|
Name |
Accession |
Description |
Interval |
E-value |
| GlmS |
COG0449 |
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ... |
1-620 |
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: 1018.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 1 MCGIVGYVGHRQALDVVLNGLRRLEYRGYDSAGVAVLTDAGLTVERKAGRLANLEARLAEvgvDSFAGTAGMGHTRWATH 80
Cdd:COG0449 1 MCGIVGYIGKRDAAPILLEGLKRLEYRGYDSAGIAVLDDGGLEVRKAVGKLANLEEKLAE---EPLSGTIGIGHTRWATH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 81 GAPIDRNSHPHRDATGRVAVVHNGIIENFAALRAELEAAGVELASDTDSETAAHLIAREYgaakERGGGLAEAVRTVCRR 160
Cdd:COG0449 78 GAPSDENAHPHTSCSGRIAVVHNGIIENYAELREELEAKGHTFKSETDTEVIAHLIEEYL----KGGGDLLEAVRKALKR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 161 LEGAFTLVVSHADEPDLIVAARRSSPLVVGLGDGETFVASDVAAFIEHTREAVELGQDQLVEITRDGYRVTDFHGEDAPV 240
Cdd:COG0449 154 LEGAYALAVISADEPDRIVAARKGSPLVIGLGEGENFLASDVPALLPYTRRVIYLEDGEIAVLTRDGVEIYDLDGEPVER 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 241 KPFTVDWDLSAAEKGGHEYFMLKEIEEQPEALANTLRGHF-VDGRVVLDEQRLSDQDLRDVDKVFVVACGSAYHSGLVAK 319
Cdd:COG0449 234 EVKTVDWDAEAAEKGGYPHFMLKEIHEQPEAIRDTLRGRLdEDGRVVLDELNLAAEDLRNIDRIYIVACGTSYHAGLVGK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 320 YAIEHWTRLPVEVELASEFRYRDPVLDRDTLVVAVSQSGETADTLEAVRHAREQKARVLAVCNTNGAQIPRESDAVLYTH 399
Cdd:COG0449 314 YLIEELARIPVEVEIASEFRYRDPVVDPGTLVIAISQSGETADTLAALREAKEKGAKVLAICNVVGSTIARESDAVLYTH 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 400 AGPEIGVASTKAFLAQIAANYLVGLALAQARGTKYADEVAREFRELEAMPKAVSRVLETVERVRALGRELADSKAVLFLG 479
Cdd:COG0449 394 AGPEIGVASTKAFTTQLAALYLLALYLARARGTLSAEEEAELLEELRKLPEKIEEVLDLEEQIEELAEKYADARNALFLG 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 480 RHVGYPVALEGALKLKELAYMHAEGFAAGELKHGPIALIEEGLPVVVVMPSPKgravLHAKLVSNISEIQARGARTVVIA 559
Cdd:COG0449 474 RGINYPVALEGALKLKEISYIHAEGYAAGELKHGPIALIDEGMPVVAIAPQDE----LYEKTLSNIQEVKARGGKVIAIA 549
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1906442648 560 EEGDETVRPFADELIEVPAVPTLLQPLVSTVPLQVLAAEIARARGYDVDKPRNLAKSVTVE 620
Cdd:COG0449 550 DEGDEEVEELADDVIEVPEVDELLAPILAVVPLQLLAYHVAVLRGTDVDQPRNLAKSVTVE 610
|
|
| PRK00331 |
PRK00331 |
isomerizing glutamine--fructose-6-phosphate transaminase; |
1-620 |
0e+00 |
|
isomerizing glutamine--fructose-6-phosphate transaminase;
Pssm-ID: 234729 [Multi-domain] Cd Length: 604 Bit Score: 1014.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 1 MCGIVGYVGHRQALDVVLNGLRRLEYRGYDSAGVAVLTDAGLTVERKAGRLANLEARLAEvgvDSFAGTAGMGHTRWATH 80
Cdd:PRK00331 1 MCGIVGYVGQRNAAEILLEGLKRLEYRGYDSAGIAVLDDGGLEVRKAVGKVANLEAKLEE---EPLPGTTGIGHTRWATH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 81 GAPIDRNSHPHRDATGRVAVVHNGIIENFAALRAELEAAGVELASDTDSETAAHLIAREYgaakERGGGLAEAVRTVCRR 160
Cdd:PRK00331 78 GKPTERNAHPHTDCSGRIAVVHNGIIENYAELKEELLAKGHVFKSETDTEVIAHLIEEEL----KEGGDLLEAVRKALKR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 161 LEGAFTLVVSHADEPDLIVAARRSSPLVVGLGDGETFVASDVAAFIEHTREAVELGQDQLVEITRDGYRVTDFHGEDAPV 240
Cdd:PRK00331 154 LEGAYALAVIDKDEPDTIVAARNGSPLVIGLGEGENFLASDALALLPYTRRVIYLEDGEIAVLTRDGVEIFDFDGNPVER 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 241 KPFTVDWDLSAAEKGGHEYFMLKEIEEQPEALANTLRGHFVDgrvvLDEQRLSDQDLRDVDKVFVVACGSAYHSGLVAKY 320
Cdd:PRK00331 234 EVYTVDWDASAAEKGGYRHFMLKEIYEQPEAIRDTLEGRLDE----LGEGELADEDLKKIDRIYIVACGTSYHAGLVAKY 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 321 AIEHWTRLPVEVELASEFRYRDPVLDRDTLVVAVSQSGETADTLEAVRHAREQKARVLAVCNTNGAQIPRESDAVLYTHA 400
Cdd:PRK00331 310 LIESLAGIPVEVEIASEFRYRDPVLSPKTLVIAISQSGETADTLAALRLAKELGAKTLAICNVPGSTIARESDAVLYTHA 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 401 GPEIGVASTKAFLAQIAANYLVGLALAQARGTKYADEVAREFRELEAMPKAVSRVLETVERVRALGRELADSKAVLFLGR 480
Cdd:PRK00331 390 GPEIGVASTKAFTAQLAVLYLLALALAKARGTLSAEEEADLVHELRELPALIEQVLDLKEQIEELAEDFADARNALFLGR 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 481 HVGYPVALEGALKLKELAYMHAEGFAAGELKHGPIALIEEGLPVVVVMPSPKgravLHAKLVSNISEIQARGARTVVIAE 560
Cdd:PRK00331 470 GVDYPVALEGALKLKEISYIHAEGYAAGELKHGPIALIDEGMPVVAIAPNDE----LYEKTKSNIQEVKARGARVIVIAD 545
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 561 EGDEtVRPFADELIEVPAVPTLLQPLVSTVPLQVLAAEIARARGYDVDKPRNLAKSVTVE 620
Cdd:PRK00331 546 EGDE-VAEEADDVIEVPEVHELLAPLLYVVPLQLLAYHVALARGTDVDKPRNLAKSVTVE 604
|
|
| glmS |
TIGR01135 |
glucosamine--fructose-6-phosphate aminotransferase (isomerizing); The member from ... |
2-620 |
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: 868.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 2 CGIVGYVGHRQALDVVLNGLRRLEYRGYDSAGVAVLTDAGLTVERKAGRLANLEARLAEVGVDsfaGTAGMGHTRWATHG 81
Cdd:TIGR01135 1 CGIVGYIGQRDAVPILLEGLKRLEYRGYDSAGIAVVDEGKLFVRKAVGKVAELANKLGEKPLP---GGVGIGHTRWATHG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 82 APIDRNSHPHRDATGRVAVVHNGIIENFAALRAELEAAGVELASDTDSETAAHLIAREYgaakERGGGLAEAVRTVCRRL 161
Cdd:TIGR01135 78 KPTDENAHPHTDEGGRIAVVHNGIIENYAELREELEARGHVFSSDTDTEVIAHLIEEEL----REGGDLLEAVQKALKQL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 162 EGAFTLVVSHADEPDLIVAARRSSPLVVGLGDGETFVASDVAAFIEHTREAVELGQDQLVEITRDGYRVTDFHGEDAPVK 241
Cdd:TIGR01135 154 RGAYALAVLHADHPETLVAARSGSPLIVGLGDGENFVASDVTALLPYTRRVIYLEDGDIAILTKDGVEIYNFEGAPVQRE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 242 PFTVDWDLSAAEKGGHEYFMLKEIEEQPEALANTLRGHFVDGRVVLDEQrLSDQDLRDVDKVFVVACGSAYHSGLVAKYA 321
Cdd:TIGR01135 234 VRVIDWDLDAAEKGGYRHFMLKEIYEQPRALRDTLEGRIEENGGVFEEL-GAEELLKNIDRIQIVACGTSYHAGLVAKYL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 322 IEHWTRLPVEVELASEFRYRDPVLDRDTLVVAVSQSGETADTLEAVRHAREQKARVLAVCNTNGAQIPRESDAVLYTHAG 401
Cdd:TIGR01135 313 IERLAGIPVEVEIASEFRYRKPVVDKDTLVIAISQSGETADTLEALRLAKELGAKTLGICNVPGSTLVREADHTLYTRAG 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 402 PEIGVASTKAFLAQIAANYLVGLALAQARGTKYADEVAREFRELEAMPKAVSRVLETVERVRALGRELADSKAVLFLGRH 481
Cdd:TIGR01135 393 PEIGVASTKAFTTQLTVLYLLALALAKARGTLSAEEEAELVDALRRLPDLVEQVLLADESIAELAERYADKRNFLFLGRG 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 482 VGYPVALEGALKLKELAYMHAEGFAAGELKHGPIALIEEGLPVVVVMPSPKgravLHAKLVSNISEIQARGARTVVIAEE 561
Cdd:TIGR01135 473 LGYPIALEGALKLKEISYIHAEGYPAGELKHGPIALIDEGLPVVAIAPKDS----LLEKTKSNVEEVKARGARVIVFAPE 548
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 1906442648 562 GDETVRPFADELIEVPAVPTLLQPLVSTVPLQVLAAEIARARGYDVDKPRNLAKSVTVE 620
Cdd:TIGR01135 549 DDETIASVADDVIKLPEVEELLAPIVYTIPLQLLAYHIALAKGTDVDKPRNLAKSVTVE 607
|
|
| PLN02981 |
PLN02981 |
glucosamine:fructose-6-phosphate aminotransferase |
1-620 |
6.18e-163 |
|
glucosamine:fructose-6-phosphate aminotransferase
Pssm-ID: 215531 [Multi-domain] Cd Length: 680 Bit Score: 481.94 E-value: 6.18e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 1 MCGIVGYVGH------RQALDVVLNGLRRLEYRGYDSAGVAVltDAGLTVE-------RKAGRLANL------EARLAEV 61
Cdd:PLN02981 1 MCGIFAYLNYnvprerRFILEVLFNGLRRLEYRGYDSAGIAI--DNDPSLEsssplvfREEGKIESLvrsvyeEVAETDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 62 GVD-SFAGTAGMGHTRWATHGAPIDRNSHPH-RDATGRVAVVHNGIIENFAALRAELEAAGVELASDTDSETAAHLIARE 139
Cdd:PLN02981 79 NLDlVFENHAGIAHTRWATHGPPAPRNSHPQsSGPGNEFLVVHNGIITNYEVLKETLLRHGFTFESDTDTEVIPKLAKFV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 140 YGAAKERGGGL--AEAVRTVCRRLEGAFTLVVSHADEPDLIVAARRSSPLVVGLGDG----------------------- 194
Cdd:PLN02981 159 FDKLNEEEGDVtfSQVVMEVMRQLEGAYALIFKSPHYPNELVACKRGSPLLLGVKELpeeknssavftsegfltknrdkp 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 195 -ETFVASDVAAFIEHTREAVELGQDQLVEITRDGYRVTDFHGE-----DAPVKPFTVDWDLSAAE-------KGGHEYFM 261
Cdd:PLN02981 239 kEFFLASDASAVVEHTKRVLVIEDNEVVHLKDGGVGIYKFENEkgrggGGLSRPASVERALSTLEmeveqimKGNYDHYM 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 262 LKEIEEQPEALANTLRGHFVDG------RVVLDEQRLSDQDLRDVDKVFVVACGSAYHSGLVAKYAIEHWTRLPVEVELA 335
Cdd:PLN02981 319 QKEIHEQPESLTTTMRGRLIRGgsgkakRVLLGGLKDHLKTIRRSRRIVFIGCGTSYNAALAARPILEELSGVPVTMELA 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 336 SEFRYRDPVLDRDTLVVAVSQSGETADTLEAVRHAREQKARVLAVCNTNGAQIPRESDAVLYTHAGPEIGVASTKAFLAQ 415
Cdd:PLN02981 399 SDLLDRQGPIYREDTAVFVSQSGETADTLRALEYAKENGALCVGITNTVGSAISRGTHCGVHINAGAEIGVASTKAYTSQ 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 416 IAANYLVGLALAQargtkyaDEVAREFR------ELEAMPKAVSRVLETVERVRALGRELADSKAVLFLGRHVGYPVALE 489
Cdd:PLN02981 479 IVAMTMLALALGE-------DSISSRSRreaiidGLFDLPNKVREVLKLDQEMKELAELLIDEQSLLVFGRGYNYATALE 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 490 GALKLKELAYMHAEGFAAGELKHGPIALIEEGLPVVVVMPspkgRAVLHAKLVSNISEIQARGARTVVIAEEGDETVRPF 569
Cdd:PLN02981 552 GALKVKEVALMHSEGILAGEMKHGPLALVDETLPIIVIAT----RDACFSKQQSVIQQLRARKGRLIVICSKGDASSVCP 627
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 1906442648 570 ADE--LIEVPAVPTLLQPLVSTVPLQVLAAEIARARGYDVDKPRNLAKSVTVE 620
Cdd:PLN02981 628 SGGcrVIEVPQVEDCLQPVINIVPLQLLAYHLTVLRGHNVDQPRNLAKSVTTQ 680
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
1-619 |
1.90e-162 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 479.13 E-value: 1.90e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 1 MCGIVGYVGHRQALDVVLNGLRRLEYRGYDSAGVAVLTDAG-LTVERKAGRLANLEA--RLAEVGVDSFAG-TAGMGHTR 76
Cdd:PTZ00295 24 CCGIVGYLGNEDASKILLEGIEILQNRGYDSCGISTISSGGeLKTTKYASDGTTSDSieILKEKLLDSHKNsTIGIAHTR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 77 WATHGAPIDRNSHPHRDATGRVAVVHNGIIENFAALRAELEAAGVELASDTDSETAAHLIAREYgaakERGGGLAEAVRT 156
Cdd:PTZ00295 104 WATHGGKTDENAHPHCDYKKRIALVHNGTIENYVELKSELIAKGIKFRSETDSEVIANLIGLEL----DQGEDFQEAVKS 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 157 VCRRLEGAFTLVVSHADEPDLIVAARRSSPLVVGLGDGETFVASDVAAFIEHTREAVELGQDQLVEITRDGyrVTDFHge 236
Cdd:PTZ00295 180 AISRLQGTWGLCIIHKDNPDSLIVARNGSPLLVGIGDDSIYVASEPSAFAKYTNEYISLKDGEIAELSLEN--VNDLY-- 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 237 dAPVKPFTVDWDLSAAEKGGHEYFMLKEIEEQPEALANTL--RGHFVDG--RVVL--DEQRlsDQDLRDVDKVFVVACGS 310
Cdd:PTZ00295 256 -TQRRVEKIPEEVIEKSPEPYPHWTLKEIFEQPIALSRALnnGGRLSGYnnRVKLggLDQY--LEELLNIKNLILVGCGT 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 311 AYHSGLVAKYAIEHWTRL-PVEVELASEF-RYRDPvlDRDTLVVAVSQSGETADTLEAVRHAREQKARVLAVCNTNGAQI 388
Cdd:PTZ00295 333 SYYAALFAASIMQKLKCFnTVQVIDASELtLYRLP--DEDAGVIFISQSGETLDVVRALNLADELNLPKISVVNTVGSLI 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 389 PRESDAVLYTHAGPEIGVASTKAFLAQIAANYLVGLALAQARGTKYADEVAREF-RELEAMPKAVSRVLETV-ERVRALG 466
Cdd:PTZ00295 411 ARSTDCGVYLNAGREVAVASTKAFTSQVTVLSLIALWFAQNKEYSCSNYKCSSLiNSLHRLPTYIGMTLKSCeEQCKRIA 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 467 RELADSKAVLFLGRHVGYPVALEGALKLKELAYMHAEGFAAGELKHGPIALI--EEGLPVVVVMPSPKgravlHAKLVSN 544
Cdd:PTZ00295 491 EKLKNAKSMFILGKGLGYPIALEGALKIKEITYIHAEGFSGGALKHGPFALIdkEKNTPVILIILDDE-----HKELMIN 565
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1906442648 545 I-SEIQARGARTVVIAEEGDEtVRPFADELIEVPAVpTLLQPLVSTVPLQVLAAEIARARGYDVDKPRNLAKSVTV 619
Cdd:PTZ00295 566 AaEQVKARGAYIIVITDDEDL-VKDFADEIILIPSN-GPLTALLAVIPLQLLAYEIAILRGINPDKPRGLAKTVTV 639
|
|
| PTZ00394 |
PTZ00394 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
1-620 |
1.64e-138 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 173585 [Multi-domain] Cd Length: 670 Bit Score: 418.90 E-value: 1.64e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 1 MCGIVGYVGH------RQALDVVLNGLRRLEYRGYDSAGVAVltDAGLTVE-----------------RKAGRLANLEAR 57
Cdd:PTZ00394 1 MCGIFGYANHnvprtvEQILNVLLDGIQKVEYRGYDSAGLAI--DANIGSEkedgtaasaptprpcvvRSVGNISQLREK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 58 LAEVGVD--------SFAGTAGMGHTRWATHGAPIDRNSHPHRDATGRVAVVHNGIIENFAALRAELEAAGVELASDTDS 129
Cdd:PTZ00394 79 VFSEAVAatlppmdaTTSHHVGIAHTRWATHGGVCERNCHPQQSNNGEFTIVHNGIVTNYMTLKELLKEEGYHFSSDTDT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 130 ETAAHLIarEYGAAKERGGGLAEAVRTVCRRLEGAFTLVVSHADEPDLIVAARRSSPLVVGL------------------ 191
Cdd:PTZ00394 159 EVISVLS--EYLYTRKGIHNFADLALEVSRMVEGSYALLVKSVYFPGQLAASRKGSPLMVGIrrtddrgcvmklqtydlt 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 192 ---GDGETFVASDVAAFIEHTREAVELGQDQLVEITRDGYRVTDFHGEDAPV---KPFTVDWDLSAAEKGGHEYFMLKEI 265
Cdd:PTZ00394 237 dlsGPLEVFFSSDVNSFAEYTREVVFLEDGDIAHYCDGALRFYNAAERQRSIvkrEVQHLDAKPEGLSKGNYPHFMLKEI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 266 EEQPEALANTLRGH--FVDGRVVLDEqrLSDQDLRDV---DKVFVVACGSAYHSGLVAKYAIEHWTRLPVEVELASEFRY 340
Cdd:PTZ00394 317 YEQPESVISSMHGRidFSSGTVQLSG--FTQQSIRAIltsRRILFIACGTSLNSCLAVRPLFEELVPLPISVENASDFLD 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 341 RDPVLDRDTLVVAVSQSGETADTLEAVRHAREQKARVLAVCNTNGAQIPRESDAVLYTHAGPEIGVASTKAFLAQIAANY 420
Cdd:PTZ00394 395 RRPRIQRDDVCFFVSQSGETADTLMALQLCKEAGAMCVGITNVVGSSISRLTHYAIHLNAGVEVGVASTKAYTSQVVVLT 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 421 LVGLALA--QARGTKYADEVareFRELEAMPKAVSRVLE-TVERVRALGRELADSKAVLFLGRHVGYPVALEGALKLKEL 497
Cdd:PTZ00394 475 LVALLLSsdSVRLQERRNEI---IRGLAELPAAISECLKiTHDPVKALAARLKESSSILVLGRGYDLATAMEAALKVKEL 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 498 AYMHAEGFAAGELKHGPIALIEEGLPVVVVMPSPKgravlHAKLV-SNISEIQARGARTVVIAEEGDETVRPFADELIEV 576
Cdd:PTZ00394 552 SYVHTEGIHSGELKHGPLALIDETSPVLAMCTHDK-----HFGLSkSAVQQVKARGGAVVVFATEVDAELKAAASEIVLV 626
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 1906442648 577 PAVPTLLQPLVSTVPLQVLAAEIARARGYDVDKPRNLAKSVTVE 620
Cdd:PTZ00394 627 PKTVDCLQCVVNVIPFQLLAYYMALLRGNNVDCPRNLAKSVTVQ 670
|
|
| GFAT |
cd00714 |
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ... |
2-223 |
6.30e-108 |
|
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: 323.63 E-value: 6.30e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 2 CGIVGYVGHRQALDVVLNGLRRLEYRGYDSAGVAVLTDAGLTVERKAGRLANLEARLAEvgvDSFAGTAGMGHTRWATHG 81
Cdd:cd00714 1 CGIVGYIGKREAVDILLEGLKRLEYRGYDSAGIAVIGDGSLEVVKAVGKVANLEEKLAE---KPLSGHVGIGHTRWATHG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 82 APIDRNSHPHRDATGRVAVVHNGIIENFAALRAELEAAGVELASDTDSETAAHLIAREYgaakERGGGLAEAVRTVCRRL 161
Cdd:cd00714 78 EPTDVNAHPHRSCDGEIAVVHNGIIENYAELKEELEAKGYKFESETDTEVIAHLIEYYY----DGGLDLLEAVKKALKRL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1906442648 162 EGAFTLVVSHADEPDLIVAARRSSPLVVGLGDGETFVASDVAAFIEHTREAVELGQDQLVEI 223
Cdd:cd00714 154 EGAYALAVISKDEPDEIVAARNGSPLVIGIGDGENFVASDAPALLEHTRRVIYLEDGDIAVI 215
|
|
| AgaS |
COG2222 |
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ... |
262-620 |
5.38e-73 |
|
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: 237.87 E-value: 5.38e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 262 LKEIEEQPEALANTLRGHFVDGRVVLDEQRLsdqdlRDVDKVFVVACGSAYHSGLVAKYAIEHWTRLPVEVELASEF-RY 340
Cdd:COG2222 1 AREIAQQPEAWRRALAALAAAIAALLARLRA-----KPPRRVVLVGAGSSDHAAQAAAYLLERLLGIPVAALAPSELvVY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 341 RDPVLDRDTLVVAVSQSGETADTLEAVRHAREQKARVLAVCNTNGAQIPRESDAVLYTHAGPEIGVASTKAFLAQIAAny 420
Cdd:COG2222 76 PAYLKLEGTLVVAISRSGNSPEVVAALELAKARGARTLAITNNPDSPLAEAADRVLPLPAGPEKSVAATKSFTTMLLA-- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 421 lvGLALAQARGtkyADEVAREfrELEAMPKAVSRVLETVERVRALGrELADSKAVLFLGRHVGYPVALEGALKLKELAYM 500
Cdd:COG2222 154 --LLALLAAWG---GDDALLA--ALDALPAALEAALAADWPAAALA-ALADAERVVFLGRGPLYGLAREAALKLKELSAG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 501 HAEGFAAGELKHGPIALIEEGLPVVVVMPSPKGRAvLHAKLvsnISEIQARGARTVVIAEEGDETVRpfadeLIEVPAVP 580
Cdd:COG2222 226 HAEAYSAAEFRHGPKSLVDPGTLVVVLASEDPTRE-LDLDL---AAELRALGARVVAIGAEDDAAIT-----LPAIPDLH 296
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1906442648 581 TLLQPLVSTVPLQVLAAEIARARGYDVDKPRNLAKSVTVE 620
Cdd:COG2222 297 DALDPLLLLVVAQRLALALALARGLDPDTPRHLNKVVKTV 336
|
|
| SIS_GlmS_GlmD_2 |
cd05009 |
SIS (Sugar ISomerase) domain repeat 2 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
460-618 |
1.44e-60 |
|
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: 198.64 E-value: 1.44e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 460 ERVRALGRELADSKAVLFLGRHVGYPVALEGALKLKELAYMHAEGFAAGELKHGPIALIEEGLPVVVVMPSPKgravLHA 539
Cdd:cd05009 1 EDIKELAEKLKEAKSFYVLGRGPNYGTALEGALKLKETSYIHAEAYSAGEFKHGPIALVDEGTPVIFLAPEDR----LEE 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1906442648 540 KLVSNISEIQARGARTVVIAEEGDEtvRPFADELIEVPAVPTLLQPLVSTVPLQVLAAEIARARGYDVDKPRNLAKSVT 618
Cdd:cd05009 77 KLESLIKEVKARGAKVIVITDDGDA--KDLADVVIRVPATVEELSPLLYIVPLQLLAYHLAVARGIDPDKPRNLAKSVT 153
|
|
| SIS_GlmS_GlmD_1 |
cd05008 |
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
302-427 |
1.48e-59 |
|
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and Glucosamine-6-phosphate deaminase (GlmD). The SIS domain is found in many phosphosugar isomerases and phosphosugar binding proteins. GlmS contains a N-terminal glutaminase domain and two C-terminal SIS domains and catalyzes the first step in hexosamine metabolism, converting fructose 6-phosphate into glucosamine 6-phosphate using glutamine as nitrogen source. The glutaminase domain hydrolyzes glutamine to glutamate and ammonia. Ammonia is transferred through a channel to the isomerase domain for glucosamine 6-phosphate synthesis. The end product of the pathway is N-acetylglucosamine, which plays multiple roles in eukaryotic cells including being a building block of bacterial and fungal cell walls. In the absence of glutamine, GlmS catalyzes the isomerization of fructose 6-phosphate into glucose 6- phosphate (PGI-like activity). Glucosamine-6-phosphate deaminase (GlmD) contains two SIS domains and catalyzes the deamination and isomerization of glucosamine-6-phosphate into fructose-6-phosphate with the release of ammonia; in presence of high ammonia concentration, GlmD can catalyze the reverse reaction.
Pssm-ID: 240141 [Multi-domain] Cd Length: 126 Bit Score: 194.64 E-value: 1.48e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 302 KVFVVACGSAYHSGLVAKYAIEHWTRLPVEVELASEFRYRDPVLDRDTLVVAVSQSGETADTLEAVRHAREQKARVLAVC 381
Cdd:cd05008 1 RILIVGCGTSYHAALVAKYLLERLAGIPVEVEAASEFRYRRPLLDEDTLVIAISQSGETADTLAALRLAKEKGAKTVAIT 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1906442648 382 NTNGAQIPRESDAVLYTHAGPEIGVASTKAFLAQIAANYLVGLALA 427
Cdd:cd05008 81 NVVGSTLAREADYVLYLRAGPEISVAATKAFTSQLLALLLLALALA 126
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
2-213 |
1.29e-54 |
|
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: 185.34 E-value: 1.29e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 2 CGIVGYVGHRQALDVVL----NGLRRLEYRGYDSAGVAVLTDAGLTVERKAGRLANLEARLAEvgvDSFAGTAGMGHTRW 77
Cdd:cd00352 1 CGIFGIVGADGAASLLLllllRGLAALEHRGPDGAGIAVYDGDGLFVEKRAGPVSDVALDLLD---EPLKSGVALGHVRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 78 ATHGAPIDRNSHPHRDATGRVAVVHNGIIENFAALRAELEAAGVELASDTDSETAAHLIAREYgaakeRGGGLAEAVRTV 157
Cdd:cd00352 78 ATNGLPSEANAQPFRSEDGRIALVHNGEIYNYRELREELEARGYRFEGESDSEVILHLLERLG-----REGGLFEAVEDA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 158 CRRLEGAFTLVVSHADePDLIVAARRS---SPLVVGLG-DGETFVASDVAAFIEHTREAV 213
Cdd:cd00352 153 LKRLDGPFAFALWDGK-PDRLFAARDRfgiRPLYYGITkDGGLVFASEPKALLALPFKGV 211
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
297-425 |
1.01e-34 |
|
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars. Presumably the SIS domains bind to the end-product of the pathway.
Pssm-ID: 426230 [Multi-domain] Cd Length: 131 Bit Score: 127.80 E-value: 1.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 297 LRDVDKVFVVACGSAYHSGLVAKYAIEHWTRLPVEVELASEFRYR-DPVLDRDTLVVAVSQSGETADTLEAVRHAREQKA 375
Cdd:pfam01380 2 LAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGvLALVDEDDLVIAISYSGETKDLLAAAELAKARGA 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1906442648 376 RVLAVCNTNGAQIPRESDAVLYTHAGPEIGVASTKAFLAQIAANYLVGLA 425
Cdd:pfam01380 82 KIIAITDSPGSPLAREADHVLYINAGPETGVASTKSITAQLAALDALAVA 131
|
|
| PurF |
COG0034 |
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ... |
1-239 |
5.55e-30 |
|
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: 123.21 E-value: 5.55e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 1 MCGIVGYVGHRQALDVVLNGLRRLEYRGYDSAGVAVLTDAGLTVERKAGRLANL--EARLaevgvDSFAGTAGMGHTRWA 78
Cdd:COG0034 7 ECGVFGIYGHEDVAQLTYYGLYALQHRGQESAGIATSDGGRFHLHKGMGLVSDVfdEEDL-----ERLKGNIAIGHVRYS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 79 THGAPIDRNSHPH--RDATGRVAVVHNGIIENFAALRAELEAAGVELASDTDSETAAHLIAREYgaakeRGGGLAEAVRT 156
Cdd:COG0034 82 TTGSSSLENAQPFyvNSPFGSIALAHNGNLTNAEELREELEEEGAIFQTTSDTEVILHLIAREL-----TKEDLEEAIKE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 157 VCRRLEGAFTLVVSHADEpdlIVAAR-----RssPLVVGLGDGETFVASDVAAF----IEHTREaVELGqdQLVEITRDG 227
Cdd:COG0034 157 ALRRVKGAYSLVILTGDG---LIAARdpngiR--PLVLGKLEDGYVVASESCALdilgAEFVRD-VEPG--EIVVIDEDG 228
|
250
....*....|..
gi 1906442648 228 YRVTDFHGEDAP 239
Cdd:COG0034 229 LRSRQFAEKPRP 240
|
|
| GPATase_N |
cd00715 |
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ... |
2-239 |
9.45e-28 |
|
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: 112.17 E-value: 9.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 2 CGIVGYVGHRQALDVVLNGLRRLEYRGYDSAGVAVLTDAGLTVERKAGRLANL--EARLaevgvDSFAGTAGMGHTRWAT 79
Cdd:cd00715 1 CGVFGIYGAEDAARLTYLGLYALQHRGQESAGIATSDGKRFHTHKGMGLVSDVfdEEKL-----RRLPGNIAIGHVRYST 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 80 HGAPIDRNSHPH--RDATGRVAVVHNGIIENFAALRAELEAAGVELASDTDSETAAHLIAREYgaakeRGGGLAEAVRTV 157
Cdd:cd00715 76 AGSSSLENAQPFvvNSPLGGIALAHNGNLVNAKELREELEEEGRIFQTTSDSEVILHLIARSL-----AKDDLFEAIIDA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 158 CRRLEGAFTLVVSHADEpdlIVAAR-----RssPLVVG-LGDGETFVASDVAAF----IEHTREaVELGqdQLVEITRDG 227
Cdd:cd00715 151 LERVKGAYSLVIMTADG---LIAVRdphgiR--PLVLGkLEGDGYVVASESCALdiigAEFVRD-VEPG--EIVVIDDDG 222
|
250
....*....|..
gi 1906442648 228 YRVTDFHGEDAP 239
Cdd:cd00715 223 LESSQRAPKPKP 234
|
|
| purF |
TIGR01134 |
amidophosphoribosyltransferase; Alternate name: glutamine phosphoribosylpyrophosphate (PRPP) ... |
2-242 |
5.46e-22 |
|
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: 98.93 E-value: 5.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 2 CGIVGYVGHRQ-ALDVVLNGLRRLEYRGYDSAGVAVLTDAGLTVERKAGRLANL--EARLAEVgvdsfAGTAGMGHTRWA 78
Cdd:TIGR01134 1 CGVVGIYGQEEvAASLTYYGLYALQHRGQESAGISVFDGNRFRLHKGNGLVSDVfnEEHLQRL-----KGNVGIGHVRYS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 79 THGAPIDRNSHP--HRDATGRVAVVHNGIIENFAALRAELEAAGVELASDTDSETAAHLIAREYgaakERGGGLAEAVRT 156
Cdd:TIGR01134 76 TAGSSGLENAQPfvVNSPYGGLALAHNGNLVNADELRRELEEEGRHFNTTSDSEVLLHLLAHND----ESKDDLFDAVAR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 157 VCRRLEGAFTLVVSHADEpdlIVAAR-----RssPLVVGLGDGETFVASDVAAF----IEHTREaVELGqdQLVEITRDG 227
Cdd:TIGR01134 152 VLERVRGAYALVLMTEDG---LVAVRdphgiR--PLVLGRRGDGYVVASESCALdilgAEFVRD-VEPG--EVVVIFDGG 223
|
250
....*....|....*
gi 1906442648 228 YRVTDFhgEDAPVKP 242
Cdd:TIGR01134 224 LESRQC--ARRPRAP 236
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
468-596 |
8.29e-21 |
|
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: 88.51 E-value: 8.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 468 ELADSKAVLFLGRHVGYPVALEGALKLKELAYMHAEGFAAGELKHGPIALIEEGLPVVVVmpSPKGRAvlhAKLVSNISE 547
Cdd:pfam01380 1 LLAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGVLALVDEDDLVIAI--SYSGET---KDLLAAAEL 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1906442648 548 IQARGARTVVIAEEGDETVRPFADELIEVPAVPTLLQPLVSTVPLQVLA 596
Cdd:pfam01380 76 AKARGAKIIAITDSPGSPLAREADHVLYINAGPETGVASTKSITAQLAA 124
|
|
| GlxB |
cd01907 |
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ... |
2-204 |
5.00e-19 |
|
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: 86.94 E-value: 5.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 2 CGIVGYV---GHRQALDVVLNGLRRLEYRG-YDSAGVAVLTDAGLTVeRKAGRlaNLEArLAEVG----------VDSFA 67
Cdd:cd01907 1 CGIFGIMskdGEPFVGALLVEMLDAMQERGpGDGAGFALYGDPDAFV-YSSGK--DMEV-FKGVGypediarrydLEEYK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 68 GTAGMGHTRWATHGaPIDR-NSHPHrdATGRVAVVHNGIIENFAALRAELEAAGVELASDTDSETAAHLIA---REYG-- 141
Cdd:cd01907 77 GYHWIAHTRQPTNS-AVWWyGAHPF--SIGDIAVVHNGEISNYGSNREYLERFGYKFETETDTEVIAYYLDlllRKGGlp 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1906442648 142 --------AAKERGGGLAEAVRTVCRRLE--GAFTLVVSHADEPDLIVAARRSSPLVVGLGDGETFVASDVAA 204
Cdd:cd01907 154 leyykhiiRMPEEERELLLALRLTYRLADldGPFTIIVGTPDGFIVIRDRIKLRPAVVAETDDYVAIASEECA 226
|
|
| SIS_1 |
cd05710 |
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ... |
303-401 |
5.09e-18 |
|
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: 80.31 E-value: 5.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 303 VFVVACGSAYHSGLVAKYAIEHWTRLPVEVELASEFRYRDPV-LDRDTLVVAVSQSGETADTLEAVRHAREQKARVLAVC 381
Cdd:cd05710 2 VFFVGCGGSLADMYPAKYFLKKESKLPVFVYNAAEFLHTGPKrLTEKSVVILASHSGNTKETVAAAKFAKEKGATVIGLT 81
|
90 100
....*....|....*....|
gi 1906442648 382 NTNGAQIPRESDAVLYTHAG 401
Cdd:cd05710 82 DDEDSPLAKLADYVIVYGFE 101
|
|
| PLN02440 |
PLN02440 |
amidophosphoribosyltransferase |
1-316 |
6.30e-17 |
|
amidophosphoribosyltransferase
Pssm-ID: 215241 [Multi-domain] Cd Length: 479 Bit Score: 83.96 E-value: 6.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 1 MCGIVGYVGHRQALDVVLNGLRRLEYRGYDSAGVaVLTDAGLTVERKAGRLanlearLAEV----GVDSFAGTAGMGHTR 76
Cdd:PLN02440 1 ECGVVGIFGDPEASRLCYLGLHALQHRGQEGAGI-VTVDGNRLQSITGNGL------VSDVfdesKLDQLPGDIAIGHVR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 77 WATHGAPIDRNSHPHRDAT--GRVAVVHNGIIENFAALRAELEAAGVELASDTDSETAAHLIareygaAKERGGGLAEAV 154
Cdd:PLN02440 74 YSTAGASSLKNVQPFVANYrfGSIGVAHNGNLVNYEELRAKLEENGSIFNTSSDTEVLLHLI------AISKARPFFSRI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 155 RTVCRRLEGAFTLVVSHADEpdlIVAARRSS---PLVVGL-GDGETFVASDVAAF--IEHTREAvELGQDQLVEITRDGY 228
Cdd:PLN02440 148 VDACEKLKGAYSMVFLTEDK---LVAVRDPHgfrPLVMGRrSNGAVVFASETCALdlIGATYER-EVNPGEVIVVDKDKG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 229 RVTDFHGEDAPVKPFTVDwdlsaaekggHEYFmlkeieeqpeALANTLrghfVDGRVVLDEQ-----RLSDQDLRDVDKV 303
Cdd:PLN02440 224 VSSQCLMPHPEPKPCIFE----------HIYF----------ARPNSI----VFGRSVYESRlefgeILATEIPVDCDVV 279
|
330 340
....*....|....*....|
gi 1906442648 304 -------FVVACGSAYHSGL 316
Cdd:PLN02440 280 ipvpdsgRVAALGYAAKLGV 299
|
|
| SIS_RpiR |
cd05013 |
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ... |
297-422 |
9.94e-15 |
|
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: 71.49 E-value: 9.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 297 LRDVDKVFVVACGsayHSGLVAKYAIEHWTRLPVEVELAS---EFRYRDPVLDRDTLVVAVSQSGETADTLEAVRHAREQ 373
Cdd:cd05013 10 LAKARRIYIFGVG---SSGLVAEYLAYKLLRLGKPVVLLSdphLQLMSAANLTPGDVVIAISFSGETKETVEAAEIAKER 86
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1906442648 374 KARVLAVCNTNGAQIPRESDAVLYTHAgpEIGVASTKAFLAQIAANYLV 422
Cdd:cd05013 87 GAKVIAITDSANSPLAKLADIVLLVSS--EEGDFRSSAFSSRIAQLALI 133
|
|
| GATase_6 |
pfam13522 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
66-201 |
5.91e-14 |
|
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: 68.87 E-value: 5.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 66 FAGTAGMGHTRWATHGAPIDRNsHPHRDATGRVAVVHNGIIENFAALRAELEAAGVELASDTDSETAAHLiAREYGAAke 145
Cdd:pfam13522 8 VEGGVALGHVRLAIVDLPDAGN-QPMLSRDGRLVLVHNGEIYNYGELREELADLGHAFRSRSDTEVLLAL-YEEWGED-- 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1906442648 146 rggglaeavrtVCRRLEGAFTLVVSHADEPDLIVAARR--SSPLVVGLGDGETFVASD 201
Cdd:pfam13522 84 -----------CLERLRGMFAFAIWDRRRRTLFLARDRlgIKPLYYGILGGGFVFASE 130
|
|
| PRK05793 |
PRK05793 |
amidophosphoribosyltransferase; Provisional |
2-205 |
1.58e-13 |
|
amidophosphoribosyltransferase; Provisional
Pssm-ID: 235611 [Multi-domain] Cd Length: 469 Bit Score: 73.14 E-value: 1.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 2 CGIVGYVGHRQALDVVLN--GLRRLEYRGYDSAGVAVLTDAGLTVERKAGRLANLearLAEVGVDSFAGTAGMGHTRWAT 79
Cdd:PRK05793 15 CGVFGVFSKNNIDVASLTyyGLYALQHRGQESAGIAVSDGEKIKVHKGMGLVSEV---FSKEKLKGLKGNSAIGHVRYST 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 80 HGAPIDRNSHP--HRDATGRVAVVHNGIIENFAALRAELEAAGVELASDTDSETAAHLIAREYgaakerGGGLAEAVRTV 157
Cdd:PRK05793 92 TGASDLDNAQPlvANYKLGSIAIAHNGNLVNADVIRELLEDGGRIFQTSIDSEVILNLIARSA------KKGLEKALVDA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1906442648 158 CRRLEGAFTLVVSHADEpdlIVAARRSS---PLVVGLGDGETFVASDVAAF 205
Cdd:PRK05793 166 IQAIKGSYALVILTEDK---LIGVRDPHgirPLCLGKLGDDYILSSESCAL 213
|
|
| RpiR |
COG1737 |
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ... |
270-448 |
2.56e-13 |
|
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains [Transcription];
Pssm-ID: 441343 [Multi-domain] Cd Length: 286 Bit Score: 70.73 E-value: 2.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 270 EALANTLRghfvdgrvVLDEQRLSD--QDLRDVDKVFVVACGSayhSGLVAKYAIEHWTRLPVEVEL----ASEFRYRDP 343
Cdd:COG1737 110 ANLEETLE--------LLDEEALERavDLLAKARRIYIFGVGA---SAPVAEDLAYKLLRLGKNVVLldgdGHLQAESAA 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 344 VLDRDTLVVAVSQSGETADTLEAVRHAREQKARVLAVCNTNGAQIPRESDAVLYTHAGPEIGVAStkAFLAQIAANYLVG 423
Cdd:COG1737 179 LLGPGDVVIAISFSGYTRETLEAARLAKERGAKVIAITDSPLSPLAKLADVVLYVPSEEPTLRSS--AFSSRVAQLALID 256
|
170 180
....*....|....*....|....*...
gi 1906442648 424 L---ALAQARGtkyaDEVAREFRELEAM 448
Cdd:COG1737 257 AlaaAVAQRDG----DKARERLERTEAL 280
|
|
| AsnB |
cd00712 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ... |
2-232 |
1.12e-11 |
|
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: 64.50 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 2 CGIVGYVGHRQALD---VVLNGLRRLEYRGYDSAGVAVLTDAGLtverkagrlanlearlaevgvdsfagtagmGHTRWA 78
Cdd:cd00712 1 CGIAGIIGLDGASVdraTLERMLDALAHRGPDGSGIWIDEGVAL------------------------------GHRRLS 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 79 THgaPIDRNSHPHRDATGRVAVVHNGIIENFAALRAELEAAGVELASDTDSETAAHLIaREYGAAkerggglaeavrtVC 158
Cdd:cd00712 51 II--DLSGGAQPMVSEDGRLVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHLY-EEWGED-------------CL 114
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1906442648 159 RRLEGAFTLVVSHADEpDLIVAAR-----RssPLVVGLGDGETFVASDVAAFIEHTREAVELGQDQLVEITRDGYRVTD 232
Cdd:cd00712 115 ERLNGMFAFALWDKRK-RRLFLARdrfgiK--PLYYGRDGGGLAFASELKALLALPGVPRELDEAALAEYLAFQYVPAP 190
|
|
| frlB |
PRK11382 |
fructoselysine 6-phosphate deglycase; |
298-534 |
3.51e-11 |
|
fructoselysine 6-phosphate deglycase;
Pssm-ID: 183111 [Multi-domain] Cd Length: 340 Bit Score: 65.02 E-value: 3.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 298 RDVDKVFVVACGSAYHSGLVAKYAIEHWTRLPVEVELASEFRYRDPV-LDRDTLVVAVSQSGETADTLEAVRHAReqkar 376
Cdd:PRK11382 42 RDIDRIYFVACGSPLNAAQTAKHLADRFSDLQVYAISGWEFCDNTPYrLDDRCAVIGVSDYGKTEEVIKALELGR----- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 377 vlaVCNTNGAQIPRESDAVLYTHAGPEIGVASTKAFLAQIAANYLVGLALAqARGTKYAdEVAREFRELEAMPKAVSRVL 456
Cdd:PRK11382 117 ---ACGALTAAFTKRADSPITSAAEFSIDYQADCIWEIHLLLCYSVVLEMI-TRLAPNA-EIGKIKNDLKQLPNALGHLV 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 457 ETVE-RVRALGrELADSKAVLFLG-----RHVGYPvalEGALKLKELAYMHAEGFAAGELKHGPIALIEEGLPVVVVMPS 530
Cdd:PRK11382 192 RTWEeKGRQLG-ELASQWPMIYTVaagplRPLGYK---EGIVTLMEFTWTHGCVIESGEFRHGPLEIVEPGVPFLFLLGN 267
|
....
gi 1906442648 531 PKGR 534
Cdd:PRK11382 268 DESR 271
|
|
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
1-208 |
8.25e-09 |
|
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: 58.31 E-value: 8.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 1 MCGIVGYVGHRQALD--VVLNGLRRLEYRGYDSAGVAVltdagltverkagrlanlearlaevgvdsfAGTAGMGHTRWA 78
Cdd:COG0367 1 MCGIAGIIDFDGGADreVLERMLDALAHRGPDGSGIWV------------------------------DGGVALGHRRLS 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 79 ThgapIDRNSH---PHRDATGRVAVVHNGIIENFAALRAELEAAGVELASDTDSETAAHLIaREYGAAkerggglaeavr 155
Cdd:COG0367 51 I----IDLSEGghqPMVSEDGRYVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVILHAY-EEWGED------------ 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1906442648 156 tVCRRLEGAFTLVVSHADEpDLIVAAR-RSS--PLVVGLGDGETFVASDVAAFIEH 208
Cdd:COG0367 114 -CLERLNGMFAFAIWDRRE-RRLFLARdRFGikPLYYAEDGGGLAFASELKALLAH 167
|
|
| GATase_7 |
pfam13537 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
91-205 |
1.72e-08 |
|
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: 52.91 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 91 HRDATGRVAVVHNGIIENFAALRAELEAAGVELASDTDSETAAHLIAREYGAAkerggglaeavrtVCRRLEGAFTLVVS 170
Cdd:pfam13537 17 VSSEDGRYVIVFNGEIYNYRELRAELEAKGYRFRTHSDTEVILHLYEAEWGED-------------CVDRLNGMFAFAIW 83
|
90 100 110
....*....|....*....|....*....|....*....
gi 1906442648 171 HADEPDLIvAAR-RSS--PLVVGLGDGETFV-ASDVAAF 205
Cdd:pfam13537 84 DRRRQRLF-LARdRFGikPLYYGRDDGGRLLfASELKAL 121
|
|
| YafJ |
cd01908 |
Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine ... |
1-186 |
2.59e-08 |
|
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: 55.47 E-value: 2.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 1 MCGIVGYVGHRQALDVVL-----NGLRR----LEYRGY---DSAGVAVLTDAGLTVERKAGRLANLEARLAEVGVDSFAG 68
Cdd:cd01908 1 MCRLLGYSGAPIPLEPLLirpshSLLVQsggpREMKGTvhaDGWGIGWYEGKGGRPFRYRSPLPAWSDINLESLARPIKS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 69 TAGMGHTRWATHGAPIDRNSHPHRDatGRVAVVHNGIIENFAALRAELEAAGVEL-ASDTDSETAAHLIAREYGAAKERG 147
Cdd:cd01908 81 PLVLAHVRAATVGPVSLENCHPFTR--GRWLFAHNGQLDGFRLLRRRLLRLLPRLpVGTTDSELAFALLLSRLLERDPLD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1906442648 148 GG-LAEAVRTVCRRLE-----GAFTLVVShadEPDLIVAARRSSP 186
Cdd:cd01908 159 PAeLLDAILQTLRELAalappGRLNLLLS---DGEYLIATRYASA 200
|
|
| SIS |
cd04795 |
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
303-381 |
9.82e-08 |
|
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars.
Pssm-ID: 240112 [Multi-domain] Cd Length: 87 Bit Score: 49.68 E-value: 9.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 303 VFVVACGSAYHSGLVAKYAIEHWTRLPVEVELASEFRYRDPV--LDRDTLVVAVSQSGETADTLEAVRHAREQKARVLAV 380
Cdd:cd04795 1 IFVIGIGGSGAIAAYFALELLELTGIEVVALIATELEHASLLslLRKGDVVIALSYSGRTEELLAALEIAKELGIPVIAI 80
|
.
gi 1906442648 381 C 381
Cdd:cd04795 81 T 81
|
|
| PRK08674 |
PRK08674 |
bifunctional phosphoglucose/phosphomannose isomerase; Validated |
261-567 |
1.28e-07 |
|
bifunctional phosphoglucose/phosphomannose isomerase; Validated
Pssm-ID: 181536 [Multi-domain] Cd Length: 337 Bit Score: 53.83 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 261 MLKEIEEQPEALANTLRghfvdgrvvLDEQRLSDQDLRDVDKVFVVACG-SAYHSGLVAKYAIEHWtrlPVEVelaseFR 339
Cdd:PRK08674 4 MLEEYLNWPEQFEEALE---------IAISLDLEEDLEKIDNIVISGMGgSGIGGDLLRILLFDEL---KVPV-----FV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 340 YRD----PVLDRDTLVVAVSQSGETADTLEAVRHAREQKARVLAVcnTNG---AQIPREsdavlytHAGPEIGVAST--- 409
Cdd:PRK08674 67 NRDytlpAFVDEKTLVIAVSYSGNTEETLSAVEQALKRGAKIIAI--TSGgklKEMAKE-------HGLPVIIVPGGyqp 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 410 --------KAFLAQIAANYLVGLALAQARGTKYADEVAREfreleampkavsRVLETVERVRALGRELA---DSKAVLFL 478
Cdd:PRK08674 138 raalgylfTPLLKILEKLGLIPDKSAEVLETKIVLSELAE------------GLKEKVPTLKNLAKRLAgklYGRIPVIY 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 479 GRHVGYPVAL-------EGAlklKELAY------MH---AEGFAAGELKHGPIAlieeglpVVVVMPSPKGRAVLHAKLV 542
Cdd:PRK08674 206 GSGLTLAVAYrwktqinENA---KYPAFyneipeLNhneIVGYERPQSLLKYFF-------VVVLRDSEHPRIKKRVEIT 275
|
330 340
....*....|....*....|....*
gi 1906442648 543 SNIseIQARGARTVVIAEEGDETVR 567
Cdd:PRK08674 276 IDI--LTEAVINVIEIYPEGNSPLA 298
|
|
| SIS_PGI_PMI_1 |
cd05017 |
The members of this protein family contain the SIS (Sugar ISomerase) domain and have both the ... |
346-381 |
4.34e-07 |
|
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: 48.80 E-value: 4.34e-07
10 20 30
....*....|....*....|....*....|....*.
gi 1906442648 346 DRDTLVVAVSQSGETADTLEAVRHAREQKARVLAVC 381
Cdd:cd05017 42 DRKTLVIAVSYSGNTEETLSAVEQAKERGAKIVAIT 77
|
|
| PRK11337 |
PRK11337 |
MurR/RpiR family transcriptional regulator; |
340-400 |
2.90e-06 |
|
MurR/RpiR family transcriptional regulator;
Pssm-ID: 183089 [Multi-domain] Cd Length: 292 Bit Score: 49.37 E-value: 2.90e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1906442648 340 YRDP--------VLDRDTLVVAVSQSGETADTLEAVRHAREQKARVLAVCNTNGAQIPRESDAVLYTHA 400
Cdd:PRK11337 172 YDDAhimlmsaaLLQEGDVVLVVSHSGRTSDVIEAVELAKKNGAKIICITNSYHSPIAKLADYVICSTA 240
|
|
| SIS_Etherase |
cd05007 |
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ... |
350-415 |
1.68e-05 |
|
N-acetylmuramic acid 6-phosphate etherase. Members of this family contain the SIS (Sugar ISomerase) domain. The SIS domain is found in many phosphosugar isomerases and phosphosugar binding proteins. The bacterial cell wall sugar N-acetylmuramic acid carries a unique D-lactyl ether substituent at the C3 position. The etherase catalyzes the cleavage of the lactyl ether bond of N-acetylmuramic acid 6-phosphate.
Pssm-ID: 240140 [Multi-domain] Cd Length: 257 Bit Score: 46.75 E-value: 1.68e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1906442648 350 LVVAVSQSGETADTLEAVRHAREQKARVLAVCNTNGAQIPRESDAVLYTHAGPEIGVAST--KAFLAQ 415
Cdd:cd05007 121 VVIGIAASGRTPYVLGALRYARARGALTIGIACNPGSPLLQLADIAIALITGPEVVAGSTrlKAGTAQ 188
|
|
| PTZ00077 |
PTZ00077 |
asparagine synthetase-like protein; Provisional |
1-204 |
4.02e-05 |
|
asparagine synthetase-like protein; Provisional
Pssm-ID: 185431 [Multi-domain] Cd Length: 586 Bit Score: 46.63 E-value: 4.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 1 MCGIVGYVGHR----QALDVVLNGLRRLEYRGYDSAGVAVL-----TDAGLTVERkagrlanlearLAEVGVDSfagtag 71
Cdd:PTZ00077 1 MCGILAIFNSKgerhELRRKALELSKRLRHRGPDWSGIIVLenspgTYNILAHER-----------LAIVDLSD------ 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 72 mGHtrwathgapidrnsHPHRDATGRVAVVHNGIIENFAALRAELEAAGVELASDTDSETAAHLIaREYGAAKergggla 151
Cdd:PTZ00077 64 -GK--------------QPLLDDDETVALMQNGEIYNHWEIRPELEKEGYKFSSNSDCEIIGHLY-KEYGPKD------- 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1906442648 152 eavrtVCRRLEGAFTLVVSHADEPDLiVAARRS---SPLVVGLG-DGETFVASDVAA 204
Cdd:PTZ00077 121 -----FWNHLDGMFATVIYDMKTNTF-FAARDHigiIPLYIGYAkDGSIWFSSELKA 171
|
|
| SIS |
cd04795 |
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
484-560 |
4.12e-05 |
|
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: 42.36 E-value: 4.12e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1906442648 484 YPVALEGALKLKELAYMHAEGFAAGELKHGP-IALIEEGLPVVVVMPSPKGRAVLHAklvsnISEIQARGARTVVIAE 560
Cdd:cd04795 10 GAIAAYFALELLELTGIEVVALIATELEHASlLSLLRKGDVVIALSYSGRTEELLAA-----LEIAKELGIPVIAITD 82
|
|
| SIS_PHI |
cd05005 |
Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) ... |
295-400 |
3.00e-03 |
|
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: 39.10 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 295 QDLRDVDKVFVVACGsayHSGLVAK-YAIehwtRL-----PVEVElasefryRD---PVLDRDTLVVAVSQSGETADTLE 365
Cdd:cd05005 28 SAILNAKRIFVYGAG---RSGLVAKaFAM----RLmhlglNVYVV-------GEtttPAIGPGDLLIAISGSGETSSVVN 93
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90 100 110
....*....|....*....|....*....|....*
gi 1906442648 366 AVRHAREQKARVLAVCNTNGAQIPRESDAVLYTHA 400
Cdd:cd05005 94 AAEKAKKAGAKVVLITSNPDSPLAKLADVVVVIPA 128
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|
| GATase_4 |
pfam13230 |
Glutamine amidotransferases class-II; This family captures members that are not found in ... |
74-170 |
9.43e-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: 38.47 E-value: 9.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906442648 74 HTRWATHGAPIDRNSHPH-RDATGRVAV-VHNGIIENFaalraELEAAGVEL-ASDTDSETA-AHL---IAREYGAAKER 146
Cdd:pfam13230 77 HIRKATQGRVTLENTHPFmRELWGRYWIfAHNGDLKGY-----APKLSGRFQpVGSTDSELAfCWLldrLASRFPYARPS 151
|
90 100
....*....|....*....|....*.
gi 1906442648 147 GGGLAEAVRTVCRRL--EGAFTLVVS 170
Cdd:pfam13230 152 AGELFRALRELAREIaaHGTFNFLLS 177
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