|
Name |
Accession |
Description |
Interval |
E-value |
| GlmS |
COG0449 |
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ... |
1-611 |
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: 1027.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 1 MCGIVGAIAERNITPILIEGLKRLEYRGYDSAGVAVFDNeGRLQRCRRVGKVASLEEGLAGTPLLGRLGIAHTRWATHGA 80
Cdd:COG0449 1 MCGIVGYIGKRDAAPILLEGLKRLEYRGYDSAGIAVLDD-GGLEVRKAVGKLANLEEKLAEEPLSGTIGIGHTRWATHGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 81 PTEGNAHPHFS-SDEVAVVHNGIIENHEPLRERLKGLGYVFTSQTDTEVIVHLLHHKLQSIGDLTLALKDAVKELHGAYG 159
Cdd:COG0449 80 PSDENAHPHTScSGRIAVVHNGIIENYAELREELEAKGHTFKSETDTEVIAHLIEEYLKGGGDLLEAVRKALKRLEGAYA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 160 LAVISAAQPDRIVAARSGSPLVIGLGLGENFLASDQLALRQVTDRFIYLEEGDIAEIRRDSVRLWDVQGNDVQRETVQYH 239
Cdd:COG0449 160 LAVISADEPDRIVAARKGSPLVIGLGEGENFLASDVPALLPYTRRVIYLEDGEIAVLTRDGVEIYDLDGEPVEREVKTVD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 240 EGAEAADKGEYRHFMLKEIHEQPSVVQRTLEGRLGQNQVLVESFGPQAAELFAKVRNVQIVACGTSYHAGMVARYWLESL 319
Cdd:COG0449 240 WDAEAAEKGGYPHFMLKEIHEQPEAIRDTLRGRLDEDGRVVLDELNLAAEDLRNIDRIYIVACGTSYHAGLVGKYLIEEL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 320 TGIPCQVEVASEFRYRKVAVQPDCLFVTISQSGETADTLAALRNAKELGfLSSVAICNVATSSLVRESDLTLLTQAGPEI 399
Cdd:COG0449 320 ARIPVEVEIASEFRYRDPVVDPGTLVIAISQSGETADTLAALREAKEKG-AKVLAICNVVGSTIARESDAVLYTHAGPEI 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 400 GVASTKAFTTQLVALLLLTLGIGQVQKRLADGVEAELVDELRRLPTRLGEALAMNRTVEKVSELFAEKHHTLFLGRGAQF 479
Cdd:COG0449 399 GVASTKAFTTQLAALYLLALYLARARGTLSAEEEAELLEELRKLPEKIEEVLDLEEQIEELAEKYADARNALFLGRGINY 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 480 PVALEGALKLKEISYIHAEAYPAGELKHGPLALVDSDMPVVTVAPNNELVEKLKSNLQEVRARGGELVVFADEGAGIEAG 559
Cdd:COG0449 479 PVALEGALKLKEISYIHAEGYAAGELKHGPIALIDEGMPVVAIAPQDELYEKTLSNIQEVKARGGKVIAIADEGDEEVEE 558
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 15600742 560 EGTHVVGMPHIGDVLSPILYTIPLQLLSYHVAVLKGTDVDQPRNLAKSVTVE 611
Cdd:COG0449 559 LADDVIEVPEVDELLAPILAVVPLQLLAYHVAVLRGTDVDQPRNLAKSVTVE 610
|
|
| PRK00331 |
PRK00331 |
isomerizing glutamine--fructose-6-phosphate transaminase; |
1-611 |
0e+00 |
|
isomerizing glutamine--fructose-6-phosphate transaminase;
Pssm-ID: 234729 [Multi-domain] Cd Length: 604 Bit Score: 1014.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 1 MCGIVGAIAERNITPILIEGLKRLEYRGYDSAGVAVFDNeGRLQRCRRVGKVASLEEGLAGTPLLGRLGIAHTRWATHGA 80
Cdd:PRK00331 1 MCGIVGYVGQRNAAEILLEGLKRLEYRGYDSAGIAVLDD-GGLEVRKAVGKVANLEAKLEEEPLPGTTGIGHTRWATHGK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 81 PTEGNAHPHFSSDE-VAVVHNGIIENHEPLRERLKGLGYVFTSQTDTEVIVHLLHHKLQSIGDLTLALKDAVKELHGAYG 159
Cdd:PRK00331 80 PTERNAHPHTDCSGrIAVVHNGIIENYAELKEELLAKGHVFKSETDTEVIAHLIEEELKEGGDLLEAVRKALKRLEGAYA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 160 LAVISAAQPDRIVAARSGSPLVIGLGLGENFLASDQLALRQVTDRFIYLEEGDIAEIRRDSVRLWDVQGNDVQRETVQYH 239
Cdd:PRK00331 160 LAVIDKDEPDTIVAARNGSPLVIGLGEGENFLASDALALLPYTRRVIYLEDGEIAVLTRDGVEIFDFDGNPVEREVYTVD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 240 EGAEAADKGEYRHFMLKEIHEQPSVVQRTLEGRLGQNqvlveSFGPQAAELFAKVRNVQIVACGTSYHAGMVARYWLESL 319
Cdd:PRK00331 240 WDASAAEKGGYRHFMLKEIYEQPEAIRDTLEGRLDEL-----GEGELADEDLKKIDRIYIVACGTSYHAGLVAKYLIESL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 320 TGIPCQVEVASEFRYRKVAVQPDCLFVTISQSGETADTLAALRNAKELGfLSSVAICNVATSSLVRESDLTLLTQAGPEI 399
Cdd:PRK00331 315 AGIPVEVEIASEFRYRDPVLSPKTLVIAISQSGETADTLAALRLAKELG-AKTLAICNVPGSTIARESDAVLYTHAGPEI 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 400 GVASTKAFTTQLVALLLLTLGIGQVQKRLADGVEAELVDELRRLPTRLGEALAMNRTVEKVSELFAEKHHTLFLGRGAQF 479
Cdd:PRK00331 394 GVASTKAFTAQLAVLYLLALALAKARGTLSAEEEADLVHELRELPALIEQVLDLKEQIEELAEDFADARNALFLGRGVDY 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 480 PVALEGALKLKEISYIHAEAYPAGELKHGPLALVDSDMPVVTVAPNNELVEKLKSNLQEVRARGGELVVFADEGaGIEAG 559
Cdd:PRK00331 474 PVALEGALKLKEISYIHAEGYAAGELKHGPIALIDEGMPVVAIAPNDELYEKTKSNIQEVKARGARVIVIADEG-DEVAE 552
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 15600742 560 EGTHVVGMPHIGDVLSPILYTIPLQLLSYHVAVLKGTDVDQPRNLAKSVTVE 611
Cdd:PRK00331 553 EADDVIEVPEVHELLAPLLYVVPLQLLAYHVALARGTDVDKPRNLAKSVTVE 604
|
|
| glmS |
TIGR01135 |
glucosamine--fructose-6-phosphate aminotransferase (isomerizing); The member from ... |
2-611 |
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: 890.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 2 CGIVGAIAERNITPILIEGLKRLEYRGYDSAGVAVFDnEGRLQRCRRVGKVASLEEGLAGTPLLGRLGIAHTRWATHGAP 81
Cdd:TIGR01135 1 CGIVGYIGQRDAVPILLEGLKRLEYRGYDSAGIAVVD-EGKLFVRKAVGKVAELANKLGEKPLPGGVGIGHTRWATHGKP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 82 TEGNAHPHFSSD-EVAVVHNGIIENHEPLRERLKGLGYVFTSQTDTEVIVHLLHHKLQSIGDLTLALKDAVKELHGAYGL 160
Cdd:TIGR01135 80 TDENAHPHTDEGgRIAVVHNGIIENYAELREELEARGHVFSSDTDTEVIAHLIEEELREGGDLLEAVQKALKQLRGAYAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 161 AVISAAQPDRIVAARSGSPLVIGLGLGENFLASDQLALRQVTDRFIYLEEGDIAEIRRDSVRLWDVQGNDVQRETVQYHE 240
Cdd:TIGR01135 160 AVLHADHPETLVAARSGSPLIVGLGDGENFVASDVTALLPYTRRVIYLEDGDIAILTKDGVEIYNFEGAPVQREVRVIDW 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 241 GAEAADKGEYRHFMLKEIHEQPSVVQRTLEGRLGQNQVLVESFGpqAAELFAKVRNVQIVACGTSYHAGMVARYWLESLT 320
Cdd:TIGR01135 240 DLDAAEKGGYRHFMLKEIYEQPRALRDTLEGRIEENGGVFEELG--AEELLKNIDRIQIVACGTSYHAGLVAKYLIERLA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 321 GIPCQVEVASEFRYRKVAVQPDCLFVTISQSGETADTLAALRNAKELGfLSSVAICNVATSSLVRESDLTLLTQAGPEIG 400
Cdd:TIGR01135 318 GIPVEVEIASEFRYRKPVVDKDTLVIAISQSGETADTLEALRLAKELG-AKTLGICNVPGSTLVREADHTLYTRAGPEIG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 401 VASTKAFTTQLVALLLLTLGIGQVQKRLADGVEAELVDELRRLPTRLGEALAMNRTVEKVSELFAEKHHTLFLGRGAQFP 480
Cdd:TIGR01135 397 VASTKAFTTQLTVLYLLALALAKARGTLSAEEEAELVDALRRLPDLVEQVLLADESIAELAERYADKRNFLFLGRGLGYP 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 481 VALEGALKLKEISYIHAEAYPAGELKHGPLALVDSDMPVVTVAPNNELVEKLKSNLQEVRARGGELVVFADEGAGIEAGE 560
Cdd:TIGR01135 477 IALEGALKLKEISYIHAEGYPAGELKHGPIALIDEGLPVVAIAPKDSLLEKTKSNVEEVKARGARVIVFAPEDDETIASV 556
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 15600742 561 GTHVVGMPHIGDVLSPILYTIPLQLLSYHVAVLKGTDVDQPRNLAKSVTVE 611
Cdd:TIGR01135 557 ADDVIKLPEVEELLAPIVYTIPLQLLAYHIALAKGTDVDKPRNLAKSVTVE 607
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
1-610 |
3.20e-162 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 478.36 E-value: 3.20e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 1 MCGIVGAIAERNITPILIEGLKRLEYRGYDSAGVAVFDNEGRLqrcrRVGKVAS----------LEEGLAGTPLLGRLGI 70
Cdd:PTZ00295 24 CCGIVGYLGNEDASKILLEGIEILQNRGYDSCGISTISSGGEL----KTTKYASdgttsdsieiLKEKLLDSHKNSTIGI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 71 AHTRWATHGAPTEGNAHPHFSSDE-VAVVHNGIIENHEPLRERLKGLGYVFTSQTDTEVIVHLLHHKLQSIGDLTLALKD 149
Cdd:PTZ00295 100 AHTRWATHGGKTDENAHPHCDYKKrIALVHNGTIENYVELKSELIAKGIKFRSETDSEVIANLIGLELDQGEDFQEAVKS 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 150 AVKELHGAYGLAVISAAQPDRIVAARSGSPLVIGLGLGENFLASDQLALRQVTDRFIYLEEGDIAEIRRDSVRLWDVQGN 229
Cdd:PTZ00295 180 AISRLQGTWGLCIIHKDNPDSLIVARNGSPLLVGIGDDSIYVASEPSAFAKYTNEYISLKDGEIAELSLENVNDLYTQRR 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 230 dVQRETVQYHEgaeaADKGEYRHFMLKEIHEQPSVVQRTLE--GRLGQNQVLVESFG-PQAAELFAKVRNVQIVACGTSY 306
Cdd:PTZ00295 260 -VEKIPEEVIE----KSPEPYPHWTLKEIFEQPIALSRALNngGRLSGYNNRVKLGGlDQYLEELLNIKNLILVGCGTSY 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 307 HAGMVARYWLESLTGI-PCQVEVASEF---RYRKvavqPDCLFVTISQSGETADTLAALRNAKELGFLsSVAICNVATSS 382
Cdd:PTZ00295 335 YAALFAASIMQKLKCFnTVQVIDASELtlyRLPD----EDAGVIFISQSGETLDVVRALNLADELNLP-KISVVNTVGSL 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 383 LVRESDLTLLTQAGPEIGVASTKAFTTQLVALLLLTLGIGQVQKRLA--DGVEaELVDELRRLPTRLGEALAMNR-TVEK 459
Cdd:PTZ00295 410 IARSTDCGVYLNAGREVAVASTKAFTSQVTVLSLIALWFAQNKEYSCsnYKCS-SLINSLHRLPTYIGMTLKSCEeQCKR 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 460 VSELFAEKHHTLFLGRGAQFPVALEGALKLKEISYIHAEAYPAGELKHGPLALVD--SDMPVVTVAPNNELVEKLKSNLQ 537
Cdd:PTZ00295 489 IAEKLKNAKSMFILGKGLGYPIALEGALKIKEITYIHAEGFSGGALKHGPFALIDkeKNTPVILIILDDEHKELMINAAE 568
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600742 538 EVRARGGELVVFADEGAgiEAGEGT-HVVGMPHIGdVLSPILYTIPLQLLSYHVAVLKGTDVDQPRNLAKSVTV 610
Cdd:PTZ00295 569 QVKARGAYIIVITDDED--LVKDFAdEIILIPSNG-PLTALLAVIPLQLLAYEIAILRGINPDKPRGLAKTVTV 639
|
|
| PLN02981 |
PLN02981 |
glucosamine:fructose-6-phosphate aminotransferase |
1-611 |
7.33e-159 |
|
glucosamine:fructose-6-phosphate aminotransferase
Pssm-ID: 215531 [Multi-domain] Cd Length: 680 Bit Score: 471.16 E-value: 7.33e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 1 MCGIVGAI------AERNITPILIEGLKRLEYRGYDSAGVAvFDNEGRLQRC-----RRVGKVASLE----EGLAGTPLL 65
Cdd:PLN02981 1 MCGIFAYLnynvprERRFILEVLFNGLRRLEYRGYDSAGIA-IDNDPSLESSsplvfREEGKIESLVrsvyEEVAETDLN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 66 GRL------GIAHTRWATHGAPTEGNAHPHFS--SDEVAVVHNGIIENHEPLRERLKGLGYVFTSQTDTEVIVHL---LH 134
Cdd:PLN02981 80 LDLvfenhaGIAHTRWATHGPPAPRNSHPQSSgpGNEFLVVHNGIITNYEVLKETLLRHGFTFESDTDTEVIPKLakfVF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 135 HKL-QSIGDLTLA--LKDAVKELHGAYGLAVISAAQPDRIVAARSGSPLVIG---LGLGEN------------------- 189
Cdd:PLN02981 160 DKLnEEEGDVTFSqvVMEVMRQLEGAYALIFKSPHYPNELVACKRGSPLLLGvkeLPEEKNssavftsegfltknrdkpk 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 190 --FLASDQLALRQVTDRFIYLEEGDIAEIRRDSVRLW------------DVQGNDVQR--ETVQYHegAEAADKGEYRHF 253
Cdd:PLN02981 240 efFLASDASAVVEHTKRVLVIEDNEVVHLKDGGVGIYkfenekgrggggLSRPASVERalSTLEME--VEQIMKGNYDHY 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 254 MLKEIHEQPSVVQRTLEGRL---GQNQVLVESFGPQAAEL--FAKVRNVQIVACGTSYHAGMVARYWLESLTGIPCQVEV 328
Cdd:PLN02981 318 MQKEIHEQPESLTTTMRGRLirgGSGKAKRVLLGGLKDHLktIRRSRRIVFIGCGTSYNAALAARPILEELSGVPVTMEL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 329 ASEFRYRKVAVQPDCLFVTISQSGETADTLAALRNAKELGFLsSVAICNVATSSLVRESDLTLLTQAGPEIGVASTKAFT 408
Cdd:PLN02981 398 ASDLLDRQGPIYREDTAVFVSQSGETADTLRALEYAKENGAL-CVGITNTVGSAISRGTHCGVHINAGAEIGVASTKAYT 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 409 TQLVALLLLTLGIGQVQKRLADGVEAeLVDELRRLPTRLGEALAMNRTVEKVSELFAEKHHTLFLGRGAQFPVALEGALK 488
Cdd:PLN02981 477 SQIVAMTMLALALGEDSISSRSRREA-IIDGLFDLPNKVREVLKLDQEMKELAELLIDEQSLLVFGRGYNYATALEGALK 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 489 LKEISYIHAEAYPAGELKHGPLALVDSDMPVVTVAPNNELVEKLKSNLQEVRARGGELVVFADEG--AGIEAGEGTHVVG 566
Cdd:PLN02981 556 VKEVALMHSEGILAGEMKHGPLALVDETLPIIVIATRDACFSKQQSVIQQLRARKGRLIVICSKGdaSSVCPSGGCRVIE 635
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 15600742 567 MPHIGDVLSPILYTIPLQLLSYHVAVLKGTDVDQPRNLAKSVTVE 611
Cdd:PLN02981 636 VPQVEDCLQPVINIVPLQLLAYHLTVLRGHNVDQPRNLAKSVTTQ 680
|
|
| PTZ00394 |
PTZ00394 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
1-611 |
2.28e-144 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 173585 [Multi-domain] Cd Length: 670 Bit Score: 433.53 E-value: 2.28e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 1 MCGIVGAI------AERNITPILIEGLKRLEYRGYDSAGVAVFDNEGRLQRC--------------RRVGKVASLEE--- 57
Cdd:PTZ00394 1 MCGIFGYAnhnvprTVEQILNVLLDGIQKVEYRGYDSAGLAIDANIGSEKEDgtaasaptprpcvvRSVGNISQLREkvf 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 58 ----GLAGTPLLGRL----GIAHTRWATHGAPTEGNAHPHFSSD-EVAVVHNGIIENHEPLRERLKGLGYVFTSQTDTEV 128
Cdd:PTZ00394 81 seavAATLPPMDATTshhvGIAHTRWATHGGVCERNCHPQQSNNgEFTIVHNGIVTNYMTLKELLKEEGYHFSSDTDTEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 129 IVHLLHH-----KLQSIGDLTLALkdaVKELHGAYGLAVISAAQPDRIVAARSGSPLVIGL------------------- 184
Cdd:PTZ00394 161 ISVLSEYlytrkGIHNFADLALEV---SRMVEGSYALLVKSVYFPGQLAASRKGSPLMVGIrrtddrgcvmklqtydltd 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 185 --GLGENFLASDQLALRQVTDRFIYLEEGDIAEIRRDSVRLWDVQGND---VQRETVQYHEGAEAADKGEYRHFMLKEIH 259
Cdd:PTZ00394 238 lsGPLEVFFSSDVNSFAEYTREVVFLEDGDIAHYCDGALRFYNAAERQrsiVKREVQHLDAKPEGLSKGNYPHFMLKEIY 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 260 EQPSVVQRTLEGRLGQN--QVLVESFGPQAAELFAKVRNVQIVACGTSYHAGMVARYWLESLTGIPCQVEVASEFRYRKV 337
Cdd:PTZ00394 318 EQPESVISSMHGRIDFSsgTVQLSGFTQQSIRAILTSRRILFIACGTSLNSCLAVRPLFEELVPLPISVENASDFLDRRP 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 338 AVQPDCLFVTISQSGETADTLAALRNAKELGFLSsVAICNVATSSLVRESDLTLLTQAGPEIGVASTKAFTTQLVALLLL 417
Cdd:PTZ00394 398 RIQRDDVCFFVSQSGETADTLMALQLCKEAGAMC-VGITNVVGSSISRLTHYAIHLNAGVEVGVASTKAYTSQVVVLTLV 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 418 TLGIGQVQKRLADGvEAELVDELRRLPTRLGEALAM-NRTVEKVSELFAEKHHTLFLGRGAQFPVALEGALKLKEISYIH 496
Cdd:PTZ00394 477 ALLLSSDSVRLQER-RNEIIRGLAELPAAISECLKItHDPVKALAARLKESSSILVLGRGYDLATAMEAALKVKELSYVH 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 497 AEAYPAGELKHGPLALVDSDMPVVTVAPNNELVEKLKSNLQEVRARGGELVVFADEGAGIEAGEGTHVVGMPHIGDVLSP 576
Cdd:PTZ00394 556 TEGIHSGELKHGPLALIDETSPVLAMCTHDKHFGLSKSAVQQVKARGGAVVVFATEVDAELKAAASEIVLVPKTVDCLQC 635
|
650 660 670
....*....|....*....|....*....|....*
gi 15600742 577 ILYTIPLQLLSYHVAVLKGTDVDQPRNLAKSVTVE 611
Cdd:PTZ00394 636 VVNVIPFQLLAYYMALLRGNNVDCPRNLAKSVTVQ 670
|
|
| GFAT |
cd00714 |
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ... |
2-216 |
9.11e-125 |
|
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus of glucosamine-6P synthase (GlmS, or GFAT in humans). The glutaminase domain catalyzes amide nitrogen transfer from glutamine to the appropriate substrate. In this process, glutamine is hydrolyzed to glutamic acid and ammonia. In humans, GFAT catalyzes the first and rate-limiting step of hexosamine metabolism, the conversion of D-fructose-6P (Fru6P) into D-glucosamine-6P using L-glutamine as a nitrogen source. The end product of this pathway, UDP-N-acetyl glucosamine, is a major building block of the bacterial peptidoglycan and fungal chitin.
Pssm-ID: 238366 [Multi-domain] Cd Length: 215 Bit Score: 366.77 E-value: 9.11e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 2 CGIVGAIAERNITPILIEGLKRLEYRGYDSAGVAVfDNEGRLQRCRRVGKVASLEEGLAGTPLLGRLGIAHTRWATHGAP 81
Cdd:cd00714 1 CGIVGYIGKREAVDILLEGLKRLEYRGYDSAGIAV-IGDGSLEVVKAVGKVANLEEKLAEKPLSGHVGIGHTRWATHGEP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 82 TEGNAHPHFSSD-EVAVVHNGIIENHEPLRERLKGLGYVFTSQTDTEVIVHLLHHKLQSIGDLTLALKDAVKELHGAYGL 160
Cdd:cd00714 80 TDVNAHPHRSCDgEIAVVHNGIIENYAELKEELEAKGYKFESETDTEVIAHLIEYYYDGGLDLLEAVKKALKRLEGAYAL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15600742 161 AVISAAQPDRIVAARSGSPLVIGLGLGENFLASDQLALRQVTDRFIYLEEGDIAEI 216
Cdd:cd00714 160 AVISKDEPDEIVAARNGSPLVIGIGDGENFVASDAPALLEHTRRVIYLEDGDIAVI 215
|
|
| AgaS |
COG2222 |
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ... |
255-611 |
1.83e-75 |
|
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441824 [Multi-domain] Cd Length: 336 Bit Score: 244.04 E-value: 1.83e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 255 LKEIHEQPSVVQRTLEgrlgQNQVLVESFGPQAAElfAKVRNVQIVACGTSYHAGMVARYWLESLTGIPCQVEVASEF-- 332
Cdd:COG2222 1 AREIAQQPEAWRRALA----ALAAAIAALLARLRA--KPPRRVVLVGAGSSDHAAQAAAYLLERLLGIPVAALAPSELvv 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 333 RYRKVAVQPDcLFVTISQSGETADTLAALRNAKELGFLSsVAICNVATSSLVRESDLTLLTQAGPEIGVASTKAFTTQLV 412
Cdd:COG2222 75 YPAYLKLEGT-LVVAISRSGNSPEVVAALELAKARGART-LAITNNPDSPLAEAADRVLPLPAGPEKSVAATKSFTTMLL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 413 ALLLLTLGIGQvqkrladgvEAELVDELRRLPTRLGEALAMNRTVEKVSELFAEKHHTlFLGRGAQFPVALEGALKLKEI 492
Cdd:COG2222 153 ALLALLAAWGG---------DDALLAALDALPAALEAALAADWPAAALAALADAERVV-FLGRGPLYGLAREAALKLKEL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 493 SYIHAEAYPAGELKHGPLALVDSDMPVVTVAPNNELVEKLKSNLQEVRARGGELVVFADEGagieaGEGTHVVGMPHIGD 572
Cdd:COG2222 223 SAGHAEAYSAAEFRHGPKSLVDPGTLVVVLASEDPTRELDLDLAAELRALGARVVAIGAED-----DAAITLPAIPDLHD 297
|
330 340 350
....*....|....*....|....*....|....*....
gi 15600742 573 VLSPILYTIPLQLLSYHVAVLKGTDVDQPRNLAKSVTVE 611
Cdd:COG2222 298 ALDPLLLLVVAQRLALALALARGLDPDTPRHLNKVVKTV 336
|
|
| SIS_GlmS_GlmD_2 |
cd05009 |
SIS (Sugar ISomerase) domain repeat 2 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
457-609 |
8.11e-68 |
|
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: 217.52 E-value: 8.11e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 457 VEKVSELFAEKHHTLFLGRGAQFPVALEGALKLKEISYIHAEAYPAGELKHGPLALVDSDMPVVTVAPNNELVEKLKSNL 536
Cdd:cd05009 3 IKELAEKLKEAKSFYVLGRGPNYGTALEGALKLKETSYIHAEAYSAGEFKHGPIALVDEGTPVIFLAPEDRLEEKLESLI 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600742 537 QEVRARGGELVVFADEGAGIEagEGTHVVGMPHIGDVLSPILYTIPLQLLSYHVAVLKGTDVDQPRNLAKSVT 609
Cdd:cd05009 83 KEVKARGAKVIVITDDGDAKD--LADVVIRVPATVEELSPLLYIVPLQLLAYHLAVARGIDPDKPRNLAKSVT 153
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
2-214 |
3.90e-62 |
|
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: 204.99 E-value: 3.90e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 2 CGIVGAIAERNITPILIE----GLKRLEYRGYDSAGVAVFDNEGRLQRcRRVGKVASLEEGLAGTPLLGRLGIAHTRWAT 77
Cdd:cd00352 1 CGIFGIVGADGAASLLLLlllrGLAALEHRGPDGAGIAVYDGDGLFVE-KRAGPVSDVALDLLDEPLKSGVALGHVRLAT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 78 HGAPTEGNAHPHFS-SDEVAVVHNGIIENHEPLRERLKGLGYVFTSQTDTEVIVHLLHHKLQSiGDLTLALKDAVKELHG 156
Cdd:cd00352 80 NGLPSEANAQPFRSeDGRIALVHNGEIYNYRELREELEARGYRFEGESDSEVILHLLERLGRE-GGLFEAVEDALKRLDG 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600742 157 AYGLAVISaAQPDRIVAARSG---SPLVIGLGL-GENFLASDQLALRQVT-DRFIYLEEGDIA 214
Cdd:cd00352 159 PFAFALWD-GKPDRLFAARDRfgiRPLYYGITKdGGLVFASEPKALLALPfKGVRRLPPGELL 220
|
|
| SIS_GlmS_GlmD_1 |
cd05008 |
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
296-407 |
2.67e-52 |
|
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: 175.38 E-value: 2.67e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 296 NVQIVACGTSYHAGMVARYWLESLTGIPCQVEVASEFRYRKVAVQPDCLFVTISQSGETADTLAALRNAKELGFLsSVAI 375
Cdd:cd05008 1 RILIVGCGTSYHAALVAKYLLERLAGIPVEVEAASEFRYRRPLLDEDTLVIAISQSGETADTLAALRLAKEKGAK-TVAI 79
|
90 100 110
....*....|....*....|....*....|..
gi 15600742 376 CNVATSSLVRESDLTLLTQAGPEIGVASTKAF 407
Cdd:cd05008 80 TNVVGSTLAREADYVLYLRAGPEISVAATKAF 111
|
|
| GPATase_N |
cd00715 |
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ... |
2-222 |
7.30e-36 |
|
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the N-terminus of glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase) . The glutaminase domain catalyzes amide nitrogen transfer from glutamine to the appropriate substrate. In this process, glutamine is hydrolyzed to glutamic acid and ammonia. GPATase catalyzes the first step in purine biosynthesis, an amide transfer from glutamine to PRPP, resulting in phosphoribosylamine, pyrophosphate and glutamate. GPATase crystalizes as a homotetramer, but can also exist as a homdimer.
Pssm-ID: 238367 [Multi-domain] Cd Length: 252 Bit Score: 134.90 E-value: 7.30e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 2 CGIVGAIAERNITPILIEGLKRLEYRGYDSAGVAVFDNEgRLQRCRRVGKVASL--EEGLAgtPLLGRLGIAHTRWATHG 79
Cdd:cd00715 1 CGVFGIYGAEDAARLTYLGLYALQHRGQESAGIATSDGK-RFHTHKGMGLVSDVfdEEKLR--RLPGNIAIGHVRYSTAG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 80 APTEGNAHP---HFSSDEVAVVHNGIIENHEPLRERLKGLGYVFTSQTDTEVIVHLLHHKLQSiGDLTLALKDAVKELHG 156
Cdd:cd00715 78 SSSLENAQPfvvNSPLGGIALAHNGNLVNAKELREELEEEGRIFQTTSDSEVILHLIARSLAK-DDLFEAIIDALERVKG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600742 157 AYGLAVISaaqPDRIVAARSGS---PLVIG-LGLGENFLASDQLALRQVTDRFIY-LEEGDIAEIRRDSVR 222
Cdd:cd00715 157 AYSLVIMT---ADGLIAVRDPHgirPLVLGkLEGDGYVVASESCALDIIGAEFVRdVEPGEIVVIDDDGLE 224
|
|
| PurF |
COG0034 |
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ... |
1-183 |
5.46e-35 |
|
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: 137.85 E-value: 5.46e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 1 MCGIVGAIAERNITPILIEGLKRLEYRGYDSAGVAVFDNeGRLQRCRRVGKVASL--EEGLAGtpLLGRLGIAHTRWATH 78
Cdd:COG0034 7 ECGVFGIYGHEDVAQLTYYGLYALQHRGQESAGIATSDG-GRFHLHKGMGLVSDVfdEEDLER--LKGNIAIGHVRYSTT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 79 GAPTEGNAHP---HFSSDEVAVVHNGIIENHEPLRERLKGLGYVFTSQTDTEVIVHLLHHKLQSiGDLTLALKDAVKELH 155
Cdd:COG0034 84 GSSSLENAQPfyvNSPFGSIALAHNGNLTNAEELREELEEEGAIFQTTSDTEVILHLIARELTK-EDLEEAIKEALRRVK 162
|
170 180 190
....*....|....*....|....*....|.
gi 15600742 156 GAYGLAVISaaqPDRIVAAR--SG-SPLVIG 183
Cdd:COG0034 163 GAYSLVILT---GDGLIAARdpNGiRPLVLG 190
|
|
| GlxB |
cd01907 |
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ... |
2-224 |
2.79e-30 |
|
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: 119.30 E-value: 2.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 2 CGIVGAI---AERNITPILIEGLKRLEYRG-YDSAGVAVF-DNEGRLQRC-------------RRVGKVASLEEglagtp 63
Cdd:cd01907 1 CGIFGIMskdGEPFVGALLVEMLDAMQERGpGDGAGFALYgDPDAFVYSSgkdmevfkgvgypEDIARRYDLEE------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 64 LLGRLGIAHTRWATHGAPTEGNAHPhFSSDEVAVVHNGIIENHEPLRERLKGLGYVFTSQTDTEVIVHLLHHKLQSIGD- 142
Cdd:cd01907 75 YKGYHWIAHTRQPTNSAVWWYGAHP-FSIGDIAVVHNGEISNYGSNREYLERFGYKFETETDTEVIAYYLDLLLRKGGLp 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 143 ------------------LTLALKDAVKELHGAYGLAVisaAQPDRIVAARSGS---PLVIGLGLGENFLASDQLALRQV 201
Cdd:cd01907 154 leyykhiirmpeeerellLALRLTYRLADLDGPFTIIV---GTPDGFIVIRDRIklrPAVVAETDDYVAIASEECAIREI 230
|
250 260
....*....|....*....|...
gi 15600742 202 TDRfiylEEGDIAEIRRDSVRLW 224
Cdd:cd01907 231 PDR----DNAKVWEPRPGEYVIW 249
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
290-407 |
4.82e-30 |
|
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: 114.70 E-value: 4.82e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 290 LFAKVRNVQIVACGTSYHAGMVARYWLESLTGIPCQVEVASEFRYRKVA-VQPDCLFVTISQSGETADTLAALRNAKELG 368
Cdd:pfam01380 1 LLAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGVLAlVDEDDLVIAISYSGETKDLLAAAELAKARG 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 15600742 369 fLSSVAICNVATSSLVRESDLTLLTQAGPEIGVASTKAF 407
Cdd:pfam01380 81 -AKIIAITDSPGSPLAREADHVLYINAGPETGVASTKSI 118
|
|
| purF |
TIGR01134 |
amidophosphoribosyltransferase; Alternate name: glutamine phosphoribosylpyrophosphate (PRPP) ... |
2-206 |
1.51e-27 |
|
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: 115.88 E-value: 1.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 2 CGIVGAIAERNITP-ILIEGLKRLEYRGYDSAGVAVFDneGRLQRCRR----VGKVASlEEGLAgtPLLGRLGIAHTRWA 76
Cdd:TIGR01134 1 CGVVGIYGQEEVAAsLTYYGLYALQHRGQESAGISVFD--GNRFRLHKgnglVSDVFN-EEHLQ--RLKGNVGIGHVRYS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 77 THGAPTEGNAHP---HFSSDEVAVVHNGIIENHEPLRERLKGLGYVFTSQTDTEVIVHLLHHKLQSIGDLTLALKDAVKE 153
Cdd:TIGR01134 76 TAGSSGLENAQPfvvNSPYGGLALAHNGNLVNADELRRELEEEGRHFNTTSDSEVLLHLLAHNDESKDDLFDAVARVLER 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15600742 154 LHGAYGLAVISaaqPDRIVAARS--G-SPLVIGlGLGENF-LASDQLALRQVTDRFI 206
Cdd:TIGR01134 156 VRGAYALVLMT---EDGLVAVRDphGiRPLVLG-RRGDGYvVASESCALDILGAEFV 208
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
463-594 |
1.10e-26 |
|
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars. Presumably the SIS domains bind to the end-product of the pathway.
Pssm-ID: 426230 [Multi-domain] Cd Length: 131 Bit Score: 105.07 E-value: 1.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 463 LFAEKHHTLFLGRGAQFPVALEGALKLKEISYIHAEAYPAGELKHGPLALVDSDMPVVTVAPNNELVEKLKsNLQEVRAR 542
Cdd:pfam01380 1 LLAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGVLALVDEDDLVIAISYSGETKDLLA-AAELAKAR 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 15600742 543 GGELVVFADEGAGIEAGEGTHVVGMPHIGDVLSPILYTIPLQLLSYHVAVLK 594
Cdd:pfam01380 80 GAKIIAITDSPGSPLAREADHVLYINAGPETGVASTKSITAQLAALDALAVA 131
|
|
| PRK05793 |
PRK05793 |
amidophosphoribosyltransferase; Provisional |
2-222 |
3.58e-26 |
|
amidophosphoribosyltransferase; Provisional
Pssm-ID: 235611 [Multi-domain] Cd Length: 469 Bit Score: 112.05 E-value: 3.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 2 CGIVGAIAERNI--TPILIEGLKRLEYRGYDSAGVAVFDNEgRLQRCRRVGKVASL--EEGLAGtpLLGRLGIAHTRWAT 77
Cdd:PRK05793 15 CGVFGVFSKNNIdvASLTYYGLYALQHRGQESAGIAVSDGE-KIKVHKGMGLVSEVfsKEKLKG--LKGNSAIGHVRYST 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 78 HGAPTEGNAHP---HFSSDEVAVVHNGIIENHEPLRERLKGLGYVFTSQTDTEVIVHLLHHKLQSigDLTLALKDAVKEL 154
Cdd:PRK05793 92 TGASDLDNAQPlvaNYKLGSIAIAHNGNLVNADVIRELLEDGGRIFQTSIDSEVILNLIARSAKK--GLEKALVDAIQAI 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600742 155 HGAYGLAVISAaqpDRIVAARSGS---PLVIGLGLGENFLASDQLALRQVTDRFIY-LEEGDIAEIRRDSVR 222
Cdd:PRK05793 170 KGSYALVILTE---DKLIGVRDPHgirPLCLGKLGDDYILSSESCALDTIGAEFIRdVEPGEIVIIDEDGIK 238
|
|
| PLN02440 |
PLN02440 |
amidophosphoribosyltransferase |
1-183 |
4.38e-24 |
|
amidophosphoribosyltransferase
Pssm-ID: 215241 [Multi-domain] Cd Length: 479 Bit Score: 105.92 E-value: 4.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 1 MCGIVGAIAERNITPILIEGLKRLEYRGYDSAGVAVFDnEGRLQRCRRVGKVASLEEGLAGTPLLGRLGIAHTRWATHGA 80
Cdd:PLN02440 1 ECGVVGIFGDPEASRLCYLGLHALQHRGQEGAGIVTVD-GNRLQSITGNGLVSDVFDESKLDQLPGDIAIGHVRYSTAGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 81 PTEGNAHPHFSS---DEVAVVHNGIIENHEPLRERLKGLGYVFTSQTDTEVIVHLLHHKLQSIgdLTLALKDAVKELHGA 157
Cdd:PLN02440 80 SSLKNVQPFVANyrfGSIGVAHNGNLVNYEELRAKLEENGSIFNTSSDTEVLLHLIAISKARP--FFSRIVDACEKLKGA 157
|
170 180
....*....|....*....|....*....
gi 15600742 158 YGLAVISAaqpDRIVAARSGS---PLVIG 183
Cdd:PLN02440 158 YSMVFLTE---DKLVAVRDPHgfrPLVMG 183
|
|
| GATase_6 |
pfam13522 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
66-175 |
2.80e-19 |
|
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain found in a variety of enzymes, such as asparagine synthetase and glutamine--fructose-6-phosphate transaminase.
Pssm-ID: 433279 [Multi-domain] Cd Length: 130 Bit Score: 84.28 E-value: 2.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 66 GRLGIAHTRWATHGAPTEGNaHPHFSSD-EVAVVHNGIIENHEPLRERLKGLGYVFTSQTDTEVIVHLLHHKlqsiGdlt 144
Cdd:pfam13522 10 GGVALGHVRLAIVDLPDAGN-QPMLSRDgRLVLVHNGEIYNYGELREELADLGHAFRSRSDTEVLLALYEEW----G--- 81
|
90 100 110
....*....|....*....|....*....|.
gi 15600742 145 lalKDAVKELHGAYGLAVISAAQpDRIVAAR 175
Cdd:pfam13522 82 ---EDCLERLRGMFAFAIWDRRR-RTLFLAR 108
|
|
| AsnB |
cd00712 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ... |
2-175 |
1.85e-16 |
|
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: 78.75 E-value: 1.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 2 CGIVGAI---AERNITPILIEGLKRLEYRGYDSAGVAVFDNegrlqrcrrvgkvasleeglagtpllgrLGIAHTRWATH 78
Cdd:cd00712 1 CGIAGIIgldGASVDRATLERMLDALAHRGPDGSGIWIDEG----------------------------VALGHRRLSII 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 79 gaPTEGNAHPHFSSDE-VAVVHNGIIENHEPLRERLKGLGYVFTSQTDTEVIVHLLHHKlqsiGDltlalkDAVKELHGA 157
Cdd:cd00712 53 --DLSGGAQPMVSEDGrLVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHLYEEW----GE------DCLERLNGM 120
|
170
....*....|....*...
gi 15600742 158 YGLAVISAAQpDRIVAAR 175
Cdd:cd00712 121 FAFALWDKRK-RRLFLAR 137
|
|
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
1-175 |
2.12e-16 |
|
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: 82.58 E-value: 2.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 1 MCGIVGAIA--ERNITPILIEGLKRLEYRGYDSAGVAVFdnegrlqrcrrvgkvasleeglagtpllGRLGIAHTRWATH 78
Cdd:COG0367 1 MCGIAGIIDfdGGADREVLERMLDALAHRGPDGSGIWVD----------------------------GGVALGHRRLSII 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 79 GaPTEGNAHPHFSSDE-VAVVHNGIIENHEPLRERLKGLGYVFTSQTDTEVIVHLLHHKlqsiGDltlalkDAVKELHGA 157
Cdd:COG0367 53 D-LSEGGHQPMVSEDGrYVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHAYEEW----GE------DCLERLNGM 121
|
170
....*....|....*...
gi 15600742 158 YGLAVISAAQpDRIVAAR 175
Cdd:COG0367 122 FAFAIWDRRE-RRLFLAR 138
|
|
| GATase_7 |
pfam13537 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
72-193 |
9.59e-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: 73.71 E-value: 9.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 72 HTRWATHGapTEGNAHPHFSSDE--VAVVHNGIIENHEPLRERLKGLGYVFTSQTDTEVIVHLLHHKlqsigdltlALKD 149
Cdd:pfam13537 1 HRRLSIID--LEGGAQPMVSSEDgrYVIVFNGEIYNYRELRAELEAKGYRFRTHSDTEVILHLYEAE---------WGED 69
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 15600742 150 AVKELHGAYGLAVISAAQpDRIVAAR--SG-SPLVIGLGLGENFL-AS 193
Cdd:pfam13537 70 CVDRLNGMFAFAIWDRRR-QRLFLARdrFGiKPLYYGRDDGGRLLfAS 116
|
|
| YafJ |
COG0121 |
Predicted glutamine amidotransferase YafJ [General function prediction only]; |
33-178 |
7.46e-13 |
|
Predicted glutamine amidotransferase YafJ [General function prediction only];
Pssm-ID: 439891 [Multi-domain] Cd Length: 248 Bit Score: 68.84 E-value: 7.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 33 GVAVFDNEGRLQRCRRVGKVAS--LEEGLAGtPLLGRLGIAHTRWATHGAPTEGNAHPhFSSDEVAVVHNGIIENHEPLR 110
Cdd:COG0121 42 GIGWYEGDGEPRLYRDPLPAWSdpNLRLLAR-PIKSRLVIAHVRKATVGPVSLENTHP-FRGGRWLFAHNGQLDGFDRLR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 111 ERLK---GLGYVFT--SQTDTEVIVHLLHHKL-QSIGDLTLALKDAVKEL------HGAYGLAVISaaqPDRIVAARSGS 178
Cdd:COG0121 120 RRLAeelPDELYFQpvGTTDSELAFALLLSRLrDGGPDPAEALAEALRELaelaraPGRLNLLLSD---GERLYATRYTS 196
|
|
| SIS_RpiR |
cd05013 |
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ... |
286-395 |
8.77e-13 |
|
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: 65.71 E-value: 8.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 286 QAAELFAKVRNVQIVACGTSYHAGMVARYWLeSLTGIPCQVEVAS-EFRYRKVAVQPDCLFVTISQSGETADTLAALRNA 364
Cdd:cd05013 5 KAVDLLAKARRIYIFGVGSSGLVAEYLAYKL-LRLGKPVVLLSDPhLQLMSAANLTPGDVVIAISFSGETKETVEAAEIA 83
|
90 100 110
....*....|....*....|....*....|.
gi 15600742 365 KELGfLSSVAICNVATSSLVRESDLTLLTQA 395
Cdd:cd05013 84 KERG-AKVIAITDSANSPLAKLADIVLLVSS 113
|
|
| asnB |
PRK09431 |
asparagine synthetase B; Provisional |
1-203 |
3.24e-11 |
|
asparagine synthetase B; Provisional
Pssm-ID: 236513 [Multi-domain] Cd Length: 554 Bit Score: 66.09 E-value: 3.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 1 MCGIVGAIAERNITPIL----IEGLKRLEYRGYDSAGVAVFDNegrlqrcrrvgkvasleeglagtpllgrlGI-AHTRW 75
Cdd:PRK09431 1 MCGIFGILDIKTDADELrkkaLEMSRLMRHRGPDWSGIYASDN-----------------------------AIlGHERL 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 76 ATHGapTEGNAHPHFSSDEVAVVH-NGIIENHEPLRERLKGlGYVFTSQTDTEVIVHLLHHKlqsiGdltlalKDAVKEL 154
Cdd:PRK09431 52 SIVD--VNGGAQPLYNEDGTHVLAvNGEIYNHQELRAELGD-KYAFQTGSDCEVILALYQEK----G------PDFLDDL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15600742 155 HGAYGLAVISAAQpDRIVAARS--G-SPLVIGLGLGENFL-ASDQLALRQVTD 203
Cdd:PRK09431 119 DGMFAFALYDSEK-DAYLIARDpiGiIPLYYGYDEHGNLYfASEMKALVPVCK 170
|
|
| RpiR |
COG1737 |
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ... |
286-395 |
3.85e-11 |
|
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains [Transcription];
Pssm-ID: 441343 [Multi-domain] Cd Length: 286 Bit Score: 64.18 E-value: 3.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 286 QAAELFAKVRNVQIVACGTSYHAGMVARYWLESLtGIPCQVEVASEFRYRKVA--VQPDCLFVTISQSGETADTLAALRN 363
Cdd:COG1737 126 RAVDLLAKARRIYIFGVGASAPVAEDLAYKLLRL-GKNVVLLDGDGHLQAESAalLGPGDVVIAISFSGYTRETLEAARL 204
|
90 100 110
....*....|....*....|....*....|..
gi 15600742 364 AKELGfLSSVAICNVATSSLVRESDLTLLTQA 395
Cdd:COG1737 205 AKERG-AKVIAITDSPLSPLAKLADVVLYVPS 235
|
|
| SIS_1 |
cd05710 |
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ... |
296-388 |
7.26e-11 |
|
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars.
Pssm-ID: 240214 [Multi-domain] Cd Length: 120 Bit Score: 59.90 E-value: 7.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 296 NVQIVACGTSYHAGMVARYWLESLTGIPCQVEVASEFRYRK-VAVQPDCLFVTISQSGETADTLAALRNAKELGfLSSVA 374
Cdd:cd05710 1 NVFFVGCGGSLADMYPAKYFLKKESKLPVFVYNAAEFLHTGpKRLTEKSVVILASHSGNTKETVAAAKFAKEKG-ATVIG 79
|
90
....*....|....
gi 15600742 375 ICNVATSSLVRESD 388
Cdd:cd05710 80 LTDDEDSPLAKLAD 93
|
|
| PLN02549 |
PLN02549 |
asparagine synthase (glutamine-hydrolyzing) |
1-205 |
7.51e-11 |
|
asparagine synthase (glutamine-hydrolyzing)
Pssm-ID: 178164 [Multi-domain] Cd Length: 578 Bit Score: 64.79 E-value: 7.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 1 MCGIVGAI----AERNITPILIEGLKRLEYRGYDSAGVAVFdnegrlqrcrrvgkvasleeglagtpllGRLGIAHTRWA 76
Cdd:PLN02549 1 MCGILAVLgcsdDSQAKRSRVLELSRRLRHRGPDWSGLYGN----------------------------EDCYLAHERLA 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 77 THgAPTEGNaHPHFSSDE-VAVVHNGIIENHEPLRERLKglGYVFTSQTDTEVIVHLLHHklqsIGDltlalkDAVKELH 155
Cdd:PLN02549 53 IM-DPESGD-QPLYNEDKtIVVTANGEIYNHKELREKLK--LHKFRTGSDCEVIAHLYEE----HGE------EFVDMLD 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15600742 156 GAYGLaVISAAQPDRIVAARSG---SPLVIGLGL-GENFLASDQLALRQVTDRF 205
Cdd:PLN02549 119 GMFSF-VLLDTRDNSFIAARDHigiTPLYIGWGLdGSVWFASEMKALCDDCERF 171
|
|
| PTZ00077 |
PTZ00077 |
asparagine synthetase-like protein; Provisional |
1-203 |
7.97e-10 |
|
asparagine synthetase-like protein; Provisional
Pssm-ID: 185431 [Multi-domain] Cd Length: 586 Bit Score: 61.65 E-value: 7.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 1 MCGIVG----AIAERNITPILIEGLKRLEYRGYDSAGVAVFDNEGRLQRCrrvgkvasleeglagtpllgrlgIAHTRWA 76
Cdd:PTZ00077 1 MCGILAifnsKGERHELRRKALELSKRLRHRGPDWSGIIVLENSPGTYNI-----------------------LAHERLA 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 77 THGaPTEGnAHPHFSSDE-VAVVHNGIIENHEPLRERLKGLGYVFTSQTDTEVIVHLLHHKlqsiGDltlalKDAVKELH 155
Cdd:PTZ00077 58 IVD-LSDG-KQPLLDDDEtVALMQNGEIYNHWEIRPELEKEGYKFSSNSDCEIIGHLYKEY----GP-----KDFWNHLD 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15600742 156 GAYGlAVISAAQPDRIVAARSG---SPLVIGLGL-GENFLASDQLAL-RQVTD 203
Cdd:PTZ00077 127 GMFA-TVIYDMKTNTFFAARDHigiIPLYIGYAKdGSIWFSSELKALhDQCVE 178
|
|
| YafJ |
cd01908 |
Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine ... |
70-179 |
9.91e-10 |
|
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: 59.71 E-value: 9.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 70 IAHTRWATHGAPTEGNAHPhFSSDEVAVVHNGIIENHEPLRERL-KGLGYVFTSQTDTEVIVHLL-----HHKLQSIGDL 143
Cdd:cd01908 84 LAHVRAATVGPVSLENCHP-FTRGRWLFAHNGQLDGFRLLRRRLlRLLPRLPVGTTDSELAFALLlsrllERDPLDPAEL 162
|
90 100 110
....*....|....*....|....*....|....*...
gi 15600742 144 TLALKDAVKELHGAYGLAVISAA--QPDRIVAARSGSP 179
Cdd:cd01908 163 LDAILQTLRELAALAPPGRLNLLlsDGEYLIATRYASA 200
|
|
| frlB |
PRK11382 |
fructoselysine 6-phosphate deglycase; |
294-602 |
2.78e-09 |
|
fructoselysine 6-phosphate deglycase;
Pssm-ID: 183111 [Multi-domain] Cd Length: 340 Bit Score: 59.24 E-value: 2.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 294 VRNVQIVACGTSYHAGMVARYWLESLTGIPCQVEVASEF----RYRkvaVQPDCLFVTISQSGETADTLAALrnakELGf 369
Cdd:PRK11382 44 IDRIYFVACGSPLNAAQTAKHLADRFSDLQVYAISGWEFcdntPYR---LDDRCAVIGVSDYGKTEEVIKAL----ELG- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 370 lssvAICNVATSSLVRESDLTLLTQAGPEIGVASTKAFTTQLVALLLLtlgIGQVQKRLADGVE-AELVDELRRLPTRLG 448
Cdd:PRK11382 116 ----RACGALTAAFTKRADSPITSAAEFSIDYQADCIWEIHLLLCYSV---VLEMITRLAPNAEiGKIKNDLKQLPNALG 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 449 EALamnRTVE----KVSELFAEKHHTLFLGRGAQFPVAL-EGALKLKEISYIHAEAYPAGELKHGPLALVDSDMPVVTVA 523
Cdd:PRK11382 189 HLV---RTWEekgrQLGELASQWPMIYTVAAGPLRPLGYkEGIVTLMEFTWTHGCVIESGEFRHGPLEIVEPGVPFLFLL 265
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600742 524 PNNELVEKLKSNLQEVRARGGELVVFADEgagiEAGEGTHvvgmphigDVLSPILYTIPLQLLSYHVAVLKGTDVDQPR 602
Cdd:PRK11382 266 GNDESRHTTERAINFVKQRTDNVIVIDYA----EISQGLH--------PWLAPFLMFVPMEWLCYYLSIYKDHNPDERR 332
|
|
| SIS |
cd04795 |
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
297-376 |
3.49e-09 |
|
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars.
Pssm-ID: 240112 [Multi-domain] Cd Length: 87 Bit Score: 53.92 E-value: 3.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 297 VQIVACGTSYHAGMVARYWLESLTGIPCQVEVASEFRY--RKVAVQPDCLFVTISQSGETADTLAALRNAKELGfLSSVA 374
Cdd:cd04795 1 IFVIGIGGSGAIAAYFALELLELTGIEVVALIATELEHasLLSLLRKGDVVIALSYSGRTEELLAALEIAKELG-IPVIA 79
|
..
gi 15600742 375 IC 376
Cdd:cd04795 80 IT 81
|
|
| asn_synth_AEB |
TIGR01536 |
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing ... |
66-132 |
9.02e-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: 55.03 E-value: 9.02e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600742 66 GRLGIAHTRWATHGapTEGNAHP-HFSSDEVAVVHNGIIENHEPLRERLKGLGYVFTSQTDTEVIVHL 132
Cdd:TIGR01536 40 GNAILGHRRLAIID--LSGGAQPmSNEGKTYVIVFNGEIYNHEELREELEAKGYTFQTDSDTEVILHL 105
|
|
| SIS_AgaS_like |
cd05010 |
AgaS-like protein. AgaS contains a SIS (Sugar ISomerase) domain which is found in many ... |
472-601 |
1.03e-06 |
|
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: 48.78 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 472 FLGRGAQFPVALEGALKLKEIS--YIHAEAYPAGELKHGPLALVDSDMPVVTVAPNNELVEKLKSNL-QEVRARGGELVV 548
Cdd:cd05010 3 YLGSGPLAGLAREAALKVLELTagKVATVYDSPLGFRHGPKSLVDDDTLVVVFVSNDPYTRQYDLDLlKELRRDGIAARV 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 15600742 549 FA---DEGAGIEAGEGTHVVGMPHIGDVLSPILYTIPLQLLSYHVAVLKGTDVDQP 601
Cdd:cd05010 83 IAispESDAGIEDNSHYYLPGSRDLDDVYLAFPYILYAQLFALFNSIALGLTPDNP 138
|
|
| SIS |
cd04795 |
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
471-551 |
1.11e-06 |
|
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: 46.98 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600742 471 LFLGRGAQFPVALEGALKLKEISYIHAEAYPAGELKHGP-LALVDSDMPVVTVAPNNELvEKLKSNLQEVRARGGELVVF 549
Cdd:cd04795 2 FVIGIGGSGAIAAYFALELLELTGIEVVALIATELEHASlLSLLRKGDVVIALSYSGRT-EELLAALEIAKELGIPVIAI 80
|
..
gi 15600742 550 AD 551
Cdd:cd04795 81 TD 82
|
|
| SIS_Etherase |
cd05007 |
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ... |
342-406 |
4.00e-04 |
|
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ISomerase) domain. The SIS domain is found in many phosphosugar isomerases and phosphosugar binding proteins. The bacterial cell wall sugar N-acetylmuramic acid carries a unique D-lactyl ether substituent at the C3 position. The etherase catalyzes the cleavage of the lactyl ether bond of N-acetylmuramic acid 6-phosphate.
Pssm-ID: 240140 [Multi-domain] Cd Length: 257 Bit Score: 42.51 E-value: 4.00e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600742 342 DCLfVTISQSGETADTLAALRNAKELGFLSsVAICNVATSSLVRESDLTLLTQAGPEIGVAST--KA 406
Cdd:cd05007 120 DVV-IGIAASGRTPYVLGALRYARARGALT-IGIACNPGSPLLQLADIAIALITGPEVVAGSTrlKA 184
|
|
| murQ |
PRK05441 |
N-acetylmuramic acid-6-phosphate etherase; Reviewed |
342-406 |
4.56e-03 |
|
N-acetylmuramic acid-6-phosphate etherase; Reviewed
Pssm-ID: 235467 [Multi-domain] Cd Length: 299 Bit Score: 39.38 E-value: 4.56e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600742 342 DCLfVTISQSGETADTLAALRNAKELGFLSsVAICNVATSSLVRESDLTLLTQAGPEIGVAST--KA 406
Cdd:PRK05441 133 DVV-VGIAASGRTPYVIGALEYARERGALT-IGISCNPGSPLSKEADIAIEVVVGPEVLTGSTrmKA 197
|
|
| SIS_PGI_PMI_1 |
cd05017 |
The members of this protein family contain the SIS (Sugar ISomerase) domain and have both the ... |
298-368 |
9.38e-03 |
|
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: 36.47 E-value: 9.38e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600742 298 QIVACGT--SYHAGMVARYWLESLTGIPCQVeVASEFRYRKVAvqPDCLFVTISQSGETADTLAALRNAKELG 368
Cdd:cd05017 1 NIVILGMggSGIGGDLLESLLLDEAKIPVYV-VKDYTLPAFVD--RKTLVIAVSYSGNTEETLSAVEQAKERG 70
|
|
| |
