTZ00394 481 SSDSVRLQERR-NEIIRGLAELPAAISECLKITHDpVKALAARLKESSSILVLGRGYDLATAMEAALKVKELSYVHTEGI 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 498 AAGELKHGTISLIEDGTLVVALATGKNLFDKTVSNVKEVKARGAVVMGVTTEEHEHMDDVADYTVKIPATHEMLLPSLTV 577
Cdd:PTZ00394 560 HSGELKHGPLALIDETSPVLAMCTHDKHFGLSKSAVQQVKARGGAVVVFATEVDAELKAAASEIVLVPKTVDCLQCVVNV 639
|
650 660 670
....*....|....*....|....*....|.
gi 1052836952 578 IPLQLFGYYVASLKGCDIDKPRNLAKSVTVE 608
Cdd:PTZ00394 640 IPFQLLAYYMALLRGNNVDCPRNLAKSVTVQ 670
|
|
| GFAT |
cd00714 |
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ... |
2-215 |
1.11e-127 |
|
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: 374.09 E-value: 1.11e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 2 CGIVGYIGKNQAAPILLEGLSKLEYRGYDSAGIAVYNNNELEVAKSKGKLAVLSEKIDGgKKLSGNMGIGHTRWATHGEP 81
Cdd:cd00714 1 CGIVGYIGKREAVDILLEGLKRLEYRGYDSAGIAVIGDGSLEVVKAVGKVANLEEKLAE-KPLSGHVGIGHTRWATHGEP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 82 SDVNAHPHLSQSGRFAVVHNGIIENYISLKKKLESKGFEFISETDTEVIAHLFEYYYKG--DIMDTMIKVINRVEGSYAL 159
Cdd:cd00714 80 TDVNAHPHRSCDGEIAVVHNGIIENYAELKEELEAKGYKFESETDTEVIAHLIEYYYDGglDLLEAVKKALKRLEGAYAL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1052836952 160 GVLCVDYPDQFIAVRKASPMIVGLGDEENFIASDVTAILKHTRDIYYLEDNEIVVL 215
Cdd:cd00714 160 AVISKDEPDEIVAARNGSPLVIGIGDGENFVASDAPALLEHTRRVIYLEDGDIAVI 215
|
|
| AgaS |
COG2222 |
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ... |
255-608 |
1.26e-80 |
|
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: 257.52 E-value: 1.26e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 255 KEIEEQPKAIRDTISprikdgkIVLDDISLTEEDIKNIN--KIYIVACGSAYHVGVVGKYVIEKMCRIPVEVQVASEF-R 331
Cdd:COG2222 2 REIAQQPEAWRRALA-------ALAAAIAALLARLRAKPprRVVLVGAGSSDHAAQAAAYLLERLLGIPVAALAPSELvV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 332 YCDPIVGKDDLVIVISQSGETADTKAALEEAKARGARVLSIVNVVGSAIAKASDDVIYTWAGPEIAVATTKAYSTQLTVI 411
Cdd:COG2222 75 YPAYLKLEGTLVVAISRSGNSPEVVAALELAKARGARTLAITNNPDSPLAEAADRVLPLPAGPEKSVAATKSFTTMLLAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 412 YLIAAYMADKlgkiskeeyADFIKEIESLPDKVAEILKSKEDVQYLASkFYNCHSIFFIGRNLDYAVSLEGSLKLKEISY 491
Cdd:COG2222 155 LALLAAWGGD---------DALLAALDALPAALEAALAADWPAAALAA-LADAERVVFLGRGPLYGLAREAALKLKELSA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 492 IHSEAYAAGELKHGTISLIEDGTLVVALATGKNLFDKTVSNVKEVKARGAVVMGVTTEehehmDDVADYTVKIPATHEML 571
Cdd:COG2222 225 GHAEAYSAAEFRHGPKSLVDPGTLVVVLASEDPTRELDLDLAAELRALGARVVAIGAE-----DDAAITLPAIPDLHDAL 299
|
330 340 350
....*....|....*....|....*....|....*..
gi 1052836952 572 LPSLTVIPLQLFGYYVASLKGCDIDKPRNLAKSVTVE 608
Cdd:COG2222 300 DPLLLLVVAQRLALALALARGLDPDTPRHLNKVVKTV 336
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
2-213 |
5.05e-69 |
|
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: 223.09 E-value: 5.05e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 2 CGIVGYIGKNQAAPILLE----GLSKLEYRGYDSAGIAVYNNNELEVAKSKGKLAVLSEKIDGgKKLSGNMGIGHTRWAT 77
Cdd:cd00352 1 CGIFGIVGADGAASLLLLlllrGLAALEHRGPDGAGIAVYDGDGLFVEKRAGPVSDVALDLLD-EPLKSGVALGHVRLAT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 78 HGEPSDVNAHPHLSQSGRFAVVHNGIIENYISLKKKLESKGFEFISETDTEVIAHLFE-YYYKGDIMDTMIKVINRVEGS 156
Cdd:cd00352 80 NGLPSEANAQPFRSEDGRIALVHNGEIYNYRELREELEARGYRFEGESDSEVILHLLErLGREGGLFEAVEDALKRLDGP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1052836952 157 YALgVLCVDYPDQFIAVRKA---SPMIVGLG-DEENFIASDVTAILKHT-RDIYYLEDNEIV 213
Cdd:cd00352 160 FAF-ALWDGKPDRLFAARDRfgiRPLYYGITkDGGLVFASEPKALLALPfKGVRRLPPGELL 220
|
|
| SIS_GlmS_GlmD_1 |
cd05008 |
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
294-419 |
1.35e-62 |
|
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and Glucosamine-6-phosphate deaminase (GlmD). The SIS domain is found in many phosphosugar isomerases and phosphosugar binding proteins. GlmS contains a N-terminal glutaminase domain and two C-terminal SIS domains and catalyzes the first step in hexosamine metabolism, converting fructose 6-phosphate into glucosamine 6-phosphate using glutamine as nitrogen source. The glutaminase domain hydrolyzes glutamine to glutamate and ammonia. Ammonia is transferred through a channel to the isomerase domain for glucosamine 6-phosphate synthesis. The end product of the pathway is N-acetylglucosamine, which plays multiple roles in eukaryotic cells including being a building block of bacterial and fungal cell walls. In the absence of glutamine, GlmS catalyzes the isomerization of fructose 6-phosphate into glucose 6- phosphate (PGI-like activity). Glucosamine-6-phosphate deaminase (GlmD) contains two SIS domains and catalyzes the deamination and isomerization of glucosamine-6-phosphate into fructose-6-phosphate with the release of ammonia; in presence of high ammonia concentration, GlmD can catalyze the reverse reaction.
Pssm-ID: 240141 [Multi-domain] Cd Length: 126 Bit Score: 202.73 E-value: 1.35e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 294 KIYIVACGSAYHVGVVGKYVIEKMCRIPVEVQVASEFRYCDPIVGKDDLVIVISQSGETADTKAALEEAKARGARVLSIV 373
Cdd:cd05008 1 RILIVGCGTSYHAALVAKYLLERLAGIPVEVEAASEFRYRRPLLDEDTLVIAISQSGETADTLAALRLAKEKGAKTVAIT 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1052836952 374 NVVGSAIAKASDDVIYTWAGPEIAVATTKAYSTQLTVIYLIAAYMA 419
Cdd:cd05008 81 NVVGSTLAREADYVLYLRAGPEISVAATKAFTSQLLALLLLALALA 126
|
|
| SIS_GlmS_GlmD_2 |
cd05009 |
SIS (Sugar ISomerase) domain repeat 2 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
452-606 |
3.45e-61 |
|
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: 199.80 E-value: 3.45e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 452 EDVQYLASKFYNCHSIFFIGRNLDYAVSLEGSLKLKEISYIHSEAYAAGELKHGTISLIEDGTLVVALATGKNLFDKTVS 531
Cdd:cd05009 1 EDIKELAEKLKEAKSFYVLGRGPNYGTALEGALKLKETSYIHAEAYSAGEFKHGPIALVDEGTPVIFLAPEDRLEEKLES 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1052836952 532 NVKEVKARGAVVMGVTTEEHEhmDDVADYTVKIPATHEMLLPSLTVIPLQLFGYYVASLKGCDIDKPRNLAKSVT 606
Cdd:cd05009 81 LIKEVKARGAKVIVITDDGDA--KDLADVVIRVPATVEELSPLLYIVPLQLLAYHLAVARGIDPDKPRNLAKSVT 153
|
|
| GPATase_N |
cd00715 |
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ... |
2-221 |
4.67e-43 |
|
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: 154.93 E-value: 4.67e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 2 CGIVGYIGKNQAAPILLEGLSKLEYRGYDSAGIAVYNNNELEVAKSKGKLA-VLSEKIDggKKLSGNMGIGHTRWATHGE 80
Cdd:cd00715 1 CGVFGIYGAEDAARLTYLGLYALQHRGQESAGIATSDGKRFHTHKGMGLVSdVFDEEKL--RRLPGNIAIGHVRYSTAGS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 81 PSDVNAHPHL--SQSGRFAVVHNGIIENYISLKKKLESKGFEFISETDTEVIAHLFEY-YYKGDIMDTMIKVINRVEGSY 157
Cdd:cd00715 79 SSLENAQPFVvnSPLGGIALAHNGNLVNAKELREELEEEGRIFQTTSDSEVILHLIARsLAKDDLFEAIIDALERVKGAY 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1052836952 158 ALGVLCvdyPDQFIAVRKAS---PMIVG-LGDEENFIASDVTAIL----KHTRDIyylEDNEIVVLKKDSVK 221
Cdd:cd00715 159 SLVIMT---ADGLIAVRDPHgirPLVLGkLEGDGYVVASESCALDiigaEFVRDV---EPGEIVVIDDDGLE 224
|
|
| PurF |
COG0034 |
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ... |
1-223 |
6.08e-43 |
|
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: 160.19 E-value: 6.08e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 1 MCGIVGYIGKNQAAPILLEGLSKLEYRGYDSAGIAVYNNNELEVAKSKGKLA-VLSEKIdgGKKLSGNMGIGHTRWATHG 79
Cdd:COG0034 7 ECGVFGIYGHEDVAQLTYYGLYALQHRGQESAGIATSDGGRFHLHKGMGLVSdVFDEED--LERLKGNIAIGHVRYSTTG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 80 EPSDVNAHPHL--SQSGRFAVVHNGIIENYISLKKKLESKGFEFISETDTEVIAHLF-EYYYKGDIMDTMIKVINRVEGS 156
Cdd:COG0034 85 SSSLENAQPFYvnSPFGSIALAHNGNLTNAEELREELEEEGAIFQTTSDTEVILHLIaRELTKEDLEEAIKEALRRVKGA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1052836952 157 YALGVLcvdYPDQFIAVR-----KasPMIVGLGDEENFIASDVTAI----LKHTRDIyylEDNEIVVLKKDSVKVY 223
Cdd:COG0034 165 YSLVIL---TGDGLIAARdpngiR--PLVLGKLEDGYVVASESCALdilgAEFVRDV---EPGEIVVIDEDGLRSR 232
|
|
| PRK05793 |
PRK05793 |
amidophosphoribosyltransferase; Provisional |
2-232 |
5.06e-34 |
|
amidophosphoribosyltransferase; Provisional
Pssm-ID: 235611 [Multi-domain] Cd Length: 469 Bit Score: 135.16 E-value: 5.06e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 2 CGIVGYIGKNQ--AAPILLEGLSKLEYRGYDSAGIAVYNNNELEVAKSKGKLA-VLSEKIDggKKLSGNMGIGHTRWATH 78
Cdd:PRK05793 15 CGVFGVFSKNNidVASLTYYGLYALQHRGQESAGIAVSDGEKIKVHKGMGLVSeVFSKEKL--KGLKGNSAIGHVRYSTT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 79 GEPSDVNAHPHLSQS--GRFAVVHNGIIENYISLKKKLESKGFEFISETDTEVIAHLFEYYYKGDIMDTMIKVINRVEGS 156
Cdd:PRK05793 93 GASDLDNAQPLVANYklGSIAIAHNGNLVNADVIRELLEDGGRIFQTSIDSEVILNLIARSAKKGLEKALVDAIQAIKGS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 157 YALGVLcvdYPDQFIAVRKAS---PMIVGLGDEENFIASDVTAI----LKHTRDIyylEDNEIVVLKKDSVKVYNADKEE 229
Cdd:PRK05793 173 YALVIL---TEDKLIGVRDPHgirPLCLGKLGDDYILSSESCALdtigAEFIRDV---EPGEIVIIDEDGIKSIKFAEKT 246
|
...
gi 1052836952 230 VKK 232
Cdd:PRK05793 247 KCQ 249
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
289-415 |
4.65e-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: 123.18 E-value: 4.65e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 289 IKNINKIYIVACGSAYHVGVVGKYVIEKMCRIPVEVQVASEFRY-CDPIVGKDDLVIVISQSGETADTKAALEEAKARGA 367
Cdd:pfam01380 2 LAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHgVLALVDEDDLVIAISYSGETKDLLAAAELAKARGA 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1052836952 368 RVLSIVNVVGSAIAKASDDVIYTWAGPEIAVATTKAYSTQLTVIYLIA 415
Cdd:pfam01380 82 KIIAITDSPGSPLAREADHVLYINAGPETGVASTKSITAQLAALDALA 129
|
|
| purF |
TIGR01134 |
amidophosphoribosyltransferase; Alternate name: glutamine phosphoribosylpyrophosphate (PRPP) ... |
2-231 |
6.67e-32 |
|
amidophosphoribosyltransferase; Alternate name: glutamine phosphoribosylpyrophosphate (PRPP) amidotransferase. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 273461 [Multi-domain] Cd Length: 442 Bit Score: 128.59 E-value: 6.67e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 2 CGIVGYIG-KNQAAPILLEGLSKLEYRGYDSAGIAVYNNNELEVAKSKGKLA-VLSEKIDggKKLSGNMGIGHTRWATHG 79
Cdd:TIGR01134 1 CGVVGIYGqEEVAASLTYYGLYALQHRGQESAGISVFDGNRFRLHKGNGLVSdVFNEEHL--QRLKGNVGIGHVRYSTAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 80 EPSDVNAHPHL--SQSGRFAVVHNGIIENYISLKKKLESKGFEFISETDTEVIAHLFEYYY--KGDIMDTMIKVINRVEG 155
Cdd:TIGR01134 79 SSGLENAQPFVvnSPYGGLALAHNGNLVNADELRRELEEEGRHFNTTSDSEVLLHLLAHNDesKDDLFDAVARVLERVRG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 156 SYALGVLcvdYPDQFIAVRK---ASPMIVGLGDEENFIASDVTAI----LKHTRDIyylEDNEIVVLKKDSVKVYNADKE 228
Cdd:TIGR01134 159 AYALVLM---TEDGLVAVRDphgIRPLVLGRRGDGYVVASESCALdilgAEFVRDV---EPGEVVVIFDGGLESRQCARR 232
|
...
gi 1052836952 229 EVK 231
Cdd:TIGR01134 233 PRA 235
|
|
| GlxB |
cd01907 |
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ... |
2-214 |
2.98e-28 |
|
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: 113.52 E-value: 2.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 2 CGIVGYI---GKNQAAPILLEGLSKLEYRG-YDSAGIAVYNNNELEVAKSKGKLAVLSE-----------KIDggkKLSG 66
Cdd:cd01907 1 CGIFGIMskdGEPFVGALLVEMLDAMQERGpGDGAGFALYGDPDAFVYSSGKDMEVFKGvgypediarryDLE---EYKG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 67 NMGIGHTRWATHgepSDVN---AHPHlsQSGRFAVVHNGIIENYISLKKKLESKGFEFISETDTEVIAHLFEYYY-KGDI 142
Cdd:cd01907 78 YHWIAHTRQPTN---SAVWwygAHPF--SIGDIAVVHNGEISNYGSNREYLERFGYKFETETDTEVIAYYLDLLLrKGGL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 143 MDTMIKVINRVEG-----------SYALGVL------CVDYPDQFIAVR---KASPMIVGLGDEENFIASDVTAI----L 198
Cdd:cd01907 153 PLEYYKHIIRMPEeerelllalrlTYRLADLdgpftiIVGTPDGFIVIRdriKLRPAVVAETDDYVAIASEECAIreipD 232
|
250
....*....|....*.
gi 1052836952 199 KHTRDIYYLEDNEIVV 214
Cdd:cd01907 233 RDNAKVWEPRPGEYVI 248
|
|
| PLN02440 |
PLN02440 |
amidophosphoribosyltransferase |
1-174 |
3.19e-28 |
|
amidophosphoribosyltransferase
Pssm-ID: 215241 [Multi-domain] Cd Length: 479 Bit Score: 118.24 E-value: 3.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 1 MCGIVGYIGKNQAAPILLEGLSKLEYRGYDSAGIAVYNNNELEVAKSKGklaVLSEKIDGGK--KLSGNMGIGHTRWATH 78
Cdd:PLN02440 1 ECGVVGIFGDPEASRLCYLGLHALQHRGQEGAGIVTVDGNRLQSITGNG---LVSDVFDESKldQLPGDIAIGHVRYSTA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 79 GEPSDVNAHPHLSQS--GRFAVVHNGIIENYISLKKKLESKGFEFISETDTEVIAHLFEYYYKGDIMDTMIKVINRVEGS 156
Cdd:PLN02440 78 GASSLKNVQPFVANYrfGSIGVAHNGNLVNYEELRAKLEENGSIFNTSSDTEVLLHLIAISKARPFFSRIVDACEKLKGA 157
|
170
....*....|....*...
gi 1052836952 157 YALGVLcvdYPDQFIAVR 174
Cdd:PLN02440 158 YSMVFL---TEDKLVAVR 172
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
460-588 |
8.26e-23 |
|
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: 94.29 E-value: 8.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 460 KFYNCHSIFFIGRNLDYAVSLEGSLKLKEISYIHSEAYAAGELKHGTISLIEDGTLVVALATGKNLFDkTVSNVKEVKAR 539
Cdd:pfam01380 1 LLAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGVLALVDEDDLVIAISYSGETKD-LLAAAELAKAR 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1052836952 540 GAVVMGVTTEEHEHMDDVADYTVKIPATHEMLLPSLTVIPLQLFGYYVA 588
Cdd:pfam01380 80 GAKIIAITDSPGSPLAREADHVLYINAGPETGVASTKSITAQLAALDAL 128
|
|
| GATase_6 |
pfam13522 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
65-161 |
1.30e-20 |
|
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain found in a variety of enzymes, such as asparagine synthetase and glutamine--fructose-6-phosphate transaminase.
Pssm-ID: 433279 [Multi-domain] Cd Length: 130 Bit Score: 87.75 E-value: 1.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 65 SGNMGIGHTRWATHGEPSDVNaHPHLSQSGRFAVVHNGIIENYISLKKKLESKGFEFISETDTEVIAHLFEYYYKgdimd 144
Cdd:pfam13522 9 EGGVALGHVRLAIVDLPDAGN-QPMLSRDGRLVLVHNGEIYNYGELREELADLGHAFRSRSDTEVLLALYEEWGE----- 82
|
90
....*....|....*..
gi 1052836952 145 tmiKVINRVEGSYALGV 161
Cdd:pfam13522 83 ---DCLERLRGMFAFAI 96
|
|
| AsnB |
cd00712 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ... |
2-200 |
1.86e-18 |
|
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: 84.53 E-value: 1.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 2 CGIVGYIGKNQAAP---ILLEGLSKLEYRGYDSAGIAVynnnelevakskgklavlsekidggkklSGNMGIGHTRWATH 78
Cdd:cd00712 1 CGIAGIIGLDGASVdraTLERMLDALAHRGPDGSGIWI----------------------------DEGVALGHRRLSII 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 79 GEpsDVNAHPHLSQSGRFAVVHNGIIENYISLKKKLESKGFEFISETDTEVIAHLFEYYykGDimdtmiKVINRVEGSYA 158
Cdd:cd00712 53 DL--SGGAQPMVSEDGRLVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHLYEEW--GE------DCLERLNGMFA 122
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1052836952 159 LGVLCVDyPDQFIAVR-----KasPMIVGLGDEENFIASDVTAILKH 200
Cdd:cd00712 123 FALWDKR-KRRLFLARdrfgiK--PLYYGRDGGGLAFASELKALLAL 166
|
|
| SIS_1 |
cd05710 |
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ... |
295-417 |
1.25e-17 |
|
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: 79.16 E-value: 1.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 295 IYIVACGSAYHVGVVGKYVIEKMCRIPVEVQVASEFRYCDPI-VGKDDLVIVISQSGETADTKAALEEAKARGARVLSIV 373
Cdd:cd05710 2 VFFVGCGGSLADMYPAKYFLKKESKLPVFVYNAAEFLHTGPKrLTEKSVVILASHSGNTKETVAAAKFAKEKGATVIGLT 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1052836952 374 NVVGSAIAKASDDVIYTwaGPEIAVATTKAYstqltVIYLIAAY 417
Cdd:cd05710 82 DDEDSPLAKLADYVIVY--GFEIDAVEEKYL-----LLYMLALR 118
|
|
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
1-137 |
2.63e-17 |
|
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: 85.27 E-value: 2.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 1 MCGIVGYIGKNQAA--PILLEGLSKLEYRGYDSAGIAVynnnelevakskgklavlsekidggkklSGNMGIGHTRWATH 78
Cdd:COG0367 1 MCGIAGIIDFDGGAdrEVLERMLDALAHRGPDGSGIWV----------------------------DGGVALGHRRLSII 52
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 79 GEpsDVNAH-PHLSQSGRFAVVHNGIIENYISLKKKLESKGFEFISETDTEVIAHLFEYY 137
Cdd:COG0367 53 DL--SEGGHqPMVSEDGRYVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHAYEEW 110
|
|
| RpiR |
COG1737 |
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ... |
227-440 |
9.40e-17 |
|
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains [Transcription];
Pssm-ID: 441343 [Multi-domain] Cd Length: 286 Bit Score: 81.13 E-value: 9.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 227 KEEVKKEKFTVDWDVSAAEKGGYEHFMMKEIEEQPKAIRDTISprikdgkiVLDDISLTE--EDIKNINKIYIVACGSAY 304
Cdd:COG1737 75 AQELAEGLSSYERLRRLSPDDSLEDILAKVLEAEIANLEETLE--------LLDEEALERavDLLAKARRIYIFGVGASA 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 305 HVGVVGKYvieKMCRIPVEVQVASEfrycDP--------IVGKDDLVIVISQSGETADTKAALEEAKARGARVLSIVNVV 376
Cdd:COG1737 147 PVAEDLAY---KLLRLGKNVVLLDG----DGhlqaesaaLLGPGDVVIAISFSGYTRETLEAARLAKERGAKVIAITDSP 219
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1052836952 377 GSAIAKASDDVIYTWA-GPEIAVATTKAYSTQLTVIYLIAAYMADKLGkiskEEYADFIKEIESL 440
Cdd:COG1737 220 LSPLAKLADVVLYVPSeEPTLRSSAFSSRVAQLALIDALAAAVAQRDG----DKARERLERTEAL 280
|
|
| SIS_RpiR |
cd05013 |
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ... |
287-416 |
4.27e-16 |
|
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: 75.34 E-value: 4.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 287 EDIKNINKIYIVACGSAYHVGVVGKYVIEKMCRIPVEVQVASEFRYCDPIVGKDDLVIVISQSGETADTKAALEEAKARG 366
Cdd:cd05013 8 DLLAKARRIYIFGVGSSGLVAEYLAYKLLRLGKPVVLLSDPHLQLMSAANLTPGDVVIAISFSGETKETVEAAEIAKERG 87
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1052836952 367 ARVLSIVNVVGSAIAKASDDVIYTWAGPEIA-VATTKAYSTQLTVIYLIAA 416
Cdd:cd05013 88 AKVIAITDSANSPLAKLADIVLLVSSEEGDFrSSAFSSRIAQLALIDALFL 138
|
|
| GATase_7 |
pfam13537 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
89-198 |
8.49e-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: 8.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 89 HLSQSGRFAVVHNGIIENYISLKKKLESKGFEFISETDTEVIAHLFEYYYKgdimdtmIKVINRVEGSYALGVLcvdypD 168
Cdd:pfam13537 17 VSSEDGRYVIVFNGEIYNYRELRAELEAKGYRFRTHSDTEVILHLYEAEWG-------EDCVDRLNGMFAFAIW-----D 84
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1052836952 169 ----QFIAVR-----KasPMIVGLGDEENFI-ASDVTAIL 198
Cdd:pfam13537 85 rrrqRLFLARdrfgiK--PLYYGRDDGGRLLfASELKALL 122
|
|
| PTZ00077 |
PTZ00077 |
asparagine synthetase-like protein; Provisional |
1-217 |
2.72e-12 |
|
asparagine synthetase-like protein; Provisional
Pssm-ID: 185431 [Multi-domain] Cd Length: 586 Bit Score: 69.36 E-value: 2.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 1 MCGIVGYIG----KNQAAPILLEGLSKLEYRGYDSAGIAVYNNnelevakSKGKLAVLSekidggkklsgnmgigHTRWA 76
Cdd:PTZ00077 1 MCGILAIFNskgeRHELRRKALELSKRLRHRGPDWSGIIVLEN-------SPGTYNILA----------------HERLA 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 77 THGePSDvNAHPHLSQSGRFAVVHNGIIENYISLKKKLESKGFEFISETDTEVIAHLFEYYYKGDImdtmikvINRVEGS 156
Cdd:PTZ00077 58 IVD-LSD-GKQPLLDDDETVALMQNGEIYNHWEIRPELEKEGYKFSSNSDCEIIGHLYKEYGPKDF-------WNHLDGM 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1052836952 157 YAlGVLCVDYPDQFIAVRK---ASPMIVGLG-DEENFIASDVTAILKHTRDI-------YYLEDNEIVVLKK 217
Cdd:PTZ00077 129 FA-TVIYDMKTNTFFAARDhigIIPLYIGYAkDGSIWFSSELKALHDQCVEVkqfppghYYDQTKEKGEFVR 199
|
|
| frlB |
PRK11382 |
fructoselysine 6-phosphate deglycase; |
283-599 |
3.08e-12 |
|
fructoselysine 6-phosphate deglycase;
Pssm-ID: 183111 [Multi-domain] Cd Length: 340 Bit Score: 68.10 E-value: 3.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 283 SLTEEDIK-NINKIYIVACGSAYHVGVVGKYVIEKMCRIpvEVQVASEFRYCDPIVGKDD---LVIVISQSGETADTKAA 358
Cdd:PRK11382 34 AIVEEMVKrDIDRIYFVACGSPLNAAQTAKHLADRFSDL--QVYAISGWEFCDNTPYRLDdrcAVIGVSDYGKTEEVIKA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 359 LEEAKARGARVLSIVNVVGSAIAKASDDVIYTWAGPEIAVATTKAYSTQLTVIYLIAAYMadKLGKISKEeyadfikeIE 438
Cdd:PRK11382 112 LELGRACGALTAAFTKRADSPITSAAEFSIDYQADCIWEIHLLLCYSVVLEMITRLAPNA--EIGKIKND--------LK 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 439 SLPDKVAEILKSKEDV-QYLASKFYNCHSIFFIG----RNLDYAvslEGSLKLKEISYIHSEAYAAGELKHGTISLIEDG 513
Cdd:PRK11382 182 QLPNALGHLVRTWEEKgRQLGELASQWPMIYTVAagplRPLGYK---EGIVTLMEFTWTHGCVIESGEFRHGPLEIVEPG 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 514 TLVVALATGKNLFDKTVSNVKEVKARGAVVMgvtteehehmddVADYTVKIPATHEMLLPSLTVIPLQLFGYYVASLKGC 593
Cdd:PRK11382 259 VPFLFLLGNDESRHTTERAINFVKQRTDNVI------------VIDYAEISQGLHPWLAPFLMFVPMEWLCYYLSIYKDH 326
|
....*.
gi 1052836952 594 DIDKPR 599
Cdd:PRK11382 327 NPDERR 332
|
|
| asnB |
PRK09431 |
asparagine synthetase B; Provisional |
1-213 |
5.34e-12 |
|
asparagine synthetase B; Provisional
Pssm-ID: 236513 [Multi-domain] Cd Length: 554 Bit Score: 68.40 E-value: 5.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 1 MCGIVGYIGKNQAAPIL----LEGLSKLEYRGYDSAGIAVynnnelevakskgklavlsekidggkklSGNMGIGHTRWA 76
Cdd:PRK09431 1 MCGIFGILDIKTDADELrkkaLEMSRLMRHRGPDWSGIYA----------------------------SDNAILGHERLS 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 77 ThgepSDVN--AHPHLSQSGRFAVVHNGIIENYISLKKKLESKgFEFISETDTEVIAHLfeYYYKGdimdtmIKVINRVE 154
Cdd:PRK09431 53 I----VDVNggAQPLYNEDGTHVLAVNGEIYNHQELRAELGDK-YAFQTGSDCEVILAL--YQEKG------PDFLDDLD 119
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1052836952 155 GSYALgVLCVDYPDQFIAVRK---ASPMIVGLGDEENF-IASDVTAILKHTRDI--------YYLEDNEIV 213
Cdd:PRK09431 120 GMFAF-ALYDSEKDAYLIARDpigIIPLYYGYDEHGNLyFASEMKALVPVCKTIkefppghyYWSKDGEFV 189
|
|
| YafJ |
cd01908 |
Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine ... |
1-179 |
1.46e-11 |
|
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: 65.10 E-value: 1.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 1 MCGIVGYIGknqaAPILLEGL-------------SKLEYRGY---DSAGIAVYNNNELEVAKSKGKLAVLS---EKIDGG 61
Cdd:cd01908 1 MCRLLGYSG----APIPLEPLlirpshsllvqsgGPREMKGTvhaDGWGIGWYEGKGGRPFRYRSPLPAWSdinLESLAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 62 KKLSGNMgIGHTRWATHGEPSDVNAHPHlsQSGRFAVVHNGIIENYISLKKKLESKGFEFI-SETDTEVIAHLF------ 134
Cdd:cd01908 77 PIKSPLV-LAHVRAATVGPVSLENCHPF--TRGRWLFAHNGQLDGFRLLRRRLLRLLPRLPvGTTDSELAFALLlsrlle 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1052836952 135 -EYYYKGDIMDTMIKVINRVEGSYALGVLCVDYPD--QFIAVRKASPM 179
Cdd:cd01908 154 rDPLDPAELLDAILQTLRELAALAPPGRLNLLLSDgeYLIATRYASAP 201
|
|
| asn_synth_AEB |
TIGR01536 |
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing ... |
3-200 |
1.30e-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: 63.89 E-value: 1.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 3 GIVGYIGK-NQAAPILLEGLSKLEYRGYDSAGIavynnnelevakskgklavlsekIDGGkklsGNMGIGHTRWAThgep 81
Cdd:TIGR01536 3 GFFDLDDKaVEEDEAIKRMSDTIAHRGPDASGI-----------------------EYKD----GNAILGHRRLAI---- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 82 SDVN--AHPHLSQSGRFAVVHNGIIENYISLKKKLESKGFEFISETDTEVIAHLFEYYYKgdimdtmiKVINRVEGSYAL 159
Cdd:TIGR01536 52 IDLSggAQPMSNEGKTYVIVFNGEIYNHEELREELEAKGYTFQTDSDTEVILHLYEEWGE--------ECVDRLDGMFAF 123
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1052836952 160 GVLCVDYPDQFIA-----VRkasPMIVGLGDEENFIASDVTAILKH 200
Cdd:TIGR01536 124 ALWDSEKGELFLArdrfgIK---PLYYAYDGGQLYFASEIKALLAH 166
|
|
| SIS |
cd04795 |
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
295-373 |
5.60e-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: 56.23 E-value: 5.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 295 IYIVACGSAYHVGVVGKYVIEKMCRIPVEVQVASEFRYCDPIV--GKDDLVIVISQSGETADTKAALEEAKARGARVLSI 372
Cdd:cd04795 1 IFVIGIGGSGAIAAYFALELLELTGIEVVALIATELEHASLLSllRKGDVVIALSYSGRTEELLAALEIAKELGIPVIAI 80
|
.
gi 1052836952 373 V 373
Cdd:cd04795 81 T 81
|
|
| SIS_Etherase |
cd05007 |
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ... |
337-425 |
1.13e-09 |
|
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: 59.46 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 337 VGKDDLVIVISQSGETADTKAALEEAKARGARVLSIVNVVGSAIAKASDDVIYTWAGPEIAVATT--KAYSTQLTVIYLI 414
Cdd:cd05007 116 LTERDVVIGIAASGRTPYVLGALRYARARGALTIGIACNPGSPLLQLADIAIALITGPEVVAGSTrlKAGTAQKLALNML 195
|
90
....*....|.
gi 1052836952 415 AAYMADKLGKI 425
Cdd:cd05007 196 STAVMIRLGKV 206
|
|
| PRK11337 |
PRK11337 |
MurR/RpiR family transcriptional regulator; |
301-388 |
2.19e-09 |
|
MurR/RpiR family transcriptional regulator;
Pssm-ID: 183089 [Multi-domain] Cd Length: 292 Bit Score: 59.00 E-value: 2.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 301 GSAyhvgVVGKYVIEKMCRIPVEVQVasefrYCDP--------IVGKDDLVIVISQSGETADTKAALEEAKARGARVLSI 372
Cdd:PRK11337 150 GSA----AIARDVQHKFLRIGVRCQA-----YDDAhimlmsaaLLQEGDVVLVVSHSGRTSDVIEAVELAKKNGAKIICI 220
|
90
....*....|....*.
gi 1052836952 373 VNVVGSAIAKASDDVI 388
Cdd:PRK11337 221 TNSYHSPIAKLADYVI 236
|
|
| SIS_PHI |
cd05005 |
Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) ... |
335-428 |
1.17e-08 |
|
Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) superfamily. In the ribulose monophosphate pathway of formaldehyde fixation, hexulose-6-phosphate synthase catalyzes the condensation of ribulose-5-phosphate with formadelhyde to become hexulose-6-phosphate, which is then isomerized to fructose-6-phosphate by PHI.
Pssm-ID: 240138 [Multi-domain] Cd Length: 179 Bit Score: 54.89 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 335 PIVGKDDLVIVISQSGETADTKAALEEAKARGARVLSIVNVVGSAIAKASDDVIY----TWAGPEIAVATTKAYST---Q 407
Cdd:cd05005 71 PAIGPGDLLIAISGSGETSSVVNAAEKAKKAGAKVVLITSNPDSPLAKLADVVVVipaaTKDDHGGEHKSIQPLGTlfeQ 150
|
90 100
....*....|....*....|...
gi 1052836952 408 LTVIYL--IAAYMADKLGKISKE 428
Cdd:cd05005 151 SALVFLdaVIAKLMEELGVSEEE 173
|
|
| PLN02549 |
PLN02549 |
asparagine synthase (glutamine-hydrolyzing) |
1-197 |
1.24e-08 |
|
asparagine synthase (glutamine-hydrolyzing)
Pssm-ID: 178164 [Multi-domain] Cd Length: 578 Bit Score: 57.85 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 1 MCGI---VGYIGKNQAAPILLEGLSK-LEYRGYDSAGIAVYNNNelevakskgklavlsekidggkklsgnmGIGHTRWA 76
Cdd:PLN02549 1 MCGIlavLGCSDDSQAKRSRVLELSRrLRHRGPDWSGLYGNEDC----------------------------YLAHERLA 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 77 THGEPSdvNAHPHLSQSGRFAVVHNGIIENYISLKKKLESKGFEfiSETDTEVIAHLFEYYykGDimdtmiKVINRVEGS 156
Cdd:PLN02549 53 IMDPES--GDQPLYNEDKTIVVTANGEIYNHKELREKLKLHKFR--TGSDCEVIAHLYEEH--GE------EFVDMLDGM 120
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1052836952 157 YALgVLCVDYPDQFIAVRKA---SPMIVGLG-DEENFIASDVTAI 197
Cdd:PLN02549 121 FSF-VLLDTRDNSFIAARDHigiTPLYIGWGlDGSVWFASEMKAL 164
|
|
| murQ |
PRK05441 |
N-acetylmuramic acid-6-phosphate etherase; Reviewed |
337-396 |
1.55e-08 |
|
N-acetylmuramic acid-6-phosphate etherase; Reviewed
Pssm-ID: 235467 [Multi-domain] Cd Length: 299 Bit Score: 56.33 E-value: 1.55e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 337 VGKDDLVIVISQSGETADTKAALEEAKARGARVLSIVNVVGSAIAKASDDVIYTWAGPEI 396
Cdd:PRK05441 129 LTAKDVVVGIAASGRTPYVIGALEYARERGALTIGISCNPGSPLSKEADIAIEVVVGPEV 188
|
|
| SIS_Kpsf |
cd05014 |
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ... |
336-388 |
6.40e-08 |
|
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ISomerase) domains. SIS domains are found in many phosphosugar isomerases and phosphosugar binding proteins. KpsF catalyzes the reversible reaction of ribulose 5-phosphate to arabinose 5-phosphate. This is the second step in the CMP-Kdo biosynthesis pathway.
Pssm-ID: 240145 [Multi-domain] Cd Length: 128 Bit Score: 51.39 E-value: 6.40e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1052836952 336 IVGKDDLVIVISQSGETADTKAALEEAKARGARVLSIVNVVGSAIAKASDDVI 388
Cdd:cd05014 44 MVTPGDVVIAISNSGETDELLNLLPHLKRRGAPIIAITGNPNSTLAKLSDVVL 96
|
|
| YafJ |
COG0121 |
Predicted glutamine amidotransferase YafJ [General function prediction only]; |
2-134 |
1.03e-07 |
|
Predicted glutamine amidotransferase YafJ [General function prediction only];
Pssm-ID: 439891 [Multi-domain] Cd Length: 248 Bit Score: 53.43 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 2 CGIVGYIGKN--QAAPILLEGLSKLEYRGYDSA--------GIAVYN-NNELEVAKSKGK------LAVLSEKIDggkkl 64
Cdd:COG0121 1 CRLLGYSGNVptDLEFLLLDPEHSLVRQSGATRegphadgwGIGWYEgDGEPRLYRDPLPawsdpnLRLLARPIK----- 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1052836952 65 SGNMgIGHTRWATHGEPSDVNAHPHlsQSGRFAVVHNGIIENYISLKKKLESK-----GFEFISETDTEVIAHLF 134
Cdd:COG0121 76 SRLV-IAHVRKATVGPVSLENTHPF--RGGRWLFAHNGQLDGFDRLRRRLAEElpdelYFQPVGTTDSELAFALL 147
|
|
| GutQ |
COG0794 |
D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall ... |
336-395 |
3.76e-06 |
|
D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440557 [Multi-domain] Cd Length: 317 Bit Score: 49.20 E-value: 3.76e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 336 IVGKDDLVIVISQSGETADTKAALEEAKARGARVLSIVNVVGSAIAKASDDVIYTWAGPE 395
Cdd:COG0794 88 MITPGDVVIAISNSGETEELLALLPLLKRLGVPLIAITGNPDSTLARAADVVLDLPVERE 147
|
|
| SIS_GlmS_GlmD_2 |
cd05009 |
SIS (Sugar ISomerase) domain repeat 2 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
280-423 |
5.65e-06 |
|
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: 46.49 E-value: 5.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 280 DDISLTEEDIKNINKIYIVacGSAYHVGVVG----KyvIEKMCRIPVEVQVASEFRYcDPI--VGKDDLVIVISQSGETA 353
Cdd:cd05009 1 EDIKELAEKLKEAKSFYVL--GRGPNYGTALegalK--LKETSYIHAEAYSAGEFKH-GPIalVDEGTPVIFLAPEDRLE 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1052836952 354 D-TKAALEEAKARGARVLSIvnvvgsaiakASDDVIYTWAGPEIAVATTKAYSTQLTVI---YLIAAYMADKLG 423
Cdd:cd05009 76 EkLESLIKEVKARGAKVIVI----------TDDGDAKDLADVVIRVPATVEELSPLLYIvplQLLAYHLAVARG 139
|
|
| PRK08674 |
PRK08674 |
bifunctional phosphoglucose/phosphomannose isomerase; Validated |
253-372 |
1.14e-05 |
|
bifunctional phosphoglucose/phosphomannose isomerase; Validated
Pssm-ID: 181536 [Multi-domain] Cd Length: 337 Bit Score: 47.67 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 253 MMKEIEEQPKAIRDTISPRIKDGKivlddisltEEDIKNINKIYIVACGSAyhvGVVGKyVIEKMCR--IPVEVQVASEF 330
Cdd:PRK08674 4 MLEEYLNWPEQFEEALEIAISLDL---------EEDLEKIDNIVISGMGGS---GIGGD-LLRILLFdeLKVPVFVNRDY 70
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1052836952 331 RYcDPIVGKDDLVIVISQSGETADTKAALEEAKARGARVLSI 372
Cdd:PRK08674 71 TL-PAFVDEKTLVIAVSYSGNTEETLSAVEQALKRGAKIIAI 111
|
|
| PRK12570 |
PRK12570 |
N-acetylmuramic acid-6-phosphate etherase; Reviewed |
339-455 |
1.76e-04 |
|
N-acetylmuramic acid-6-phosphate etherase; Reviewed
Pssm-ID: 237142 [Multi-domain] Cd Length: 296 Bit Score: 43.91 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 339 KDDLVIVISQSGETADTKAALEEAKARGARVLSIVNVVGSAIAKASDDVIYTWAGPEIAVATT--KAYSTQLTVI-YLIA 415
Cdd:PRK12570 127 ADDVVVGIAASGRTPYVIGALEYAKQIGATTIALSCNPDSPIAKIADIAISPVVGPEVLTGSTrlKSGTAQKMVLnMLST 206
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1052836952 416 AYMAdKLGKISKEEYADFIKEIESLPDKVAEILKSKEDVQ 455
Cdd:PRK12570 207 ASMI-RLGKSYQNLMVDVKATNEKLVARAVRIVMQATGCS 245
|
|
| SIS_PGI_PMI_1 |
cd05017 |
The members of this protein family contain the SIS (Sugar ISomerase) domain and have both the ... |
335-372 |
6.08e-04 |
|
The members of this protein family contain the SIS (Sugar ISomerase) domain and have both the phosphoglucose isomerase (PGI) and the phosphomannose isomerase (PMI) functions. These functions catalyze the reversible reactions of glucose 6-phosphate to fructose 6-phosphate, and mannose 6-phosphate to fructose 6-phosphate, respectively at an equal rate. This protein contains two SIS domains. This alignment is based on the first SIS domain.
Pssm-ID: 240148 [Multi-domain] Cd Length: 119 Bit Score: 39.94 E-value: 6.08e-04
10 20 30
....*....|....*....|....*....|....*...
gi 1052836952 335 PIVGKDDLVIVISQSGETADTKAALEEAKARGARVLSI 372
Cdd:cd05017 39 AFVDRKTLVIAVSYSGNTEETLSAVEQAKERGAKIVAI 76
|
|
| GATase_4 |
pfam13230 |
Glutamine amidotransferases class-II; This family captures members that are not found in ... |
70-207 |
1.79e-03 |
|
Glutamine amidotransferases class-II; This family captures members that are not found in pfam00310.
Pssm-ID: 433047 [Multi-domain] Cd Length: 272 Bit Score: 40.39 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 70 IGHTRWATHGEPSDVNAHPHL-SQSGR---FAvvHNGIIENYislKKKLeSKGFEFISETDTEviaHLFEYyykgdIMDT 145
Cdd:pfam13230 75 IAHIRKATQGRVTLENTHPFMrELWGRywiFA--HNGDLKGY---APKL-SGRFQPVGSTDSE---LAFCW-----LLDR 140
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1052836952 146 MikvinRVEGSYALgvlcVDYPDQFIAVRKASPMIVGLGdEENFIASDVTAILKHT-RDIYYL 207
Cdd:pfam13230 141 L-----ASRFPYAR----PSAGELFRALRELAREIAAHG-TFNFLLSDGRDLFAHCsTRLHYI 193
|
|
| SIS_GmhA |
cd05006 |
Phosphoheptose isomerase is a member of the SIS (Sugar ISomerase) superfamily. Phosphoheptose ... |
339-389 |
5.51e-03 |
|
Phosphoheptose isomerase is a member of the SIS (Sugar ISomerase) superfamily. Phosphoheptose isomerase catalyzes the isomerization of sedoheptulose 7-phosphate into D-glycero-D-mannoheptose 7-phosphate. This is the first step of the biosynthesis of gram-negative bacteria inner core lipopolysaccharide precursor, L-glycero-D-mannoheptose (Gmh).
Pssm-ID: 240139 [Multi-domain] Cd Length: 177 Bit Score: 38.26 E-value: 5.51e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1052836952 339 KDDLVIVISQSGETADTKAALEEAKARGARVLSIVNVVGSAIAKASDDVIY 389
Cdd:cd05006 101 PGDVLIGISTSGNSPNVLKALEAAKERGMKTIALTGRDGGKLLELADIEIH 151
|
|
| PRK11557 |
PRK11557 |
MurR/RpiR family transcriptional regulator; |
338-419 |
9.49e-03 |
|
MurR/RpiR family transcriptional regulator;
Pssm-ID: 183195 [Multi-domain] Cd Length: 278 Bit Score: 38.21 E-value: 9.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052836952 338 GKDDLVIVISQSGETADTKAALEEAKARGARVLSIVNVVGSAIAKASDDVIYTWA-GPEIAVATTKAYSTQLTVIYLIaa 416
Cdd:PRK11557 174 SPDDLLLAISYSGERRELNLAADEALRVGAKVLAITGFTPNALQQRASHCLYTIAeEQATRSAAISSTHAQGMLTDLL-- 251
|
...
gi 1052836952 417 YMA 419
Cdd:PRK11557 252 FMA 254
|
|
| |
